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Conserved domains on  [gi|1621998274|ref|XP_028572703|]
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caskin-2 isoform X3 [Podarcis muralis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-356 3.74e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 3.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   87 LLGSTKRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMAS 166
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  167 LDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNShmcvalleGQSKDTSDPNYTTP 246
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------GADVNAQDNDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  247 LHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDIVNQfttsHASK 325
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE----NGNL 232

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1621998274  326 DIKQLLREASGILKVRALKDFWNLHDPTALN 356
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 562-632 2.38e-42

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


:

Pssm-ID: 188897  Cd Length: 71  Bit Score: 148.98  E-value: 2.38e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  562 WLPNYIPDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKLTDLRK 632
Cdd:cd09498      1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 338-399 1.16e-41

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


:

Pssm-ID: 212996  Cd Length: 62  Bit Score: 146.65  E-value: 1.16e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  338 LKVRALKDFWNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKGTDRVGYFPPSIVEVI 399
Cdd:cd12063      1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 496-561 1.52e-36

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


:

Pssm-ID: 188896  Cd Length: 66  Bit Score: 132.38  E-value: 1.52e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  496 GKDAEAIYNWLSEFQLEGYTANFLNAGYDVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSIAE 561
Cdd:cd09497      1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 926-1011 3.17e-30

Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. This region is predicted to be natively unstructured. Its function is not known.


:

Pssm-ID: 465308  Cd Length: 91  Bit Score: 115.29  E-value: 3.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  926 HKKRSHSLNRYALSD---GEGEEEEPPASSVGSYATLTRRPGRSQVPRTQPSSTAKVSRSQSFAIRARRKGPPPPPPKRL 1002
Cdd:pfam16907    1 PKKRSQSLNRYALSDgepEEEEEPPLGSGTLGSYATLTRRPGRSQLARLQPSPEKNVNRSQSFAVRARKKGPPPPPPKRL 80


                   ....*....
gi 1621998274 1003 SSVSSAQVG 1011
Cdd:pfam16907   81 SSVSSSTSS 89
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1420-1479 3.65e-27

C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. Part of this region is predicted to be in coiled-coil conformation. Its function is not known.


:

Pssm-ID: 465209  Cd Length: 61  Bit Score: 105.24  E-value: 3.65e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274 1420 QQRLEQTNSSLASTLEAAEKKINAEEA-DSNYGTAHSAKNILEDISNMFDDLAEQLDAMLD 1479
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESqSSGSAEVKSAGNILDDIGNMFDDLADQLDAMLD 61
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 404-437 6.92e-06

Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this region.CASK and Caskin1 are synaptic scaffolding proteins. The binding motif on human Caskin1 is EEIWVLRK. A similar motif is found on protein MINT1 and protein TIAM1, both shown to be able to bind to CASK though the motif. MINT1 and TIAM1 are not part of this family. This region is predicted to be natively unstructured.


:

Pssm-ID: 465190  Cd Length: 55  Bit Score: 44.65  E-value: 6.92e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1621998274  404 AGDRNSVGSEGSIGSIRSAGSGQSTEGTNGQITG 437
Cdd:pfam16600   12 GGDRSSVGSTGSVGSVRSSGSGQSSHALHAGSEG 45
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-356 3.74e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 3.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   87 LLGSTKRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMAS 166
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  167 LDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNShmcvalleGQSKDTSDPNYTTP 246
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------GADVNAQDNDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  247 LHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDIVNQfttsHASK 325
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE----NGNL 232

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1621998274  326 DIKQLLREASGILKVRALKDFWNLHDPTALN 356
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 562-632 2.38e-42

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 148.98  E-value: 2.38e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  562 WLPNYIPDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKLTDLRK 632
Cdd:cd09498      1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 338-399 1.16e-41

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212996  Cd Length: 62  Bit Score: 146.65  E-value: 1.16e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  338 LKVRALKDFWNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKGTDRVGYFPPSIVEVI 399
Cdd:cd12063      1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 496-561 1.52e-36

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 132.38  E-value: 1.52e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  496 GKDAEAIYNWLSEFQLEGYTANFLNAGYDVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSIAE 561
Cdd:cd09497      1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 926-1011 3.17e-30

Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. This region is predicted to be natively unstructured. Its function is not known.


Pssm-ID: 465308  Cd Length: 91  Bit Score: 115.29  E-value: 3.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  926 HKKRSHSLNRYALSD---GEGEEEEPPASSVGSYATLTRRPGRSQVPRTQPSSTAKVSRSQSFAIRARRKGPPPPPPKRL 1002
Cdd:pfam16907    1 PKKRSQSLNRYALSDgepEEEEEPPLGSGTLGSYATLTRRPGRSQLARLQPSPEKNVNRSQSFAVRARKKGPPPPPPKRL 80


                   ....*....
gi 1621998274 1003 SSVSSAQVG 1011
Cdd:pfam16907   81 SSVSSSTSS 89
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1420-1479 3.65e-27

C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. Part of this region is predicted to be in coiled-coil conformation. Its function is not known.


Pssm-ID: 465209  Cd Length: 61  Bit Score: 105.24  E-value: 3.65e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274 1420 QQRLEQTNSSLASTLEAAEKKINAEEA-DSNYGTAHSAKNILEDISNMFDDLAEQLDAMLD 1479
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESqSSGSAEVKSAGNILDDIGNMFDDLADQLDAMLD 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-305 1.02e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  206 LDLACEFGRLKVAQLLLNshmcvallEGQSKDTSDPNYTTPLHLAAKNGHKEIIRQLLKaGIEINKQTKTGTALHEAALY 285
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE--------NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARS 71

                           90       100
                   ....*....|....*....|
gi 1621998274  286 GKTEVVRLLLQGGIDVNIRN 305
Cdd:pfam12796   72 GHLEIVKLLLEKGADINVKD 91
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 568-627 4.57e-17

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 76.54  E-value: 4.57e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  568 PDDLMEWLSALGLPQYhKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:pfam00536    5 VEDVGEWLESIGLGQY-IDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PHA03095 PHA03095
ankyrin-like protein; Provisional
 95-312 2.21e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 2.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   95 NVNYQDVDGFSALH---HAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEP-ARLLLRAAASVNMASLDGQ 170
Cdd:PHA03095    39 DVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGR 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  171 IPLH--LSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLacefgrlkvaqLLLNSHMCVALLE-----GQSKDTSDPNY 243
Cdd:PHA03095   119 TPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRNANVELLRllidaGADVYAVDDRF 187

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  244 TTPLHLAAKNGH--KEIIRQLLKAGIEINKQTKTG-TALHEAALYG--KTEVVRLLLQGGIDVNIRNTYNQTAL 312
Cdd:PHA03095   188 RSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPL 261
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 568-627 1.74e-15

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 72.33  E-value: 1.74e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   568 PDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 495-557 6.18e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 6.18e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  495 EGKDAEAIYNWLSEFQLEGYTANFLnAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFR-AGYiDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 339-397 5.31e-09

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 53.31  E-value: 5.31e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274   339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGhihdsQKGTDRVGYFPPSIVE 397
Cdd:smart00326    4 QVRALYDY-TAQDPDELSFKKGDIITVLEKSDDGWWKG-----RLGRGKEGLFPSNYVE 56
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 495-557 5.76e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.84  E-value: 5.76e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274   495 EGKDAEAIYNWLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:smart00454    2 SQWSPESVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 139-314 3.13e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  139 PLHYAAWQGKVEP-ARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQhqSNPCLINKAkktpldlacefgrlkv 217
Cdd:cd22192     20 PLLLAAKENDVQAiKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEP---------------- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  218 aqlllnshMCVALLEGQskdtsdpnytTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTGTA---------------LHEA 282
Cdd:cd22192     82 --------MTSDLYQGE----------TALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFA 143

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1621998274  283 ALYGKTEVVRLLLQGGIDVNIRNTYNQTALDI 314
Cdd:cd22192    144 ACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 245-271 4.65e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 4.65e-06
                            10        20
                    ....*....|....*....|....*..
gi 1621998274   245 TPLHLAAKNGHKEIIRQLLKAGIEINK 271
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 404-437 6.92e-06

Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this region.CASK and Caskin1 are synaptic scaffolding proteins. The binding motif on human Caskin1 is EEIWVLRK. A similar motif is found on protein MINT1 and protein TIAM1, both shown to be able to bind to CASK though the motif. MINT1 and TIAM1 are not part of this family. This region is predicted to be natively unstructured.


Pssm-ID: 465190  Cd Length: 55  Bit Score: 44.65  E-value: 6.92e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1621998274  404 AGDRNSVGSEGSIGSIRSAGSGQSTEGTNGQITG 437
Cdd:pfam16600   12 GGDRSSVGSTGSVGSVRSSGSGQSSHALHAGSEG 45
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 339-399 9.18e-06

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 44.12  E-value: 9.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGhihdSQKGtdRVGYFPPSIVEVI 399
Cdd:pfam07653    1 YGRVIFDY-VGTDKNGLTLKKGDVVKVLGKDNDGWWEG----ETGG--RVGLVPSTAVEEI 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-356 3.74e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 3.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   87 LLGSTKRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMAS 166
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  167 LDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNShmcvalleGQSKDTSDPNYTTP 246
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------GADVNAQDNDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  247 LHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDIVNQfttsHASK 325
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE----NGNL 232

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1621998274  326 DIKQLLREASGILKVRALKDFWNLHDPTALN 356
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 562-632 2.38e-42

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 148.98  E-value: 2.38e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  562 WLPNYIPDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKLTDLRK 632
Cdd:cd09498      1 WLPDYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLKDLQK 71
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
76-345 7.66e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 7.66e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   76 LVAKVKASKSKLLGSTKRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLL 155
Cdd:COG0666     27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  156 LRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNShmcvalleGQS 235
Cdd:COG0666    107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA--------GAD 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  236 KDTSDPNYTTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDI 314
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1621998274  315 VNQFTTSHASKDIKQLLREASGILKVRALKD 345
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SH3_Caskin2 cd12063
Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein ...
 338-399 1.16e-41

Src Homology 3 domain of CASK interacting protein 2; Caskin2 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It shares a domain architecture with Caskin1, but does not bind CASK. The function of Caskin2 is still unknown. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212996  Cd Length: 62  Bit Score: 146.65  E-value: 1.16e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  338 LKVRALKDFWNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKGTDRVGYFPPSIVEVI 399
Cdd:cd12063      1 LKVRALKDFWNLHDPTALNVRAGDVITVLEQHPDGRWKGHIHDSQRGTDRVGYFPPSIVEVI 62
SH3_Caskin cd11880
Src Homology 3 domain of CASK interacting protein; Caskin proteins are multidomain adaptor ...
 338-398 1.92e-38

Src Homology 3 domain of CASK interacting protein; Caskin proteins are multidomain adaptor proteins that contain six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. There are two Caskin proteins called Caskin1 and Caskin2. Caskin1 binds to the multidomain scaffolding protein CASK through the CaM domain in competition with Munc-interacting protein 1 (Mint1). CASK participates in one of two evolutionarily conserved tripartite complexes containing either Mint1 and Velis or Caskin1 and Velis. Caskin1 may play a role in infantile myoclonic epilepsy. There is not much known about Caskin2; despite sharing a domain architecture with Caskin1, Caskin2 does not bind CASK. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212813  Cd Length: 61  Bit Score: 137.69  E-value: 1.92e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  338 LKVRALKDFWNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKGTDRVGYFPPSIVEV 398
Cdd:cd11880      1 LQVRATKDYWNNHDLTALNVRAGDIITVLEQHPDGRWKGHIHDNQTGNDRVGYFPPSLVEV 61
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 496-561 1.52e-36

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 132.38  E-value: 1.52e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  496 GKDAEAIYNWLSEFQLEGYTANFLNAGYDVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSIAE 561
Cdd:cd09497      1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQIPD 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
127-370 4.47e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 4.47e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  127 ATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPL 206
Cdd:COG0666     12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  207 DLACEFGRLKVAQLLLNShmcvalleGQSKDTSDPNYTTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALY 285
Cdd:COG0666     92 HAAARNGDLEIVKLLLEA--------GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGnTPLHLAAAN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  286 GKTEVVRLLLQGGIDVNIRNTYNQTALDIVnqftTSHASKDIKQLLREASGILKVRALKDFWNLHDptALNVRAGDIITV 365
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLA----AENGHLEIVKLLLEAGADVNAKDNDGKTALDL--AAENGNLEIVKL 237


                   ....*
gi 1621998274  366 LEQHA 370
Cdd:COG0666    238 LLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
61-280 2.84e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 2.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   61 LIQAVKNGDVPGVQKLVAKvkaskskllgstkRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPL 140
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEA-------------GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  141 HYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQL 220
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  221 LLNshmcvallEGQSKDTSDPNYTTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTGTALH 280
Cdd:COG0666    238 LLE--------AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Caskin-Pro-rich pfam16907
Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. ...
 926-1011 3.17e-30

Proline rich region of Caskin proteins; This proline rich region is found in Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. This region is predicted to be natively unstructured. Its function is not known.


Pssm-ID: 465308  Cd Length: 91  Bit Score: 115.29  E-value: 3.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  926 HKKRSHSLNRYALSD---GEGEEEEPPASSVGSYATLTRRPGRSQVPRTQPSSTAKVSRSQSFAIRARRKGPPPPPPKRL 1002
Cdd:pfam16907    1 PKKRSQSLNRYALSDgepEEEEEPPLGSGTLGSYATLTRRPGRSQLARLQPSPEKNVNRSQSFAVRARKKGPPPPPPKRL 80


                   ....*....
gi 1621998274 1003 SSVSSAQVG 1011
Cdd:pfam16907   81 SSVSSSTSS 89
Caskin-tail pfam16632
C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. ...
 1420-1479 3.65e-27

C-terminal region of Caskin; This region is found at the C-terminus of Caskin proteins. Caskins are CASK-binding synaptic scaffolding proteins. Part of this region is predicted to be in coiled-coil conformation. Its function is not known.


Pssm-ID: 465209  Cd Length: 61  Bit Score: 105.24  E-value: 3.65e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274 1420 QQRLEQTNSSLASTLEAAEKKINAEEA-DSNYGTAHSAKNILEDISNMFDDLAEQLDAMLD 1479
Cdd:pfam16632    1 QQRLEQTSTSLAAALQAVEKKIAQEESqSSGSAEVKSAGNILDDIGNMFDDLADQLDAMLD 61
SH3_Caskin1 cd12062
Src Homology 3 domain of CASK interacting protein 1; Caskin1 is a multidomain adaptor protein ...
 338-399 4.42e-26

Src Homology 3 domain of CASK interacting protein 1; Caskin1 is a multidomain adaptor protein that contains six ankyrin repeats, a single SH3 domain, tandem sterile alpha motif (SAM) domains, and a long disordered proline-rich region. It is expressed at high levels in the brain and is localized in presynaptic regions. It binds to the multidomain scaffolding protein CASK through the CaMK domain in competition with Munc-interacting protein 1 (Mint1). CASK participates in one of two evolutionarily conserved tripartite complexes containing either Mint1 and Velis or Caskin1 and Velis. Caskin1 may play a role in infantile myoclonic epilepsy. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212995  Cd Length: 62  Bit Score: 102.39  E-value: 4.42e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  338 LKVRALKDFWNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKGTDRVGYFPPSIVEVI 399
Cdd:cd12062      1 LQVRALKDYCNNYDLTSLNIKAGDVITVLEQHPDGRWKGCIHDNRTGNDRVGYFPSSLVEAI 62
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-305 1.02e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  206 LDLACEFGRLKVAQLLLNshmcvallEGQSKDTSDPNYTTPLHLAAKNGHKEIIRQLLKaGIEINKQTKTGTALHEAALY 285
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE--------NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARS 71

                           90       100
                   ....*....|....*....|
gi 1621998274  286 GKTEVVRLLLQGGIDVNIRN 305
Cdd:pfam12796   72 GHLEIVKLLLEKGADINVKD 91
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 568-627 4.57e-17

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 76.54  E-value: 4.57e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  568 PDDLMEWLSALGLPQYhKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:pfam00536    5 VEDVGEWLESIGLGQY-IDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PHA03095 PHA03095
ankyrin-like protein; Provisional
 95-312 2.21e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 2.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   95 NVNYQDVDGFSALH---HAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEP-ARLLLRAAASVNMASLDGQ 170
Cdd:PHA03095    39 DVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGR 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  171 IPLH--LSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLacefgrlkvaqLLLNSHMCVALLE-----GQSKDTSDPNY 243
Cdd:PHA03095   119 TPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRNANVELLRllidaGADVYAVDDRF 187

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  244 TTPLHLAAKNGH--KEIIRQLLKAGIEINKQTKTG-TALHEAALYG--KTEVVRLLLQGGIDVNIRNTYNQTAL 312
Cdd:PHA03095   188 RSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPL 261
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-333 4.79e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 4.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   94 LNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVN-MASLDGQIP 172
Cdd:PHA02875    26 INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTP 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  173 LHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNSHMCVallegqskDTSDPNYTTPLHLAAK 252
Cdd:PHA02875   106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL--------DIEDCCGCTPLIIAMA 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  253 NGHKEIIRQLLKAGIEINKQTKTG--TALHEAALYGKTEVVRLLLQGGIDVNIRNTY---NQTALDIVNQFTTSHASKDI 327
Cdd:PHA02875   178 KGDIAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADCNIMFMIegeECTILDMICNMCTNLESEAI 257


                   ....*.
gi 1621998274  328 KQLLRE 333
Cdd:PHA02875   258 DALIAD 263
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 568-627 1.74e-15

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 72.33  E-value: 1.74e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   568 PDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:smart00454    6 PESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-272 9.83e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 9.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  140 LHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHqsnpCLINkakktpldlacefgrlkvaq 219
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVN-------------------- 56

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  220 lllnshmcvallegqskdtSDPNYTTPLHLAAKNGHKEIIRQLLKAGIEINKQ 272
Cdd:pfam12796   57 -------------------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
568-627 9.18e-14

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 67.29  E-value: 9.18e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  568 PDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:pfam07647    6 LESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 94-302 1.26e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   94 LNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPL 173
Cdd:PHA02874   115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  174 HLSAQYGHYEVSEMLLQHQSNpcLINKAKK--TPLDLACEFGRlKVAQLLLNShmcvallegQSKDTSDPNYTTPLHLAA 251
Cdd:PHA02874   195 HNAAEYGDYACIKLLIDHGNH--IMNKCKNgfTPLHNAIIHNR-SAIELLINN---------ASINDQDIDGSTPLHHAI 262

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  252 KNG-HKEIIRQLL--KAGIEInKQTKTGTALHEAALY-GKTEVVRLLLQGGIDVN 302
Cdd:PHA02874   263 NPPcDIDIIDILLyhKADISI-KDNKGENPIDTAFKYiNKDPVIKDIIANAVLIK 316
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 570-626 3.66e-13

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 65.34  E-value: 3.66e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  570 DLMEWLSALGLPQYHKKLVSNgYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKK 626
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKN-EIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 495-557 6.18e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 6.18e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  495 EGKDAEAIYNWLSEFQLEGYTANFLnAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFR-AGYiDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 129-345 1.75e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  129 VDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDL 208
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  209 ACEFGRLKVAQLLLN--SHMCVALLEGqskdtsdpnyTTPLHLAAKngHKEIIRQLLKAGIEINKQTKTG-TALHEAALY 285
Cdd:PHA02874   197 AAEYGDYACIKLLIDhgNHIMNKCKNG----------FTPLHNAII--HNRSAIELLINNASINDQDIDGsTPLHHAINP 264

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  286 G-KTEVVRLLLQGGIDVNIRNTYNQTALDIVNQFTTSHASkdIKQLLREASGILKVRALKD 345
Cdd:PHA02874   265 PcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV--IKDIIANAVLIKEADKLKD 323
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 153-315 5.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 5.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  153 RLLLRAAASVNMASLD-GQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNShmcvall 231
Cdd:PHA02878   151 KLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN------- 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  232 eGQSKDTSDPNYTTPLHLAAKN-GHKEIIRQLLKAGIEINKQT--KTGTALHEAAlygKTE-VVRLLLQGGIDVNIRNTY 307
Cdd:PHA02878   224 -GASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyiLGLTALHSSI---KSErKLKLLLEYGADINSLNSY 299


                   ....*...
gi 1621998274  308 NQTALDIV 315
Cdd:PHA02878   300 KLTPLSSA 307
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 568-625 9.47e-12

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 61.38  E-value: 9.47e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  568 PDDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVK 625
Cdd:cd09491      5 PKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQ 62
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 505-550 3.00e-11

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 59.94  E-value: 3.00e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1621998274  505 WLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09488      8 WLESIKMGRYKENFTAAGYtSLDAVAQMTAEDLTRLGVTLVGHQKKI 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 127-350 3.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.17  E-value: 3.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  127 ATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNpclINKAKKTPL 206
Cdd:PHA02876   169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN---INKNDLSLL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  207 DlACEFGRLKVAQLLLNShmcvalleGQSKDTSDPNYTTPLHLAAKNGH-KEIIRQLLKAGIEIN-KQTKTGTALHEAAL 284
Cdd:PHA02876   246 K-AIRNEDLETSLLLYDA--------GFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNaKNIKGETPLYLMAK 316

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  285 YG-KTEVVRLLLQGGIDVNIRNTYNQTALdivNQFTTSHASKDIKQLLREASGILKVRALKDFWNLH 350
Cdd:PHA02876   317 NGyDTENIRTLIMLGADVNAADRLYITPL---HQASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 573-629 6.91e-11

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 59.00  E-value: 6.91e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKLTD 629
Cdd:cd09527      7 DWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDLDAIGVMNPAHRKRILEAVRRLKE 63
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 573-627 2.02e-10

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 57.63  E-value: 2.02e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09488      7 EWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 573-627 2.47e-10

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 57.69  E-value: 2.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTD--LTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09499      7 QWLESIGLPQYESKLLLNGFDDVDFLGSgvMEDQDLKEIGITDEQHRQIILQAARSL 63
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 129-332 2.74e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  129 VDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHY-----EVSEMLLQHQSNPCLINKAKK 203
Cdd:PHA03100    28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGI 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  204 TPLDLAcefgrlkvAQLLLNSHMCVALLEGQSKDTSDPNYT--TPLHLAAKNGH--KEIIRQLLKAGIEINKQTKTG--- 276
Cdd:PHA03100   108 TPLLYA--------ISKKSNSYSIVEYLLDNGANVNIKNSDgeNLLHLYLESNKidLKILKLLIDKGVDINAKNRVNyll 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  277 --------------TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTAL---------DIVNQFTTSHAS-KDIKQLLR 332
Cdd:PHA03100   180 sygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiailnnnkEIFKLLLNNGPSiKTIIETLL 259
Ank_2 pfam12796
Ankyrin repeats (3 copies);
107-199 2.87e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 2.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  107 LHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAAsVNMASlDGQIPLHLSAQYGHYEVSE 186
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1621998274  187 MLLQHQSNPCLIN 199
Cdd:pfam12796   79 LLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 152-239 2.95e-10

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 2.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  152 ARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLLNSHMCVALL 231
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                   ....*...
gi 1621998274  232 EGQSKDTS 239
Cdd:PTZ00322   178 GANAKPDS 185
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
495-557 4.21e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 56.89  E-value: 4.21e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  495 EGKDAEAIYNWLSEFQLEGYTANFLNAGYDVPT-ISRMTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:pfam07647    2 ESWSLESVADWLRSIGLEQYTDNFRDQGITGAElLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
243-295 4.97e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 4.97e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  243 YTTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLL 295
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-627 7.12e-10

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 56.48  E-value: 7.12e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09546      8 EWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEM 62
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 339-392 2.27e-09

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 54.39  E-value: 2.27e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSqkgtdRVGYFP 392
Cdd:cd00174      1 YARALYDY-EAQDDDELSFKKGDIITVLEKDDDGWWEGELNGG-----REGLFP 48
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 502-554 2.31e-09

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 54.55  E-value: 2.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  502 IYNWLSEFQLEGYTANFLNAGYDVPTISRMTPEDLTAIGVTKPGHRKKISAEI 554
Cdd:cd09487      2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 155-309 2.92e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 2.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  155 LLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLlnsHMCVALlegq 234
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL---YHFASI---- 616

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  235 skdtSDPNYTTP-LHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQ 309
Cdd:PLN03192   617 ----SDPHAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGaTALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-627 3.06e-09

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 54.66  E-value: 3.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09551     11 DWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSM 65
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 339-397 5.31e-09

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 53.31  E-value: 5.31e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274   339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGhihdsQKGTDRVGYFPPSIVE 397
Cdd:smart00326    4 QVRALYDY-TAQDPDELSFKKGDIITVLEKSDDGWWKG-----RLGRGKEGLFPSNYVE 56
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 495-557 5.76e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.84  E-value: 5.76e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274   495 EGKDAEAIYNWLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:smart00454    2 SQWSPESVADWLESIGLEQYADNFRKNGIDgALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 95-346 7.67e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 7.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   95 NVNYQDVDGFSALHhAALVGSLELISLLLE---AQATVDIKDINGMRPLHYAAWQGKVEPA--RLLLRAAASVNMASLDG 169
Cdd:PHA03095   109 DVNAKDKVGRTPLH-VYLSGFNINPKVIRLllrKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRF 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  170 QIPLHLSAQYGH--YEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKvaqlllNSHMCVALLEGQSKDTSDPNYTTPL 247
Cdd:PHA03095   188 RSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCK------RSLVLPLLIAGISINARNRYGQTPL 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  248 HLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVN-IRNTYNQTALDIVNQFTTSHASK 325
Cdd:PHA03095   262 HYAAVFNNPRACRRLIALGADINAVSSDGnTPLSLMVRNNNGRAVRAALAKNPSAEtVAATLNTASVAGGDIPSDATRLC 341

                          250       260
                   ....*....|....*....|.
gi 1621998274  326 DIKQLLREASGILKVRALKDF 346
Cdd:PHA03095   342 VAKVVLRGAFSLLPEPIRAYH 362
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-314 8.84e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 8.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   93 RLNVNYQDVDGFSALHHAALvgslELISLLLEAQATVDIKDINGMRPLHYAAWQGKVepARL---LLRAAASVNMASLDG 169
Cdd:PHA02876   234 RSNINKNDLSLLKAIRNEDL----ETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSL--SRLvpkLLERGADVNAKNIKG 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  170 QIPLHLSAQYGH-YEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRlkvaqlllNSHMCVALLE-GQSKDTSDPNYTTPL 247
Cdd:PHA02876   308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR--------NKDIVITLLElGANVNARDYCDKTPI 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  248 HLAAKNGHKEIIRQLLKAGIEINKQT-KTGTALHeAALYG------------------------------------KTEV 290
Cdd:PHA02876   380 HYAAVRNNVVIINTLLDYGADIEALSqKIGTALH-FALCGtnpymsvktlidrganvnsknkdlstplhyackkncKLDV 458

                          250       260
                   ....*....|....*....|....
gi 1621998274  291 VRLLLQGGIDVNIRNTYNQTALDI 314
Cdd:PHA02876   459 IEMLLDNGADVNAINIQNQYPLLI 482
PHA03095 PHA03095
ankyrin-like protein; Provisional
 148-314 1.84e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  148 KVEPARLLLRAAASVNMASLDGQIPLHLsaqYGHYEVSEmllqhqsnpclinkakktpldlacefgRLKVAQLLLNShmc 227
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHL---YLHYSSEK---------------------------VKDIVRLLLEA--- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  228 valleGQSKDTSDPNYTTPLHLAAKNGHKE-IIRQLLKAGIEINKQTKTG-TALHeAALYGK---TEVVRLLLQGGIDVN 302
Cdd:PHA03095    73 -----GADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGrTPLH-VYLSGFninPKVIRLLLRKGADVN 146

                          170
                   ....*....|..
gi 1621998274  303 IRNTYNQTALDI 314
Cdd:PHA03095   147 ALDLYGMTPLAV 158
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 569-627 1.91e-08

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 52.24  E-value: 1.91e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274  569 DDLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09555      7 DSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLL 65
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 340-394 1.92e-08

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 51.90  E-value: 1.92e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  340 VRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKGTDRvGYFPPS 394
Cdd:cd11883      2 VVALYDF-TPKSKNQLSFKAGDIIYVLNKDPSGWWDGVIISSSGKVKR-GWFPSN 54
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 567-621 3.23e-08

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 51.49  E-value: 3.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  567 IPDD--LMEWLSALGLPQYHKKLVSNGYDSISIvTDLTWEDLQEIGINKLGHQKKLM 621
Cdd:cd09497      1 NPDAeaIFDWLREFGLEEYTPNFIKAGYDLPTI-SRMTPEDLTAIGITKPGHRKKLK 56
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 501-559 4.51e-08

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 51.19  E-value: 4.51e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  501 AIYNWLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSI 559
Cdd:cd09551      8 SVEDWLSAIKMSQYRDNFLSSGFtSLQLVAQMTSEDLLRIGVTLAGHQKKILNSIQSMRV 67
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 92-312 5.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 5.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   92 KRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDgqi 171
Cdd:PHA02876   167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS--- 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  172 pLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLkvaqlllnSHMCVALLE-GQSKDTSDPNYTTPLHLA 250
Cdd:PHA02876   244 -LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSL--------SRLVPKLLErGADVNAKNIKGETPLYLM 314

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  251 AKNGH-KEIIRQLLKAGIEINKQTKT-GTALHEAALYGK-TEVVRLLLQGGIDVNIRNTYNQTAL 312
Cdd:PHA02876   315 AKNGYdTENIRTLIMLGADVNAADRLyITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPI 379
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-627 6.49e-08

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 50.80  E-value: 6.49e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09553     11 DWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDM 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
61-163 7.04e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 7.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   61 LIQAVKNGDVPGVQKLVakvkaskskllgsTKRLNVNYQDVDGFSALHHAALVGslelisLLLEAQATVDIKDIN----G 136
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-------------ENGADANLQDKNGRTALHLAAKNG------HLEIVKLLLEHADVNlkdnG 61

                           90       100
                   ....*....|....*....|....*..
gi 1621998274  137 MRPLHYAAWQGKVEPARLLLRAAASVN 163
Cdd:pfam12796   62 RTALHYAARSGHLEIVKLLLEKGADIN 88
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 501-550 1.09e-07

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 50.14  E-value: 1.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  501 AIYNWLSEFQLEGYTANFLNAGYDVPTISR-MTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09527      4 IVYDWLRTLQLEQYAEKFVDNGYDDLEVCKqIGDPDLDAIGVMNPAHRKRI 54
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 135-221 1.10e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 52.96  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  135 NGMRPLHYAAWQGKVEP---ARLLLRAAASVN-MASLDGQIPLHLSAQYGHYEVSEMLLQH-QSNPCLINKAKKTPLDLA 209
Cdd:PHA02736    54 HGKQCVHIVSNPDKADPqekLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVA 133

                           90
                   ....*....|..
gi 1621998274  210 CEFGRLKVAQLL 221
Cdd:PHA02736   134 CERHDAKMMNIL 145
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 162-312 3.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  162 VNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLL--------------LNSHMC 227
Cdd:PHA02874    28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipcIEKDMI 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  228 VALLE-GQSKDTSDPNYTTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTGT-ALHEAALYGKTEVVRLLLQGGIDVNIRN 305
Cdd:PHA02874   108 KTILDcGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCyPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                   ....*..
gi 1621998274  306 TYNQTAL 312
Cdd:PHA02874   188 NNGESPL 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 139-314 3.13e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  139 PLHYAAWQGKVEP-ARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQhqSNPCLINKAkktpldlacefgrlkv 217
Cdd:cd22192     20 PLLLAAKENDVQAiKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEP---------------- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  218 aqlllnshMCVALLEGQskdtsdpnytTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTGTA---------------LHEA 282
Cdd:cd22192     82 --------MTSDLYQGE----------TALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFA 143

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1621998274  283 ALYGKTEVVRLLLQGGIDVNIRNTYNQTALDI 314
Cdd:cd22192    144 ACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-625 3.15e-07

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 49.23  E-value: 3.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVK 625
Cdd:cd09552     11 EWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQ 63
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 501-554 4.76e-07

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 48.46  E-value: 4.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  501 AIYNWLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEI 554
Cdd:cd09542      6 SVSEWLESIRMKRYILHFRSAGLDtMECVLELTAEDLTQMGITLPGHQKRILCSI 60
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 495-554 5.00e-07

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 48.29  E-value: 5.00e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  495 EGKDAEAIYNWLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEI 554
Cdd:cd09543      1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNsIDKVLQMTQEDIKHIGVRLPGHQKRIAYSI 61
Ank_5 pfam13857
Ankyrin repeats (many copies);
262-315 5.27e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 5.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  262 LLKAG-IEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDIV 315
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 505-561 5.35e-07

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 48.32  E-value: 5.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  505 WLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSIAE 561
Cdd:cd09554      9 WLRAIKMERYEDSFLQAGFtTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMGIQN 66
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 573-629 5.63e-07

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 48.29  E-value: 5.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKLTD 629
Cdd:cd09543     10 EWLESIKMQQYTEHFMAAGYNSIDKVLQMTQEDIKHIGVRLPGHQKRIAYSILGLKE 66
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 339-398 6.83e-07

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 47.62  E-value: 6.83e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHdsqkgtDRVGYFPPSIVEV 398
Cdd:cd11805      1 RVQALYDF-NPQEPGELEFRRGDIITVLDSSDPDWWKGELR------GRVGIFPANYVQP 53
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 502-559 9.22e-07

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 47.72  E-value: 9.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274  502 IYNWLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSI 559
Cdd:cd09553      9 VGDWLDAIKMGRYKENFVSAGFaSFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRL 67
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-625 1.03e-06

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 47.31  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVK 625
Cdd:cd09542      9 EWLESIRMKRYILHFRSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQ 61
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-628 1.18e-06

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 47.17  E-value: 1.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKLT 628
Cdd:cd09554      8 EWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLRMGVTLAGHQKKILSSIQAMG 63
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-636 1.38e-06

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 47.25  E-value: 1.38e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKkltDLRKSLSQ 636
Cdd:cd09545      8 DWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGISAIAHQNKILSSVQ---GMRSQMQQ 68
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 505-554 1.52e-06

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188947  Cd Length: 70  Bit Score: 46.94  E-value: 1.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  505 WLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEI 554
Cdd:cd09548     13 WLEAIKMERYKDNFTAAGYNsLESVARMTIEDVMSLGITLVGHQKKIMSSI 63
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-621 1.83e-06

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188947  Cd Length: 70  Bit Score: 46.94  E-value: 1.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLM 621
Cdd:cd09548     12 EWLEAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIM 60
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 569-632 1.97e-06

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 46.52  E-value: 1.97e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  569 DDLMEWLSALGLPQYHKKLVSNGYDSISIVTdLTWEDLQEIGINKLGHQKKLMLAVkklTDLRK 632
Cdd:cd09520      5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLT-LTDQDLKELGITAFGARRKMLLAI---SELNK 64
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-189 2.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  136 GMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLL 189
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-263 2.20e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 2.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  204 TPLDLACEFGRLKVAQLLLNSHMCVallegqskDTSDPNYTTPLHLAAKNGHKEIIRQLL 263
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADI--------NAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 56-222 2.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   56 GREQELIQAVKNGDVPGVQKLvakvkaskskLLGSTKRLNVNYQDvdGFSALHHAALVGSLELISLLLEAQATVDIKDIN 135
Cdd:PHA02875    67 DIESELHDAVEEGDVKAVEEL----------LDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  136 GMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINK-AKKTPLDLACEFGR 214
Cdd:PHA02875   135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKnGCVAALCYAIENNK 214


                   ....*...
gi 1621998274  215 LKVAQLLL 222
Cdd:PHA02875   215 IDIVRLFI 222
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 570-624 2.44e-06

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.15  E-value: 2.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  570 DLMEWLSALGLPQYHKKLVSNGYDSISIVTdLTWEDLQEIGINKLGHQKKLMLAV 624
Cdd:cd09533      1 DVADWLSSLGLPQYEDQFIENGITGDVLVA-LDHEDLKEMGITSVGHRLTILKAV 54
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 500-559 2.48e-06

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 46.46  E-value: 2.48e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  500 EAIYNWLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSI 559
Cdd:cd09546      4 RSVGEWLEAIKMGRYTEIFMENGYSsMDAVAQVTLEDLRRLGVTLVGHQKKIMNSIQEMRV 64
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 505-550 2.80e-06

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 46.46  E-value: 2.80e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1621998274  505 WLSEFQLEGYTANFLNAG---YDVptISRMTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09555     12 WLSAIGLECYQDNFSKFGlctFSD--VAQLSLEDLPALGITLAGHQKKL 58
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-625 4.34e-06

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 45.63  E-value: 4.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVK 625
Cdd:cd09550      7 DWLDSIKMGRYKDHFAAGGYSSLGMVMRMNIEDIRRLGITLMGHQKKILTSIQ 59
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-627 4.42e-06

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 45.65  E-value: 4.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09547      8 DWLDSIKMGQYKNNFMAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTL 62
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 245-271 4.65e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.50  E-value: 4.65e-06
                            10        20
                    ....*....|....*....|....*..
gi 1621998274   245 TPLHLAAKNGHKEIIRQLLKAGIEINK 271
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 501-559 5.12e-06

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 45.26  E-value: 5.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  501 AIYNWLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLSI 559
Cdd:cd09547      5 TVSDWLDSIKMGQYKNNFMAAGFTtLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
SH3_CRK_C cd11759
C-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
 348-398 6.73e-06

C-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The C-terminal SH3 domain of CRK has not been shown to bind any target protein; it acts as a negative regulator of CRK function by stabilizing a structure that inhibits the access by target proteins to the N-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212693 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 6.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  348 NLHDPTALNVRAGDIITVLEQHADGRWKGHIHdsqkgtDRVGYFPPSIVEV 398
Cdd:cd11759     13 NAYDKTALALEVGDLVKVTKINVSGQWEGELN------GKVGHFPFTHVEL 57
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 573-623 6.88e-06

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 44.99  E-value: 6.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLtWE-DLQEI-GINKLGHQKKlMLA 623
Cdd:cd09500     10 EWLDSIGLGDYIETFLKHGYTSMERVKRI-WEvELTNVlEINKLGHRKR-ILA 60
Caskin1-CID pfam16600
Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this ...
 404-437 6.92e-06

Caskin1 CASK-interaction domain; The Caskin1 protein interacts with the CASK protein via this region.CASK and Caskin1 are synaptic scaffolding proteins. The binding motif on human Caskin1 is EEIWVLRK. A similar motif is found on protein MINT1 and protein TIAM1, both shown to be able to bind to CASK though the motif. MINT1 and TIAM1 are not part of this family. This region is predicted to be natively unstructured.


Pssm-ID: 465190  Cd Length: 55  Bit Score: 44.65  E-value: 6.92e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1621998274  404 AGDRNSVGSEGSIGSIRSAGSGQSTEGTNGQITG 437
Cdd:pfam16600   12 GGDRSSVGSTGSVGSVRSSGSGQSSHALHAGSEG 45
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 505-550 6.93e-06

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 45.36  E-value: 6.93e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1621998274  505 WLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09498     13 WLSLLGLPQYHKVLVENGYDsIDFVTDLTWEDLQDIGITKLGHQKKL 59
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 569-627 7.27e-06

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 45.00  E-value: 7.27e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274  569 DDLMEWLSALGLPQYHKKLVSNGYDSiSIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09506      8 DDVGDWLESLNLGEHRERFMDNEIDG-SHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 339-399 9.18e-06

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 44.12  E-value: 9.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGhihdSQKGtdRVGYFPPSIVEVI 399
Cdd:pfam07653    1 YGRVIFDY-VGTDKNGLTLKKGDVVKVLGKDNDGWWEG----ETGG--RVGLVPSTAVEEI 54
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 505-550 9.25e-06

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 45.00  E-value: 9.25e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1621998274  505 WLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09552     12 WLDAIKMGQYKESFANAGFtSFDVVSQMTMEDILRVGVTLAGHQKKI 58
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 245-371 1.07e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  245 TPLHLAAKNGHKEIIRQLLKAGIEINKQTKTGTA-LHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDIVNQFTTSHa 323
Cdd:PHA02878   170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSpLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY- 248

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  324 skDIKQLLRE-------ASGILKVRALKDfwNLHDPTALNVragdiitVLEQHAD 371
Cdd:PHA02878   249 --DILKLLLEhgvdvnaKSYILGLTALHS--SIKSERKLKL-------LLEYGAD 292
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 95-318 1.11e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   95 NVNYQDVDGFSALHHAA--LVGSLELisllleaqatvdikdingmrplhyaawqgkVEparLLLRAAASVNMASLDGQIP 172
Cdd:PHA03100    98 NVNAPDNNGITPLLYAIskKSNSYSI------------------------------VE---YLLDNGANVNIKNSDGENL 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  173 LHLSAQYGHY--EVSEMLLQHQSNpclINkaKKTPLDlacefgrlkvaqLLLNShmcvalleGQSKDTSDPNYTTPLHLA 250
Cdd:PHA03100   145 LHLYLESNKIdlKILKLLIDKGVD---IN--AKNRVN------------YLLSY--------GVPINIKDVYGFTPLHYA 199

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  251 AKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTY----NQTALDIVNQF 318
Cdd:PHA03100   200 VYNNNPEFVKYLLDLGANPNLVNKYGdTPLHIAILNNNKEIFKLLLNNGPSIKTIIETllyfKDKDLNTITKI 272
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 501-550 1.17e-05

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 44.56  E-value: 1.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  501 AIYNWLSEFQLEGYTANFLNAGYDVP-TISRMTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09545      5 SVDDWLQAIKMERYKDNFTAAGYTTLeAVVHMNQDDLARIGISAIAHQNKI 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 277-305 1.17e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.17e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1621998274  277 TALHEAAL-YGKTEVVRLLLQGGIDVNIRN 305
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
SAM_SASH1_repeat2 cd09492
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ...
 571-625 1.38e-05

SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.


Pssm-ID: 188891  Cd Length: 70  Bit Score: 44.42  E-value: 1.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  571 LMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVK 625
Cdd:cd09492     10 VSDWLVSIGLPMYSPPLLEAGFSTLSRVSSLSETCLREAGITEERHIRKLLSAAR 64
Ank_4 pfam13637
Ankyrin repeats (many copies);
172-222 1.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  172 PLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLACEFGRLKVAQLLL 222
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 339-398 1.75e-05

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 43.47  E-value: 1.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHA-DGRWKGHihdSQKGtdRVGYFPPSIVEV 398
Cdd:cd11763      1 KVRALYDF-DSQPSGELSLRAGEVLTITRQDVgDGWLEGR---NSRG--EVGLFPSSYVEI 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
277-315 2.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1621998274  277 TALHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTALDIV 315
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 245-274 2.28e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 2.28e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1621998274  245 TPLHLAA-KNGHKEIIRQLLKAGIEINKQTK 274
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 573-627 3.46e-05

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 43.31  E-value: 3.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  573 EWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09549     12 EWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQAL 66
SH3_Stac_1 cd11833
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ...
 355-396 4.73e-05

First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins; Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212767 [Multi-domain]  Cd Length: 53  Bit Score: 42.10  E-value: 4.73e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1621998274  355 LNVRAGDIITVLEQHADGRWKGHIHdsqkgtDRVGYFPPSIV 396
Cdd:cd11833     16 LEMRPGDKITLLDDSNEDWWKGKIE------DRVGFFPANFV 51
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 245-271 6.52e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 6.52e-05
                           10        20
                   ....*....|....*....|....*..
gi 1621998274  245 TPLHLAAKNGHKEIIRQLLKAGIEINK 271
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 340-396 6.71e-05

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212884  Cd Length: 53  Bit Score: 41.71  E-value: 6.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  340 VRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIhdsqkgTDRVGYFPPSIV 396
Cdd:cd11951      2 VQAQYDF-SAEDPSQLSFRRGDIIEVLDCPDPNWWRGRI------SGRVGFFPRNYV 51
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 564-627 7.07e-05

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 42.01  E-value: 7.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  564 PNYIPDDLMEWLSALGLPQYHKKLVSNGYDSISIVTdLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09507      3 TNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLH-LERRDLKDLGITKVGHVKRILQAIKDL 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
279-312 8.43e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 8.43e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1621998274  279 LHEAALYGKTEVVRLLLQGGIDVNIRNTYNQTAL 312
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 277-303 1.04e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 1.04e-04
                           10        20
                   ....*....|....*....|....*..
gi 1621998274  277 TALHEAALYGKTEVVRLLLQGGIDVNI 303
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 61-349 1.25e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.54  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   61 LIQAVKNGDVPGVQKLVakvkaskskllgSTKRLNVNYQDVDGFSALHHAALVGSLelisllleaQATVDIKD-----IN 135
Cdd:cd22192     21 LLLAAKENDVQAIKKLL------------KCPSCDLFQRGALGETALHVAALYDNL---------EAAVVLMEaapelVN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  136 ---------GMRPLHYAAWQGKVEPARLLLRAAASVNMASLD--------------GQIPLHLSAQYGHYEVSEMLLQHQ 192
Cdd:cd22192     80 epmtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  193 SNP----CLINkakkTPL---------DLACEfgrlkVAQLLLNShmcVALLEGQSKDTSdPNYT--TPLHLAAKNGHKE 257
Cdd:cd22192    160 ADIraqdSLGN----TVLhilvlqpnkTFACQ-----MYDLILSY---DKEDDLQPLDLV-PNNQglTPFKLAAKEGNIV 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  258 IIRQLLKA--GIEINKQTKTGTalheaaLYGKTEvvrlllqggIDvnirnTY--NQTALDIVnqfTTSHAskdikqllRE 333
Cdd:cd22192    227 MFQHLVQKrrHIQWTYGPLTST------LYDLTE---------ID-----SWgdEQSVLELI---VSSKK--------RE 275

                          330       340
                   ....*....|....*....|
gi 1621998274  334 ASGILKVRALKDF----WNL 349
Cdd:cd22192    276 ARKILDVTPVKELvslkWKR 295
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 341-392 1.27e-04

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 41.04  E-value: 1.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  341 RALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGhihdsQKGTDRVGYFP 392
Cdd:pfam00018    1 VALYDY-TAQEPDELSFKKGDIIIVLEKSEDGWWKG-----RNKGGKEGLIP 46
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 495-555 1.28e-04

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 41.52  E-value: 1.28e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  495 EGKDAEAIYNWLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAI-GVTKPGHRKKISAEIG 555
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYtSMERVKRIWEVELTNVlEINKLGHRKRILASLA 63
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
 339-396 1.69e-04

Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212897 [Multi-domain]  Cd Length: 55  Bit Score: 40.70  E-value: 1.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  339 KVRALKDFWNLHDpTALNVRAGDIITVLEQHADGRWKGHIHDSqkgtdrVGYFPPSIV 396
Cdd:cd11964      2 KVRAIYDFEAAED-NELTFKAGDIITILDDSDPNWWKGETPQG------TGLFPSNFV 52
SH3_Intersectin_2 cd11837
Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor ...
 355-396 1.79e-04

Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212771 [Multi-domain]  Cd Length: 53  Bit Score: 40.81  E-value: 1.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1621998274  355 LNVRAGDIITVLEQhADGRWKGHIHDSqkgtdRVGYFPPSIV 396
Cdd:cd11837     16 LSFAKGDIITVLEQ-QEMWWFGELEGG-----EEGWFPKSYV 51
SH3_9 pfam14604
Variant SH3 domain;
342-397 2.15e-04

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 40.29  E-value: 2.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  342 ALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGhihdsqKGTDRVGYFPPSIVE 397
Cdd:pfam14604    1 ALYPY-EPKDDDELSLQRGDVITVIEESEDGWWEG------INTGRTGLVPANYVE 49
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 570-627 2.27e-04

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 40.77  E-value: 2.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  570 DLMEWLSALGLPQYHKkLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09524      7 SISQFLSSLGLEHLRE-IFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERL 63
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 505-557 2.57e-04

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 40.74  E-value: 2.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  505 WLSEFQLEGYTANFLNAGYD-VPTISR--MTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:cd09499      8 WLESIGLPQYESKLLLNGFDdVDFLGSgvMEDQDLKEIGITDEQHRQIILQAARSL 63
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 505-558 2.59e-04

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 40.76  E-value: 2.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  505 WLSEFQLEGYTANFLNAGYDVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLS 558
Cdd:cd09506     13 WLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKLL 66
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 505-557 2.66e-04

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 40.62  E-value: 2.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  505 WLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:cd09549     13 WLEALDLCRYKDNFAAAGYgSLEAVARMTAQDVLSLGITSLEHQELLLAGIQAL 66
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 568-627 2.86e-04

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 40.27  E-value: 2.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  568 PDDLMEWLSALGLPQYHKKLVSNGYDSiSIVTDLTWEDLQEIGINKLGHQKKLMLAVKKL 627
Cdd:cd09534      3 EEFVEEWLNELNCGQYLDIFEKNLITG-DLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 127-191 3.27e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 3.27e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621998274  127 ATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQH 191
Cdd:PTZ00322   106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
 339-396 3.56e-04

Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212754 [Multi-domain]  Cd Length: 54  Bit Score: 39.76  E-value: 3.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  339 KVRALKDFWNLHDpTALNVRAGDIITVLEQHADGRWKGHIHDSQkgtdrvGYFPPSIV 396
Cdd:cd11820      2 KVRALYDFEAAED-NELTFKAGEIITVLDDSDPNWWKGSNHRGE------GLFPANFV 52
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 505-554 3.60e-04

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 40.23  E-value: 3.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  505 WLSEFQLEGYTANFLNAGY-DVPTISRMTPEDLTAIGVTKPGHRKKISAEI 554
Cdd:cd09550      8 WLDSIKMGRYKDHFAAGGYsSLGMVMRMNIEDIRRLGITLMGHQKKILTSI 58
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 559-627 3.82e-04

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 40.31  E-value: 3.82e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  559 IAEWlpnyIPDDLMEWLSALGLPQYHKKLVS-NGYDSISIVTdLTWEDLQE--IGINKLGHQKKLMLAVKKL 627
Cdd:cd09515      1 VHEW----TCEDVAKWLKKEGFSKYVDLLCNkHRIDGKVLLS-LTEEDLRSppLEIKVLGDIKRLWLAIRKL 67
SAM_tumor-p63,p73 cd09503
SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 ...
 566-611 3.82e-04

SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain.


Pssm-ID: 188902  Cd Length: 65  Bit Score: 39.99  E-value: 3.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1621998274  566 YIPDD-LMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGI 611
Cdd:cd09503      1 YPTDNsVASWLTKLGCSNYIDNFHQQGLLSIFQLDEFTLEDLAAMKI 47
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 506-558 4.07e-04

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 39.97  E-value: 4.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  506 LSEFQLEGYTANFLNAGYDVPTISRMTPEDLTAIGVTKPGHRKKISAEIGQLS 558
Cdd:cd09520     11 LAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELN 63
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 502-550 4.35e-04

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 39.97  E-value: 4.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1621998274  502 IYNWLSEFQLEGYTANFLNAGYDVPTISR-MTPEDLTAIGVTKPGHRKKI 550
Cdd:cd09490      6 IAEWLASIHLEQYLDLFREHGYVTATDCQgINDSRLKQIGISPTGHRRRI 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-282 5.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 5.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  230 LLEGQSKDTSDPNY--TTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEA 282
Cdd:pfam13857    1 LLEHGPIDLNRLDGegYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGlTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-212 5.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   61 LIQAVKNGDVPGVQKLVakvkaskskllgsTKRLNVNYQDVDGFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPL 140
Cdd:PHA02874   128 LHYAIKKGDLESIKMLF-------------EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  141 HYAAWQGKVEPARLLL------------------------RAA-------ASVNMASLDGQIPLHLSAQYG-HYEVSEML 188
Cdd:PHA02874   195 HNAAEYGDYACIKLLIdhgnhimnkckngftplhnaiihnRSAiellinnASINDQDIDGSTPLHHAINPPcDIDIIDIL 274

                          170       180
                   ....*....|....*....|....
gi 1621998274  189 LQHQSNPCLINKAKKTPLDLACEF 212
Cdd:PHA02874   275 LYHKADISIKDNKGENPIDTAFKY 298
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
 339-396 6.14e-04

Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212896 [Multi-domain]  Cd Length: 57  Bit Score: 39.23  E-value: 6.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  339 KVRALKDFWNLHDpTALNVRAGDIITVLEQHADGRWKGHIHdsqKGtdrVGYFPPSIV 396
Cdd:cd11963      3 KVRALYDFEAVED-NELTFKHGEIIIVLDDSDANWWKGENH---RG---VGLFPSNFV 53
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 355-398 6.17e-04

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 39.25  E-value: 6.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1621998274  355 LNVRAGDIITVLEQHADGRWKGhihdSQKGTdrVGYFPPSIVEV 398
Cdd:cd11823     16 LSLQPGDIIEVHEKQDDGWWLG----ELNGK--KGIFPATYVEE 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 277-303 6.23e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 6.23e-04
                            10        20
                    ....*....|....*....|....*..
gi 1621998274   277 TALHEAALYGKTEVVRLLLQGGIDVNI 303
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 569-633 6.71e-04

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 39.61  E-value: 6.71e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  569 DDLMEWLSALGLPQYHKKLVSNGYDSiSIVTDLTWEDLQ-EIGINKLGHQKKLMLAVKKLTDLRKS 633
Cdd:cd09505      8 EDVCTWLRSIGLEQYVEVFRANNIDG-KELLNLTKESLSkDLKIESLGHRNKILRKIEELKMKSDS 72
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 230-312 7.03e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  230 LLEGQSKDTSDPNYTTPLHLAAKNGHKEIIRQLLKAGIEINKQTKTG-TALHEAALYGKTEVVRLLLQGGIDVNIRNTYN 308
Cdd:PLN03192   512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGrTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591


                   ....
gi 1621998274  309 QTAL 312
Cdd:PLN03192   592 NTAL 595
Ank_5 pfam13857
Ankyrin repeats (many copies);
154-209 8.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 8.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621998274  154 LLLRAAASVNMASLDGQIPLHLSAQYGHYEVSEMLLQHQSNPCLINKAKKTPLDLA 209
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-191 8.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 8.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274   95 NVNYQDVD-GFSALHHAALVGSLELISLLLEAQATVDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPL 173
Cdd:PHA02878   159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                           90
                   ....*....|....*....
gi 1621998274  174 HLSAQY-GHYEVSEMLLQH 191
Cdd:PHA02878   239 HISVGYcKDYDILKLLLEH 257
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 355-397 9.75e-04

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 38.40  E-value: 9.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1621998274  355 LNVRAGDIITVLEQHADGRWKGHIHdsqkgtDRVGYFPPSIVE 397
Cdd:cd11766     16 LSLRKGDRVLVLEKSSDGWWRGECN------GQVGWFPSNYVT 52
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 218-342 1.04e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.46  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  218 AQLLLNSHMCvallegQSKDTSDpnytTPLHLAAKNGHKEIIRQLLK-AGIEINKQTKTG-TALHEAALYGKTEVVRLLL 295
Cdd:cd22192      2 AQMLDELHLL------QQKRISE----SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGeTALHVAALYDNLEAAVVLM 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1621998274  296 QGGID-VNIRNTYN----QTALDI--VNQFTTShaskdIKQLLREASGILKVRA 342
Cdd:cd22192     72 EAAPElVNEPMTSDlyqgETALHIavVNQNLNL-----VRELIARGADVVSPRA 120
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 168-200 1.46e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1621998274  168 DGQIPLHLSA-QYGHYEVSEMLLQHQSNPCLINK 200
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 570-621 1.49e-03

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 38.43  E-value: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  570 DLMEWLSALGLPQYHKKLVSNGYDSISIVTDLTWEDLQEIGINKLGHQKKLM 621
Cdd:cd09490      5 DIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRLKQIGISPTGHRRRIL 56
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
 340-396 1.78e-03

Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212746 [Multi-domain]  Cd Length: 52  Bit Score: 37.88  E-value: 1.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621998274  340 VRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQKgtdrvGYFPPSIV 396
Cdd:cd11812      2 VVALYDY-TANRSDELTIHRGDIIRVLYKDNDNWWFGSLVNGQQ-----GYFPANYV 52
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 505-556 1.80e-03

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 38.27  E-value: 1.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1621998274  505 WLSEFQLEGYTANFLNAGYD-VPTISRMTPEDLTAIGVTKPGHRKKISAEIGQ 556
Cdd:cd09491     11 WLMNLGLQQYEEGLMHNGWDsLEFLSDITEEDLEEAGVTNPAHKRRLLDSLQD 63
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 499-557 2.46e-03

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 37.78  E-value: 2.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621998274  499 AEAIYNWLSEFQLEGYTANFLN---AGYDVPTISRmtpEDLTAIGVTKPGHRKKISAEIGQL 557
Cdd:cd09507      7 TEEVGAWLESLQLGEYRDIFARndiRGSELLHLER---RDLKDLGITKVGHVKRILQAIKDL 65
SH3_Abp1_eu cd11960
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ...
 339-397 2.75e-03

Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212893 [Multi-domain]  Cd Length: 54  Bit Score: 37.38  E-value: 2.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSqkgtdRVGYFPPSIVE 397
Cdd:cd11960      1 RARALYDY-QAADDTEISFDPGDIITDIEQIDEGWWRGTGPDG-----TYGLFPANYVE 53
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
 339-397 3.07e-03

Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212760 [Multi-domain]  Cd Length: 52  Bit Score: 37.30  E-value: 3.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274  339 KVRALKDFWNLHDpTALNVRAGDIITVLEQHADGRWKGhihdSQKGtdRVGYFPPSIVE 397
Cdd:cd11826      1 KVVALYDYTADKD-DELSFQEGDIIYVTKKNDDGWYEG----VLNG--VTGLFPGNYVE 52
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 339-397 3.16e-03

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 3.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQkgtdrvGYFPPSIVE 397
Cdd:cd11827      1 QCKALYAY-DAQDTDELSFNEGDIIEILKEDPSGWWTGRLRGKE------GLFPGNYVE 52
Ank_5 pfam13857
Ankyrin repeats (many copies);
129-175 3.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 3.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1621998274  129 VDIKDINGMRPLHYAAWQGKVEPARLLLRAAASVNMASLDGQIPLHL 175
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
SH3_SGSM3 cd11813
Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called ...
 339-398 3.89e-03

Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called Merlin-associated protein (MAP), RUN and SH3 domain-containing protein (RUSC3), RUN and TBC1 domain-containing protein 3 (RUTBC3), Rab GTPase-activating protein 5 (RabGAP5), or Rab GAP-like protein (RabGAPLP). It is expressed ubiquitously and functions as a regulator of small G protein RAP- and RAB-mediated neuronal signaling. It is involved in modulating NGF-mediated neurite outgrowth and differentiation. It also interacts with the tumor suppressor merlin and may play a role in the merlin-associated suppression of cell growth. SGSM3 contains TBC, SH3, and RUN domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212747  Cd Length: 53  Bit Score: 36.71  E-value: 3.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWKGHIHDSQkgtdrvGYFPPSIVEV 398
Cdd:cd11813      1 RAKALLDF-ERHDDDELGFRKNDIITIISQKDEHCWVGELNGLR------GWFPAKFVEL 53
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 340-397 4.77e-03

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 36.73  E-value: 4.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621998274  340 VRALKDFWNLhDPTALNVRAGDIITVLEQHADGRWKGHIHdsqkgtDRVGYFPPSIVE 397
Cdd:cd11950      2 VRALYDFEAL-EDDELGFNSGDVIEVLDSSNPSWWKGRLH------GKLGLFPANYVA 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 168-195 6.92e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 6.92e-03
                            10        20
                    ....*....|....*....|....*...
gi 1621998274   168 DGQIPLHLSAQYGHYEVSEMLLQHQSNP 195
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 339-375 7.46e-03

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 36.20  E-value: 7.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1621998274  339 KVRALKDFwNLHDPTALNVRAGDIITVLEQHADGRWK 375
Cdd:cd11824      1 KYSVLYDY-TAQEDDELSISKGDVVAVIEKGEDGWWT 36
SH3_Bbc1 cd11887
Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces ...
 339-398 8.41e-03

Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces cerevisiae Bbc1p, also called Mti1p (Myosin tail region-interacting protein), and similar proteins. Bbc1p interacts with and regulates type I myosins in yeast, Myo3p and Myo5p, which are involved in actin cytoskeletal reorganization. It also binds and inhibits Las17, a WASp family protein that functions as an activator of the Arp2/3 complex. Bbc1p contains an N-terminal SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212820 [Multi-domain]  Cd Length: 60  Bit Score: 36.17  E-value: 8.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621998274  339 KVRALKDFWNLHDPTaLNVRAGDIITVLEQhADGRW-KGHIHDSQkGTDRVGYFPPSIVEV 398
Cdd:cd11887      3 KVKALYPYESDHEDD-LNFDVGQLITVTEE-EDADWyFGEYVDSN-GNTKEGIFPKNFVEV 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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