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Conserved domains on  [gi|1938958478|ref|NP_446409|]
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amyloid-beta A4 precursor protein-binding family B member 3 [Rattus norvegicus]

Protein Classification

Fe65 family protein( domain architecture ID 10648645)

Fe65 family protein contains WW and PTB (phosphotyrosine-binding) domains, similar to human protein protein Fe65-like 2, also called amyloid-beta A4 precursor protein-binding family B member 3, that may modulate the internalization of amyloid-beta precursor protein

Gene Ontology:  GO:0005515|GO:0001540
PubMed:  15567406|8987385|10610414|11812645

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 114-252 1.61e-84

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269970  Cd Length: 138  Bit Score: 256.46  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 114 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQPL 193
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938958478 194 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQILSER 252
Cdd:cd01272    81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 281-411 5.78e-62

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269969  Cd Length: 127  Bit Score: 197.82  E-value: 5.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 281 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTGRGDRKTWVPAMLSVSDSLMTAHPIQAEagaeEEPLWQCPVRLV 360
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1938958478 361 TFIGVGHDPHTFGLIADLGCQSFQCAAFWCQPHAGGLSEAVQAACMVQYQK 411
Cdd:cd01271    77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 30-61 6.94e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 6.94e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1938958478   30 GLPPGWRKIRDAAG-TYYWHVPSGSTQWQRPTW 61
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 114-252 1.61e-84

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269970  Cd Length: 138  Bit Score: 256.46  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 114 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQPL 193
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938958478 194 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQILSER 252
Cdd:cd01272    81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 281-411 5.78e-62

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269969  Cd Length: 127  Bit Score: 197.82  E-value: 5.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 281 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTGRGDRKTWVPAMLSVSDSLMTAHPIQAEagaeEEPLWQCPVRLV 360
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1938958478 361 TFIGVGHDPHTFGLIADLGCQSFQCAAFWCQPHAGGLSEAVQAACMVQYQK 411
Cdd:cd01271    77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
117-248 1.93e-49

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 165.61  E-value: 1.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 117 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRNRSQPHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQPL 193
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938958478 194 VHIRVWGVGsSKGRDRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQI 248
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 112-252 6.35e-32

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 118.96  E-value: 6.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478  112 PGAKCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTrnrsqpHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQ 191
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAA------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938958478  192 PLVHIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQILSER 252
Cdd:smart00462  70 PLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 284-416 2.40e-29

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 112.02  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478  284 QAAQKYEALYMGILPVTKAMGMDVLNEAIGTL--TGRGDRKTWVPAMLSVSDSLMTAHPIQAEAgaeeePLWQCPVRLVT 361
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958478  362 FIGVG-HDPHTFGLIADLGCQS-FQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVAS 416
Cdd:smart00462  76 FCAVGpDDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 30-61 6.94e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 6.94e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1938958478   30 GLPPGWRKIRDAAG-TYYWHVPSGSTQWQRPTW 61
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 31-59 2.22e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 46.73  E-value: 2.22e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1938958478  31 LPPGWRKIRDAAG-TYYWHVPSGSTQWQRP 59
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 32-61 8.17e-07

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 45.21  E-value: 8.17e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1938958478  32 PPGWRKIRDAAG-TYYWHVPSGSTQWQRPTW 61
Cdd:cd00201     1 PPGWEERWDPDGrVYYYNHNTKETQWEDPRE 31
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 114-252 1.61e-84

Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269970  Cd Length: 138  Bit Score: 256.46  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 114 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQPL 193
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938958478 194 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQILSER 252
Cdd:cd01272    81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 281-411 5.78e-62

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269969  Cd Length: 127  Bit Score: 197.82  E-value: 5.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 281 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTGRGDRKTWVPAMLSVSDSLMTAHPIQAEagaeEEPLWQCPVRLV 360
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1938958478 361 TFIGVGHDPHTFGLIADLGCQSFQCAAFWCQPHAGGLSEAVQAACMVQYQK 411
Cdd:cd01271    77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
117-248 1.93e-49

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 165.61  E-value: 1.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 117 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRNRSQPHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQPL 193
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938958478 194 VHIRVWGVGsSKGRDRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQI 248
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 112-252 6.35e-32

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 118.96  E-value: 6.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478  112 PGAKCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTrnrsqpHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQ 191
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAA------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938958478  192 PLVHIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASALQGLCAQILSER 252
Cdd:smart00462  70 PLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 284-416 2.40e-29

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 112.02  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478  284 QAAQKYEALYMGILPVTKAMGMDVLNEAIGTL--TGRGDRKTWVPAMLSVSDSLMTAHPIQAEAgaeeePLWQCPVRLVT 361
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958478  362 FIGVG-HDPHTFGLIADLGCQS-FQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVAS 416
Cdd:smart00462  76 FCAVGpDDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 116-242 2.30e-14

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 69.46  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 116 CFAVRSLGWVEVPEEDlapGKSSIAVNNCIQQLAQTRNRSQPhdgawgegQNMLMVLKKDAMSLLNPLDHSLIHCQPLVH 195
Cdd:cd00934     2 SFQVKYLGSVEVGSSR---GVDVVEEALKALAAALKSSKRKP--------GPVLLEVSSKGVKLLDLDTKELLLRHPLHR 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1938958478 196 IRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFRCD--VPAKAIASALQ 242
Cdd:cd00934    71 ISYCGRDPD--NPNVFAFIAGEEGGSGFRCHVFQCEdeEEAEEILQAIG 117
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 30-61 6.94e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 6.94e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1938958478   30 GLPPGWRKIRDAAG-TYYWHVPSGSTQWQRPTW 61
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 31-59 2.22e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 46.73  E-value: 2.22e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1938958478  31 LPPGWRKIRDAAG-TYYWHVPSGSTQWQRP 59
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 32-61 8.17e-07

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 45.21  E-value: 8.17e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1938958478  32 PPGWRKIRDAAG-TYYWHVPSGSTQWQRPTW 61
Cdd:cd00201     1 PPGWEERWDPDGrVYYYNHNTKETQWEDPRE 31
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 287-405 2.84e-04

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 40.57  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 287 QKYEALYMGILPVTKAMGMDVLNEAIGTL--TGRGDRKTWVPAMLSVSDSLMTAHPIQaeagaEEEPLWQCPVRLVTFIG 364
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALaaALKSSKRKPGPVLLEVSSKGVKLLDLD-----TKELLLRHPLHRISYCG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1938958478 365 VGHD-PHTFGLIA-DLGCQSFQCAAFWCQP--HAGGLSEAVQAAC 405
Cdd:cd00934    76 RDPDnPNVFAFIAgEEGGSGFRCHVFQCEDeeEAEEILQAIGQAF 120
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 179-233 3.13e-03

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 37.61  E-value: 3.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938958478 179 LLNPLDHSLIHCQPLVHIRVWGVGSSKGRDRD-FAFVAGDKDSCMLKCHVFRCDVP 233
Cdd:cd01211    54 LYDPTSNTEIASYPIYRILFCARGPDGTSESDcFAFTWSHGETAIFQCHVFRCEIP 109
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 116-240 3.35e-03

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 37.61  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 116 CFAVRSLGWVEVPEedlapGKSSIAVNNCIQQLaQTRNRsqphdgawgEGQNMLMVLKKDAMSLLNPLDHSLIHCQPLVH 195
Cdd:cd13161     3 VFEAKYLGSVPVKE-----PKGNDVVMAAVKRL-KDLKL---------KPKPVVLVVSSEGIRVVERLTGEVLTNVPIKD 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1938958478 196 IRVWGVGsskGRDRD-FAFVAGDKDSCMLKCHVFRCDVPAKAIASA 240
Cdd:cd13161    68 ISFVTVD---PKDKKlFAFISHDPRLGRITCHVFRCKRGAQEICDT 110
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 289-404 3.72e-03

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 37.23  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958478 289 YEALYMGILPVTKAMGMDVLNEAIGTLtgRGDRKTWVPAMLSVSDSlmtahPIQAEAGAEEEPLWQCPVRLVTFIGVGH- 367
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRL--KDLKLKPKPVVLVVSSE-----GIRVVERLTGEVLTNVPIKDISFVTVDPk 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1938958478 368 DPHTFGLIA---DLG---CQSFQCAafwcqPHAGGLSEAVQAA 404
Cdd:cd13161    77 DKKLFAFIShdpRLGritCHVFRCK-----RGAQEICDTIAEA 114
 
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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