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Conserved domains on  [gi|22122589|ref|NP_666197|]
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amyloid-beta A4 precursor protein-binding family B member 3 isoform 1 [Mus musculus]

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 ...
 116-254 9.11e-83

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: 252.22  E-value: 9.11e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 116 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 195
Cdd:cd01272   1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22122589 196 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 254
Cdd:cd01272  81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 283-413 2.02e-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: 199.37  E-value: 2.02e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 283 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEagaeEEPLWQCPVRLV 362
Cdd:cd01271   1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22122589 363 TFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQK 413
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 6.77e-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: 6.77e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22122589     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 ...
 116-254 9.11e-83

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: 252.22  E-value: 9.11e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 116 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 195
Cdd:cd01272   1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22122589 196 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 254
Cdd:cd01272  81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 283-413 2.02e-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: 199.37  E-value: 2.02e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 283 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEagaeEEPLWQCPVRLV 362
Cdd:cd01271   1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22122589 363 TFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQK 413
Cdd:cd01271  77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
119-250 9.05e-49

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 163.69  E-value: 9.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589   119 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 195
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22122589   196 VHIRVWGVGsSKGRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQI 250
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 114-254 7.96e-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: 118.57  E-value: 7.96e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589    114 PGAKCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTrnrsqpHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQ 193
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAA------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22122589    194 PLVHIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 254
Cdd:smart00462  70 PLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 286-418 4.92e-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: 110.87  E-value: 4.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589    286 QAAQKYEALYMGILPVTKAMGMDVLNEAIGTL--TARGDRKTWVPAMLSVSDSLMTAHAIQAEAgaeeePLWQCPVRLVT 363
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 22122589    364 FIGVGR-DPHTFGLIADLGCQS-FQCAAFWCEPHAGGLSEAVQAACMVQYQKCLVAS 418
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 6.77e-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: 6.77e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22122589     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 2.23e-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: 2.23e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 22122589    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 8.28e-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: 8.28e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 22122589  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 ...
 116-254 9.11e-83

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: 252.22  E-value: 9.11e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 116 AKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 195
Cdd:cd01272   1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22122589 196 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 254
Cdd:cd01272  81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 283-413 2.02e-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: 199.37  E-value: 2.02e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 283 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEagaeEEPLWQCPVRLV 362
Cdd:cd01271   1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22122589 363 TFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQK 413
Cdd:cd01271  77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
119-250 9.05e-49

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 163.69  E-value: 9.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589   119 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 195
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22122589   196 VHIRVWGVGsSKGRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQI 250
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 114-254 7.96e-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: 118.57  E-value: 7.96e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589    114 PGAKCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTrnrsqpHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQ 193
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAA------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22122589    194 PLVHIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 254
Cdd:smart00462  70 PLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 286-418 4.92e-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: 110.87  E-value: 4.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589    286 QAAQKYEALYMGILPVTKAMGMDVLNEAIGTL--TARGDRKTWVPAMLSVSDSLMTAHAIQAEAgaeeePLWQCPVRLVT 363
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 22122589    364 FIGVGR-DPHTFGLIADLGCQS-FQCAAFWCEPHAGGLSEAVQAACMVQYQKCLVAS 418
Cdd:smart00462  76 FCAVGPdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 118-244 4.84e-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: 68.69  E-value: 4.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 118 CFAVRSLGWVEVPEEDlapGKSSIAVNNCIQQLAQTRNRSQPhdgtwgegQNMLMILKKDAMSLLNPLDHSLIHCQPLVH 197
Cdd:cd00934   2 SFQVKYLGSVEVGSSR---GVDVVEEALKALAAALKSSKRKP--------GPVLLEVSSKGVKLLDLDTKELLLRHPLHR 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22122589 198 IRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFHCD--VPAKAIASALQ 244
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 6.77e-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: 6.77e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22122589     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 2.23e-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: 2.23e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 22122589    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 8.28e-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: 8.28e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 22122589  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 ...
 289-407 4.04e-05

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: 42.88  E-value: 4.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 289 QKYEALYMGILPVTKAMGMDVLNEAIGTL--TARGDRKTWVPAMLSVSDSlmtahAIQAEAGAEEEPLWQCPVRLVTFIG 366
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALaaALKSSKRKPGPVLLEVSSK-----GVKLLDLDTKELLLRHPLHRISYCG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 22122589 367 VGRD-PHTFGLIA-DLGCQSFQCAAFWCEP--HAGGLSEAVQAAC 407
Cdd:cd00934  76 RDPDnPNVFAFIAgEEGGSGFRCHVFQCEDeeEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 291-406 1.20e-04

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: 41.46  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589 291 YEALYMGILPVTKAMGMDVLNEAIGTLTARGdrKTWVPAMLSVSDSlmtahAIQAEAGAEEEPLWQCPVRLVTFIGV-GR 369
Cdd:cd13161   4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLK--LKPKPVVLVVSSE-----GIRVVERLTGEVLTNVPIKDISFVTVdPK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22122589 370 DPHTFGLIA---DLG---CQSFQCAafwcePHAGGLSEAVQAA 406
Cdd:cd13161  77 DKKLFAFIShdpRLGritCHVFRCK-----RGAQEICDTIAEA 114
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 142-244 4.09e-03

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 37.33  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122589   142 AVNNCIQQLAQTRNRSQPhdgtWGegQNMLMILKKDAMSLLNP-----LDH----SLIHCQPLVHIRVWgvgsskgrDRD 212
Cdd:pfam08416  20 AVEDAIRKLQLLDAQGRV----WT--QEMLLQVSDQGITLTDNetkeeLESypldSISHCQAVLNDGRY--------NSI 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 22122589   213 FAFVAGDKDSCMLKCHVFHC-----DVPAKAIASALQ 244
Cdd:pfam08416  86 LALVCQEPGQSKPDVHLFQCdelgaELIAEDIESALS 122
 
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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