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Conserved domains on  [gi|26350793|dbj|BAC39033|]
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unnamed protein product [Mus musculus]

Protein Classification

Fe65 family protein( domain architecture ID 11093636)

Fe65 family protein contains WW and PTB (phosphotyrosine-binding) domains, similar to human protein Fe65, also called amyloid-beta A4 precursor protein-binding family B member 1, that have both coactivator and corepressor functions

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 ...
368-507 2.97e-92

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: 283.04  E-value: 2.97e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 368 KCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPmAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 447
Cdd:cd01272   2 KRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDT-VGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 448 VSIRVWGVGRDSGreRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERR 507
Cdd:cd01272  81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
535-660 5.13e-75

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: 237.50  E-value: 5.13e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 535 PKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQ-TEAVLGECRVRFLSFLA 613
Cdd:cd01271   1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKdEEEVLVECRVRFLSFMG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26350793 614 VGRDVHTFAFIMAAGPSSFCCHMFWCEPNAASLSEAVQAACMLRYQK 660
Cdd:cd01271  81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
255-283 1.08e-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: 48.27  E-value: 1.08e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 26350793   255 LPAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
368-507 2.97e-92

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: 283.04  E-value: 2.97e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 368 KCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPmAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 447
Cdd:cd01272   2 KRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDT-VGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 448 VSIRVWGVGRDSGreRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERR 507
Cdd:cd01272  81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
535-660 5.13e-75

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: 237.50  E-value: 5.13e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 535 PKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQ-TEAVLGECRVRFLSFLA 613
Cdd:cd01271   1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKdEEEVLVECRVRFLSFMG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26350793 614 VGRDVHTFAFIMAAGPSSFCCHMFWCEPNAASLSEAVQAACMLRYQK 660
Cdd:cd01271  81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
370-502 4.15e-50

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 171.01  E-value: 4.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793   370 FAVRSLGWVEMTEEeLAPGRS--SVAVNNCIRQLSYHKNNLHDPMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 447
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26350793   448 VSIRVWGVGrDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKI 502
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
365-512 4.34e-37

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: 135.13  E-value: 4.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793    365 PGIKCFAVRSLGWVEMTEEelapgRSSVAVNNCIRQLSYHknnlhdpMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHA 444
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEA-----RGLQVVQEAIRKLRAA-------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHE 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26350793    445 QPIVSIRVWGVGRDsgRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCL 512
Cdd:smart00462  69 HPLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
538-667 1.27e-33

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: 125.50  E-value: 1.27e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793    538 ELVQKFQVYYLGNVPVAKPVGVDVINGALESVLS--SSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVG 615
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 26350793    616 R-DVHTFAFIMAAGPSS-FCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQ 667
Cdd:smart00462  81 PdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
255-283 1.08e-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: 48.27  E-value: 1.08e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 26350793   255 LPAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
254-283 1.45e-06

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: 44.90  E-value: 1.45e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 26350793    254 DLPAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
256-283 4.60e-06

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: 43.67  E-value: 4.60e-06
                        10        20
                ....*....|....*....|....*....
gi 26350793 256 PAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:cd00201   1 PPGWEERWDPDGrVYYYNHNTKETQWEDP 29
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
368-507 2.97e-92

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: 283.04  E-value: 2.97e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 368 KCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPmAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 447
Cdd:cd01272   2 KRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDT-VGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 448 VSIRVWGVGRDSGreRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERR 507
Cdd:cd01272  81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
535-660 5.13e-75

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: 237.50  E-value: 5.13e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 535 PKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQ-TEAVLGECRVRFLSFLA 613
Cdd:cd01271   1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKdEEEVLVECRVRFLSFMG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26350793 614 VGRDVHTFAFIMAAGPSSFCCHMFWCEPNAASLSEAVQAACMLRYQK 660
Cdd:cd01271  81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
370-502 4.15e-50

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 171.01  E-value: 4.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793   370 FAVRSLGWVEMTEEeLAPGRS--SVAVNNCIRQLSYHKNNLHDPMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 447
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26350793   448 VSIRVWGVGrDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKI 502
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
365-512 4.34e-37

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: 135.13  E-value: 4.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793    365 PGIKCFAVRSLGWVEMTEEelapgRSSVAVNNCIRQLSYHknnlhdpMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHA 444
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEA-----RGLQVVQEAIRKLRAA-------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHE 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26350793    445 QPIVSIRVWGVGRDsgRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCL 512
Cdd:smart00462  69 HPLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
538-667 1.27e-33

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: 125.50  E-value: 1.27e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793    538 ELVQKFQVYYLGNVPVAKPVGVDVINGALESVLS--SSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVG 615
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 26350793    616 R-DVHTFAFIMAAGPSS-FCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQ 667
Cdd:smart00462  81 PdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
541-654 9.67e-19

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: 82.56  E-value: 9.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 541 QKFQVYYLGNVPVAKPVGVDVINGALESVL--SSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDV 618
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAaaLKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 26350793 619 -HTFAFIMAAGPSS-FCCHMFWCEPN--AASLSEAVQAAC 654
Cdd:cd00934  81 pNVFAFIAGEEGGSgFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
369-499 3.40e-16

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: 75.24  E-value: 3.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 369 CFAVRSLGWVEMTEEELAPgRSSVAVNNCIRQLSYHKNnlhdpmaggwgEGKDLLLQLEDETLKLVEPQNQTLLHAQPIV 448
Cdd:cd00934   2 SFQVKYLGSVEVGSSRGVD-VVEEALKALAAALKSSKR-----------KPGPVLLEVSSKGVKLLDLDTKELLLRHPLH 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 26350793 449 SIRVwgVGRDSGRERDFAYVARDKLTQMLKCHVFRC--EAPAKNIATSLHEIC 499
Cdd:cd00934  70 RISY--CGRDPDNPNVFAFIAGEEGGSGFRCHVFQCedEEEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
543-653 8.74e-11

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: 59.57  E-value: 8.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 543 FQVYYLGNVPVAKPVGVDVINGALESVLSSSSREqwTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAV-GRDVHTF 621
Cdd:cd13161   4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKP--KPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVdPKDKKLF 81
                        90       100       110
                ....*....|....*....|....*....|...
gi 26350793 622 AFIMAAGPSSFC-CHMFWCEPNAASLSEAVQAA 653
Cdd:cd13161  82 AFISHDPRLGRItCHVFRCKRGAQEICDTIAEA 114
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
255-283 1.08e-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: 48.27  E-value: 1.08e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 26350793   255 LPAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
254-283 1.45e-06

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: 44.90  E-value: 1.45e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 26350793    254 DLPAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
256-283 4.60e-06

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: 43.67  E-value: 4.60e-06
                        10        20
                ....*....|....*....|....*....
gi 26350793 256 PAGWMRVQDTSG-TYYWHIPTGTTQWEPP 283
Cdd:cd00201   1 PPGWEERWDPDGrVYYYNHNTKETQWEDP 29
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
424-493 1.37e-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: 41.85  E-value: 1.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 424 LQLEDETLKLVEPQNQTLLHAQPIVSIrVWgVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIAT 493
Cdd:cd13161  42 LVVSSEGIRVVERLTGEVLTNVPIKDI-SF-VTVDPKDKKLFAFISHDPRLGRITCHVFRCKRGAQEICD 109
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
430-509 4.37e-04

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: 40.69  E-value: 4.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 430 TLKLVEPQNQTLLHAQPIVSIRVWGVGRDSGRERD-FAYVARDKLTQMLKCHVFRCEAPakniatslhEICSKIMSERRN 508
Cdd:cd01211  51 SVRLYDPTSNTEIASYPIYRILFCARGPDGTSESDcFAFTWSHGETAIFQCHVFRCEIP---------EAVSKVLYSFAK 121

                .
gi 26350793 509 A 509
Cdd:cd01211 122 A 122
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
366-482 1.19e-03

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF 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: 241298  Cd Length: 135  Bit Score: 39.60  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 366 GIKCFAVRSLGWVEMTEeelapgrsSVAVNNCIRQLSYHKNNLHDPMAGgwgegkdlLLQLEDETLKLVEPQNQTLLHAQ 445
Cdd:cd01268  13 GTCSFPVKYLGCVEVGE--------SRGMQVCEEALKKLKASRKKPVRA--------VLWVSGDGLRVVDEKTKGLIVDQ 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 26350793 446 PI--VSIrvwgVGRDSGRERDFAYVARDKLTQMLKCHVF 482
Cdd:cd01268  77 TIekVSF----CAPDRNHERAFSYICRDGTTRRWMCHCF 111
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
438-484 2.09e-03

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB 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 contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 38.85  E-value: 2.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 26350793 438 NQTLLHaqpiVSI-RVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRC 484
Cdd:cd13159  62 NETILE----VSIyRISYCTADANHDKVFAFIATNQDNEKLECHAFLC 105
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
543-663 4.00e-03

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. 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: 269971  Cd Length: 144  Bit Score: 38.41  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350793 543 FQVYYLGNVPVAKPVGVDVINGALESV-----LSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRD 617
Cdd:cd01273  14 YLVKFLGCTEVEQPKGTEVVKEAIRKLkfarqLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKT 93
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 26350793 618 V-HTFAFIMAAGPSS-FCCHMFWCEPNAASLSEAVQAACMLRYQKCLD 663
Cdd:cd01273  94 DkRIFSFIAKDSESEkHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLE 141
 
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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