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Conserved domains on  [gi|578808528|ref|XP_006714068|]
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amyloid beta precursor protein binding family B member 2 isoform X1 [Homo sapiens]

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 ...
 417-556 1.47e-102

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: 311.16  E-value: 1.47e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 417 AKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 496
Cdd:cd01272    1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 497 VSIRVWGVGRDNGreRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERK 556
Cdd:cd01272   81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 585-711 1.16e-85

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: 266.39  E-value: 1.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 585 PKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 664
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578808528 665 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQK 711
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 293-321 2.32e-08

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: 50.20  E-value: 2.32e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 578808528  293 LPPGWKRVSDIAG-TYYWHIPTGTTQWERP 321
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 ...
 417-556 1.47e-102

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: 311.16  E-value: 1.47e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 417 AKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 496
Cdd:cd01272    1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 497 VSIRVWGVGRDNGreRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERK 556
Cdd:cd01272   81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 585-711 1.16e-85

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: 266.39  E-value: 1.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 585 PKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 664
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578808528 665 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQK 711
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
420-551 1.41e-50

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 172.93  E-value: 1.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528  420 FAVRSLGWVEMAEEdLAPGKS--SVAVNNCIRQLSYCK-NDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 496
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKiNKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578808528  497 VSIRVWGVGrDNGRERDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKI 551
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 588-718 1.50e-36

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: 133.98  E-value: 1.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528   588 ELVQKFHVQYLGMLPVDKPVGMDILNSAIENL--MTSSNKEDWLSVNMNVADATVTVISEKNEEeVLVECRVRFLSFMGV 665
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-VLHEHPLRRISFCAV 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 578808528   666 G-KDVHTFAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCLVARPP 718
Cdd:smart00462  80 GpDDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 415-559 4.11e-36

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: 132.44  E-value: 4.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528   415 PEAKCFAVRSLGWVEMAEEDlapgkSSVAVNNCIRQLSYCKndirdtVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQ 494
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAAQ------GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578808528   495 PIVSIRVWGVGRDNGRerDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERKNAK 559
Cdd:smart00462  70 PLRRISFCAVGPDDLD--VFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 293-321 2.32e-08

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: 50.20  E-value: 2.32e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 578808528  293 LPPGWKRVSDIAG-TYYWHIPTGTTQWERP 321
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 292-323 5.85e-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: 49.14  E-value: 5.85e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 578808528   292 DLPPGWKRVSDIAG-TYYWHIPTGTTQWERPVS 323
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 294-322 2.00e-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: 47.52  E-value: 2.00e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 578808528 294 PPGWKRVSDIAG-TYYWHIPTGTTQWERPV 322
Cdd:cd00201    1 PPGWEERWDPDGrVYYYNHNTKETQWEDPR 30
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 417-556 1.47e-102

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: 311.16  E-value: 1.47e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 417 AKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 496
Cdd:cd01272    1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 497 VSIRVWGVGRDNGreRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERK 556
Cdd:cd01272   81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 585-711 1.16e-85

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: 266.39  E-value: 1.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 585 PKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 664
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578808528 665 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQK 711
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
420-551 1.41e-50

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 172.93  E-value: 1.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528  420 FAVRSLGWVEMAEEdLAPGKS--SVAVNNCIRQLSYCK-NDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 496
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKiNKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578808528  497 VSIRVWGVGrDNGRERDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKI 551
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 588-718 1.50e-36

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: 133.98  E-value: 1.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528   588 ELVQKFHVQYLGMLPVDKPVGMDILNSAIENL--MTSSNKEDWLSVNMNVADATVTVISEKNEEeVLVECRVRFLSFMGV 665
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-VLHEHPLRRISFCAV 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 578808528   666 G-KDVHTFAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCLVARPP 718
Cdd:smart00462  80 GpDDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 415-559 4.11e-36

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: 132.44  E-value: 4.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528   415 PEAKCFAVRSLGWVEMAEEDlapgkSSVAVNNCIRQLSYCKndirdtVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQ 494
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAAQ------GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578808528   495 PIVSIRVWGVGRDNGRerDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERKNAK 559
Cdd:smart00462  70 PLRRISFCAVGPDDLD--VFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 591-705 2.02e-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: 70.23  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 591 QKFHVQYLGMLPVDKPVGMDILNSAIENLMT--SSNKEDWLSVNMNVADATVTVIsEKNEEEVLVECRVRFLSFMGVGKD 668
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAalKSSKRKPGPVLLEVSSKGVKLL-DLDTKELLLRHPLHRISYCGRDPD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 578808528 669 V-HTFAFI-MDTGNQRFECHVFWCEPN--AGNVSEAVQAAC 705
Cdd:cd00934   80 NpNVFAFIaGEEGGSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 419-548 4.88e-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: 69.07  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 419 CFAVRSLGWVEMAEEDLAPGkSSVAVNNCIRQLSYCKNdirdtvgiwgEGKDMYLILENDMLSLVDPMDRSVLHSQPIVS 498
Cdd:cd00934    2 SFQVKYLGSVEVGSSRGVDV-VEEALKALAAALKSSKR----------KPGPVLLEVSSKGVKLLDLDTKELLLRHPLHR 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578808528 499 IRVWGVGRDNgrERDFAYVARDKDTRILKCHVFRCDTP--AKAIATSLHEIC 548
Cdd:cd00934   71 ISYCGRDPDN--PNVFAFIAGEEGGSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 593-704 4.28e-13

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: 66.50  E-value: 4.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 593 FHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDwlSVNMNVADATVTVIsEKNEEEVLVECRVRFLSFMGV-GKDVHT 671
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPK--PVVLVVSSEGIRVV-ERLTGEVLTNVPIKDISFVTVdPKDKKL 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 578808528 672 FAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAA 704
Cdd:cd13161   81 FAFIShDPRLGRITCHVFRCKRGAQEICDTIAEA 114
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 419-542 2.26e-08

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: 53.02  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 419 CFAVRSLGWVEMAEedlaPGKSSVaVNNCIRqlsycknDIRDTvgiWGEGKDMYLILENDMLSLVDPMDRSVLHSQPIVS 498
Cdd:cd13161    3 VFEAKYLGSVPVKE----PKGNDV-VMAAVK-------RLKDL---KLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKD 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578808528 499 IrVWgVGRDNGRERDFAYVARDKDTRILKCHVFRCDTPAKAIAT 542
Cdd:cd13161   68 I-SF-VTVDPKDKKLFAFISHDPRLGRITCHVFRCKRGAQEICD 109
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 293-321 2.32e-08

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: 50.20  E-value: 2.32e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 578808528  293 LPPGWKRVSDIAG-TYYWHIPTGTTQWERP 321
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 292-323 5.85e-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: 49.14  E-value: 5.85e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 578808528   292 DLPPGWKRVSDIAG-TYYWHIPTGTTQWERPVS 323
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 294-322 2.00e-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: 47.52  E-value: 2.00e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 578808528 294 PPGWKRVSDIAG-TYYWHIPTGTTQWERPV 322
Cdd:cd00201    1 PPGWEERWDPDGrVYYYNHNTKETQWEDPR 30
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 482-558 2.81e-06

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: 47.24  E-value: 2.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578808528 482 LVDPMDRSVLHSQPIVSIRVWGVGRDNGRERD-FAYVARDKDTRILKCHVFRCDTPakaiatslhEICSKIMAERKNA 558
Cdd:cd01211   54 LYDPTSNTEIASYPIYRILFCARGPDGTSESDcFAFTWSHGETAIFQCHVFRCEIP---------EAVSKVLYSFAKA 122
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 593-690 4.94e-05

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: 43.47  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 593 FHVQYLGMLPVDKPVGMDILNSAIENL--MTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRfLSFMGVGK-DV 669
Cdd:cd13159    5 FYLKYLGSTLVEKPKGEGATAEAVKTIiaMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYR-ISYCTADAnHD 83

                         90       100
                 ....*....|....*....|..
gi 578808528 670 HTFAFIMDTG-NQRFECHVFWC 690
Cdd:cd13159   84 KVFAFIATNQdNEKLECHAFLC 105
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 588-713 3.51e-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: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578808528 588 ELVQKFHVQY----LGMLPVDKPVGMDILNSAIENL-----MTSSNKEDWLSVNMNVADATVTVISEKNeEEVLVECRVR 658
Cdd:cd01273    5 EALIKGHVAYlvkfLGCTEVEQPKGTEVVKEAIRKLkfarqLKKSEGAKLPKVELQISIDGVKIQDPKT-KVIMHQFPLH 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578808528 659 FLSFMGVGKDV-HTFAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCL 713
Cdd:cd01273   84 RISFCADDKTDkRIFSFIAkDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFL 140
 
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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