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Conserved domains on  [gi|319738665|ref|NP_001188345|]
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amyloid beta precursor protein binding family B member 2 isoform 5 [Mus musculus]

Protein Classification

Fe65 family PTB domain-containing protein( domain architecture ID 10101050)

Fe65 family PTB (phosphotyrosine-binding) domain-containing protein similar to PTB domain region of Homo sapiens neuronal adaptor protein Fe65 and homologs

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  15567406|8987385|10610414
SCOP:  4002427

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 34-160 5.85e-88

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: 254.83  E-value: 5.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  34 PKTELVQKFRVQYLGMLPVDRPVGMDTLNSAIENLMTSSSKEDWPSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 113
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 319738665 114 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAANVSEAVQAACMLRYQK 160
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
 
Name Accession Description Interval E-value
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 34-160 5.85e-88

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: 254.83  E-value: 5.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  34 PKTELVQKFRVQYLGMLPVDRPVGMDTLNSAIENLMTSSSKEDWPSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 113
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 319738665 114 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAANVSEAVQAACMLRYQK 160
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-167 9.49e-39

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: 130.13  E-value: 9.49e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665    37 ELVQKFRVQYLGMLPVDRPVGMDTLNSAIENLMT--SSSKEDWPSVNMNVADATVTVISEKNEEeVLVECRVRFLSFMGV 114
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaqGSEKKEPQKVILSISSRGVKLIDEDTKA-VLHEHPLRRISFCAV 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 319738665   115 G-KDVHTFAFIM-DTGNQRFECHVFWCEPNAANVSEAVQAACMLRYQKCLVARPP 167
Cdd:smart00462  80 GpDDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
42-157 2.44e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 39.65  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665   42 FRVQYLGMLPVDRP------VGMDTLNSAI-----ENLMTSSSKE-DW---PSVNMNVADATVTVISEKNEEeVLVECRV 106
Cdd:pfam00640   1 FAVRYLGSVEVPEErapdknTRMQQAREAIrrvkaAKINKIRGLSgETgpgTKVDLFISTDGLKLLNPDTQE-LIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 319738665  107 RFLSFMGVG--KDVHTFAFIMDTG-NQRFECHVFWCEPNAANVSEAVQAACMLR 157
Cdd:pfam00640  80 VSISFCADGdpDLMRYFAYIARDKaTNKFACHVFESEDGAQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 34-160 5.85e-88

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: 254.83  E-value: 5.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  34 PKTELVQKFRVQYLGMLPVDRPVGMDTLNSAIENLMTSSSKEDWPSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 113
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 319738665 114 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAANVSEAVQAACMLRYQK 160
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-167 9.49e-39

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: 130.13  E-value: 9.49e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665    37 ELVQKFRVQYLGMLPVDRPVGMDTLNSAIENLMT--SSSKEDWPSVNMNVADATVTVISEKNEEeVLVECRVRFLSFMGV 114
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaqGSEKKEPQKVILSISSRGVKLIDEDTKA-VLHEHPLRRISFCAV 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 319738665   115 G-KDVHTFAFIM-DTGNQRFECHVFWCEPNAANVSEAVQAACMLRYQKCLVARPP 167
Cdd:smart00462  80 GpDDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 40-154 5.51e-17

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: 73.70  E-value: 5.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  40 QKFRVQYLGMLPVDRPVGMDTLNSAIENLMT--SSSKEDWPSVNMNVADATVTVIsEKNEEEVLVECRVRFLSFMGVGKD 117
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAalKSSKRKPGPVLLEVSSKGVKLL-DLDTKELLLRHPLHRISYCGRDPD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 319738665 118 V-HTFAFI-MDTGNQRFECHVFWCEPN--AANVSEAVQAAC 154
Cdd:cd00934   80 NpNVFAFIaGEEGGSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 42-153 3.08e-14

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: 66.12  E-value: 3.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  42 FRVQYLGMLPVDRPVGMDTLNSAIENLmtSSSKEDWPSVNMNVADATVTVIsEKNEEEVLVECRVRFLSFMGV-GKDVHT 120
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRL--KDLKLKPKPVVLVVSSEGIRVV-ERLTGEVLTNVPIKDISFVTVdPKDKKL 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 319738665 121 FAFIM-DTGNQRFECHVFWCEPNAANVSEAVQAA 153
Cdd:cd13161   81 FAFIShDPRLGRITCHVFRCKRGAQEICDTIAEA 114
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 42-139 4.66e-06

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: 44.24  E-value: 4.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  42 FRVQYLGMLPVDRPVGMDTLNSAIENL--MTSSSKEDWPSVNMNVADATVTVISEKNEEEVLVECRVRfLSFMGVGK-DV 118
Cdd:cd13159    5 FYLKYLGSTLVEKPKGEGATAEAVKTIiaMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYR-ISYCTADAnHD 83

                         90       100
                 ....*....|....*....|..
gi 319738665 119 HTFAFIMDTG-NQRFECHVFWC 139
Cdd:cd13159   84 KVFAFIATNQdNEKLECHAFLC 105
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 42-162 6.70e-05

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: 41.49  E-value: 6.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665  42 FRVQYLGMLPVDRPVGMDTLNSAIENL-----MTSSSKEDWPSVNMNVADATVTVISEKNeEEVLVECRVRFLSFMGVGK 116
Cdd:cd01273   14 YLVKFLGCTEVEQPKGTEVVKEAIRKLkfarqLKKSEGAKLPKVELQISIDGVKIQDPKT-KVIMHQFPLHRISFCADDK 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 319738665 117 DV-HTFAFIM-DTGNQRFECHVFWCEPNAANVSEAVQAACMLRYQKCL 162
Cdd:cd01273   93 TDkRIFSFIAkDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFL 140
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
42-157 2.44e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 39.65  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319738665   42 FRVQYLGMLPVDRP------VGMDTLNSAI-----ENLMTSSSKE-DW---PSVNMNVADATVTVISEKNEEeVLVECRV 106
Cdd:pfam00640   1 FAVRYLGSVEVPEErapdknTRMQQAREAIrrvkaAKINKIRGLSgETgpgTKVDLFISTDGLKLLNPDTQE-LIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 319738665  107 RFLSFMGVG--KDVHTFAFIMDTG-NQRFECHVFWCEPNAANVSEAVQAACMLR 157
Cdd:pfam00640  80 VSISFCADGdpDLMRYFAYIARDKaTNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 113-154 7.33e-03

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: 35.36  E-value: 7.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 319738665 113 GVGKDV-HTFAFIM-DTGNQRFECHVFWCEPNAANVSEAVQAAC 154
Cdd:cd01272   87 GVGRDNgRDFAYVArDKDTRVLKCHVFRCDTPAKAIATALHEIC 130
 
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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