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Conserved domains on  [gi|1054385726|ref|NP_001317087|]
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PTB-containing, cubilin and LRP1-interacting protein isoform 5 [Homo sapiens]

Protein Classification

PTB-containing, cubilin and LRP1-interacting protein( domain architecture ID 10192180)

PTB-containing, cubilin and LRP1-interacting protein (P-CLI1) increases proliferation of preadipocytes without affecting adipocytic differentiation

Gene Symbol:  PID1
Gene Ontology:  GO:0005515|GO:0071398
PubMed:  15567406|8987385|10610414

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 42-180 1.63e-107

PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold; P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 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.


:

Pssm-ID: 269988  Cd Length: 139  Bit Score: 304.60  E-value: 1.63e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  42 SGCKVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAY 121
Cdd:cd13167     1 TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHMDTFQVARIAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054385726 122 CTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMK 180
Cdd:cd13167    81 CTADHNISPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAMMEAFKKTFHSMR 139
 
Name Accession Description Interval E-value
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 42-180 1.63e-107

PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold; P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 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.


Pssm-ID: 269988  Cd Length: 139  Bit Score: 304.60  E-value: 1.63e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  42 SGCKVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAY 121
Cdd:cd13167     1 TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHMDTFQVARIAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054385726 122 CTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMK 180
Cdd:cd13167    81 CTADHNISPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAMMEAFKKTFHSMR 139
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
45-195 1.41e-17

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 76.73  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  45 KVTYLGKVsTTGMQFLSGCTEKPVIELWKKHTLAREDVfpaNALLEIRPFQVWLHHLDHKGEAtvhmdtFQVARIAYCTA 124
Cdd:pfam14719   3 KVVYLGNV-LTIHAKGEGCTDKPLGTIWKNYCQGKSGT---KMKLTVTRSGLKATTKEHGLTE------YWSHRITYCSA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054385726 125 DHNVsPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMKSDGRIHSNSSSEEVS 195
Cdd:pfam14719  73 PPNY-PRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCARHAQNARLS 142
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 44-177 3.14e-07

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: 47.69  E-value: 3.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726   44 CKVTYLGKVST---TGMQFLSGCTEKpvieLWKKHTLAREDvfPANALLEIRPFQVWLHHLDHKGEATvhmdTFQVARIA 120
Cdd:smart00462   6 FRVKYLGSVEVpeaRGLQVVQEAIRK----LRAAQGSEKKE--PQKVILSISSRGVKLIDEDTKAVLH----EHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054385726  121 YCTADHNvSPNIFAWVYREINDDlsyQMDCHAVECESklEAKKLAHAMMEAFRKTFH 177
Cdd:smart00462  76 FCAVGPD-DLDVFGYIARDPGSS---RFACHVFRCEK--AAEDIALAIGQAFQLAYE 126
 
Name Accession Description Interval E-value
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 42-180 1.63e-107

PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold; P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 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.


Pssm-ID: 269988  Cd Length: 139  Bit Score: 304.60  E-value: 1.63e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  42 SGCKVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAY 121
Cdd:cd13167     1 TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHMDTFQVARIAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054385726 122 CTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMK 180
Cdd:cd13167    81 CTADHNISPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAMMEAFKKTFHSMR 139
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 42-172 1.04e-25

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: 96.04  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  42 SGCKVTYLGKVSTTGMQFLSGCTEkpvIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKgeatVHMDTFQVARIAY 121
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEE---ALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTK----ELLLRHPLHRISY 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054385726 122 CTADHNvSPNIFAWVYREINddlSYQMDCHAVECESKLEAKKLAHAMMEAF 172
Cdd:cd00934    74 CGRDPD-NPNVFAFIAGEEG---GSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
45-195 1.41e-17

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 76.73  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  45 KVTYLGKVsTTGMQFLSGCTEKPVIELWKKHTLAREDVfpaNALLEIRPFQVWLHHLDHKGEAtvhmdtFQVARIAYCTA 124
Cdd:pfam14719   3 KVVYLGNV-LTIHAKGEGCTDKPLGTIWKNYCQGKSGT---KMKLTVTRSGLKATTKEHGLTE------YWSHRITYCSA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054385726 125 DHNVsPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMKSDGRIHSNSSSEEVS 195
Cdd:pfam14719  73 PPNY-PRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCARHAQNARLS 142
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 45-165 1.01e-13

Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. 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.


Pssm-ID: 269925  Cd Length: 125  Bit Score: 65.00  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  45 KVTYLGKVsTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANalLEIRPFQVWLHHLDHKG-EATVHmdtfqvaRIAYCT 123
Cdd:cd01214     9 TVVYLGNV-LTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMK--LTVTPSGLKATTKQHGLtEYWLH-------RITYCS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1054385726 124 ADHNVsPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLA 165
Cdd:cd01214    79 APPNY-PRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIA 119
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 44-177 3.14e-07

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: 47.69  E-value: 3.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726   44 CKVTYLGKVST---TGMQFLSGCTEKpvieLWKKHTLAREDvfPANALLEIRPFQVWLHHLDHKGEATvhmdTFQVARIA 120
Cdd:smart00462   6 FRVKYLGSVEVpeaRGLQVVQEAIRK----LRAAQGSEKKE--PQKVILSISSRGVKLIDEDTKAVLH----EHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054385726  121 YCTADHNvSPNIFAWVYREINDDlsyQMDCHAVECESklEAKKLAHAMMEAFRKTFH 177
Cdd:smart00462  76 FCAVGPD-DLDVFGYIARDPGSS---RFACHVFRCEK--AAEDIALAIGQAFQLAYE 126
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 45-172 2.15e-05

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects 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 insects, ticks, sea urchins, and nematodes.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 42.32  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054385726  45 KVTYLGKVSTTGMqFLSGCTEKPVIELWKKhtLAREDVFPaNALLEIRPFQVWLHHLDHKGEATVHMdTFQVARIAYCTA 124
Cdd:cd13160     4 TVKYLGRMPARGL-WGIKHTRKPLVDALKN--LPKGKTLP-KTKLEVSSDGVKLEELRGGFGSSKTV-FFPIHTISYGVQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1054385726 125 DhNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAF 172
Cdd:cd13160    79 D-LVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWLAKAF 125
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
111-172 3.80e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 38.88  E-value: 3.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054385726 111 MDTFQVARIAYCTADHNVSPNIFAWVYReinDDLSYQMDCHAVECESKleAKKLAHAMMEAF 172
Cdd:pfam00640  74 IHDHPLVSISFCADGDPDLMRYFAYIAR---DKATNKFACHVFESEDG--AQDIAQSIGQAF 130
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 118-173 1.52e-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: 37.31  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054385726 118 RIAYCTADHNvSPNIFAWVYREindDLSYQMDCHAVECESKLEAKKLAHAMMEAFR 173
Cdd:cd13159    72 RISYCTADAN-HDKVFAFIATN---QDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
 
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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