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Conserved domains on  [gi|1054304539|ref|NP_001317086|]
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PTB-containing, cubilin and LRP1-interacting protein isoform 4 [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 ...
 7-145 2.71e-106

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: 299.98  E-value: 2.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539   7 ERLQVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAY 86
Cdd:cd13167     1 TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHMDTFQVARIAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054304539  87 CTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMK 145
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 ...
 7-145 2.71e-106

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: 299.98  E-value: 2.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539   7 ERLQVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAY 86
Cdd:cd13167     1 TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHMDTFQVARIAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054304539  87 CTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMK 145
Cdd:cd13167    81 CTADHNISPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAMMEAFKKTFHSMR 139
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
11-160 8.35e-18

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 76.35  E-value: 8.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539  11 VTYLGKVsTTGMQFLSGCTEKPVIELWKKHTLAREDVfpaNALLEIRPFQVWLHHLDHKGEAtvhmdtFQVARIAYCTAD 90
Cdd:pfam14719   4 VVYLGNV-LTIHAKGEGCTDKPLGTIWKNYCQGKSGT---KMKLTVTRSGLKATTKEHGLTE------YWSHRITYCSAP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539  91 HNVsPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMKSDGRIHSNSSSEEVS 160
Cdd:pfam14719  74 PNY-PRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCARHAQNARLS 142
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 4-142 4.82e-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: 46.54  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539    4 PATERLQVTYLGKVST---TGMQFLSGCTEKpvieLWKKHTLAREDvfPANALLEIRPFQVWLHHLDHKGEATvhmdTFQ 80
Cdd:smart00462   1 GSGVSFRVKYLGSVEVpeaRGLQVVQEAIRK----LRAAQGSEKKE--PQKVILSISSRGVKLIDEDTKAVLH----EHP 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054304539   81 VARIAYCTADHNvSPNIFAWVYREINDDlsyQMDCHAVECESklEAKKLAHAMMEAFRKTFH 142
Cdd:smart00462  71 LRRISFCAVGPD-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 ...
 7-145 2.71e-106

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: 299.98  E-value: 2.71e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539   7 ERLQVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAY 86
Cdd:cd13167     1 TGYKVTYLGKVSTTGTQFLSGCTESPVIELWKKHTLAREDIFPSNALLEIRPFQVRLHHLDLRGEATVHMDTFQVARIAY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054304539  87 CTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMK 145
Cdd:cd13167    81 CTADHNISPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLAHAMMEAFKKTFHSMR 139
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 7-137 6.90e-27

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: 97.96  E-value: 6.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539   7 ERLQVTYLGKVSTTGMQFLSGCTEkpvIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKgeatVHMDTFQVARIAY 86
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEE---ALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTK----ELLLRHPLHRISY 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054304539  87 CTADHNvSPNIFAWVYREINddlSYQMDCHAVECESKLEAKKLAHAMMEAF 137
Cdd:cd00934    74 CGRDPD-NPNVFAFIAGEEG---GSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
11-160 8.35e-18

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 76.35  E-value: 8.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539  11 VTYLGKVsTTGMQFLSGCTEKPVIELWKKHTLAREDVfpaNALLEIRPFQVWLHHLDHKGEAtvhmdtFQVARIAYCTAD 90
Cdd:pfam14719   4 VVYLGNV-LTIHAKGEGCTDKPLGTIWKNYCQGKSGT---KMKLTVTRSGLKATTKEHGLTE------YWSHRITYCSAP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539  91 HNVsPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMKSDGRIHSNSSSEEVS 160
Cdd:pfam14719  74 PNY-PRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCARHAQNARLS 142
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 11-130 8.47e-14

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: 64.23  E-value: 8.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539  11 VTYLGKVsTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANalLEIRPFQVWLHHLDHKG-EATVHmdtfqvaRIAYCTA 89
Cdd:cd01214    10 VVYLGNV-LTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMK--LTVTPSGLKATTKQHGLtEYWLH-------RITYCSA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1054304539  90 DHNVsPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLA 130
Cdd:cd01214    80 PPNY-PRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIA 119
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 4-142 4.82e-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: 46.54  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539    4 PATERLQVTYLGKVST---TGMQFLSGCTEKpvieLWKKHTLAREDvfPANALLEIRPFQVWLHHLDHKGEATvhmdTFQ 80
Cdd:smart00462   1 GSGVSFRVKYLGSVEVpeaRGLQVVQEAIRK----LRAAQGSEKKE--PQKVILSISSRGVKLIDEDTKAVLH----EHP 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054304539   81 VARIAYCTADHNvSPNIFAWVYREINDDlsyQMDCHAVECESklEAKKLAHAMMEAFRKTFH 142
Cdd:smart00462  71 LRRISFCAVGPD-DLDVFGYIARDPGSS---RFACHVFRCEK--AAEDIALAIGQAFQLAYE 126
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 10-137 1.51e-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: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054304539  10 QVTYLGKVSTTGMqFLSGCTEKPVIELWKKhtLAREDVFPaNALLEIRPFQVWLHHLDHKGEATVHMdTFQVARIAYCTA 89
Cdd:cd13160     4 TVKYLGRMPARGL-WGIKHTRKPLVDALKN--LPKGKTLP-KTKLEVSSDGVKLEELRGGFGSSKTV-FFPIHTISYGVQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1054304539  90 DhNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAF 137
Cdd:cd13160    79 D-LVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWLAKAF 125
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
76-137 2.90e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 38.88  E-value: 2.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054304539  76 MDTFQVARIAYCTADHNVSPNIFAWVYReinDDLSYQMDCHAVECESKleAKKLAHAMMEAF 137
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 ...
 83-133 5.28e-04

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: 38.08  E-value: 5.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054304539  83 RIAYCTADHNvSPNIFAWVYREindDLSYQMDCHAVECeSKleaKKLAHAM 133
Cdd:cd13159    72 RISYCTADAN-HDKVFAFIATN---QDNEKLECHAFLC-AK---RKMAQAV 114
 
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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