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Conserved domains on  [gi|126157459|ref|NP_001075141|]
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protein FAM43B [Mus musculus]

Protein Classification

FAM43A/B family PTB domain-containing protein( domain architecture ID 10631605)

FAM43A/B family (phosphotyrosine-binding) domain-containing protein similar to mammalian proteins FAM43A and FAM43B

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
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-263 7.83e-91

Phosphotyrosine interaction domain (PTB/PID);


:

Pssm-ID: 405418  Cd Length: 184  Bit Score: 268.95  E-value: 7.83e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459   71 TYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG-GTKMKLTLGPHGIRMQPSERssgasggrrPAHAYLLPRITYCA 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH---------GLTEYWSHRITYCS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  150 ADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAAS 229
Cdd:pfam14719  72 APPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAYD 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 126157459  230 VPRAPLRRLLNAKCAYRpPPGERGRGAPRLSSIQ 263
Cdd:pfam14719 150 PPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSIT 182
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-263 7.83e-91

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 268.95  E-value: 7.83e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459   71 TYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG-GTKMKLTLGPHGIRMQPSERssgasggrrPAHAYLLPRITYCA 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH---------GLTEYWSHRITYCS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  150 ADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAAS 229
Cdd:pfam14719  72 APPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAYD 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 126157459  230 VPRAPLRRLLNAKCAYRpPPGERGRGAPRLSSIQ 263
Cdd:pfam14719 150 PPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSIT 182
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 65-196 9.20e-63

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: 195.20  E-value: 9.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  65 LNKEDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG--GTKMKLTLGPHGIRMQPSERssgasggrrPAHAYLL 142
Cdd:cd01214    1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKkpDVKMKLTVTPSGLKATTKQH---------GLTEYWL 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 126157459 143 PRITYCAADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQT 196
Cdd:cd01214   72 HRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 68-211 7.44e-13

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: 64.64  E-value: 7.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459    68 EDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGG--TKMKLTLGPHGIRMQPSERssgasggRRPAHAYLLPRI 145
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepQKVILSISSRGVKLIDEDT-------KAVLHEHPLRRI 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126157459   146 TYCAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKArslarlLHQTALAAFSD-FKRLQRQS 211
Cdd:smart00462  75 SFCAVGPDDLDVFGYIARDPGSSR---FACHVFRCEKAAED------IALAIGQAFQLaYELKLKAR 132
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-263 7.83e-91

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 268.95  E-value: 7.83e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459   71 TYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG-GTKMKLTLGPHGIRMQPSERssgasggrrPAHAYLLPRITYCA 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH---------GLTEYWSHRITYCS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  150 ADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAAS 229
Cdd:pfam14719  72 APPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAYD 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 126157459  230 VPRAPLRRLLNAKCAYRpPPGERGRGAPRLSSIQ 263
Cdd:pfam14719 150 PPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSIT 182
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 65-196 9.20e-63

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: 195.20  E-value: 9.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  65 LNKEDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGG--GTKMKLTLGPHGIRMQPSERssgasggrrPAHAYLL 142
Cdd:cd01214    1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKkpDVKMKLTVTPSGLKATTKQH---------GLTEYWL 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 126157459 143 PRITYCAADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLHQT 196
Cdd:cd01214   72 HRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 70-195 3.30e-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: 68.30  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  70 PTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGG--TKMKLTLGPHGIRMQPSERssgasggRRPAHAYLLPRITY 147
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRkpGPVLLEVSSKGVKLLDLDT-------KELLLRHPLHRISY 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 126157459 148 CAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKARSLARLLHQ 195
Cdd:cd00934   74 CGRDPDNPNVFAFIAGEEGGSG---FRCHVFQCEDEEEAEEILQAIGQ 118
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 68-211 7.44e-13

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: 64.64  E-value: 7.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459    68 EDPTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGG--TKMKLTLGPHGIRMQPSERssgasggRRPAHAYLLPRI 145
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepQKVILSISSRGVKLIDEDT-------KAVLHEHPLRRI 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126157459   146 TYCAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKArslarlLHQTALAAFSD-FKRLQRQS 211
Cdd:smart00462  75 SFCAVGPDDLDVFGYIARDPGSSR---FACHVFRCEKAAED------IALAIGQAFQLaYELKLKAR 132
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 71-190 4.33e-12

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: 62.35  E-value: 4.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  71 TYTVWYLGNAVTLHAKGDGCTDDAVGRI--WARCGPGGGTKMKLTLGPHGIRMQPSERSSgasggrrpahaYLLP----R 144
Cdd:cd13159    4 TFYLKYLGSTLVEKPKGEGATAEAVKTIiaMAKASGKKLQKVTLTVSPKGIKVTDSATNE-----------TILEvsiyR 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 126157459 145 ITYCAADGRHPRVFTWVYRHQARHKavvLRCHAVLLARAHKARSLA 190
Cdd:cd13159   73 ISYCTADANHDKVFAFIATNQDNEK---LECHAFLCAKRKMAQAVT 115
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 72-190 8.80e-07

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: 47.68  E-value: 8.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  72 YTVWYLGNAVTLHAK-GDGCTDDAVGRIWARCGPGGGT----KMKLTLGPHGIRMQPSERSSGASggrRPAHAYLLPRIT 146
Cdd:cd13167    3 YKVTYLGKVSTTGTQfLSGCTESPVIELWKKHTLAREDifpsNALLEIRPFQVRLHHLDLRGEAT---VHMDTFQVARIA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 126157459 147 YCAADGR-HPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLA 190
Cdd:cd13167   80 YCTADHNiSPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLA 124
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 70-201 4.72e-06

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: 45.40  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126157459  70 PTYTVWYLGNAVTLHAKGDGCTDDAVGRIWARCGPGGGT-KMKLTLGPHGIRMQPserssgASGGRRPAHAYLLP--RIT 146
Cdd:cd13160    1 PVFTVKYLGRMPARGLWGIKHTRKPLVDALKNLPKGKTLpKTKLEVSSDGVKLEE------LRGGFGSSKTVFFPihTIS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 126157459 147 YCAADGRHPRVFTWVYRHQARHKAVVLRCHAVLLARAHKARSLARLLhqtaLAAF 201
Cdd:cd13160   75 YGVQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWL----AKAF 125
 
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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