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Conserved domains on  [gi|46409306|ref|NP_997217|]
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protein FAM43B [Homo sapiens]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 71-263 4.82e-89

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member pfam14719:

Pssm-ID: 473070  Cd Length: 184  Bit Score: 264.32  E-value: 4.82e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306    71 TYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGG-GTKMKLTLGPHGIRMQPCERsaaggsggrrPAHAYLLPRITYC 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH----------GLTEYWSHRITYC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306   150 TADGRHPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALARLLRQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAA 229
Cdd:pfam14719  71 SAPPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAY 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 46409306   230 SVPRAPLRRLLNAKCAYRpPPSERSRGAPRLSSI 263
Cdd:pfam14719 149 DPPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSI 181
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-263 4.82e-89

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 264.32  E-value: 4.82e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306    71 TYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGG-GTKMKLTLGPHGIRMQPCERsaaggsggrrPAHAYLLPRITYC 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH----------GLTEYWSHRITYC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306   150 TADGRHPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALARLLRQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAA 229
Cdd:pfam14719  71 SAPPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAY 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 46409306   230 SVPRAPLRRLLNAKCAYRpPPSERSRGAPRLSSI 263
Cdd:pfam14719 149 DPPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSI 181
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 65-197 1.31e-64

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: 199.82  E-value: 1.31e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306  65 LNKEDPTYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGG--GTKMKLTLGPHGIRMqpCERSAaggsggrrPAHAYL 142
Cdd:cd01214   1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKkpDVKMKLTVTPSGLKA--TTKQH--------GLTEYW 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46409306 143 LPRITYCTADGRHPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALARLLRQT 197
Cdd:cd01214  71 LHRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 68-212 1.25e-12

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: 64.26  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306     68 EDPTYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGGG--TKMKLTLGPHGIRMQPCERSAaggsggrrPAHAYLLPR 145
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepQKVILSISSRGVKLIDEDTKA--------VLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46409306    146 ITYCTADGRHPRVFAWVYRHQARHKavvLRCHAVLLARAHKARAlarllrQTALAAFSD-FKRLQRQS 212
Cdd:smart00462  74 ISFCAVGPDDLDVFGYIARDPGSSR---FACHVFRCEKAAEDIA------LAIGQAFQLaYELKLKAR 132
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
71-263 4.82e-89

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 264.32  E-value: 4.82e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306    71 TYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGG-GTKMKLTLGPHGIRMQPCERsaaggsggrrPAHAYLLPRITYC 149
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKsGTKMKLTVTRSGLKATTKEH----------GLTEYWSHRITYC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306   150 TADGRHPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALARLLRQTALAAFSDFKRLQRQsdARHVRQQHLRAGGAAA 229
Cdd:pfam14719  71 SAPPNYPRVFCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLC--ARHAQNARLSLGNAAY 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 46409306   230 SVPRAPLRRLLNAKCAYRpPPSERSRGAPRLSSI 263
Cdd:pfam14719 149 DPPSVPRRKLLTGTCNYR-PPVERSKSAPKLGSI 181
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 65-197 1.31e-64

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: 199.82  E-value: 1.31e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306  65 LNKEDPTYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGG--GTKMKLTLGPHGIRMqpCERSAaggsggrrPAHAYL 142
Cdd:cd01214   1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKkpDVKMKLTVTPSGLKA--TTKQH--------GLTEYW 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46409306 143 LPRITYCTADGRHPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALARLLRQT 197
Cdd:cd01214  71 LHRITYCSAPPNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 70-196 9.66e-15

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: 69.46  E-value: 9.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306  70 PTYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGGG--TKMKLTLGPHGIRMqpCERSaaggsgGRRPAHAYLLPRIT 147
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRkpGPVLLEVSSKGVKL--LDLD------TKELLLRHPLHRIS 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46409306 148 YCTADGRHPRVFAWVYRHQARHKavvLRCHAVLLARAHKARALARLLRQ 196
Cdd:cd00934  73 YCGRDPDNPNVFAFIAGEEGGSG---FRCHVFQCEDEEEAEEILQAIGQ 118
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 71-191 5.49e-14

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: 67.74  E-value: 5.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306  71 TYTVWYLGNAVTLHAKGDGCTDDAVGKI--WARCGPGGGTKMKLTLGPHGIRMqpcERSAAGGSGGRRPAHayllpRITY 148
Cdd:cd13159   4 TFYLKYLGSTLVEKPKGEGATAEAVKTIiaMAKASGKKLQKVTLTVSPKGIKV---TDSATNETILEVSIY-----RISY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 46409306 149 CTADGRHPRVFAWVYRHQARHKavvLRCHAVLLARAHKARALA 191
Cdd:cd13159  76 CTADANHDKVFAFIATNQDNEK---LECHAFLCAKRKMAQAVT 115
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 68-212 1.25e-12

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: 64.26  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306     68 EDPTYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGGG--TKMKLTLGPHGIRMQPCERSAaggsggrrPAHAYLLPR 145
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKepQKVILSISSRGVKLIDEDTKA--------VLHEHPLRR 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46409306    146 ITYCTADGRHPRVFAWVYRHQARHKavvLRCHAVLLARAHKARAlarllrQTALAAFSD-FKRLQRQS 212
Cdd:smart00462  74 ISFCAVGPDDLDVFGYIARDPGSSR---FACHVFRCEKAAEDIA------LAIGQAFQLaYELKLKAR 132
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 72-191 6.79e-08

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: 50.76  E-value: 6.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306  72 YTVWYLGNAVTLHAK-GDGCTDDAVGKIWARCGPGGGT----KMKLTLGPHGIRMQPCERSaaggsgGRRPAH--AYLLP 144
Cdd:cd13167   3 YKVTYLGKVSTTGTQfLSGCTESPVIELWKKHTLAREDifpsNALLEIRPFQVRLHHLDLR------GEATVHmdTFQVA 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46409306 145 RITYCTADGR-HPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALA 191
Cdd:cd13167  77 RIAYCTADHNiSPNIFAWVYREINDDLSFQMDCHAVECESKLEAKKLA 124
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 70-202 2.08e-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: 46.17  E-value: 2.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46409306  70 PTYTVWYLGNAVTLHAKGDGCTDDAVGKIWARCGPGGGT-KMKLTLGPHGIRMQPcersaAGGSGGRRPAHAYLLPRITY 148
Cdd:cd13160   1 PVFTVKYLGRMPARGLWGIKHTRKPLVDALKNLPKGKTLpKTKLEVSSDGVKLEE-----LRGGFGSSKTVFFPIHTISY 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46409306 149 CTADGRHPRVFAWVYRHQARHKAVVLRCHAVLLARAHKARALARLLrqtaLAAF 202
Cdd:cd13160  76 GVQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNLTYWL----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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