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Conserved domains on  [gi|241896900|ref|NP_001155918|]
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low density lipoprotein receptor adapter protein 1-like [Acyrthosiphon pisum]

Protein Classification

low density lipoprotein receptor adapter protein 1 family protein( domain architecture ID 10192159)

low density lipoprotein receptor adapter protein 1 family protein similar to human low density lipoprotein receptor adapter protein 1 (LDLRAP1) which is an adaptor protein needed for efficient endocytosis of low density lipoprotein receptor (LDLR); contains a Phosphotyrosine-binding (PTB) domain/Phosphotyrosine-interaction (PI) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 41-161 1.14e-55

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: 174.44  E-value: 1.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  41 DQTTFEVKYLGNTPVD--STAGAIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIETSDEkKTVLETPIERVSHCFTD 118
Cdd:cd13159    1 DGVTFYLKYLGSTLVEkpKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATN-ETILEVSIYRISYCTAD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 241896900 119 SAHSNVFAFVTASGLT-MSECHAFMCAKRKMAQNMSVTIGQSIS 161
Cdd:cd13159   80 ANHDKVFAFIATNQDNeKLECHAFLCAKRKMAQAVTLTVAQAFN 123
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 41-161 1.14e-55

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: 174.44  E-value: 1.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  41 DQTTFEVKYLGNTPVD--STAGAIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIETSDEkKTVLETPIERVSHCFTD 118
Cdd:cd13159    1 DGVTFYLKYLGSTLVEkpKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATN-ETILEVSIYRISYCTAD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 241896900 119 SAHSNVFAFVTASGLT-MSECHAFMCAKRKMAQNMSVTIGQSIS 161
Cdd:cd13159   80 ANHDKVFAFIATNQDNeKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 44-161 3.02e-18

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: 78.51  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900    44 TFEVKYLGNTPVDSTAG--AIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIetSDEKKTVLET-PIERVSHCFTDSA 120
Cdd:smart00462   5 SFRVKYLGSVEVPEARGlqVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLI--DEDTKAVLHEhPLRRISFCAVGPD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 241896900   121 HSNVFAFVTASGLT-MSECHAFMCAKRKMAQnmSVTIGQSIS 161
Cdd:smart00462  83 DLDVFGYIARDPGSsRFACHVFRCEKAAEDI--ALAIGQAFQ 122
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
45-158 8.25e-09

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 52.75  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900   45 FEVKYLGNTPVD-------STAGAIV-EAVKTILVMAKASKR-------KPQNVTVTLNGQGIKVIeTSDEKKTVLETPI 109
Cdd:pfam00640   1 FAVRYLGSVEVPeerapdkNTRMQQArEAIRRVKAAKINKIRglsgetgPGTKVDLFISTDGLKLL-NPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 241896900  110 ERVSHC-FTDSAHSNVFAFVTASGLT-MSECHAFMCAKRkmAQNMSVTIGQ 158
Cdd:pfam00640  80 VSISFCaDGDPDLMRYFAYIARDKATnKFACHVFESEDG--AQDIAQSIGQ 128
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 41-161 1.14e-55

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: 174.44  E-value: 1.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  41 DQTTFEVKYLGNTPVD--STAGAIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIETSDEkKTVLETPIERVSHCFTD 118
Cdd:cd13159    1 DGVTFYLKYLGSTLVEkpKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATN-ETILEVSIYRISYCTAD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 241896900 119 SAHSNVFAFVTASGLT-MSECHAFMCAKRKMAQNMSVTIGQSIS 161
Cdd:cd13159   80 ANHDKVFAFIATNQDNeKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 44-159 1.29e-24

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: 94.88  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  44 TFEVKYLGNTPVDSTAG--AIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIETsDEKKTVLETPIERVSHCFTDSAH 121
Cdd:cd00934    2 SFQVKYLGSVEVGSSRGvdVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDL-DTKELLLRHPLHRISYCGRDPDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 241896900 122 SNVFAFVT-ASGLTMSECHAFMCAKRKMAQNMSVTIGQS 159
Cdd:cd00934   81 PNVFAFIAgEEGGSGFRCHVFQCEDEEEAEEILQAIGQA 119
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 44-161 3.02e-18

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: 78.51  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900    44 TFEVKYLGNTPVDSTAG--AIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIetSDEKKTVLET-PIERVSHCFTDSA 120
Cdd:smart00462   5 SFRVKYLGSVEVPEARGlqVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLI--DEDTKAVLHEhPLRRISFCAVGPD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 241896900   121 HSNVFAFVTASGLT-MSECHAFMCAKRKMAQnmSVTIGQSIS 161
Cdd:smart00462  83 DLDVFGYIARDPGSsRFACHVFRCEKAAEDI--ALAIGQAFQ 122
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 44-158 8.41e-16

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: 71.51  E-value: 8.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  44 TFEVKYLGNTPVDSTAGAivEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIETsDEKKTVLETPIERVSHCFTDSAHSN 123
Cdd:cd13161    3 VFEAKYLGSVPVKEPKGN--DVVMAAVKRLKDLKLKPKPVVLVVSSEGIRVVER-LTGEVLTNVPIKDISFVTVDPKDKK 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 241896900 124 VFAFVT-ASGLTMSECHAFMCAKRkmAQNMSVTIGQ 158
Cdd:cd13161   80 LFAFIShDPRLGRITCHVFRCKRG--AQEICDTIAE 113
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 44-152 4.37e-13

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: 64.28  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  44 TFEVKYLGNTPVDSTAG--AIVEAVKTILVMAKASKrKPQNVTVTLNGQGIKVIETSD---EKKTVLeTPIERVSHCFTD 118
Cdd:cd13160    2 VFTVKYLGRMPARGLWGikHTRKPLVDALKNLPKGK-TLPKTKLEVSSDGVKLEELRGgfgSSKTVF-FPIHTISYGVQD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 241896900 119 SAHSNVFAFVTAsGLTMS-----ECHAFMCAKRKMAQNM 152
Cdd:cd13160   80 LVHTRVFSMIVV-GEQDSsnhpfECHAFVCDSRADARNL 117
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 36-145 5.19e-12

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF 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 is part of the Dab-like subgroup.


Pssm-ID: 241298  Cd Length: 135  Bit Score: 61.55  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  36 IAVEDDQTTFEVKYLGNTPVDSTAGAIV--EAVKTIlvmaKASKRKPQNVTVTLNGQGIKVIETSDeKKTVLETPIERVS 113
Cdd:cd01268    8 EAVRSGTCSFPVKYLGCVEVGESRGMQVceEALKKL----KASRKKPVRAVLWVSGDGLRVVDEKT-KGLIVDQTIEKVS 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 241896900 114 HCFTDSAHSNVFAFVTASGLTMS-ECHAFMCAK 145
Cdd:cd01268   83 FCAPDRNHERAFSYICRDGTTRRwMCHCFLAVK 115
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 45-159 4.91e-10

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: 56.52  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  45 FEVKYLGNTPVDSTAGAIV--EAVKTI---LVMAKASKRKPQNVTVTLNGQGIKVIEtSDEKKTVLETPIERVSHCFTDS 119
Cdd:cd01273   14 YLVKFLGCTEVEQPKGTEVvkEAIRKLkfaRQLKKSEGAKLPKVELQISIDGVKIQD-PKTKVIMHQFPLHRISFCADDK 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 241896900 120 AHSNVFAFV-TASGLTMSECHAFMCakRKMAQNMSVTIGQS 159
Cdd:cd01273   93 TDKRIFSFIaKDSESEKHLCFVFDS--EKLAEEITLTIGQA 131
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
45-158 8.25e-09

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 52.75  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900   45 FEVKYLGNTPVD-------STAGAIV-EAVKTILVMAKASKR-------KPQNVTVTLNGQGIKVIeTSDEKKTVLETPI 109
Cdd:pfam00640   1 FAVRYLGSVEVPeerapdkNTRMQQArEAIRRVKAAKINKIRglsgetgPGTKVDLFISTDGLKLL-NPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 241896900  110 ERVSHC-FTDSAHSNVFAFVTASGLT-MSECHAFMCAKRkmAQNMSVTIGQ 158
Cdd:pfam00640  80 VSISFCaDGDPDLMRYFAYIARDKATnKFACHVFESEDG--AQDIAQSIGQ 128
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
44-162 3.40e-07

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 49.00  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900   44 TFEVKYLGN--TPVDSTAGAIVEAVKTILVMAKASKRK-PQNVTVTlnGQGIKViETSDEKKTvlETPIERVSHCFTDSA 120
Cdd:pfam14719   1 TYKVVYLGNvlTIHAKGEGCTDKPLGTIWKNYCQGKSGtKMKLTVT--RSGLKA-TTKEHGLT--EYWSHRITYCSAPPN 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 241896900  121 HSNVFAFVTASGL----TMSECHAFMCAKRKMAQNMSVTIGQSISS 162
Cdd:pfam14719  76 YPRVFCWVYRHEGrklkVELRCHAVLCKKEEKARAMALLLYQTLRA 121
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 47-159 3.65e-07

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 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: 269979  Cd Length: 129  Bit Score: 48.15  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  47 VKYLGNTPVDSTAGAI-VEAVKTILVMAKASKRKPQNVTVTLNGQGIKVIetSDEKKTVLET-PIERVSHCFTDSAHSNv 124
Cdd:cd13157    6 AQYIGSFPVSGLDVADrADSVRKQLESLKESGSRGRPVILSVSLSGIKIC--SEDGKVVLMAhALRRVSYSTCRPAHAQ- 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 241896900 125 FAFVT--ASGLTMSE-CHAFMCAKRKMAQNMSVTIGQS 159
Cdd:cd13157   83 FAFVArnPGGPTNRQyCHVFVTRSPREAQELNLLLCRA 120
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 36-159 4.36e-07

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: 47.67  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  36 IAVEDDqtTFEVKYLGN--TPVDSTAGAIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKViETSDEKKTvlETPIERVS 113
Cdd:cd01214    1 ITEEDP--TYTVVYLGNvlTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKA-TTKQHGLT--EYWLHRIT 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 241896900 114 HCFTDSAHSNVFAFV----TASGLTMSECHAFMCAKRKMAQNMSVTIGQS 159
Cdd:cd01214   76 YCSAPPNYPRVFCWIyrheGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 44-158 9.70e-06

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have 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 is part of the Dab-like subgroup.


Pssm-ID: 269968  Cd Length: 179  Bit Score: 44.97  E-value: 9.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  44 TFEVKYLG--NTPVDSTAGAIVEAVKTILVMAKASKRKPQNVTVTLNGQGIKVI----------ETSDEKKTVLETPIER 111
Cdd:cd01270   30 TFQAKYIGslEVPRPSSRVEIVAAMRRIRYEFKAKNIKKKKVTITVSVDGVKVVlrkkkkkkgwTWDESKLLLMQHPIYR 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 241896900 112 ---VSHcftDSAHSNVFAFVTASGLT-MSECHAFMCAKRKMAQNMSVTIGQ 158
Cdd:cd01270  110 ifyVSH---DSQDLKIFSYIARDGSSnVFKCNVFKSKKKSQAMRIVRTIGQ 157
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 44-158 9.96e-06

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. 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: 269972  Cd Length: 146  Bit Score: 44.19  E-value: 9.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  44 TFEVKYLGNTPVDSTAGaiVEAVKTILVMAKASKRKPQNV-TVTLN--GQGIKVIETsDEKKTVLETPIERVSHCFTDSA 120
Cdd:cd01274   16 NYEAHYLGSTEIKELRG--TESTKKAIQKLKKSTREMKKIpTIILSisYKGVKFIDA-TTKNLICEHEIRNISCACQDPE 92

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 241896900 121 HSNVFAFVTASGLTMSE-CHAFMCAKRKMAQNMSVTIGQ 158
Cdd:cd01274   93 DLNTFAYITKDLKTDHHyCHVFCVLTVDLATEIILTLGQ 131
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 44-143 3.46e-04

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: 39.51  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241896900  44 TFEVKYLGNTPVDSTAGAIV--EAVKTilVMAKASKRKPQNVTVTLNGQGIKVIETSDEKKTVLETPIERVSHC--FTDS 119
Cdd:cd01271    8 KLKALYLGSTPVSKPTGMDVlnEAIDT--LLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMgiGKDV 85

                         90       100
                 ....*....|....*....|....
gi 241896900 120 AHsnvFAFVTASGLTMSECHAFMC 143
Cdd:cd01271   86 HT---FAFIMDTGPQLFQCHVFWC 106
 
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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