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Conserved domains on  [gi|1370452769|ref|XP_024302083|]
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low density lipoprotein receptor adapter protein 1 isoform X10 [Homo sapiens]

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 ...
 1-121 1.66e-80

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: 238.00  E-value: 1.66e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   1 MLFSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMH 80
Cdd:cd13159     3 VTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANH 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370452769  81 DKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFK 121
Cdd:cd13159    83 DKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 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 ...
 1-121 1.66e-80

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: 238.00  E-value: 1.66e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   1 MLFSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMH 80
Cdd:cd13159     3 VTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANH 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370452769  81 DKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFK 121
Cdd:cd13159    83 DKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 3-133 3.03e-38

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: 130.51  E-value: 3.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769    3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDK 82
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLD 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370452769   83 VFAYIAQSQHNQSLECHAFLCTKRkmAQAVTLTVAQAFKVAFEFWQVSKEE 133
Cdd:smart00462  86 VFGYIARDPGSSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKLKARSE 134
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
3-143 1.46e-16

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 75.19  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLqKVTLKVSPRGIILTdnlTNQ--LIENVSiYRISYCTADKMH 80
Cdd:pfam14719   2 YKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGT-KMKLTVTRSGLKAT---TKEhgLTEYWS-HRITYCSAPPNY 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452769  81 DKVFAYIAQSQ---HNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAF-EFwqvsKEEKEKRDKASQE 143
Cdd:pfam14719  77 PRVFCWVYRHEgrkLKVELRCHAVLCKKEEKARAMALLLYQTLRAALqEF----KREKLCARHAQNA 139
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 1-121 1.66e-80

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: 238.00  E-value: 1.66e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   1 MLFSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMH 80
Cdd:cd13159     3 VTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADANH 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370452769  81 DKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFK 121
Cdd:cd13159    83 DKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 3-133 3.03e-38

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: 130.51  E-value: 3.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769    3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDK 82
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLD 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370452769   83 VFAYIAQSQHNQSLECHAFLCTKRkmAQAVTLTVAQAFKVAFEFWQVSKEE 133
Cdd:smart00462  86 VFGYIARDPGSSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 3-120 8.16e-37

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: 126.47  E-value: 8.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDK 82
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPN 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1370452769  83 VFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAF 120
Cdd:cd00934    83 VFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 3-124 2.53e-26

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: 100.05  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIVAT---AKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKM 79
Cdd:cd01273    14 YLVKFLGCTEVEQPKGTEVVKEAIRKLKFArqlKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKT 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370452769  80 HDKVFAYIAQSQHNQSLECHAFLCTkrKMAQAVTLTVAQAFKVAF 124
Cdd:cd01273    94 DKRIFSFIAKDSESEKHLCFVFDSE--KLAEEITLTIGQAFDLAY 136
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 2-125 3.42e-25

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: 96.16  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   2 LFSLKYLGMTLVEQPKGEELSAAAIKRIvataKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHD 81
Cdd:cd13161     3 VFEAKYLGSVPVKEPKGNDVVMAAVKRL----KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370452769  82 KVFAYIAQSQHNQSLECHAFLCTKRkmAQAVTLTVAQAFKVAFE 125
Cdd:cd13161    79 KLFAFISHDPRLGRITCHVFRCKRG--AQEICDTIAEAFKAAAE 120
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 3-120 1.58e-18

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: 78.92  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGmtlVEQPKGEELSAAAIKRIVATAK--ASGKKLQKVTLKVSPRGIILTDnLTNQLIENVS----IYRISYCTA 76
Cdd:cd13160     3 FTVKYLG---RMPARGLWGIKHTRKPLVDALKnlPKGKTLPKTKLEVSSDGVKLEE-LRGGFGSSKTvffpIHTISYGVQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370452769  77 DKMHDKVFAYI---AQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAF 120
Cdd:cd13160    79 DLVHTRVFSMIvvgEQDSSNHPFECHAFVCDSRADARNLTYWLAKAF 125
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 3-125 4.41e-17

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: 75.42  E-value: 4.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIvataKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDK 82
Cdd:cd01268    17 FPVKYLGCVEVGESRGMQVCEEALKKL----KASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHER 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370452769  83 VFAYIAQSQHNQSLECHAFLCTK---RKMAQAvtltVAQAFKVAFE 125
Cdd:cd01268    93 AFSYICRDGTTRRWMCHCFLAVKdsgERLSHA----VGCAFAACLE 134
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
3-143 1.46e-16

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 75.19  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLqKVTLKVSPRGIILTdnlTNQ--LIENVSiYRISYCTADKMH 80
Cdd:pfam14719   2 YKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGT-KMKLTVTRSGLKAT---TKEhgLTEYWS-HRITYCSAPPNY 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452769  81 DKVFAYIAQSQ---HNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAF-EFwqvsKEEKEKRDKASQE 143
Cdd:pfam14719  77 PRVFCWVYRHEgrkLKVELRCHAVLCKKEEKARAMALLLYQTLRAALqEF----KREKLCARHAQNA 139
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 7-125 2.13e-16

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: 73.85  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   7 YLGMTLVEQPKGEELSAAAIKRIVaTAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDKVFAY 86
Cdd:cd01274    21 YLGSTEIKELRGTESTKKAIQKLK-KSTREMKKIPTIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAY 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370452769  87 IAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAFE 125
Cdd:cd01274   100 ITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQ 138
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
3-123 8.36e-15

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 69.31  E-value: 8.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAA------AIKRIVATAKASGKKL-------QKVTLKVSPRGIILTDNLTNQLIENVSIY 69
Cdd:pfam00640   1 FAVRYLGSVEVPEERAPDKNTRmqqareAIRRVKAAKINKIRGLsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370452769  70 RISYCT-ADKMHDKVFAYIAQSQHNQSLECHAFLCtkRKMAQAVTLTVAQAFKVA 123
Cdd:pfam00640  81 SISFCAdGDPDLMRYFAYIARDKATNKFACHVFES--EDGAQDIAQSIGQAFALA 133
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 7-118 2.46e-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: 67.70  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   7 YLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTdnlTNQ--LIENVSiYRISYCTADKMHDKVF 84
Cdd:cd01214    12 YLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKAT---TKQhgLTEYWL-HRITYCSAPPNYPRVF 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370452769  85 AYIAQSQ---HNQSLECHAFLCTKRKMAQAVTLTVAQ 118
Cdd:cd01214    88 CWIYRHEgrkLKVELRCHAVLCSKESKARAIALLLYQ 124
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 3-136 4.45e-13

Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. 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: 269926  Cd Length: 147  Bit Score: 64.97  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDK 82
Cdd:cd01215    18 FKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNR 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370452769  83 VFAYIAQSQHNqslecHAFLCTKR-KMAQAVTLTVAQAFKVAFEFWQVSKEEKEK 136
Cdd:cd01215    98 AFGYVCGLDGG-----HRFFAIKTaKAAEPVVLDLRDLFQVVFELKKKEIEEKKA 147
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 3-122 6.61e-12

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: 62.30  E-value: 6.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   3 FSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILT-------DNLTN----QLIENVSIYRI 71
Cdd:cd01270    31 FQAKYIGSLEVPRPSSRVEIVAAMRRIRYEFKAKNIKKKKVTITVSVDGVKVVlrkkkkkKGWTWdeskLLLMQHPIYRI 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370452769  72 SYCTADkMHD-KVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFKV 122
Cdd:cd01270   111 FYVSHD-SQDlKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEV 161
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 2-121 5.35e-09

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC 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: 269922  Cd Length: 129  Bit Score: 53.02  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   2 LFS-LKYLGMTLVEQPKGEelsaAAIKRIVATAKASGKKLQKVTLKV--SPRG-IILTDNLTNQLIENVSIYRISYC--- 74
Cdd:cd01211     2 IFNgVTYLGCAKVNAPRSE----TEALRIMAILREQSAQPIKVTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILFCarg 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370452769  75 ---TADKmhdKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFK 121
Cdd:cd01211    78 pdgTSES---DCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFR 124
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 6-124 1.97e-08

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: 51.62  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   6 KYLGMTLVEQPKGEElSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHdKVFA 85
Cdd:cd13157     7 QYIGSFPVSGLDVAD-RADSVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH-AQFA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370452769  86 YIAQS--QHNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAF 124
Cdd:cd13157    85 FVARNpgGPTNRQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 41-103 7.68e-07

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 47.34  E-value: 7.68e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452769  41 QKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTAD---KMHDKVFAYIAQSQHNQSLECHAFLC 103
Cdd:pfam08416  40 QEMLLQVSDQGITLTDNETKEELESYPLDSISHCQAVlndGRYNSILALVCQEPGQSKPDVHLFQC 105
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 25-125 2.70e-06

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an 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. This cd is part of the Shc-like subgroup.


Pssm-ID: 269920  Cd Length: 170  Bit Score: 46.43  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769  25 AIKRI--------VATAKASGKKLQK-------------VTLKVSPRGIILTDNLTNQLIENVSIYRISYCTA-DKMHDK 82
Cdd:cd01209    46 AINRVceavggakGAKRKRKSKALSSilgksnlqfagmnISLTISTDGLNLVTPDTGQIIANHHMQSISFASGgDPDTYD 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370452769  83 VFAYIAQSQHNQSlECHAFLCTKRkMAQAVTLTVAQAFKVAFE 125
Cdd:cd01209   126 YVAYVAKDPVNQR-ACHVLECGDG-LAQDVIATIGQAFELRFK 166
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 7-103 5.06e-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: 39.12  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452769   7 YLGMTLVEQPKGEELSAAAIKRIVATAKASgkKLQKVTLKVSPRGI-ILTDNLTNQLIENVSIYRISYCTADKmHDKVFA 85
Cdd:cd01271    13 YLGSTPVSKPTGMDVLNEAIDTLLSSVPKE--QWTPVNVSVAPSTVtILSQKDEEEVLVECRVRFLSFMGIGK-DVHTFA 89

                          90
                  ....*....|....*...
gi 1370452769  86 YIAQsQHNQSLECHAFLC 103
Cdd:cd01271    90 FIMD-TGPQLFQCHVFWC 106
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 63-125 2.07e-03

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: 37.66  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370452769  63 IENVSIYRISYCTADkmHD---KVFAYIAQSQHNQ---SLECHAFLCTKRKMAQAVTLTVAQAFKVAFE 125
Cdd:cd13167    70 MDTFQVARIAYCTAD--HNispNIFAWVYREINDDlsfQMDCHAVECESKLEAKKLAHAMMEAFKKTFH 136
 
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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