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Conserved domains on  [gi|77024624|gb|ABA61315|]
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autosomal recessive hypercholesterolemia-like protein [Doryteuthis pealeii]

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 ...
 38-165 1.69e-71

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: 216.43  E-value: 1.69e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  38 EGMTFYLKYLGSTLVEEISdgesyGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRISF 117
Cdd:cd13159   1 DGVTFYLKYLGSTLVEKPK-----GEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 77024624 118 CTADRNHERVFAFIARNTINETMECYVYVCAKRKIAQAVTLTASQAFH 165
Cdd:cd13159  76 CTADANHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 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 ...
 38-165 1.69e-71

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: 216.43  E-value: 1.69e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  38 EGMTFYLKYLGSTLVEEISdgesyGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRISF 117
Cdd:cd13159   1 DGVTFYLKYLGSTLVEKPK-----GEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 77024624 118 CTADRNHERVFAFIARNTINETMECYVYVCAKRKIAQAVTLTASQAFH 165
Cdd:cd13159  76 CTADANHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-164 3.68e-25

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: 97.77  E-value: 3.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624     37 NEGMTFYLKYLGSTLVEEisdgeSYGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRIS 116
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPE-----ARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRIS 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 77024624    117 FCTADRNHERVFAFIARNTINETMECYVYVCAKRkiAQAVTLTASQAF 164
Cdd:smart00462  76 FCAVGPDDLDVFGYIARDPGSSRFACHVFRCEKA--AEDIALAIGQAF 121
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
42-167 3.86e-13

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 65.08  E-value: 3.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624    42 FYLKYLGST-LVEEISDGESYGDGISTKAIQRViSMEKSSGKKWR--------KVALNVSPRGIKMCDMISNEMLLDVCI 112
Cdd:pfam00640   1 FAVRYLGSVeVPEERAPDKNTRMQQAREAIRRV-KAAKINKIRGLsgetgpgtKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 77024624   113 YRISFCT-ADRNHERVFAFIARNTINETMECYVYVCAKRkiAQAVTLTASQAFHIA 167
Cdd:pfam00640  80 VSISFCAdGDPDLMRYFAYIARDKATNKFACHVFESEDG--AQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 38-165 1.69e-71

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: 216.43  E-value: 1.69e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  38 EGMTFYLKYLGSTLVEEISdgesyGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRISF 117
Cdd:cd13159   1 DGVTFYLKYLGSTLVEKPK-----GEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 77024624 118 CTADRNHERVFAFIARNTINETMECYVYVCAKRKIAQAVTLTASQAFH 165
Cdd:cd13159  76 CTADANHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 40-164 6.39e-30

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: 109.52  E-value: 6.39e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  40 MTFYLKYLGSTLVeeisdGESYGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRISFCT 119
Cdd:cd00934   1 ASFQVKYLGSVEV-----GSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 77024624 120 ADRNHERVFAFIARNTINETMECYVYVCAKRKIAQAVTLTASQAF 164
Cdd:cd00934  76 RDPDNPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 37-164 3.68e-25

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: 97.77  E-value: 3.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624     37 NEGMTFYLKYLGSTLVEEisdgeSYGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRIS 116
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPE-----ARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRIS 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 77024624    117 FCTADRNHERVFAFIARNTINETMECYVYVCAKRkiAQAVTLTASQAF 164
Cdd:smart00462  76 FCAVGPDDLDVFGYIARDPGSSRFACHVFRCEKA--AEDIALAIGQAF 121
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 34-167 6.79e-20

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: 83.87  E-value: 6.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  34 ETLNEGMTFYL-KYLGSTLVEEISDGESYGDGISTKAIQRviSMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCI 112
Cdd:cd01273   5 EALIKGHVAYLvKFLGCTEVEQPKGTEVVKEAIRKLKFAR--QLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPL 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 77024624 113 YRISFCTADRNHERVFAFIARNTINETMECYVYVCakRKIAQAVTLTASQAFHIA 167
Cdd:cd01273  83 HRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDS--EKLAEEITLTIGQAFDLA 135
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 41-167 7.92e-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: 72.28  E-value: 7.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  41 TFYLKYLGSTLVEEISdgesyGDGISTKAIQRVismeKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRISFCTA 120
Cdd:cd13161   3 VFEAKYLGSVPVKEPK-----GNDVVMAAVKRL----KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTV 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 77024624 121 DRNHERVFAFIARNTINETMECYVYVCAKRkiAQAVTLTASQAFHIA 167
Cdd:cd13161  74 DPKDKKLFAFISHDPRLGRITCHVFRCKRG--AQEICDTIAEAFKAA 118
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 46-167 2.46e-14

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: 68.85  E-value: 2.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  46 YLGSTLVEEISDGESygdgiSTKAIQRVismeKSSGKKWRK---VALNVSPRGIKMCDMISNEMLLDVCIYRISFCTADR 122
Cdd:cd01274  21 YLGSTEIKELRGTES-----TKKAIQKL----KKSTREMKKiptIILSISYKGVKFIDATTKNLICEHEIRNISCACQDP 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 77024624 123 NHERVFAFIARNTINETMECYVYVCAKRKIAQAVTLTASQAFHIA 167
Cdd:cd01274  92 EDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVA 136
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 29-143 1.21e-13

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: 66.56  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  29 WGENNETLNEGM-TFYLKYLGSTLVeeisdGESYGDGISTKAIQRVismeKSSGKKWRKVALNVSPRGIKMCDMISNEML 107
Cdd:cd01268   3 WQADEEAVRSGTcSFPVKYLGCVEV-----GESRGMQVCEEALKKL----KASRKKPVRAVLWVSGDGLRVVDEKTKGLI 73

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 77024624 108 LDVCIYRISFCTADRNHERVFAFIARNTINETMECY 143
Cdd:cd01268  74 VDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCH 109
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
42-167 3.86e-13

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 65.08  E-value: 3.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624    42 FYLKYLGST-LVEEISDGESYGDGISTKAIQRViSMEKSSGKKWR--------KVALNVSPRGIKMCDMISNEMLLDVCI 112
Cdd:pfam00640   1 FAVRYLGSVeVPEERAPDKNTRMQQAREAIRRV-KAAKINKIRGLsgetgpgtKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 77024624   113 YRISFCT-ADRNHERVFAFIARNTINETMECYVYVCAKRkiAQAVTLTASQAFHIA 167
Cdd:pfam00640  80 VSISFCAdGDPDLMRYFAYIARDKATNKFACHVFESEDG--AQDIAQSIGQAFALA 133
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 41-164 4.25e-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: 65.05  E-value: 4.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  41 TFYLKYLGStlveEISDGEsYGDGISTKAIqrVISMEKS-SGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIY---RIS 116
Cdd:cd13160   2 VFTVKYLGR----MPARGL-WGIKHTRKPL--VDALKNLpKGKTLPKTKLEVSSDGVKLEELRGGFGSSKTVFFpihTIS 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 77024624 117 FCTADRNHERVFAFIARNT---INETMECYVYVCAKRKIAQAVTLTASQAF 164
Cdd:cd13160  75 YGVQDLVHTRVFSMIVVGEqdsSNHPFECHAFVCDSRADARNLTYWLAKAF 125
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 46-159 7.57e-10

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: 55.76  E-value: 7.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  46 YLGSTLVeeisdGESYGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMC--DMISNEMLLdvciYRISFCTADRN 123
Cdd:cd01214  12 YLGNVLT-----IWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKATtkQHGLTEYWL----HRITYCSAPPN 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 77024624 124 HERVFAFI----ARNTINEtMECYVYVCAKRKIAQAVTLT 159
Cdd:cd01214  83 YPRVFCWIyrheGRKLKVE-LRCHAVLCSKESKARAIALL 121
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
41-167 9.86e-10

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 56.70  E-value: 9.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624    41 TFYLKYLGSTLVeeisdGESYGDGISTKAIQRvISMEKSSGKKWRKVALNVSPRGIKMcdMISNEMLLDVCIYRISFCTA 120
Cdd:pfam14719   1 TYKVVYLGNVLT-----IHAKGEGCTDKPLGT-IWKNYCQGKSGTKMKLTVTRSGLKA--TTKEHGLTEYWSHRITYCSA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 77024624   121 DRNHERVFAFIARNT---INETMECYVYVCAKRKIAQAVTLTASQAFHIA 167
Cdd:pfam14719  73 PPNYPRVFCWVYRHEgrkLKVELRCHAVLCKKEEKARAMALLLYQTLRAA 122
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 45-167 5.35e-09

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: 53.54  E-value: 5.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  45 KYLGSTLVEEiSDGESYGDGIStkaiQRVISMEKSSGKKwRKVALNVSPRGIKMCDMISNEMLLDVCIYRISFCTADRNH 124
Cdd:cd13157   7 QYIGSFPVSG-LDVADRADSVR----KQLESLKESGSRG-RPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 77024624 125 eRVFAFIARNTINETME--CYVYVCAKRKIAQAVTLTASQAFHIA 167
Cdd:cd13157  81 -AQFAFVARNPGGPTNRqyCHVFVTRSPREAQELNLLLCRAFQLA 124
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 37-131 3.36e-08

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: 51.87  E-value: 3.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  37 NEGMTFYLKYLGstlVEEISdgESYGDGISTKAIQRVISMEKSSGKKWRKVALNVSPRGIKMCDMISNEMLLDVCIYRIS 116
Cdd:cd01215  13 GDGVRFKAKLIG---IDEVP--AARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKIS 87

                        90
                ....*....|....*
gi 77024624 117 FCTADRNHERVFAFI 131
Cdd:cd01215  88 FIARDTTDNRAFGYV 102
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 40-156 1.56e-06

JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a 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: 269923  Cd Length: 149  Bit Score: 46.88  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  40 MTFYLKYLGStlVEeisDGESYGDGISTKAIQRVISMEKSSGKKW--RKVALNVSPRGIKMCDMIS-NEMLLDVCIY--- 113
Cdd:cd01212   3 ERFLLGFLGS--VE---VPYHKGNDVLCQAMQKIATARRLTVHLRppQSCILEISDRGLKMVDRSKpNKKDGKPCIHyfy 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 77024624 114 ---RISFCTADRNHERVFAFIARNTINETMECYVYVCAK--RKIAQAV 156
Cdd:cd01212  78 slkNISFCGFHPRNSRYFGFITKHPLLQRFACHVFVSQEstRPVAESV 125
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 32-166 4.83e-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: 46.12  E-value: 4.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77024624  32 NNETLNEGMTFYLKYLGStlvEEISDGESYgdgISTKAIQRVISME-KSSGKKWRKVALNVSPRGIKMC----------- 99
Cdd:cd01270  21 NEEAFQHGITFQAKYIGS---LEVPRPSSR---VEIVAAMRRIRYEfKAKNIKKKKVTITVSVDGVKVVlrkkkkkkgwt 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77024624 100 -DMISNEMLLDvCIYRISFCTADRNHERVFAFIARNTINETMECYVYVCAKRKIAQAVTLTASQAFHI 166
Cdd:cd01270  95 wDESKLLLMQH-PIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEV 161
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
 115-164 4.16e-03

TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. 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: 269967  Cd Length: 143  Bit Score: 36.89  E-value: 4.16e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 77024624 115 ISFCTADRNHERVFAFIARNTINETME---CYVYVCAKRKIAQAVTLTASQAF 164
Cdd:cd01269  91 ISSCSQGIKHVDHFGFICRESSEGGGFhfvCYVFKCQSESVVDEIMLTIKQAF 143
 
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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