NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|389609131|dbj|BAM18177|]
View 

unknown unsecreted protein [Papilio xuthus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
40-164 3.05e-51

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: 161.73  E-value: 3.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  40 GEQGEVRYAGVVPVERAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAA 119
Cdd:cd13159    2 GVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADAN 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 389609131 120 NARVFAVVEGkkeSGSEENHVVHVFVCARAKQARALALSLAHAFN 164
Cdd:cd13159   82 HDKVFAFIAT---NQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 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 ...
40-164 3.05e-51

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: 161.73  E-value: 3.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  40 GEQGEVRYAGVVPVERAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAA 119
Cdd:cd13159    2 GVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADAN 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 389609131 120 NARVFAVVEGkkeSGSEENHVVHVFVCARAKQARALALSLAHAFN 164
Cdd:cd13159   82 HDKVFAFIAT---NQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
38-171 7.16e-17

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: 73.89  E-value: 7.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131    38 GAGEQGEVRYAGVVPVERAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSAD 117
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 389609131   118 AANARVFAVVEGKKesgSEENHVVHVFVCARAkqARALALSLAHAFNDAYQAWQ 171
Cdd:smart00462  81 PDDLDVFGYIARDP---GSSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKL 129
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
44-163 4.63e-09

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 52.75  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131   44 EVRYAGVVPV--ERAASAPATALAVRSALHTIKSSNKKLQR-----------VTLDISAKGILVIDVDSQQNVLSVSIYR 110
Cdd:pfam00640   2 AVRYLGSVEVpeERAPDKNTRMQQAREAIRRVKAAKINKIRglsgetgpgtkVDLFISTDGLKLLNPDTQELIHDHPLVS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 389609131  111 ISYCS-ADAANARVFAVVEGKKESgseENHVVHVFVCarAKQARALALSLAHAF 163
Cdd:pfam00640  82 ISFCAdGDPDLMRYFAYIARDKAT---NKFACHVFES--EDGAQDIAQSIGQAF 130
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
40-164 3.05e-51

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: 161.73  E-value: 3.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  40 GEQGEVRYAGVVPVERAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAA 119
Cdd:cd13159    2 GVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADAN 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 389609131 120 NARVFAVVEGkkeSGSEENHVVHVFVCARAKQARALALSLAHAFN 164
Cdd:cd13159   82 HDKVFAFIAT---NQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
44-163 5.08e-26

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: 97.19  E-value: 5.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  44 EVRYAGVVPVERAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARV 123
Cdd:cd00934    4 QVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNV 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 389609131 124 FAVVEGKKesgSEENHVVHVFVCARAKQARALALSLAHAF 163
Cdd:cd00934   84 FAFIAGEE---GGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
38-171 7.16e-17

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: 73.89  E-value: 7.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131    38 GAGEQGEVRYAGVVPVERAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSAD 117
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 389609131   118 AANARVFAVVEGKKesgSEENHVVHVFVCARAkqARALALSLAHAFNDAYQAWQ 171
Cdd:smart00462  81 PDDLDVFGYIARDP---GSSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKL 129
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
45-168 5.09e-13

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: 63.84  E-value: 5.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  45 VRYAGVVPVERAASAPATALAVRS---ALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANA 121
Cdd:cd01273   16 VKFLGCTEVEQPKGTEVVKEAIRKlkfARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDK 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 389609131 122 RVFAVVegKKESGSEEnHVVHVFVCarAKQARALALSLAHAFNDAYQ 168
Cdd:cd01273   96 RIFSFI--AKDSESEK-HLCFVFDS--EKLAEEITLTIGQAFDLAYR 137
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
44-163 5.34e-12

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: 60.34  E-value: 5.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  44 EVRYAGVVPVERAASAPAtalaVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARV 123
Cdd:cd13161    5 EAKYLGSVPVKEPKGNDV----VMAAVKRLKDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 389609131 124 FAVVEGKKESGSeenHVVHVFVCARAkqARALALSLAHAF 163
Cdd:cd13161   81 FAFISHDPRLGR---ITCHVFRCKRG--AQEICDTIAEAF 115
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
76-163 5.61e-11

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: 57.73  E-value: 5.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  76 SNKKLQRVTLDISAKGILVIDVDSQQ---NVLSVSIYRISYCSADAANARVFAVVEGKKESGSEENHVVHVFVCARAKQA 152
Cdd:cd13160   35 KGKTLPKTKLEVSSDGVKLEELRGGFgssKTVFFPIHTISYGVQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADA 114
                         90
                 ....*....|.
gi 389609131 153 RALALSLAHAF 163
Cdd:cd13160  115 RNLTYWLAKAF 125
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
78-168 1.42e-10

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: 57.29  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  78 KKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARVFAVVEGKKESGSeenHVVHVFVCARAKQARALAL 157
Cdd:cd01274   51 KKIPTIILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKTDH---HYCHVFCVLTVDLATEIIL 127
                         90
                 ....*....|.
gi 389609131 158 SLAHAFNDAYQ 168
Cdd:cd01274  128 TLGQAFEVAYQ 138
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
44-163 4.63e-09

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 52.75  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131   44 EVRYAGVVPV--ERAASAPATALAVRSALHTIKSSNKKLQR-----------VTLDISAKGILVIDVDSQQNVLSVSIYR 110
Cdd:pfam00640   2 AVRYLGSVEVpeERAPDKNTRMQQAREAIRRVKAAKINKIRglsgetgpgtkVDLFISTDGLKLLNPDTQELIHDHPLVS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 389609131  111 ISYCS-ADAANARVFAVVEGKKESgseENHVVHVFVCarAKQARALALSLAHAF 163
Cdd:pfam00640  82 ISFCAdGDPDLMRYFAYIARDKAT---NKFACHVFES--EDGAQDIAQSIGQAF 130
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
45-167 1.58e-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: 51.23  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  45 VRYAGVVPVErAASAPATALAVRSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARvF 124
Cdd:cd13157    6 AQYIGSFPVS-GLDVADRADSVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAHAQ-F 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 389609131 125 AVVegKKESGSEEN-HVVHVFVCARAKQARALALSLAHAFNDAY 167
Cdd:cd13157   84 AFV--ARNPGGPTNrQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
73-159 2.45e-06

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: 45.71  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  73 IKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARVFAVVegkkeSGSEENHvvHVFVCARAKQA 152
Cdd:cd01215   48 VKAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNRAFGYV-----CGLDGGH--RFFAIKTAKAA 120

                 ....*..
gi 389609131 153 RALALSL 159
Cdd:cd01215  121 EPVVLDL 127
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
109-159 9.21e-06

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: 43.43  E-value: 9.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 389609131 109 YRISYCSADAANARVFAVV---EGKKESgseenHVV--HVFVCARAKQARALALSL 159
Cdd:cd01214   72 HRITYCSAPPNYPRVFCWIyrhEGRKLK-----VELrcHAVLCSKESKARAIALLL 122
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
82-168 3.59e-05

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 42.83  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131   82 RVTLDISAKGILVidVDSQQNVLSVSIYRISYCSADAANARVFAVV---EGKKESGSEENHVVhvfVCARAKQARALALS 158
Cdd:pfam14719  40 KMKLTVTRSGLKA--TTKEHGLTEYWSHRITYCSAPPNYPRVFCWVyrhEGRKLKVELRCHAV---LCKKEEKARAMALL 114
                          90
                  ....*....|
gi 389609131  159 LAHAFNDAYQ 168
Cdd:pfam14719 115 LYQTLRAALQ 124
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
67-141 5.55e-05

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: 41.52  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  67 RSALHTIKSSNKKLQRVTLDISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARVFAVV--EG------------KKE 132
Cdd:cd01268   37 EEALKKLKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHERAFSYIcrDGttrrwmchcflaVKD 116

                 ....*....
gi 389609131 133 SGSEENHVV 141
Cdd:cd01268  117 SGERLSHAV 125
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
72-163 1.74e-04

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: 39.92  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389609131  72 TIKSSNKKLQRVTLDI--SAKGILVI-DVDSQQNVLSVSIYRISYCS---ADAANARVFAVVEGKKESgseENHVVHVFV 145
Cdd:cd01211   29 ILREQSAQPIKVTLSVpnSSEGSVRLyDPTSNTEIASYPIYRILFCArgpDGTSESDCFAFTWSHGET---AIFQCHVFR 105
                         90
                 ....*....|....*...
gi 389609131 146 CARAKQARALALSLAHAF 163
Cdd:cd01211  106 CEIPEAVSKVLYSFAKAF 123
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
87-144 4.00e-03

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain; APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. 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: 269980  Cd Length: 135  Bit Score: 36.17  E-value: 4.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 389609131  87 ISAKGILVIDVDSQQNVLSVSIYRISYCSADAANARVFA-VVEGKKESGSEENHVVHVF 144
Cdd:cd13158   58 VTSDCLRLIDPQTQVTRARFPLADVVQFAAHQENKRLFGfVVRTPEGDGEEPSFSCYVF 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH