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Insulin receptor (IR) (EC 2 7 10 1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]

 INSR_RAT                Reviewed;        1383 AA.
P15127; P97681;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
17-JUN-2020, entry version 197.
RecName: Full=Insulin receptor;
Short=IR;
EC=2.7.10.1;
AltName: CD_antigen=CD220;
Contains:
RecName: Full=Insulin receptor subunit alpha;
Contains:
RecName: Full=Insulin receptor subunit beta;
Flags: Precursor;
Name=Insr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND ALTERNATIVE SPLICING
(ISOFORM SHORT).
PubMed=2330003; DOI=10.1210/mend-4-2-235;
Goldstein B.J., Dudley A.L.;
"The rat insulin receptor: primary structure and conservation of tissue-
specific alternative messenger RNA splicing.";
Mol. Endocrinol. 4:235-244(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 731-756; 758-819; 969-994 AND
1119-1177.
STRAIN=Sprague-Dawley;
Liu Y., Tam J.W.O.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH GRB7.
PubMed=10803466; DOI=10.1038/sj.onc.1203469;
Kasus-Jacobi A., Bereziat V., Perdereau D., Girard J., Burnol A.F.;
"Evidence for an interaction between the insulin receptor and Grb7. A role
for two of its binding domains, PIR and SH2.";
Oncogene 19:2052-2059(2000).
[4]
FUNCTION, AND FORMATION OF A HYBRID RECEPTOR WITH IGF1R.
PubMed=16803852; DOI=10.1152/ajpendo.00565.2005;
Johansson G.S., Arnqvist H.J.;
"Insulin and IGF-I action on insulin receptors, IGF-I receptors, and hybrid
insulin/IGF-I receptors in vascular smooth muscle cells.";
Am. J. Physiol. 291:E1124-E1130(2006).
[5]
INTERACTION WITH CAV2.
PubMed=19778377; DOI=10.1111/j.1582-4934.2009.00391.x;
Kwon H., Jeong K., Pak Y.;
"Identification of pY19-caveolin-2 as a positive regulator of insulin-
stimulated actin cytoskeleton-dependent mitogenesis.";
J. Cell. Mol. Med. 13:1549-1564(2009).
[6]
INTERACTION WITH CCDC88A AND GNAI3.
PubMed=25187647; DOI=10.1091/mbc.e14-05-0978;
Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M.,
Kufareva I., Abagyan R., Ghosh P.;
"Structural basis for activation of trimeric Gi proteins by multiple growth
factor receptors via GIV/Girdin.";
Mol. Biol. Cell 25:3654-3671(2014).
[7]
INTERACTION WITH ATIC.
PubMed=25687571; DOI=10.1074/mcp.m114.047159;
Boutchueng-Djidjou M., Collard-Simard G., Fortier S., Hebert S.S.,
Kelly I., Landry C.R., Faure R.L.;
"The last enzyme of the de novo purine synthesis pathway 5-aminoimidazole-
4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC)
plays a central role in insulin signaling and the Golgi/endosomes protein
network.";
Mol. Cell. Proteomics 14:1079-1092(2015).
-!- FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic
actions of insulin. Binding of insulin leads to phosphorylation of
several intracellular substrates, including, insulin receptor
substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling
intermediates. Each of these phosphorylated proteins serve as docking
proteins for other signaling proteins that contain Src-homology-2
domains (SH2 domain) that specifically recognize different
phosphotyrosine residues, including the p85 regulatory subunit of PI3K
and SHP2. Phosphorylation of IRSs proteins lead to the activation of
two main signaling pathways: the PI3K-AKT/PKB pathway, which is
responsible for most of the metabolic actions of insulin, and the Ras-
MAPK pathway, which regulates expression of some genes and cooperates
with the PI3K pathway to control cell growth and differentiation.
Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to
the activation of PI3K and the generation of phosphatidylinositol-(3,
4, 5)-triphosphate (PIP3), a lipid second messenger, which activates
several PIP3-dependent serine/threonine kinases, such as PDPK1 and
subsequently AKT/PKB. The net effect of this pathway is to produce a
translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic
vesicles to the cell membrane to facilitate glucose transport.
Moreover, upon insulin stimulation, activated AKT/PKB is responsible
for: anti-apoptotic effect of insulin by inducing phosphorylation of
BAD; regulates the expression of gluconeogenic and lipogenic enzymes by
controlling the activity of the winged helix or forkhead (FOX) class of
transcription factors. Another pathway regulated by PI3K-AKT/PKB
activation is mTORC1 signaling pathway which regulates cell growth and
metabolism and integrates signals from insulin. AKT mediates insulin-
stimulated protein synthesis by phosphorylating TSC2 thereby activating
mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in
mediating cell growth, survival and cellular differentiation of
insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers
the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to
binding insulin, the insulin receptor can bind insulin-like growth
factors (IGFI and IGFII). When present in a hybrid receptor with IGF1R,
binds IGF1 (By similarity). In adipocytes, inhibits lipolysis (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P15208,
ECO:0000269|PubMed:16803852}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- ACTIVITY REGULATION: Activated in response to insulin.
Autophosphorylation activates the kinase activity. PTPN1, PTPRE and
PTPRF dephosphorylate important tyrosine residues, thereby reducing
INSR activity. Inhibited by ENPP1. GRB10 and GRB14 inhibit the
catalytic activity of the INSR, they block access of substrates to the
activated receptor. SOCS1 and SOCS3 act as negative regulators of INSR
activity, they bind to the activated INRS and interfere with the
phosphorylation of INSR substrates (By similarity). {ECO:0000250}.
-!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
bonds. The alpha chains carry the insulin-binding regions, while the
beta chains carry the kinase domain. Forms a hybrid receptor with
IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta
chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts
with SORBS1 but dissociates from it following insulin stimulation.
Binds SH2B2. Activated form of INSR interacts (via Tyr-1000) with the
PTB/PID domains of IRS1 and SHC1. The sequences surrounding the
phosphorylated NPXY motif contribute differentially to either IRS1 or
SHC1 recognition. Interacts (via tyrosines in the C-terminus) with IRS2
(via PTB domain and 591-786 AA); the 591-786 would be the primary
anchor of IRS2 to INSR while the PTB domain would have a stabilizing
action on the interaction with INSR. Interacts with the SH2 domains of
the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, when
autophosphorylated on tyrosine residues. Interacts with SOCS7.
Interacts (via the phosphorylated Tyr-1000), with SOCS3. Interacts (via
the phosphorylated Tyr-1186, Tyr-1190, Tyr-1191) with SOCS1. Interacts
with ARRB2 (By similarity). Interacts with GRB10; this interaction
blocks the association between IRS1/IRS2 and INSR, significantly
reduces insulin-stimulated tyrosine phosphorylation of IRS1 and IRS2
and thus decreases insulin signaling. Interacts with PDPK1. Interacts
(via Tyr-1191) with GRB14 (via BPS domain); this interaction protects
the tyrosines in the activation loop from dephosphorylation, but
promotes dephosphorylation of Tyr-1000, this results in decreased
interaction with, and phosphorylation of, IRS1. Interacts (via subunit
alpha) with ENPP1 (via 485-599 AA); this interaction blocks
autophosphorylation. Interacts with PTPRE; this interaction is
dependent of Tyr-1186, Tyr-1190 and Tyr-1191 of the INSR. Interacts
with STAT5B (via SH2 domain). Interacts with PTPRF (By similarity).
Interacts with GRB7. Interacts with CAV2 (tyrosine-phosphorylated
form); the interaction is increased with 'Tyr-27'phosphorylation of
CAV2. Interacts with ATIC; ATIC together with PRKAA2/AMPK2 and
HACD3/PTPLAD1 is proposed to be part of a signaling netwok regulating
INSR autophosphorylation and endocytosis (PubMed:25687571). Interacts
with the insulin receptor SORL1; this interaction strongly increases
its surface exposure, hence strengthens insulin signal reception (By
similarity). Interacts (tyrosine phosphorylated) with CCDC88A/GIV (via
SH2-like region); binding requires autophosphorylation of the INSR C-
terminal region (PubMed:25187647). Interacts with GNAI3; the
interaction is probably mediated by CCDC88A/GIV (PubMed:25187647).
{ECO:0000250, ECO:0000250|UniProtKB:P15208,
ECO:0000269|PubMed:10803466, ECO:0000269|PubMed:19778377,
ECO:0000269|PubMed:25187647, ECO:0000269|PubMed:25687571}.
-!- INTERACTION:
P15127; Q62689: Jak2; NbExp=2; IntAct=EBI-7472166, EBI-8656708;
PRO_0000016698; O35567: Atic; NbExp=3; IntAct=EBI-10768746, EBI-10768817;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15208};
Single-pass type I membrane protein {ECO:0000305}. Late endosome
{ECO:0000250|UniProtKB:P15208}. Lysosome
{ECO:0000250|UniProtKB:P15208}. Note=Binding of insulin to INSR induces
internalization and lysosomal degradation of the receptor, a means for
downregulating this signaling pathway after stimulation. In the
presence of SORL1, internalized INSR molecules are redirected back to
the cell surface, thereby preventing their lysosomal catabolism and
strengthening insulin signal reception. {ECO:0000250|UniProtKB:P15208}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long; Synonyms=RIR-B;
IsoId=P15127-1; Sequence=Displayed;
Name=Short; Synonyms=RIR-A;
IsoId=P15127-2; Sequence=VSP_036680;
-!- DOMAIN: The tetrameric insulin receptor binds insulin via non-identical
regions from two alpha chains, primarily via the C-terminal region of
the first INSR alpha chain. Residues from the leucine-rich N-terminus
of the other INSR alpha chain also contribute to this insulin binding
site. A secondary insulin-binding site is formed by residues at the
junction of fibronectin type-III domain 1 and 2 (By similarity).
{ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues in response to insulin.
Phosphorylation of Tyr-1000 is required for binding to IRS1, SHC1, and
STAT5B. Dephosphorylated by PTPRE on Tyr-1000, Tyr-1186, Tyr-1190 and
Tyr-1191 residues. Dephosphorylated by PTPRF and PTPN1.
Dephosphorylated by PTPN2; down-regulates insulin-induced signaling.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M29014; AAA41441.1; -; mRNA.
EMBL; AF005776; AAB61414.1; -; Genomic_DNA.
EMBL; AF005777; AAB61415.1; -; Genomic_DNA.
EMBL; AH004882; AAB38967.1; -; Genomic_DNA.
EMBL; AH004883; AAB38968.1; -; Genomic_DNA.
EMBL; U80633; AAB38746.1; -; Genomic_DNA.
PIR; A36080; A36080.
PDB; 4XST; X-ray; 3.00 A; F=726-748.
PDB; 5TQ1; X-ray; 1.49 A; B=1008-1018.
PDBsum; 4XST; -.
PDBsum; 5TQ1; -.
SMR; P15127; -.
DIP; DIP-42209N; -.
IntAct; P15127; 460.
MINT; P15127; -.
STRING; 10116.ENSRNOP00000060141; -.
BindingDB; P15127; -.
ChEMBL; CHEMBL5486; -.
DrugCentral; P15127; -.
iPTMnet; P15127; -.
PhosphoSitePlus; P15127; -.
UniCarbKB; P15127; -.
jPOST; P15127; -.
PaxDb; P15127; -.
PeptideAtlas; P15127; -.
PRIDE; P15127; -.
UCSC; RGD:2917; rat. [P15127-1]
RGD; 2917; Insr.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
InParanoid; P15127; -.
PhylomeDB; P15127; -.
BRENDA; 2.7.10.1; 5301.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-74713; IRS activation.
Reactome; R-RNO-74749; Signal attenuation.
Reactome; R-RNO-74751; Insulin receptor signalling cascade.
Reactome; R-RNO-74752; Signaling by Insulin receptor.
Reactome; R-RNO-77387; Insulin receptor recycling.
PRO; PR:P15127; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005901; C:caveola; ISO:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0032590; C:dendrite membrane; IDA:ARUK-UCL.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:ARUK-UCL.
GO; GO:0005899; C:insulin receptor complex; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:ARUK-UCL.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0060417; C:yolk; IDA:RGD.
GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; IDA:RGD.
GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
GO; GO:0005524; F:ATP binding; ISO:RGD.
GO; GO:0038024; F:cargo receptor activity; IMP:ARUK-UCL.
GO; GO:0005525; F:GTP binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0043559; F:insulin binding; IDA:RGD.
GO; GO:0043560; F:insulin receptor substrate binding; IMP:RGD.
GO; GO:0005009; F:insulin-activated receptor activity; IDA:RGD.
GO; GO:0031994; F:insulin-like growth factor I binding; ISO:RGD.
GO; GO:0031995; F:insulin-like growth factor II binding; ISO:RGD.
GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:RGD.
GO; GO:0031405; F:lipoic acid binding; IPI:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IMP:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
GO; GO:0051425; F:PTB domain binding; ISO:RGD.
GO; GO:0005198; F:structural molecule activity; ISO:RGD.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0000187; P:activation of MAPK activity; ISO:RGD.
GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
GO; GO:0032148; P:activation of protein kinase B activity; ISO:RGD.
GO; GO:0030325; P:adrenal gland development; ISO:RGD.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEP:RGD.
GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0097062; P:dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:1990402; P:embryonic liver development; IEP:RGD.
GO; GO:0008544; P:epidermis development; ISO:RGD.
GO; GO:0031017; P:exocrine pancreas development; ISO:RGD.
GO; GO:0045444; P:fat cell differentiation; IEP:RGD.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
GO; GO:0042593; P:glucose homeostasis; IDA:RGD.
GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0008584; P:male gonad development; ISO:RGD.
GO; GO:0030238; P:male sex determination; ISO:RGD.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:2000252; P:negative regulation of feeding behavior; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:0032410; P:negative regulation of transporter activity; IMP:RGD.
GO; GO:1990535; P:neuron projection maintenance; IGI:ARUK-UCL.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:RGD.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
GO; GO:0048639; P:positive regulation of developmental growth; ISO:RGD.
GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:RGD.
GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; IMP:RGD.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
GO; GO:0051446; P:positive regulation of meiotic cell cycle; ISO:RGD.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; IGI:ARUK-UCL.
GO; GO:0002092; P:positive regulation of receptor internalization; ISO:RGD.
GO; GO:0060267; P:positive regulation of respiratory burst; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
GO; GO:0045995; P:regulation of embryonic development; ISO:RGD.
GO; GO:2000194; P:regulation of female gonad development; ISO:RGD.
GO; GO:0006111; P:regulation of gluconeogenesis; IEP:RGD.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IDA:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0032094; P:response to food; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:BHF-UCL.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:BHF-UCL.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:1904638; P:response to resveratrol; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IMP:RGD.
GO; GO:1902438; P:response to vanadate(3-); IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0019087; P:transformation of host cell by virus; ISO:RGD.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd00063; FN3; 2.
CDD; cd00064; FU; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR040969; Insulin_TMD.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00041; fn3; 1.
Pfam; PF00757; Furin-like; 1.
Pfam; PF17870; Insulin_TMD; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000620; Insulin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 3.
SMART; SM00261; FU; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 3.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Cleavage on pair of basic residues; Disulfide bond; Endosome; Glycoprotein;
Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1..26
CHAIN 27..759
/note="Insulin receptor subunit alpha"
/id="PRO_0000016696"
CHAIN 764..1383
/note="Insulin receptor subunit beta"
/id="PRO_0000016698"
TOPO_DOM 27..759
/note="Extracellular"
/evidence="ECO:0000305"
TOPO_DOM 764..957
/note="Extracellular"
/evidence="ECO:0000305"
TRANSMEM 958..978
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 979..1383
/note="Cytoplasmic"
/evidence="ECO:0000305"
DOMAIN 625..727
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 754..848
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 854..948
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1024..1299
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 1105..1111
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 1164..1165
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 734..742
/note="Insulin-binding"
/evidence="ECO:0000250"
REGION 997..1000
/note="Important for interaction with IRS1, SHC1 and
STAT5B"
REGION 1362..1365
/note="PIK3R1 binding"
/evidence="ECO:0000250"
COMPBIAS 27..173
/note="Leu-rich"
ACT_SITE 1160
/note="Proton donor/acceptor"
/evidence="ECO:0000250"
BINDING 1034
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 1058
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 1178
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SITE 65
/note="Insulin-binding"
/evidence="ECO:0000250"
MOD_RES 399
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 400
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 406
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1000
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1186
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1190
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1191
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1356
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1362
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
CARBOHYD 42
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 51
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 104
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 137
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 241
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 281
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 321
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 363
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 423
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 444
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 540
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 634
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 652
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 699
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 770
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 783
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 921
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 934
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 34..52
/evidence="ECO:0000250"
DISULFID 152..181
/evidence="ECO:0000250"
DISULFID 185..208
/evidence="ECO:0000250"
DISULFID 195..214
/evidence="ECO:0000250"
DISULFID 218..227
/evidence="ECO:0000250"
DISULFID 222..233
/evidence="ECO:0000250"
DISULFID 234..242
/evidence="ECO:0000250"
DISULFID 238..251
/evidence="ECO:0000250"
DISULFID 254..263
/evidence="ECO:0000250"
DISULFID 267..279
/evidence="ECO:0000250"
DISULFID 285..310
/evidence="ECO:0000250"
DISULFID 292..300
/evidence="ECO:0000250"
DISULFID 314..327
/evidence="ECO:0000250"
DISULFID 330..334
/evidence="ECO:0000250"
DISULFID 338..359
/evidence="ECO:0000250"
DISULFID 461..494
/evidence="ECO:0000250"
DISULFID 550
/note="Interchain"
/evidence="ECO:0000250"
DISULFID 675..900
/evidence="ECO:0000250"
VAR_SEQ 746..757
/note="Missing (in isoform Short)"
/evidence="ECO:0000305"
/id="VSP_036680"
HELIX 727..736
/evidence="ECO:0000244|PDB:4XST"
SEQUENCE 1383 AA; 156757 MW; 4B919566902A944A CRC64;
MGSGRGCETT AVPLLMAVAV AGGTAGHLYP GEVCPGMDIR NNLTRLHELE NCSVIEGHLQ
ILLMFKTRPE DFRDLSFPKL IMITDYLLLF RVYGLESLKD LFPNLTVIRG SRLFFNYALV
IFEMVHLKEL GLYNLMNITR GSVRIEKNNE LCYLATIDWS RILDYVEDNY IVLNKDDNEE
CGDVCPGTAK GKTNCPATVI NGQFVERCWT HSHCQKVCPT ICKSHGCTAE GLCCHKECLG
NCSEPDDPTK CVACRNFYLD GQCVETCPPP YYHFQDWRCV NFSFCQDLHY KCRNSRKPGC
HQYVIHNNKC IPECPSGYTM NSSNLMCTPC LGPCPKVCQI LEGEKTIDSV TSAQELRGCT
VINGSLIINI RGGNNLAAEL EANLGLIEEI SGFLKIRRSY ALVSLSFFRK LHLIRGETLE
IGNYSFYALD NQNLRQLWDW NKHNLTITQG KLFFHYNPKL CLSEIHKMEE VSGTKGRQER
NDIALKTNGD QASCENELLK FSFIRTSFDK ILLRWEPYWP PDFRDLLGFM LFYKEAPYQN
VTEFDGQDAC GSNSWTVVDI DPPQRSNDPK SQTPSHPGWL MRGLKPWTQY AIFVKTLVTF
SDERRTYGAK SDIIYVQTDA TNPSVPLDPI SVSNSSSQII LKWKPPSDPN GNITHYLVYW
ERQAEDSELF ELDYCLKGLK LPSRTWSPPF ESDDSQKHNQ SEYDDSASEC CSCPKTDSQI
LKELEESSFR KTFEDYLHNV VFVPRKTSSG NGAEDTRPSR KRRSLEEVGN VTATTPTLPD
FPNISSTIAP TSHEEHRPFE KVVNKESLVI SGLRHFTGYR IELQACNQDS PEERSGVAAY
VSARTMPEAK ADDIVGPVTH EIFENNVVHL MWQEPKEPNG LIVLYEVSYR RYGDEELHLC
VSRKHFALER GCRLRGLSPG NYSVRVRATS LAGNGSWTEP TYFYVTDYLD VPSNIAKIII
GPLIFVFLFS VVIGSIYLFL RKRQPDGPMG PLYASSNPEY LSASDVFPSS VYVPDEWEVP
REKITLLREL GQGSFGMVYE GNAKDIIKGE VETRVAVKTV NESASLRERI EFLNEASVMK
GFTCHHVVRL LGVVSKGQPT LVVMELMAHG DLKSHLRSLR PDAENNPGRP PPTLQEMIQM
TAEIADGMAY LNAKKFVHRD LAARNCMVAH DFTVKIGDFG MTRDIYETDY YRKGGKGLLP
VRWMSPESLK DGVFTASSDM WSFGVVLWEI TSLAEQPYQG LSNEQVLKFV MDGGYLDPPD
NCPERLTDLM RMCWQFNPKM RPTFLEIVNL LKDDLHPSFP EVSFFYSEEN KAPESEELEM
EFEDMENVPL DRSSHCQREE AGCREGGSSL SIKRTYDEHI PYTHMNGGKK NGRVLTLPRS
NPS


Related products :

Catalog number Product name Quantity
18-783-75598 RABBIT ANTI HUMAN CD220 - INSULIN RECEPTOR; EC 2.7.10.1; IR; CD220 antigen Polyclonal 0.05 mg
BMMS-636-R1 Insulin Receptor (Beta-Subunit ) 1mL
BMMS-636-B Insulin Receptor (Beta-Subunit ) 1mL
BMMS-636-BCS Insulin Receptor (Beta-Subunit ) 5sld
BMMS-636-MX Insulin Receptor (Beta-Subunit ) MTO
BMMS-635-X Insulin Receptor (Beta-Subunit ) 0.2mL
BMMS-635-B1X Insulin Receptor (Beta-Subunit ) 0.1mL
BMMS-635-B1 Insulin Receptor (Beta-Subunit ) 0.5mL
BMMS-635-B0 Insulin Receptor (Beta-Subunit ) 0.1mL
BMMS-635-B Insulin Receptor (Beta-Subunit ) 1mL
BMMS-635-MX Insulin Receptor (Beta-Subunit ) MTO
BMMS-636-X Insulin Receptor (Beta-Subunit) 0.2mL
BMMS-636-BCL Insulin Receptor (Beta-Subunit) 0.1mL
BMMS-636-R1 Insulin Receptor (Beta-Subunit) 1mL
BMMS-636-R7 Insulin Receptor (Beta-Subunit) 7mL
BMMS-636-B0 Insulin Receptor (Beta-Subunit ) 0.1mL
BMMS-636-B1X Insulin Receptor (Beta-Subunit) 0.1mL
BMMS-636-BCL Insulin Receptor (Beta-Subunit ) 0.1mL
BMMS-636-R7 Insulin Receptor (Beta-Subunit ) 7mL
BMMS-635-X Insulin Receptor (Beta-Subunit) 0.2mL
BMMS-636-X Insulin Receptor (Beta-Subunit ) 0.2mL
BMMS-635-B1X Insulin Receptor (Beta-Subunit) 0.1mL
BMMS-636-MX Insulin Receptor (Beta-Subunit) MTO
BMMS-635-B1 Insulin Receptor (Beta-Subunit) 0.5mL
BMMS-635-B0 Insulin Receptor (Beta-Subunit) 0.1mL
Pathways :
WP1913: Signaling by Insulin receptor
WP2292: Chemokine signaling pathway
WP566: canonical wnt - zebrafish
WP2272: Pathogenic Escherichia coli infection
WP1367: TGF-beta Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP2328: Allograft rejection
WP926: TGF-beta Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1963: The effect of Glucocorticoids on target gene expression
WP1161: TGF-beta Receptor Signaling Pathway
WP1655: Geraniol degradation
WP578: Leptin Insulin Overlap
WP768: EPO Receptor Signaling
WP1112: EPO Receptor Signaling
WP1345: T Cell Receptor Signaling Pathway
WP352: T Cell Receptor Signaling Pathway
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP780: T Cell Receptor Signaling Pathway
WP966: Insulin Signaling
WP590: Cardiovascular Signaling

Related Genes :
[INSR] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[daf-2 Y55D5A.5] Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[InR dinr Dir-a Inr-a CG18402] Insulin-like receptor (dIR) (dInr) (EC 2.7.10.1) (dIRH) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta 1; Insulin-like receptor subunit beta 2]
[INSR] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta] (Fragment)
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] (Fragment)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) (Fragments)
[BAIAP2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Protein BAP2) (Fas ligand-associated factor 3) (FLAF3) (Insulin receptor substrate p53/p58) (IRS-58) (IRSp53/58) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53)
[Znf106 H3a Sh3bp3 Sirm Zfp106 Znf474] Zinc finger protein 106 (Zfp-106) (H3a minor histocompatibility antigen) (Son of insulin receptor mutant) (Zinc finger protein 474)
[Baiap2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase 53 kDa substrate)
[Baiap2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase substrate protein p53)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[IRS1] Insulin receptor substrate 1 (IRS-1)
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1) (pp185)
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1)
[ITGAV MSK8 VNRA VTNR] Integrin alpha-V (Vitronectin receptor) (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]
[LRP1 A2MR APR] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (Apolipoprotein E receptor) (APOER) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[Lrp1 A2mr] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[SIRPA BIT MFR MYD1 PTPNS1 SHPS1 SIRP] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory protein alpha-2) (Sirp-alpha-2) (Signal-regulatory protein alpha-3) (Sirp-alpha-3) (p84) (CD antigen CD172a)
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[Fgfr4 Fgfr-4 Mpk-11] Fibroblast growth factor receptor 4 (FGFR-4) (EC 2.7.10.1) (Protein-tyrosine kinase receptor MPK-11) (CD antigen CD334)
[IL4R IL4RA 582J2.1] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[Itgav] Integrin alpha-V (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]
[PTPRN ICA3 ICA512] Receptor-type tyrosine-protein phosphatase-like N (R-PTP-N) (Islet cell antigen 512) (ICA 512) (Islet cell autoantigen 3) (PTP IA-2) [Cleaved into: ICA512-N-terminal fragment (ICA512-NTF); ICA512-transmembrane fragment (ICA512-TMF); ICA512-cleaved cytosolic fragment (ICA512-CCF)]

Bibliography :