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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_MOUSE              Reviewed;        1372 AA.
P15208; F8VPU4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
17-JUN-2020, entry version 218.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2557333;
Flores-Riveros J.R., Sibley E., Kastelic T., Lane M.D.;
"Substrate phosphorylation catalyzed by the insulin receptor tyrosine
kinase. Kinetic correlation to autophosphorylation of specific sites in the
beta subunit.";
J. Biol. Chem. 264:21557-21572(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
PubMed=2602374; DOI=10.1073/pnas.86.24.9732;
Sibley E., Kastelic T., Kelly T.J., Lane M.D.;
"Characterization of the mouse insulin receptor gene promoter.";
Proc. Natl. Acad. Sci. U.S.A. 86:9732-9736(1989).
[4]
INTERACTION WITH IRS1 AND IRS2, AND MUTAGENESIS OF TYR-989.
PubMed=8626379; DOI=10.1074/jbc.271.11.5980;
Sawka-Verhelle D., Tartare-Deckert S., White M.F., Van Obberghen E.;
"Insulin receptor substrate-2 binds to the insulin receptor through its
phosphotyrosine-binding domain and through a newly identified domain
comprising amino acids 591-786.";
J. Biol. Chem. 271:5980-5983(1996).
[5]
INTERACTION WITH SORBS1.
PubMed=9447983; DOI=10.1128/mcb.18.2.872;
Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.;
"A novel, multifunctional c-Cbl binding protein in insulin receptor
signaling in 3T3-L1 adipocytes.";
Mol. Cell. Biol. 18:872-879(1998).
[6]
MUTAGENESIS OF TYR-989.
PubMed=10207032; DOI=10.1074/jbc.274.17.12075;
Chaika O.V., Chaika N., Volle D.J., Hayashi H., Ebina Y., Wang L.M.,
Pierce J.H., Lewis R.E.;
"Mutation of tyrosine 960 within the insulin receptor juxtamembrane domain
impairs glucose transport but does not inhibit ligand-mediated
phosphorylation of insulin receptor substrate-2 in 3T3-L1 adipocytes.";
J. Biol. Chem. 274:12075-12080(1999).
[7]
INTERACTION WITH SOCS3.
PubMed=10821852; DOI=10.1074/jbc.275.21.15985;
Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D.,
Van Obberghen E.;
"SOCS-3 is an insulin-induced negative regulator of insulin signaling.";
J. Biol. Chem. 275:15985-15991(2000).
[8]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
PubMed=12612081; DOI=10.1128/mcb.23.6.2096-2108.2003;
Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A.,
Meng T.C., Tonks N.K., Tiganis T.;
"Regulation of insulin receptor signaling by the protein tyrosine
phosphatase TCPTP.";
Mol. Cell. Biol. 23:2096-2108(2003).
[9]
INTERACTION WITH SOCS1 AND SOCS3.
PubMed=15169905; DOI=10.1128/mcb.24.12.5434-5446.2004;
Ueki K., Kondo T., Kahn C.R.;
"Suppressor of cytokine signaling 1 (SOCS-1) and SOCS-3 cause insulin
resistance through inhibition of tyrosine phosphorylation of insulin
receptor substrate proteins by discrete mechanisms.";
Mol. Cell. Biol. 24:5434-5446(2004).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-linked
cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[12]
INTERACTION WITH ARRB2.
PubMed=19122674; DOI=10.1038/nature07617;
Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J.,
Pei G.;
"Deficiency of a beta-arrestin-2 signal complex contributes to insulin
resistance.";
Nature 457:1146-1149(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[14]
FUNCTION, INTERACTION WITH SORL1, AND SUBCELLULAR LOCATION.
PubMed=27322061; DOI=10.1172/jci84708;
Schmidt V., Schulz N., Yan X., Schuermann A., Kempa S., Kern M.,
Blueher M., Poy M.N., Olivecrona G., Willnow T.E.;
"SORLA facilitates insulin receptor signaling in adipocytes and exacerbates
obesity.";
J. Clin. Invest. 126:2706-2720(2016).
-!- 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
(PubMed:27322061). {ECO:0000250, ECO:0000269|PubMed:27322061}.
-!- 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). Interacts with
PTPRF (By similarity). 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 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P15127}.
-!- 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 (By similarity). Activated form of INSR interacts (via Tyr-
989) 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 (By
similarity). Interacts (via the phosphorylated Tyr-989), with SOCS3.
Interacts (via the phosphorylated Tyr-1175, Tyr-1179, Tyr-1180) with
SOCS1. Interacts with CAV2 (tyrosine-phosphorylated form); the
interaction is increased with 'Tyr-27'phosphorylation of CAV2 (By
similarity). Interacts with ARRB2. 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 (By similarity).
Interacts with GRB7 (By similarity). Interacts with PDPK1 (By
similarity). Interacts (via Tyr-1180) with GRB14 (via BPS domain); this
interaction protects the tyrosines in the activation loop from
dephosphorylation, but promotes dephosphorylation of Tyr-989, this
results in decreased interaction with, and phosphorylation of, IRS1 (By
similarity). Interacts (via subunit alpha) with ENPP1 (via 485-599 AA);
this interaction blocks autophosphorylation (By similarity). Interacts
with PTPRE; this interaction is dependent of Tyr-1175, Tyr-1179 and
Tyr-1180 of the INSR (By similarity). Interacts with STAT5B (via SH2
domain) (By similarity). Interacts with PTPRF (By similarity).
Interacts with the insulin receptor SORL1; this interaction strongly
increases its surface exposure, hence strengthens insulin signal
reception (PubMed:27322061). Interacts (tyrosine phosphorylated) with
CCDC88A/GIV (via SH2-like region); binding requires autophosphorylation
of the INSR C-terminal region (By similarity). Interacts with GNAI3;
the interaction is probably mediated by CCDC88A/GIV (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P06213,
ECO:0000269|PubMed:27322061}.
-!- INTERACTION:
P15208; P49817: Cav1; NbExp=2; IntAct=EBI-6999015, EBI-1161338;
P15208; Q60760: Grb10; NbExp=6; IntAct=EBI-6999015, EBI-861810;
P15208; Q1XH17: Trim72; NbExp=2; IntAct=EBI-6999015, EBI-16034016;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27322061};
Single-pass type I membrane protein {ECO:0000305}. Recycling endosome
membrane {ECO:0000269|PubMed:27322061}. Late endosome
{ECO:0000269|PubMed:27322061}. Lysosome {ECO:0000305|PubMed:27322061}.
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:0000269|PubMed:27322061}.
-!- 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 (By
similarity). Phosphorylation of Tyr-989 is required for IRS1-, SHC1-,
and STAT5B-binding (By similarity). Dephosphorylated by PTPRE on Tyr-
989, Tyr-1175, Tyr-1179 and Tyr-1180 residues (By similarity).
Dephosphorylated by PTPRF and PTPN1 (By similarity). Dephosphorylated
by PTPN2; down-regulates insulin-induced signaling. {ECO:0000250,
ECO:0000269|PubMed:12612081}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; J05149; AAA39318.1; -; mRNA.
EMBL; AC168068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M28869; AAA39319.1; -; Genomic_DNA.
CCDS; CCDS22059.1; -.
PIR; A34157; A34157.
RefSeq; NP_034698.2; NM_010568.3.
PDB; 1LK2; X-ray; 1.35 A; P=423-430.
PDBsum; 1LK2; -.
SMR; P15208; -.
BioGRID; 200774; 23.
CORUM; P15208; -.
DIP; DIP-41452N; -.
IntAct; P15208; 21.
MINT; P15208; -.
STRING; 10090.ENSMUSP00000088837; -.
BindingDB; P15208; -.
ChEMBL; CHEMBL3187; -.
CarbonylDB; P15208; -.
GlyConnect; 2393; -.
iPTMnet; P15208; -.
PhosphoSitePlus; P15208; -.
jPOST; P15208; -.
MaxQB; P15208; -.
PaxDb; P15208; -.
PeptideAtlas; P15208; -.
PRIDE; P15208; -.
Antibodypedia; 3403; 2024 antibodies.
Ensembl; ENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.
GeneID; 16337; -.
KEGG; mmu:16337; -.
UCSC; uc009krc.2; mouse.
CTD; 3643; -.
MGI; MGI:96575; Insr.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000155404; -.
HOGENOM; CLU_000288_166_0_1; -.
InParanoid; P15208; -.
KO; K04527; -.
OMA; SDGQCCH; -.
TreeFam; TF351636; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-74713; IRS activation.
Reactome; R-MMU-74749; Signal attenuation.
Reactome; R-MMU-74751; Insulin receptor signalling cascade.
Reactome; R-MMU-74752; Signaling by Insulin receptor.
Reactome; R-MMU-77387; Insulin receptor recycling.
BioGRID-ORCS; 16337; 0 hits in 12 CRISPR screens.
ChiTaRS; Insr; mouse.
EvolutionaryTrace; P15208; -.
PRO; PR:P15208; -.
Proteomes; UP000000589; Chromosome 8.
RNAct; P15208; protein.
Bgee; ENSMUSG00000005534; Expressed in quadriceps femoris and 241 other tissues.
ExpressionAtlas; P15208; baseline and differential.
Genevisible; P15208; MM.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005901; C:caveola; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0032590; C:dendrite membrane; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0005899; C:insulin receptor complex; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0031981; C:nuclear lumen; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0060417; C:yolk; ISO:MGI.
GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; ISO:MGI.
GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0038024; F:cargo receptor activity; ISO:MGI.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0043559; F:insulin binding; ISS:UniProtKB.
GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB.
GO; GO:0005009; F:insulin-activated receptor activity; ISS:UniProtKB.
GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI.
GO; GO:0031995; F:insulin-like growth factor II binding; ISO:MGI.
GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
GO; GO:0031405; F:lipoic acid binding; ISO:MGI.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0051425; F:PTB domain binding; ISS:UniProtKB.
GO; GO:0005198; F:structural molecule activity; ISO:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI.
GO; GO:0030325; P:adrenal gland development; IGI:CACAO.
GO; GO:0097242; P:amyloid-beta clearance; ISO:MGI.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0097062; P:dendritic spine maintenance; ISO:MGI.
GO; GO:0008544; P:epidermis development; IMP:MGI.
GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
GO; GO:0003007; P:heart morphogenesis; ISO:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
GO; GO:0008584; P:male gonad development; IGI:CACAO.
GO; GO:0030238; P:male sex determination; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:2000252; P:negative regulation of feeding behavior; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:0032410; P:negative regulation of transporter activity; ISO:MGI.
GO; GO:1990535; P:neuron projection maintenance; ISO:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI.
GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISO:MGI.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0051446; P:positive regulation of meiotic cell cycle; IGI:CACAO.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISO:MGI.
GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI.
GO; GO:0060267; P:positive regulation of respiratory burst; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:CACAO.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
GO; GO:0045995; P:regulation of embryonic development; ISO:MGI.
GO; GO:2000194; P:regulation of female gonad development; IGI:CACAO.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
GO; GO:0019087; P:transformation of host cell by virus; ISO:MGI.
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; 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..27
CHAIN 28..748
/note="Insulin receptor subunit alpha"
/id="PRO_0000016693"
CHAIN 753..1372
/note="Insulin receptor subunit beta"
/id="PRO_0000016695"
TOPO_DOM 28..748
/note="Extracellular"
/evidence="ECO:0000305"
TOPO_DOM 753..946
/note="Extracellular"
/evidence="ECO:0000305"
TRANSMEM 947..967
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 968..1372
/note="Cytoplasmic"
/evidence="ECO:0000305"
DOMAIN 626..728
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 744..838
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 843..937
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1013..1288
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 1094..1100
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 1153..1154
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 735..743
/note="Insulin-binding"
/evidence="ECO:0000250"
REGION 986..989
/note="Important for interaction with IRS1, SHC1 and
STAT5B"
/evidence="ECO:0000250"
REGION 1351..1354
/note="PIK3R1 binding"
/evidence="ECO:0000250"
COMPBIAS 28..174
/note="Leu-rich"
ACT_SITE 1149
/note="Proton donor/acceptor"
/evidence="ECO:0000250"
BINDING 1023
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 1047
/note="ATP"
BINDING 1167
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SITE 66
/note="Insulin-binding"
/evidence="ECO:0000250"
MOD_RES 400
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 401
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 407
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 989
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1175
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1179
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1180
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1345
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
MOD_RES 1351
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P06213"
CARBOHYD 43
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 52
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 105
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 138
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 242
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 282
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 322
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 364
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 424
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 445
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770"
CARBOHYD 541
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 635
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 653
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 700
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 759
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 772
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 910
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 923
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 35..53
/evidence="ECO:0000250"
DISULFID 153..182
/evidence="ECO:0000250"
DISULFID 186..209
/evidence="ECO:0000250"
DISULFID 196..215
/evidence="ECO:0000250"
DISULFID 219..228
/evidence="ECO:0000250"
DISULFID 223..234
/evidence="ECO:0000250"
DISULFID 235..243
/evidence="ECO:0000250"
DISULFID 239..252
/evidence="ECO:0000250"
DISULFID 255..264
/evidence="ECO:0000250"
DISULFID 268..280
/evidence="ECO:0000250"
DISULFID 286..311
/evidence="ECO:0000250"
DISULFID 293..301
/evidence="ECO:0000250"
DISULFID 315..328
/evidence="ECO:0000250"
DISULFID 331..335
/evidence="ECO:0000250"
DISULFID 339..360
/evidence="ECO:0000250"
DISULFID 462..495
/evidence="ECO:0000250"
DISULFID 551
/note="Interchain"
/evidence="ECO:0000250"
DISULFID 676..889
/evidence="ECO:0000250"
DISULFID 815..824
/evidence="ECO:0000250"
MUTAGEN 989
/note="Y->F: Abolishes interaction with IRS1 but not with
IRS2."
/evidence="ECO:0000269|PubMed:10207032,
ECO:0000269|PubMed:8626379"
CONFLICT 1089
/note="T -> M (in Ref. 1; AAA39318)"
/evidence="ECO:0000305"
SEQUENCE 1372 AA; 155610 MW; B0FA7DBD2AD4646A CRC64;
MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL
QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL
VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE
ECGDVCPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL
GNCSEPDDPT KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG
CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS VTSAQELRGC
TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS YALVSLSFFR KLHLIRGETL
EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE
RNDIALKTNG DQASCENELL KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ
NVTEFDGQDA CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT
FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP NGNITHYLVY
WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN QSEYDDSASE CCSCPKTDSQ
ILKELEESSF RKTFEDYLHN VVFVPRPSRK RRSLEEVGNV TATTLTLPDF PNVSSTIVPT
SQEEHRPFEK VVNKESLVIS GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA
DDIVGPVTHE IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG
CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG PLIFVFLFSV
VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV YVPDEWEVPR EKITLLRELG
QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG FTCHHVVRLL
GVVSKGQPTL VVMELMAHGD LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL
NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD
GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN CPERLTDLMR
MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK APESEELEME FEDMENVPLD
RSSHCQREEA GGREGGSSLS IKRTYDEHIP YTHMNGGKKN GRVLTLPRSN PS


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 :