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P15208 (INSR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin receptor

Short name=IR
EC=2.7.10.1
Alternative name(s):
CD_antigen=CD220
Gene names
Name:Insr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 phosphotyrosines 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.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme 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.

Subunit structure

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. Ref.4 Ref.5 Ref.7 Ref.9 Ref.12

Subcellular location

Cell membrane; Single-pass type I membrane protein.

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.

Post-translational modification

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. Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 3 fibronectin type-III domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase B activity

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from direct assay PubMed 19744960. Source: MGI

epidermis development

Inferred from mutant phenotype PubMed 23906066. Source: MGI

exocrine pancreas development

Inferred from mutant phenotype PubMed 12101187. Source: MGI

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 12488434. Source: MGI

male sex determination

Inferred from mutant phenotype PubMed 14628051. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 12101187. Source: MGI

peptidyl-tyrosine autophosphorylation

Inferred from direct assay PubMed 10100151. Source: MGI

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of developmental growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of glycogen biosynthetic process

Inferred from mutant phenotype PubMed 20032056. Source: BHF-UCL

positive regulation of glycolytic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from mutant phenotype PubMed 23906066. Source: MGI

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of respiratory burst

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

transformation of host cell by virus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from direct assay PubMed 16513830. Source: MGI

insulin receptor complex

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay Ref.5. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 14562105PubMed 24078630. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: Ensembl

PTB domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

SH2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

insulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor substrate binding

Inferred from sequence or structural similarity. Source: UniProtKB

insulin-activated receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Grb10Q607606EBI-6999015,EBI-861810

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 748721Insulin receptor subunit alpha
PRO_0000016693
Chain753 – 1372620Insulin receptor subunit beta
PRO_0000016695

Regions

Topological domain28 – 748721Extracellular Probable
Topological domain753 – 946194Extracellular Probable
Transmembrane947 – 96721Helical; Potential
Topological domain968 – 1372405Cytoplasmic Probable
Domain626 – 728103Fibronectin type-III 1
Domain744 – 83895Fibronectin type-III 2
Domain843 – 93795Fibronectin type-III 3
Domain1013 – 1288276Protein kinase
Nucleotide binding1094 – 11007ATP By similarity
Nucleotide binding1153 – 11542ATP By similarity
Region735 – 7439Insulin-binding By similarity
Region986 – 9894Important for interaction with IRS1, SHC1 and STAT5B By similarity
Region1351 – 13544PIK3R1 binding By similarity
Compositional bias28 – 174147Leu-rich

Sites

Active site11491Proton donor/acceptor By similarity
Binding site10231ATP By similarity
Binding site10471ATP
Binding site11671ATP By similarity
Site661Insulin-binding By similarity

Amino acid modifications

Modified residue4001Phosphoserine By similarity
Modified residue4011Phosphotyrosine By similarity
Modified residue4071Phosphoserine By similarity
Modified residue9891Phosphotyrosine; by autocatalysis By similarity
Modified residue11751Phosphotyrosine; by autocatalysis By similarity
Modified residue11791Phosphotyrosine; by autocatalysis By similarity
Modified residue11801Phosphotyrosine; by autocatalysis By similarity
Modified residue13451Phosphotyrosine; by autocatalysis By similarity
Modified residue13511Phosphotyrosine; by autocatalysis By similarity
Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Ref.10 Ref.11
Glycosylation5411N-linked (GlcNAc...) Potential
Glycosylation6351N-linked (GlcNAc...) Potential
Glycosylation6531N-linked (GlcNAc...) Potential
Glycosylation7001N-linked (GlcNAc...) Potential
Glycosylation7591N-linked (GlcNAc...) Potential
Glycosylation7721N-linked (GlcNAc...) Potential
Glycosylation9101N-linked (GlcNAc...) Potential
Glycosylation9231N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 53 By similarity
Disulfide bond153 ↔ 182 By similarity
Disulfide bond186 ↔ 209 By similarity
Disulfide bond196 ↔ 215 By similarity
Disulfide bond219 ↔ 228 By similarity
Disulfide bond223 ↔ 234 By similarity
Disulfide bond235 ↔ 243 By similarity
Disulfide bond239 ↔ 252 By similarity
Disulfide bond255 ↔ 264 By similarity
Disulfide bond268 ↔ 280 By similarity
Disulfide bond286 ↔ 311 By similarity
Disulfide bond293 ↔ 301 By similarity
Disulfide bond315 ↔ 328 By similarity
Disulfide bond331 ↔ 335 By similarity
Disulfide bond339 ↔ 360 By similarity
Disulfide bond462 ↔ 495 By similarity
Disulfide bond551Interchain By similarity
Disulfide bond676 ↔ 889 By similarity
Disulfide bond815 ↔ 824 By similarity

Experimental info

Mutagenesis9891Y → F: Abolishes interaction with IRS1 but not with IRS2. Ref.4 Ref.6
Sequence conflict10891T → M in AAA39318. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15208 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: B0FA7DBD2AD4646A

FASTA1,372155,610
        10         20         30         40         50         60 
MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL 

        70         80         90        100        110        120 
QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL 

       130        140        150        160        170        180 
VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE 

       190        200        210        220        230        240 
ECGDVCPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL 

       250        260        270        280        290        300 
GNCSEPDDPT KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG 

       310        320        330        340        350        360 
CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS VTSAQELRGC 

       370        380        390        400        410        420 
TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS YALVSLSFFR KLHLIRGETL 

       430        440        450        460        470        480 
EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE 

       490        500        510        520        530        540 
RNDIALKTNG DQASCENELL KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ 

       550        560        570        580        590        600 
NVTEFDGQDA CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT 

       610        620        630        640        650        660 
FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP NGNITHYLVY 

       670        680        690        700        710        720 
WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN QSEYDDSASE CCSCPKTDSQ 

       730        740        750        760        770        780 
ILKELEESSF RKTFEDYLHN VVFVPRPSRK RRSLEEVGNV TATTLTLPDF PNVSSTIVPT 

       790        800        810        820        830        840 
SQEEHRPFEK VVNKESLVIS GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA 

       850        860        870        880        890        900 
DDIVGPVTHE IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG 

       910        920        930        940        950        960 
CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG PLIFVFLFSV 

       970        980        990       1000       1010       1020 
VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV YVPDEWEVPR EKITLLRELG 

      1030       1040       1050       1060       1070       1080 
QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG FTCHHVVRLL 

      1090       1100       1110       1120       1130       1140 
GVVSKGQPTL VVMELMAHGD LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL 

      1150       1160       1170       1180       1190       1200 
NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD 

      1210       1220       1230       1240       1250       1260 
GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN CPERLTDLMR 

      1270       1280       1290       1300       1310       1320 
MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK APESEELEME FEDMENVPLD 

      1330       1340       1350       1360       1370 
RSSHCQREEA GGREGGSSLS IKRTYDEHIP YTHMNGGKKN GRVLTLPRSN PS 

« Hide

References

« Hide 'large scale' references
[1]"Substrate phosphorylation catalyzed by the insulin receptor tyrosine kinase. Kinetic correlation to autophosphorylation of specific sites in the beta subunit."
Flores-Riveros J.R., Sibley E., Kastelic T., Lane M.D.
J. Biol. Chem. 264:21557-21572(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Characterization of the mouse insulin receptor gene promoter."
Sibley E., Kastelic T., Kelly T.J., Lane M.D.
Proc. Natl. Acad. Sci. U.S.A. 86:9732-9736(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[4]"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."
Sawka-Verhelle D., Tartare-Deckert S., White M.F., Van Obberghen E.
J. Biol. Chem. 271:5980-5983(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRS1 AND IRS2, MUTAGENESIS OF TYR-989.
[5]"A novel, multifunctional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes."
Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.
Mol. Cell. Biol. 18:872-879(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORBS1.
[6]"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."
Chaika O.V., Chaika N., Volle D.J., Hayashi H., Ebina Y., Wang L.M., Pierce J.H., Lewis R.E.
J. Biol. Chem. 274:12075-12080(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-989.
[7]"SOCS-3 is an insulin-induced negative regulator of insulin signaling."
Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D., Van Obberghen E.
J. Biol. Chem. 275:15985-15991(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SOCS3.
[8]"Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP."
Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A., Meng T.C., Tonks N.K., Tiganis T.
Mol. Cell. Biol. 23:2096-2108(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
[9]"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."
Ueki K., Kondo T., Kahn C.R.
Mol. Cell. Biol. 24:5434-5446(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SOCS1 AND SOCS3.
[10]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445.
Tissue: Myoblast.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445.
[12]"Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance."
Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J., Pei G.
Nature 457:1146-1149(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05149 mRNA. Translation: AAA39318.1.
AC168068 Genomic DNA. No translation available.
M28869 Genomic DNA. Translation: AAA39319.1.
CCDSCCDS22059.1.
PIRA34157.
RefSeqNP_034698.2. NM_010568.2.
UniGeneMm.268003.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK2X-ray1.35P423-430[»]
ProteinModelPortalP15208.
SMRP15208. Positions 31-938, 998-1300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200774. 13 interactions.
DIPDIP-41452N.
IntActP15208. 4 interactions.
MINTMINT-1516207.

Chemistry

BindingDBP15208.
ChEMBLCHEMBL3187.

PTM databases

PhosphoSiteP15208.

Proteomic databases

MaxQBP15208.
PaxDbP15208.
PRIDEP15208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.
GeneID16337.
KEGGmmu:16337.

Organism-specific databases

CTD3643.
MGIMGI:96575. Insr.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117239.
HOGENOMHOG000038045.
HOVERGENHBG006134.
InParanoidP15208.
KOK04527.
OMACPERVTD.
OrthoDBEOG73RB9N.
TreeFamTF351636.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressP15208.
CleanExMM_INSR.
GenevestigatorP15208.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProIPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000620. Insulin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINSR. mouse.
EvolutionaryTraceP15208.
NextBio289438.
PROP15208.
SOURCESearch...

Entry information

Entry nameINSR_MOUSE
AccessionPrimary (citable) accession number: P15208
Secondary accession number(s): F8VPU4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot