P15208 (INSR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Insulin receptor
Short name=IR
EC=2.7.10.1

Alternative name(s):
CD_antigen=CD220

Cleaved into the following 2 chains:

1. Insulin receptor subunit alpha
2. Insulin receptor subunit beta

Gene names

Name:

Insr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.8 Ref.13
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.
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 component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from electronic annotation. Source: Compara activation of protein kinase B activity Inferred from electronic annotation. Source: Compara cellular response to growth factor stimulus Inferred from direct assay PubMed 19744960. Source: MGI exocrine pancreas development Inferred from mutant phenotype PubMed 12101187. Source: MGI glucose homeostasis Inferred from electronic annotation. Source: Compara heart morphogenesis Inferred from electronic annotation. Source: Compara male sex determination Inferred from mutant phenotype PubMed 14628051. Source: MGI organ morphogenesis Inferred from mutant phenotype PubMed 12101187. Source: MGI peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of developmental growth Inferred from electronic annotation. Source: Compara positive regulation of glycogen biosynthetic process Inferred from mutant phenotype PubMed 20032056. Source: BHF-UCL positive regulation of glycolysis Inferred from electronic annotation. Source: Compara positive regulation of mitosis Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of respiratory burst Inferred from electronic annotation. Source: Compara 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: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara transformation of host cell by virus Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from direct assay PubMed 16513830. Source: MGI insulin receptor complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: Compara 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 receptor signaling protein tyrosine kinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27
	Chain	28 – 748	721	Insulin receptor subunit alpha		PRO_0000016693
	Chain	753 – 1372	620	Insulin receptor subunit beta		PRO_0000016695
Regions
	Topological domain	28 – 748	721	Extracellular Probable
	Topological domain	753 – 946	194	Extracellular Probable
	Transmembrane	947 – 967	21	Helical; Potential
	Topological domain	968 – 1372	405	Cytoplasmic Probable
	Domain	624 – 697	74	Fibronectin type-III 1
	Domain	747 – 832	86	Fibronectin type-III 2
	Domain	840 – 936	97	Fibronectin type-III 3
	Domain	1013 – 1288	276	Protein kinase
	Nucleotide binding	1094 – 1100	7	ATP By similarity
	Nucleotide binding	1153 – 1154	2	ATP By similarity
	Region	735 – 743	9	Insulin-binding By similarity
	Region	986 – 989	4	Important for interaction with IRS1, SHC1 and STAT5B By similarity
	Region	1351 – 1354	4	PIK3R1 binding By similarity
	Compositional bias	28 – 174	147	Leu-rich
Sites
	Active site	1149	1	Proton donor/acceptor By similarity
	Binding site	1023	1	ATP By similarity
	Binding site	1047	1	ATP
	Binding site	1167	1	ATP By similarity
	Site	66	1	Insulin-binding By similarity
Amino acid modifications
	Modified residue	400	1	Phosphoserine By similarity
	Modified residue	401	1	Phosphotyrosine By similarity
	Modified residue	407	1	Phosphoserine By similarity
	Modified residue	989	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1175	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1179	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1180	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1345	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1351	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	43	1	N-linked (GlcNAc...) Potential
	Glycosylation	52	1	N-linked (GlcNAc...) Potential
	Glycosylation	105	1	N-linked (GlcNAc...) Potential
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	282	1	N-linked (GlcNAc...) Potential
	Glycosylation	322	1	N-linked (GlcNAc...) Potential
	Glycosylation	364	1	N-linked (GlcNAc...) Potential
	Glycosylation	424	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Ref.11 Ref.12
	Glycosylation	541	1	N-linked (GlcNAc...) Potential
	Glycosylation	635	1	N-linked (GlcNAc...) Potential
	Glycosylation	653	1	N-linked (GlcNAc...) Potential
	Glycosylation	700	1	N-linked (GlcNAc...) Potential
	Glycosylation	759	1	N-linked (GlcNAc...) Potential
	Glycosylation	772	1	N-linked (GlcNAc...) Potential
	Glycosylation	910	1	N-linked (GlcNAc...) Potential
	Glycosylation	923	1	N-linked (GlcNAc...) Potential
	Disulfide bond	35 ↔ 53		By similarity
	Disulfide bond	153 ↔ 182		By similarity
	Disulfide bond	186 ↔ 209		By similarity
	Disulfide bond	196 ↔ 215		By similarity
	Disulfide bond	219 ↔ 228		By similarity
	Disulfide bond	223 ↔ 234		By similarity
	Disulfide bond	235 ↔ 243		By similarity
	Disulfide bond	239 ↔ 252		By similarity
	Disulfide bond	255 ↔ 264		By similarity
	Disulfide bond	268 ↔ 280		By similarity
	Disulfide bond	286 ↔ 311		By similarity
	Disulfide bond	293 ↔ 301		By similarity
	Disulfide bond	315 ↔ 328		By similarity
	Disulfide bond	331 ↔ 335		By similarity
	Disulfide bond	339 ↔ 360		By similarity
	Disulfide bond	462 ↔ 495		By similarity
	Disulfide bond	551		Interchain By similarity
	Disulfide bond	676 ↔ 889		By similarity
	Disulfide bond	815 ↔ 824		By similarity
Experimental info
	Mutagenesis	989	1	Y → F: Abolishes interaction with IRS1 but not with IRS2. Ref.4 Ref.6
	Sequence conflict	1089	1	T → M in AAA39318. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15208 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: B0FA7DBD2AD4646A	FASTA	1,372	155,610
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[9]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1179, MASS SPECTROMETRY. Tissue: Mast cell.
[10]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1179, MASS SPECTROMETRY. Tissue: Brain.
[11]	"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, MASS SPECTROMETRY. Tissue: Myoblast.
[12]	"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, MASS SPECTROMETRY.
[13]	"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.

IPI

IPI00128358.
IPI01026785.

PIR

A34157.

RefSeq

NP_034698.2. NM_010568.2.

UniGene

Mm.268003.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LK2	X-ray	1.35	P	423-430	[»]

ProteinModelPortal

P15208.

SMR

P15208. Positions 31-938, 998-1300.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41452N.

MINT

MINT-1516207.

PTM databases

PhosphoSite

P15208.

Proteomic databases

PaxDb

P15208.

PRIDE

P15208.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.

GeneID

16337.

KEGG

mmu:16337.

UCSC

uc009krc.2. mouse.

Organism-specific databases

CTD

3643.

MGI

MGI:96575. Insr.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00690000101688.

HOGENOM

HOG000038045.

HOVERGEN

HBG006134.

InParanoid

P15208.

KO

K04527.

OMA

DNCPERL.

OrthoDB

EOG48WC15.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Gene expression databases

CleanEx

MM_INSR.

Genevestigator

P15208.

GermOnline

ENSMUSG00000005534. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

IPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]

PIRSF

PIRSF000620. Insulin_receptor. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.
SSF57184. Grow_fac_recept. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS50853. 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]

ProtoNet

Search...

Other

BindingDB

P15208.

ChEMBL

CHEMBL3187.

ChiTaRS

INSR. mouse.

EvolutionaryTrace

P15208.

NextBio

289438.

SOURCE

Search...

Entry information

Entry name

INSR_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program