UniProtKB - P15208 (INSR_MOUSE)
Insulin receptor
Insr
Functioni
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).
By similarity1 PublicationCatalytic activityi
- EC:2.7.10.1PROSITE-ProRule annotation
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 66 | Insulin-bindingBy similarity | 1 | |
Binding sitei | 1023 | ATPPROSITE-ProRule annotation | 1 | |
Binding sitei | 1047 | ATP | 1 | |
Active sitei | 1149 | Proton donor/acceptorBy similarity | 1 | |
Binding sitei | 1167 | ATPPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1094 – 1100 | ATPPROSITE-ProRule annotation | 7 | |
Nucleotide bindingi | 1153 – 1154 | ATPPROSITE-ProRule annotation | 2 |
GO - Molecular functioni
- 3-phosphoinositide-dependent protein kinase binding Source: MGI
- amyloid-beta binding Source: MGI
- ATP binding Source: MGI
- cargo receptor activity Source: MGI
- GTP binding Source: MGI
- identical protein binding Source: MGI
- insulin-activated receptor activity Source: UniProtKB
- insulin binding Source: UniProtKB
- insulin-like growth factor I binding Source: MGI
- insulin-like growth factor II binding Source: MGI
- insulin-like growth factor receptor binding Source: MGI
- insulin receptor substrate binding Source: UniProtKB
- lipoic acid binding Source: MGI
- phosphatidylinositol 3-kinase binding Source: UniProtKB
- protein-containing complex binding Source: MGI
- protein domain specific binding Source: MGI
- protein kinase activity Source: MGI
- protein kinase binding Source: MGI
- protein phosphatase binding Source: MGI
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein tyrosine kinase activity Source: MGI
- PTB domain binding Source: UniProtKB
- structural molecule activity Source: MGI
- transmembrane receptor protein tyrosine kinase activity Source: GO_Central
GO - Biological processi
- activation of protein kinase activity Source: MGI
- activation of protein kinase B activity Source: MGI
- adrenal gland development Source: CACAO
- amyloid-beta clearance Source: MGI
- animal organ morphogenesis Source: MGI
- cellular response to growth factor stimulus Source: MGI
- cellular response to insulin stimulus Source: MGI
- dendritic spine maintenance Source: MGI
- epidermis development Source: MGI
- exocrine pancreas development Source: MGI
- glucose homeostasis Source: MGI
- G protein-coupled receptor signaling pathway Source: MGI
- heart morphogenesis Source: MGI
- insulin receptor signaling pathway Source: MGI
- male gonad development Source: CACAO
- male sex determination Source: MGI
- negative regulation of feeding behavior Source: MGI
- negative regulation of gene expression Source: MGI
- negative regulation of protein phosphorylation Source: MGI
- negative regulation of transporter activity Source: MGI
- neuron projection maintenance Source: MGI
- peptidyl-tyrosine autophosphorylation Source: MGI
- peptidyl-tyrosine phosphorylation Source: MGI
- positive regulation of cell migration Source: MGI
- positive regulation of cell population proliferation Source: MGI
- positive regulation of developmental growth Source: MGI
- positive regulation of glucose import Source: MGI
- positive regulation of glycogen biosynthetic process Source: BHF-UCL
- positive regulation of glycolytic process Source: MGI
- positive regulation of glycoprotein biosynthetic process Source: MGI
- positive regulation of kinase activity Source: GO_Central
- positive regulation of MAPK cascade Source: MGI
- positive regulation of MAP kinase activity Source: MGI
- positive regulation of meiotic cell cycle Source: CACAO
- positive regulation of mitotic nuclear division Source: MGI
- positive regulation of nitric oxide biosynthetic process Source: MGI
- positive regulation of phosphatidylinositol 3-kinase signaling Source: GO_Central
- positive regulation of phosphorylation Source: MGI
- positive regulation of protein-containing complex disassembly Source: MGI
- positive regulation of protein kinase B signaling Source: MGI
- positive regulation of protein phosphorylation Source: MGI
- positive regulation of receptor internalization Source: MGI
- positive regulation of respiratory burst Source: MGI
- positive regulation of transcription, DNA-templated Source: CACAO
- protein autophosphorylation Source: UniProtKB
- protein phosphorylation Source: MGI
- receptor-mediated endocytosis Source: MGI
- regulation of embryonic development Source: MGI
- regulation of female gonad development Source: CACAO
- regulation of hydrogen peroxide metabolic process Source: MGI
- regulation of transcription, DNA-templated Source: MGI
- response to nutrient levels Source: MGI
- response to tumor necrosis factor Source: MGI
- transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
- viral entry into host cell Source: MGI
Keywordsi
Molecular function | Kinase, Receptor, Transferase, Tyrosine-protein kinase |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.10.1, 3474 |
Reactomei | R-MMU-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-MMU-74713, IRS activation R-MMU-74749, Signal attenuation R-MMU-74751, Insulin receptor signalling cascade R-MMU-74752, Signaling by Insulin receptor R-MMU-77387, Insulin receptor recycling |
Names & Taxonomyi
Protein namesi | Recommended name: Insulin receptor (EC:2.7.10.1)Short name: IR Alternative name(s): CD_antigen: CD220 Cleaved into the following 2 chains: |
Gene namesi | Name:Insr |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:96575, Insr |
VEuPathDBi | HostDB:ENSMUSG00000005534 |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Single-pass type I membrane protein Curated
Endosome
- Recycling endosome membrane 1 Publication
- Late endosome 1 Publication
Lysosome
- Lysosome 1 Publication
Note: Binding of insulin to INSR induces internalization and lysosomal degradation of the receptor, a means for down-regulating 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.1 Publication
Cytosol
- cytosol Source: MGI
Endosome
- endosome Source: MGI
- late endosome Source: UniProtKB-SubCell
- recycling endosome membrane Source: UniProtKB-SubCell
Lysosome
- lysosome Source: UniProtKB-SubCell
Nucleus
- nuclear envelope Source: Ensembl
- nuclear lumen Source: Ensembl
- nucleus Source: MGI
Plasma Membrane
- caveola Source: MGI
- dendrite membrane Source: MGI
- external side of plasma membrane Source: MGI
- insulin receptor complex Source: MGI
- integral component of plasma membrane Source: MGI
- neuronal cell body membrane Source: MGI
- plasma membrane Source: MGI
Other locations
- axon Source: GO_Central
- cytoplasmic vesicle Source: MGI
- intracellular membrane-bounded organelle Source: MGI
- membrane Source: BHF-UCL
- neuronal cell body Source: MGI
- receptor complex Source: MGI
- synapse Source: MGI
- yolk Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 28 – 748 | ExtracellularCuratedAdd BLAST | 721 | |
Topological domaini | 753 – 946 | ExtracellularCuratedAdd BLAST | 194 | |
Transmembranei | 947 – 967 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 968 – 1372 | CytoplasmicCuratedAdd BLAST | 405 |
Keywords - Cellular componenti
Cell membrane, Endosome, Lysosome, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 989 | Y → F: Abolishes interaction with IRS1 but not with IRS2. 2 Publications | 1 |
Chemistry databases
ChEMBLi | CHEMBL3187 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 27 | Add BLAST | 27 | |
ChainiPRO_0000016693 | 28 – 748 | Insulin receptor subunit alphaAdd BLAST | 721 | |
ChainiPRO_0000016695 | 753 – 1372 | Insulin receptor subunit betaAdd BLAST | 620 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 35 ↔ 53 | By similarity | ||
Glycosylationi | 43 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 52 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 105 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 138 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 153 ↔ 182 | By similarity | ||
Disulfide bondi | 186 ↔ 209 | By similarity | ||
Disulfide bondi | 196 ↔ 215 | By similarity | ||
Disulfide bondi | 219 ↔ 228 | By similarity | ||
Disulfide bondi | 223 ↔ 234 | By similarity | ||
Disulfide bondi | 235 ↔ 243 | By similarity | ||
Disulfide bondi | 239 ↔ 252 | By similarity | ||
Glycosylationi | 242 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 255 ↔ 264 | By similarity | ||
Disulfide bondi | 268 ↔ 280 | By similarity | ||
Glycosylationi | 282 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 286 ↔ 311 | By similarity | ||
Disulfide bondi | 293 ↔ 301 | By similarity | ||
Disulfide bondi | 315 ↔ 328 | By similarity | ||
Glycosylationi | 322 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 331 ↔ 335 | By similarity | ||
Disulfide bondi | 339 ↔ 360 | By similarity | ||
Glycosylationi | 364 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 400 | PhosphoserineBy similarity | 1 | |
Modified residuei | 401 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 407 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 424 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 445 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 462 ↔ 495 | By similarity | ||
Glycosylationi | 541 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 551 | InterchainBy similarity | ||
Glycosylationi | 635 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 653 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 676 ↔ 889 | By similarity | ||
Glycosylationi | 700 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 759 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 772 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 815 ↔ 824 | By similarity | ||
Glycosylationi | 910 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 923 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 989 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
Modified residuei | 1175 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
Modified residuei | 1179 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
Modified residuei | 1180 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
Modified residuei | 1345 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
Modified residuei | 1351 | Phosphotyrosine; by autocatalysisBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
jPOSTi | P15208 |
MaxQBi | P15208 |
PaxDbi | P15208 |
PeptideAtlasi | P15208 |
PRIDEi | P15208 |
ProteomicsDBi | 267252 |
PTM databases
CarbonylDBi | P15208 |
GlyConnecti | 2393, 7 N-Linked glycans (4 sites) |
GlyGeni | P15208, 18 sites, 7 N-linked glycans (4 sites) |
iPTMneti | P15208 |
PhosphoSitePlusi | P15208 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000005534, Expressed in quadriceps femoris and 267 other tissues |
ExpressionAtlasi | P15208, baseline and differential |
Genevisiblei | P15208, MM |
Interactioni
Subunit structurei
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).
Interacts with LMBRD1 (PubMed:24078630).
By similarity2 PublicationsBinary interactionsi
P15208
With | #Exp. | IntAct |
---|---|---|
Cav1 [P49817] | 2 | EBI-6999015,EBI-1161338 |
Grb10 [Q60760] | 6 | EBI-6999015,EBI-861810 |
Trim72 [Q1XH17] | 2 | EBI-6999015,EBI-16034016 |
GO - Molecular functioni
- 3-phosphoinositide-dependent protein kinase binding Source: MGI
- identical protein binding Source: MGI
- insulin binding Source: UniProtKB
- insulin-like growth factor I binding Source: MGI
- insulin-like growth factor II binding Source: MGI
- insulin-like growth factor receptor binding Source: MGI
- insulin receptor substrate binding Source: UniProtKB
- phosphatidylinositol 3-kinase binding Source: UniProtKB
- protein domain specific binding Source: MGI
- protein kinase binding Source: MGI
- protein phosphatase binding Source: MGI
- PTB domain binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 200774, 28 interactors |
CORUMi | P15208 |
DIPi | DIP-41452N |
IntActi | P15208, 21 interactors |
MINTi | P15208 |
STRINGi | 10090.ENSMUSP00000088837 |
Chemistry databases
BindingDBi | P15208 |
Miscellaneous databases
RNActi | P15208, protein |
Structurei
3D structure databases
AlphaFoldDBi | P15208 |
BMRBi | P15208 |
SMRi | P15208 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P15208 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 626 – 728 | Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST | 103 | |
Domaini | 744 – 838 | Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST | 95 | |
Domaini | 843 – 937 | Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST | 95 | |
Domaini | 1013 – 1288 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 276 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 688 – 709 | DisorderedSequence analysisAdd BLAST | 22 | |
Regioni | 735 – 743 | Insulin-bindingBy similarity | 9 | |
Regioni | 986 – 989 | Important for interaction with IRS1, SHC1 and STAT5BBy similarity | 4 | |
Regioni | 1349 – 1372 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 1351 – 1354 | PIK3R1 bindingBy similarity | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG4258, Eukaryota |
GeneTreei | ENSGT00940000155404 |
HOGENOMi | CLU_000288_166_0_1 |
InParanoidi | P15208 |
OMAi | QYIPDDW |
PhylomeDBi | P15208 |
TreeFami | TF351636 |
Family and domain databases
CDDi | cd00063, FN3, 2 hits cd00064, FU, 1 hit |
Gene3Di | 2.60.40.10, 3 hits 3.80.20.20, 2 hits |
InterProi | View protein in InterPro IPR003961, FN3_dom IPR036116, FN3_sf IPR006211, Furin-like_Cys-rich_dom IPR006212, Furin_repeat IPR009030, Growth_fac_rcpt_cys_sf IPR013783, Ig-like_fold IPR040969, Insulin_TMD IPR011009, Kinase-like_dom_sf IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR000494, Rcpt_L-dom IPR036941, Rcpt_L-dom_sf 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 |
Pfami | View protein in Pfam PF00041, fn3, 1 hit PF00757, Furin-like, 1 hit PF17870, Insulin_TMD, 1 hit PF07714, PK_Tyr_Ser-Thr, 1 hit PF01030, Recep_L_domain, 2 hits |
PIRSFi | PIRSF000620, Insulin_receptor, 1 hit |
PRINTSi | PR00109, TYRKINASE |
SMARTi | View protein in SMART SM00060, FN3, 3 hits SM00261, FU, 1 hit SM00219, TyrKc, 1 hit |
SUPFAMi | SSF49265, SSF49265, 3 hits SSF56112, SSF56112, 1 hit SSF57184, SSF57184, 1 hit |
PROSITEi | View protein in 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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL
60 70 80 90 100
ENCSVIEGHL QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK
110 120 130 140 150
DLFPNLTVIR GSRLFFNYAL VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN
160 170 180 190 200
ELCYLATIDW SRILDSVEDN YIVLNKDDNE ECGDVCPGTA KGKTNCPATV
210 220 230 240 250
INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL GNCSEPDDPT
260 270 280 290 300
KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG
310 320 330 340 350
CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS
360 370 380 390 400
VTSAQELRGC TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS
410 420 430 440 450
YALVSLSFFR KLHLIRGETL EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ
460 470 480 490 500
GKLFFHYNPK LCLSEIHKME EVSGTKGRQE RNDIALKTNG DQASCENELL
510 520 530 540 550
KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ NVTEFDGQDA
560 570 580 590 600
CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT
610 620 630 640 650
FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP
660 670 680 690 700
NGNITHYLVY WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN
710 720 730 740 750
QSEYDDSASE CCSCPKTDSQ ILKELEESSF RKTFEDYLHN VVFVPRPSRK
760 770 780 790 800
RRSLEEVGNV TATTLTLPDF PNVSSTIVPT SQEEHRPFEK VVNKESLVIS
810 820 830 840 850
GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA DDIVGPVTHE
860 870 880 890 900
IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG
910 920 930 940 950
CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG
960 970 980 990 1000
PLIFVFLFSV VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV
1010 1020 1030 1040 1050
YVPDEWEVPR EKITLLRELG QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN
1060 1070 1080 1090 1100
ESASLRERIE FLNEASVMKG FTCHHVVRLL GVVSKGQPTL VVMELMAHGD
1110 1120 1130 1140 1150
LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL NAKKFVHRDL
1160 1170 1180 1190 1200
AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD
1210 1220 1230 1240 1250
GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN
1260 1270 1280 1290 1300
CPERLTDLMR MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK
1310 1320 1330 1340 1350
APESEELEME FEDMENVPLD RSSHCQREEA GGREGGSSLS IKRTYDEHIP
1360 1370
YTHMNGGKKN GRVLTLPRSN PS
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A140LI30 | A0A140LI30_MOUSE | Insulin receptor | Insr | 90 | Annotation score: | ||
B8Q3N4 | B8Q3N4_MOUSE | Insulin receptor | Insr | 224 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 1089 | T → M in AAA39318 (PubMed:2557333).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J05149 mRNA Translation: AAA39318.1 AC168068 Genomic DNA No translation available. M28869 Genomic DNA Translation: AAA39319.1 |
CCDSi | CCDS22059.1 |
PIRi | A34157 |
RefSeqi | NP_034698.2, NM_010568.3 |
Genome annotation databases
Ensembli | ENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534 |
GeneIDi | 16337 |
KEGGi | mmu:16337 |
UCSCi | uc009krc.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J05149 mRNA Translation: AAA39318.1 AC168068 Genomic DNA No translation available. M28869 Genomic DNA Translation: AAA39319.1 |
CCDSi | CCDS22059.1 |
PIRi | A34157 |
RefSeqi | NP_034698.2, NM_010568.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1LK2 | X-ray | 1.35 | P | 423-430 | [»] | |
AlphaFoldDBi | P15208 | |||||
BMRBi | P15208 | |||||
SMRi | P15208 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 200774, 28 interactors |
CORUMi | P15208 |
DIPi | DIP-41452N |
IntActi | P15208, 21 interactors |
MINTi | P15208 |
STRINGi | 10090.ENSMUSP00000088837 |
Chemistry databases
BindingDBi | P15208 |
ChEMBLi | CHEMBL3187 |
PTM databases
CarbonylDBi | P15208 |
GlyConnecti | 2393, 7 N-Linked glycans (4 sites) |
GlyGeni | P15208, 18 sites, 7 N-linked glycans (4 sites) |
iPTMneti | P15208 |
PhosphoSitePlusi | P15208 |
Proteomic databases
jPOSTi | P15208 |
MaxQBi | P15208 |
PaxDbi | P15208 |
PeptideAtlasi | P15208 |
PRIDEi | P15208 |
ProteomicsDBi | 267252 |
Protocols and materials databases
Antibodypediai | 3403, 2152 antibodies from 52 providers |
DNASUi | 16337 |
Genome annotation databases
Ensembli | ENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534 |
GeneIDi | 16337 |
KEGGi | mmu:16337 |
UCSCi | uc009krc.2, mouse |
Organism-specific databases
CTDi | 3643 |
MGIi | MGI:96575, Insr |
VEuPathDBi | HostDB:ENSMUSG00000005534 |
Phylogenomic databases
eggNOGi | KOG4258, Eukaryota |
GeneTreei | ENSGT00940000155404 |
HOGENOMi | CLU_000288_166_0_1 |
InParanoidi | P15208 |
OMAi | QYIPDDW |
PhylomeDBi | P15208 |
TreeFami | TF351636 |
Enzyme and pathway databases
BRENDAi | 2.7.10.1, 3474 |
Reactomei | R-MMU-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-MMU-74713, IRS activation R-MMU-74749, Signal attenuation R-MMU-74751, Insulin receptor signalling cascade R-MMU-74752, Signaling by Insulin receptor R-MMU-77387, Insulin receptor recycling |
Miscellaneous databases
BioGRID-ORCSi | 16337, 2 hits in 74 CRISPR screens |
ChiTaRSi | Insr, mouse |
EvolutionaryTracei | P15208 |
PROi | PR:P15208 |
RNActi | P15208, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000005534, Expressed in quadriceps femoris and 267 other tissues |
ExpressionAtlasi | P15208, baseline and differential |
Genevisiblei | P15208, MM |
Family and domain databases
CDDi | cd00063, FN3, 2 hits cd00064, FU, 1 hit |
Gene3Di | 2.60.40.10, 3 hits 3.80.20.20, 2 hits |
InterProi | View protein in InterPro IPR003961, FN3_dom IPR036116, FN3_sf IPR006211, Furin-like_Cys-rich_dom IPR006212, Furin_repeat IPR009030, Growth_fac_rcpt_cys_sf IPR013783, Ig-like_fold IPR040969, Insulin_TMD IPR011009, Kinase-like_dom_sf IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR000494, Rcpt_L-dom IPR036941, Rcpt_L-dom_sf 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 |
Pfami | View protein in Pfam PF00041, fn3, 1 hit PF00757, Furin-like, 1 hit PF17870, Insulin_TMD, 1 hit PF07714, PK_Tyr_Ser-Thr, 1 hit PF01030, Recep_L_domain, 2 hits |
PIRSFi | PIRSF000620, Insulin_receptor, 1 hit |
PRINTSi | PR00109, TYRKINASE |
SMARTi | View protein in SMART SM00060, FN3, 3 hits SM00261, FU, 1 hit SM00219, TyrKc, 1 hit |
SUPFAMi | SSF49265, SSF49265, 3 hits SSF56112, SSF56112, 1 hit SSF57184, SSF57184, 1 hit |
PROSITEi | View protein in 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | INSR_MOUSE | |
Accessioni | P15208Primary (citable) accession number: P15208 Secondary accession number(s): F8VPU4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | October 3, 2012 | |
Last modified: | May 25, 2022 | |
This is version 227 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human and mouse protein kinases
Human and mouse protein kinases: classification and index - MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families