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P15208

- INSR_MOUSE

UniProt

P15208 - INSR_MOUSE

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Protein

Insulin receptor

Gene

Insr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 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).By similarity

Catalytic activityi

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

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei66 – 661Insulin-bindingBy similarity
Binding sitei1023 – 10231ATPPROSITE-ProRule annotation
Binding sitei1047 – 10471ATP
Active sitei1149 – 11491Proton donor/acceptorBy similarity
Binding sitei1167 – 11671ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1094 – 11007ATPPROSITE-ProRule annotation
Nucleotide bindingi1153 – 11542ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTP binding Source: Ensembl
  3. insulin-activated receptor activity Source: UniProtKB
  4. insulin binding Source: UniProtKB
  5. insulin receptor substrate binding Source: UniProtKB
  6. phosphatidylinositol 3-kinase binding Source: UniProtKB
  7. PTB domain binding Source: UniProtKB
  8. receptor signaling protein tyrosine kinase activity Source: Ensembl

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. activation of protein kinase B activity Source: Ensembl
  3. cellular response to growth factor stimulus Source: MGI
  4. epidermis development Source: MGI
  5. exocrine pancreas development Source: MGI
  6. glucose homeostasis Source: Ensembl
  7. G-protein coupled receptor signaling pathway Source: Ensembl
  8. heart morphogenesis Source: Ensembl
  9. insulin receptor signaling pathway Source: MGI
  10. male sex determination Source: MGI
  11. organ morphogenesis Source: MGI
  12. peptidyl-tyrosine autophosphorylation Source: MGI
  13. positive regulation of cell migration Source: Ensembl
  14. positive regulation of developmental growth Source: Ensembl
  15. positive regulation of DNA replication Source: Ensembl
  16. positive regulation of glycogen biosynthetic process Source: BHF-UCL
  17. positive regulation of glycolytic process Source: Ensembl
  18. positive regulation of mitosis Source: MGI
  19. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  20. positive regulation of protein kinase B signaling Source: Ensembl
  21. positive regulation of respiratory burst Source: Ensembl
  22. protein autophosphorylation Source: UniProtKB
  23. protein heterotetramerization Source: UniProtKB
  24. regulation of embryonic development Source: Ensembl
  25. regulation of transcription, DNA-templated Source: Ensembl
  26. transformation of host cell by virus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:96575. Insr.

Subcellular locationi

GO - Cellular componenti

  1. caveola Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. insulin receptor complex Source: Ensembl
  4. membrane Source: BHF-UCL
  5. plasma membrane Source: MGI
  6. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi989 – 9891Y → F: Abolishes interaction with IRS1 but not with IRS2. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 748721Insulin receptor subunit alphaPRO_0000016693Add
BLAST
Chaini753 – 1372620Insulin receptor subunit betaPRO_0000016695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 53By similarity
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi153 ↔ 182By similarity
Disulfide bondi186 ↔ 209By similarity
Disulfide bondi196 ↔ 215By similarity
Disulfide bondi219 ↔ 228By similarity
Disulfide bondi223 ↔ 234By similarity
Disulfide bondi235 ↔ 243By similarity
Disulfide bondi239 ↔ 252By similarity
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi255 ↔ 264By similarity
Disulfide bondi268 ↔ 280By similarity
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi286 ↔ 311By similarity
Disulfide bondi293 ↔ 301By similarity
Disulfide bondi315 ↔ 328By similarity
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi331 ↔ 335By similarity
Disulfide bondi339 ↔ 360By similarity
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei401 – 4011PhosphotyrosineBy similarity
Modified residuei407 – 4071PhosphoserineBy similarity
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi445 – 4451N-linked (GlcNAc...)2 Publications
Disulfide bondi462 ↔ 495By similarity
Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi551 – 551InterchainBy similarity
Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi653 – 6531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi676 ↔ 889By similarity
Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi815 ↔ 824By similarity
Glycosylationi910 – 9101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi923 – 9231N-linked (GlcNAc...)Sequence Analysis
Modified residuei989 – 9891Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1175 – 11751Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1179 – 11791Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1180 – 11801Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1345 – 13451Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1351 – 13511Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

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.By similarity1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP15208.
PaxDbiP15208.
PRIDEiP15208.

PTM databases

PhosphoSiteiP15208.

Expressioni

Gene expression databases

CleanExiMM_INSR.
ExpressionAtlasiP15208. baseline and differential.
GenevestigatoriP15208.

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Grb10Q607606EBI-6999015,EBI-861810

Protein-protein interaction databases

BioGridi200774. 13 interactions.
DIPiDIP-41452N.
IntActiP15208. 4 interactions.
MINTiMINT-1516207.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK2X-ray1.35P423-430[»]
ProteinModelPortaliP15208.
SMRiP15208. Positions 31-978, 999-1299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15208.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 748721ExtracellularCuratedAdd
BLAST
Topological domaini753 – 946194ExtracellularCuratedAdd
BLAST
Topological domaini968 – 1372405CytoplasmicCuratedAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei947 – 96721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini626 – 728103Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini744 – 83895Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini843 – 93795Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1013 – 1288276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni735 – 7439Insulin-bindingBy similarity
Regioni986 – 9894Important for interaction with IRS1, SHC1 and STAT5BBy similarity
Regioni1351 – 13544PIK3R1 bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 174147Leu-richAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP15208.
KOiK04527.
OMAiCPERVTD.
OrthoDBiEOG73RB9N.
TreeFamiTF351636.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR000494. 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]
PfamiPF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000620. Insulin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15208-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:1,372
Mass (Da):155,610
Last modified:October 3, 2012 - v2
Checksum:iB0FA7DBD2AD4646A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1089 – 10891T → M in AAA39318. (PubMed:2557333)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05149 mRNA. Translation: AAA39318.1.
AC168068 Genomic DNA. No translation available.
M28869 Genomic DNA. Translation: AAA39319.1.
CCDSiCCDS22059.1.
PIRiA34157.
RefSeqiNP_034698.2. NM_010568.2.
UniGeneiMm.268003.

Genome annotation databases

EnsembliENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.
GeneIDi16337.
KEGGimmu:16337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_010568.2.
UniGenei Mm.268003.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LK2 X-ray 1.35 P 423-430 [» ]
ProteinModelPortali P15208.
SMRi P15208. Positions 31-978, 999-1299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200774. 13 interactions.
DIPi DIP-41452N.
IntActi P15208. 4 interactions.
MINTi MINT-1516207.

Chemistry

BindingDBi P15208.
ChEMBLi CHEMBL3187.

PTM databases

PhosphoSitei P15208.

Proteomic databases

MaxQBi P15208.
PaxDbi P15208.
PRIDEi P15208.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000091291 ; ENSMUSP00000088837 ; ENSMUSG00000005534 .
GeneIDi 16337.
KEGGi mmu:16337.

Organism-specific databases

CTDi 3643.
MGIi MGI:96575. Insr.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000038045.
HOVERGENi HBG006134.
InParanoidi P15208.
KOi K04527.
OMAi CPERVTD.
OrthoDBi EOG73RB9N.
TreeFami TF351636.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.

Miscellaneous databases

ChiTaRSi INSR. mouse.
EvolutionaryTracei P15208.
NextBioi 289438.
PROi P15208.
SOURCEi Search...

Gene expression databases

CleanExi MM_INSR.
ExpressionAtlasi P15208. baseline and differential.
Genevestigatori P15208.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProi IPR000494. 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 ]
Pfami PF00041. fn3. 2 hits.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view ]
PIRSFi PIRSF000620. Insulin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiINSR_MOUSE
AccessioniPrimary (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: October 29, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3