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Protein

Insulin receptor

Gene

Insr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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). Interacts with PTPRF (By similarity). Interacts with ATIC; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling netwok regulating INSR autophosphorylation and endocytosis (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei66Insulin-bindingBy similarity1
Binding sitei1023ATPPROSITE-ProRule annotation1
Binding sitei1047ATP1
Active sitei1149Proton donor/acceptorBy similarity1
Binding sitei1167ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1094 – 1100ATPPROSITE-ProRule annotation7
Nucleotide bindingi1153 – 1154ATPPROSITE-ProRule annotation2

GO - Molecular functioni

GO - Biological processi

  • activation of MAPK activity Source: MGI
  • activation of protein kinase activity Source: MGI
  • activation of protein kinase B activity Source: MGI
  • adrenal gland development Source: CACAO
  • animal organ morphogenesis Source: MGI
  • cellular response to growth factor stimulus Source: MGI
  • cellular response to insulin stimulus 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
  • peptidyl-tyrosine autophosphorylation Source: MGI
  • peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of developmental growth Source: MGI
  • positive regulation of DNA replication 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 MAPK cascade 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 protein kinase B signaling Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of respiratory burst Source: MGI
  • positive regulation of transcription, DNA-templated Source: CACAO
  • protein autophosphorylation Source: UniProtKB
  • protein heterotetramerization Source: UniProtKB
  • regulation of embryonic development Source: MGI
  • regulation of female gonad development Source: CACAO
  • regulation of transcription, DNA-templated Source: MGI
  • transformation of host cell by virus Source: MGI
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.
ReactomeiR-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96575. Insr.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 748ExtracellularCuratedAdd BLAST721
Topological domaini753 – 946ExtracellularCuratedAdd BLAST194
Transmembranei947 – 967HelicalSequence analysisAdd BLAST21
Topological domaini968 – 1372CytoplasmicCuratedAdd BLAST405

GO - Cellular componenti

  • caveola Source: MGI
  • extracellular exosome Source: MGI
  • insulin receptor complex Source: MGI
  • integral component of plasma membrane Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • membrane Source: BHF-UCL
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi989Y → F: Abolishes interaction with IRS1 but not with IRS2. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL3187.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000001669328 – 748Insulin receptor subunit alphaAdd BLAST721
ChainiPRO_0000016695753 – 1372Insulin receptor subunit betaAdd BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 53By similarity
Glycosylationi43N-linked (GlcNAc...)Sequence analysis1
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi105N-linked (GlcNAc...)Sequence analysis1
Glycosylationi138N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi242N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi255 ↔ 264By similarity
Disulfide bondi268 ↔ 280By similarity
Glycosylationi282N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi286 ↔ 311By similarity
Disulfide bondi293 ↔ 301By similarity
Disulfide bondi315 ↔ 328By similarity
Glycosylationi322N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi331 ↔ 335By similarity
Disulfide bondi339 ↔ 360By similarity
Glycosylationi364N-linked (GlcNAc...)Sequence analysis1
Modified residuei400PhosphoserineBy similarity1
Modified residuei401PhosphotyrosineBy similarity1
Modified residuei407PhosphoserineBy similarity1
Glycosylationi424N-linked (GlcNAc...)Sequence analysis1
Glycosylationi445N-linked (GlcNAc...)2 Publications1
Disulfide bondi462 ↔ 495By similarity
Glycosylationi541N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi551InterchainBy similarity
Glycosylationi635N-linked (GlcNAc...)Sequence analysis1
Glycosylationi653N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi676 ↔ 889By similarity
Glycosylationi700N-linked (GlcNAc...)Sequence analysis1
Glycosylationi759N-linked (GlcNAc...)Sequence analysis1
Glycosylationi772N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi815 ↔ 824By similarity
Glycosylationi910N-linked (GlcNAc...)Sequence analysis1
Glycosylationi923N-linked (GlcNAc...)Sequence analysis1
Modified residuei989Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1175Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1179Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1180Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1345Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1351Phosphotyrosine; by autocatalysisBy similarity1

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.
PeptideAtlasiP15208.
PRIDEiP15208.

PTM databases

iPTMnetiP15208.
PhosphoSitePlusiP15208.

Expressioni

Gene expression databases

BgeeiENSMUSG00000005534.
CleanExiMM_INSR.
ExpressionAtlasiP15208. baseline and differential.
GenevisibleiP15208. 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).By similarity

Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200774. 22 interactors.
DIPiDIP-41452N.
IntActiP15208. 13 interactors.
MINTiMINT-1516207.
STRINGi10090.ENSMUSP00000088837.

Chemistry databases

BindingDBiP15208.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LK2X-ray1.35P423-430[»]
ProteinModelPortaliP15208.
SMRiP15208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15208.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini626 – 728Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST103
Domaini744 – 838Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini843 – 937Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST95
Domaini1013 – 1288Protein kinasePROSITE-ProRule annotationAdd BLAST276

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni735 – 743Insulin-bindingBy similarity9
Regioni986 – 989Important for interaction with IRS1, SHC1 and STAT5BBy similarity4
Regioni1351 – 1354PIK3R1 bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi28 – 174Leu-richAdd BLAST147

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

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP15208.
KOiK04527.
OMAiGAAGHLY.
OrthoDBiEOG091G00GE.
TreeFamiTF351636.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
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. 1 hit.
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.
SSF52058. SSF52058. 2 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)DescriptionActionsGraphical viewLength
Sequence conflicti1089T → M in AAA39318 (PubMed:2557333).Curated1

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.
CCDSiCCDS22059.1.
PIRiA34157.
RefSeqiNP_034698.2. NM_010568.3.
UniGeneiMm.268003.

Genome annotation databases

EnsembliENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.
GeneIDi16337.
KEGGimmu:16337.
UCSCiuc009krc.2. mouse.

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.
CCDSiCCDS22059.1.
PIRiA34157.
RefSeqiNP_034698.2. NM_010568.3.
UniGeneiMm.268003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LK2X-ray1.35P423-430[»]
ProteinModelPortaliP15208.
SMRiP15208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200774. 22 interactors.
DIPiDIP-41452N.
IntActiP15208. 13 interactors.
MINTiMINT-1516207.
STRINGi10090.ENSMUSP00000088837.

Chemistry databases

BindingDBiP15208.
ChEMBLiCHEMBL3187.

PTM databases

iPTMnetiP15208.
PhosphoSitePlusiP15208.

Proteomic databases

MaxQBiP15208.
PaxDbiP15208.
PeptideAtlasiP15208.
PRIDEiP15208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.
GeneIDi16337.
KEGGimmu:16337.
UCSCiuc009krc.2. mouse.

Organism-specific databases

CTDi3643.
MGIiMGI:96575. Insr.

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP15208.
KOiK04527.
OMAiGAAGHLY.
OrthoDBiEOG091G00GE.
TreeFamiTF351636.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-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

ChiTaRSiInsr. mouse.
EvolutionaryTraceiP15208.
PROiP15208.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005534.
CleanExiMM_INSR.
ExpressionAtlasiP15208. baseline and differential.
GenevisibleiP15208. MM.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
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. 1 hit.
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.
SSF52058. SSF52058. 2 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.
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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: November 30, 2016
This is version 189 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.