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UniProtKB - P15208 (INSR_MOUSE)

Protein

Insulin receptor

Gene

Insr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 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).By similarity

Catalytic activityi

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

Activity 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-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:
Insulin receptor subunit alpha
Insulin receptor subunit beta
Gene namesi
Name:Insr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96575 Insr

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

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

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...) asparagineSequence analysis1
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi138N-linked (GlcNAc...) asparagineSequence 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...) asparagineSequence analysis1
Disulfide bondi255 ↔ 264By similarity
Disulfide bondi268 ↔ 280By similarity
Glycosylationi282N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi286 ↔ 311By similarity
Disulfide bondi293 ↔ 301By similarity
Disulfide bondi315 ↔ 328By similarity
Glycosylationi322N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi331 ↔ 335By similarity
Disulfide bondi339 ↔ 360By similarity
Glycosylationi364N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei400PhosphoserineBy similarity1
Modified residuei401PhosphotyrosineBy similarity1
Modified residuei407PhosphoserineBy similarity1
Glycosylationi424N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi445N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi462 ↔ 495By similarity
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi551InterchainBy similarity
Glycosylationi635N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi653N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi676 ↔ 889By similarity
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi759N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi772N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi815 ↔ 824By similarity
Glycosylationi910N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi923N-linked (GlcNAc...) asparagineSequence 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

CarbonylDBiP15208
iPTMnetiP15208
PhosphoSitePlusiP15208

Expressioni

Gene expression databases

BgeeiENSMUSG00000005534 Expressed in 242 organ(s), highest expression level in quadriceps femoris
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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi200774, 22 interactors
CORUMiP15208
DIPiDIP-41452N
IntActiP15208, 19 interactors
MINTiP15208
STRINGi10090.ENSMUSP00000088837

Chemistry databases

BindingDBiP15208

Structurei

3D structure databases

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4258 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118818
HOGENOMiHOG000038045
HOVERGENiHBG006134
InParanoidiP15208
KOiK04527
OMAiRHFTSYQ
OrthoDBiEOG091G00GE
TreeFamiTF351636

Family and domain databases

CDDicd00063 FN3, 2 hits
cd00064 FU, 1 hit
Gene3Di2.60.40.10, 2 hits
3.80.20.20, 2 hits
InterProiView 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
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
PfamiView protein in Pfam
PF00041 fn3, 1 hit
PF00757 Furin-like, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PIRSFiPIRSF000620 Insulin_receptor, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00060 FN3, 3 hits
SM00261 FU, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF49265 SSF49265, 3 hits
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView 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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B8Q3N4B8Q3N4_MOUSE
Insulin receptor
Insr
224Annotation score:
A0A140LI30A0A140LI30_MOUSE
Insulin receptor
Insr
90Annotation score:

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

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
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
CORUMiP15208
DIPiDIP-41452N
IntActiP15208, 19 interactors
MINTiP15208
STRINGi10090.ENSMUSP00000088837

Chemistry databases

BindingDBiP15208
ChEMBLiCHEMBL3187

PTM databases

CarbonylDBiP15208
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
OMAiRHFTSYQ
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
PROiPR:P15208
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005534 Expressed in 242 organ(s), highest expression level in quadriceps femoris
CleanExiMM_INSR
ExpressionAtlasiP15208 baseline and differential
GenevisibleiP15208 MM

Family and domain databases

CDDicd00063 FN3, 2 hits
cd00064 FU, 1 hit
Gene3Di2.60.40.10, 2 hits
3.80.20.20, 2 hits
InterProiView 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
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
PfamiView protein in Pfam
PF00041 fn3, 1 hit
PF00757 Furin-like, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PIRSFiPIRSF000620 Insulin_receptor, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00060 FN3, 3 hits
SM00261 FU, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF49265 SSF49265, 3 hits
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView 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
ProtoNetiSearch...

Entry informationi

Entry nameiINSR_MOUSE
AccessioniPrimary (citable) accession number: P15208
Secondary accession number(s): F8VPU4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 3, 2012
Last modified: November 7, 2018
This is version 206 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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