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P15127

- INSR_RAT

UniProt

P15127 - INSR_RAT

Protein

Insulin receptor

Gene

Insr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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
    Sitei65 – 651Insulin-bindingBy similarity
    Binding sitei1034 – 10341ATPPROSITE-ProRule annotation
    Binding sitei1058 – 10581ATPPROSITE-ProRule annotation
    Active sitei1160 – 11601Proton donor/acceptorBy similarity
    Binding sitei1178 – 11781ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1105 – 11117ATPPROSITE-ProRule annotation
    Nucleotide bindingi1164 – 11652ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-phosphoinositide-dependent protein kinase binding Source: RGD
    2. ATP binding Source: UniProtKB-KW
    3. insulin-activated receptor activity Source: RGD
    4. insulin binding Source: RGD
    5. insulin receptor substrate binding Source: RGD
    6. lipoic acid binding Source: RGD
    7. protein binding Source: IntAct
    8. protein complex binding Source: RGD
    9. protein domain specific binding Source: RGD
    10. protein kinase activity Source: RGD
    11. protein kinase binding Source: RGD
    12. protein phosphatase binding Source: RGD
    13. protein tyrosine kinase activity Source: RGD

    GO - Biological processi

    1. fat cell differentiation Source: RGD
    2. glucose homeostasis Source: RGD
    3. insulin receptor signaling pathway Source: RGD
    4. negative regulation of gene expression Source: RGD
    5. negative regulation of protein phosphorylation Source: RGD
    6. negative regulation of transporter activity Source: RGD
    7. peptidyl-tyrosine phosphorylation Source: RGD
    8. positive regulation of glycoprotein biosynthetic process Source: RGD
    9. positive regulation of phosphorylation Source: BHF-UCL
    10. protein autophosphorylation Source: RGD
    11. protein heterotetramerization Source: RGD
    12. protein phosphorylation Source: RGD
    13. regulation of hydrogen peroxide metabolic process Source: RGD
    14. response to activity Source: RGD
    15. response to estradiol Source: RGD
    16. response to ethanol Source: RGD
    17. response to glucocorticoid Source: RGD
    18. response to glucose Source: BHF-UCL
    19. response to hormone Source: RGD
    20. response to insulin Source: BHF-UCL
    21. response to manganese ion Source: RGD
    22. response to nutrient levels Source: RGD
    23. response to testosterone Source: RGD
    24. response to tumor necrosis factor Source: RGD
    25. response to vitamin D Source: RGD

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 5301.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2917. Insr.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. endosome Source: RGD
    3. integral component of membrane Source: UniProtKB-KW
    4. intracellular membrane-bounded organelle Source: RGD
    5. nucleus Source: RGD
    6. plasma membrane Source: RGD
    7. synapse Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 759733Insulin receptor subunit alphaPRO_0000016696Add
    BLAST
    Chaini764 – 1383620Insulin receptor subunit betaPRO_0000016698Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 52By similarity
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi152 ↔ 181By similarity
    Disulfide bondi185 ↔ 208By similarity
    Disulfide bondi195 ↔ 214By similarity
    Disulfide bondi218 ↔ 227By similarity
    Disulfide bondi222 ↔ 233By similarity
    Disulfide bondi234 ↔ 242By similarity
    Disulfide bondi238 ↔ 251By similarity
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi254 ↔ 263By similarity
    Disulfide bondi267 ↔ 279By similarity
    Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi285 ↔ 310By similarity
    Disulfide bondi292 ↔ 300By similarity
    Disulfide bondi314 ↔ 327By similarity
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi330 ↔ 334By similarity
    Disulfide bondi338 ↔ 359By similarity
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Modified residuei399 – 3991PhosphoserineBy similarity
    Modified residuei400 – 4001PhosphotyrosineBy similarity
    Modified residuei406 – 4061PhosphoserineBy similarity
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi461 ↔ 494By similarity
    Glycosylationi540 – 5401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi550 – 550InterchainBy similarity
    Glycosylationi634 – 6341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi675 ↔ 900By similarity
    Glycosylationi699 – 6991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi770 – 7701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi921 – 9211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi934 – 9341N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1000 – 10001Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1186 – 11861Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1190 – 11901Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1191 – 11911Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1356 – 13561Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1362 – 13621Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated on tyrosine residues in response to insulin. Phosphorylation of Tyr-1000 is required for binding to IRS1, SHC1, and STAT5B. Dephosphorylated by PTPRE on Tyr-1000, Tyr-1186, Tyr-1190 and Tyr-1191 residues. Dephosphorylated by PTPRF and PTPN1. Dephosphorylated by PTPN2; down-regulates insulin-induced signaling.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP15127.
    PRIDEiP15127.

    PTM databases

    PhosphoSiteiP15127.

    Expressioni

    Gene expression databases

    GenevestigatoriP15127.

    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. Activated form of INSR interacts (via Tyr-1000) 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. Interacts (via the phosphorylated Tyr-1000), with SOCS3. Interacts (via the phosphorylated Tyr-1186, Tyr-1190, Tyr-1191) with SOCS1. Interacts with ARRB2 By similarity. 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. Interacts with PDPK1. Interacts (via Tyr-1191) with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop from dephosphorylation, but promotes dephosphorylation of Tyr-1000, this results in decreased interaction with, and phosphorylation of, IRS1. Interacts (via subunit alpha) with ENPP1 (via 485-599 AA); this interaction blocks autophosphorylation. Interacts with PTPRE; this interaction is dependent of Tyr-1186, Tyr-1190 and Tyr-1191 of the INSR. Interacts with STAT5B (via SH2 domain). Interacts with PTPRF By similarity. Interacts with GRB7. Interacts with CAV2 (tyrosine-phosphorylated form); the interaction is increased with 'Tyr-27'phosphorylation of CAV2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Jak2Q626892EBI-7472166,EBI-8656708

    Protein-protein interaction databases

    IntActiP15127. 5 interactions.
    MINTiMINT-1348005.

    Structurei

    3D structure databases

    ProteinModelPortaliP15127.
    SMRiP15127. Positions 30-949, 1009-1311.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 759733ExtracellularCuratedAdd
    BLAST
    Topological domaini764 – 957194ExtracellularCuratedAdd
    BLAST
    Topological domaini979 – 1383405CytoplasmicCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei958 – 97821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini625 – 727103Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini754 – 84895Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini854 – 94895Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1024 – 1299276Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni734 – 7429Insulin-bindingBy similarity
    Regioni997 – 10004Important for interaction with IRS1, SHC1 and STAT5B
    Regioni1362 – 13654PIK3R1 bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi27 – 173147Leu-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.
    HOGENOMiHOG000038045.
    HOVERGENiHBG006134.
    InParanoidiP15127.
    PhylomeDBiP15127.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P15127-1) [UniParc]FASTAAdd to Basket

    Also known as: RIR-B

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGSGRGCETT AVPLLMAVAV AGGTAGHLYP GEVCPGMDIR NNLTRLHELE     50
    NCSVIEGHLQ ILLMFKTRPE DFRDLSFPKL IMITDYLLLF RVYGLESLKD 100
    LFPNLTVIRG SRLFFNYALV IFEMVHLKEL GLYNLMNITR GSVRIEKNNE 150
    LCYLATIDWS RILDYVEDNY IVLNKDDNEE CGDVCPGTAK GKTNCPATVI 200
    NGQFVERCWT HSHCQKVCPT ICKSHGCTAE GLCCHKECLG NCSEPDDPTK 250
    CVACRNFYLD GQCVETCPPP YYHFQDWRCV NFSFCQDLHY KCRNSRKPGC 300
    HQYVIHNNKC IPECPSGYTM NSSNLMCTPC LGPCPKVCQI LEGEKTIDSV 350
    TSAQELRGCT VINGSLIINI RGGNNLAAEL EANLGLIEEI SGFLKIRRSY 400
    ALVSLSFFRK LHLIRGETLE IGNYSFYALD NQNLRQLWDW NKHNLTITQG 450
    KLFFHYNPKL CLSEIHKMEE VSGTKGRQER NDIALKTNGD QASCENELLK 500
    FSFIRTSFDK ILLRWEPYWP PDFRDLLGFM LFYKEAPYQN VTEFDGQDAC 550
    GSNSWTVVDI DPPQRSNDPK SQTPSHPGWL MRGLKPWTQY AIFVKTLVTF 600
    SDERRTYGAK SDIIYVQTDA TNPSVPLDPI SVSNSSSQII LKWKPPSDPN 650
    GNITHYLVYW ERQAEDSELF ELDYCLKGLK LPSRTWSPPF ESDDSQKHNQ 700
    SEYDDSASEC CSCPKTDSQI LKELEESSFR KTFEDYLHNV VFVPRKTSSG 750
    NGAEDTRPSR KRRSLEEVGN VTATTPTLPD FPNISSTIAP TSHEEHRPFE 800
    KVVNKESLVI SGLRHFTGYR IELQACNQDS PEERSGVAAY VSARTMPEAK 850
    ADDIVGPVTH EIFENNVVHL MWQEPKEPNG LIVLYEVSYR RYGDEELHLC 900
    VSRKHFALER GCRLRGLSPG NYSVRVRATS LAGNGSWTEP TYFYVTDYLD 950
    VPSNIAKIII GPLIFVFLFS VVIGSIYLFL RKRQPDGPMG PLYASSNPEY 1000
    LSASDVFPSS VYVPDEWEVP REKITLLREL GQGSFGMVYE GNAKDIIKGE 1050
    VETRVAVKTV NESASLRERI EFLNEASVMK GFTCHHVVRL LGVVSKGQPT 1100
    LVVMELMAHG DLKSHLRSLR PDAENNPGRP PPTLQEMIQM TAEIADGMAY 1150
    LNAKKFVHRD LAARNCMVAH DFTVKIGDFG MTRDIYETDY YRKGGKGLLP 1200
    VRWMSPESLK DGVFTASSDM WSFGVVLWEI TSLAEQPYQG LSNEQVLKFV 1250
    MDGGYLDPPD NCPERLTDLM RMCWQFNPKM RPTFLEIVNL LKDDLHPSFP 1300
    EVSFFYSEEN KAPESEELEM EFEDMENVPL DRSSHCQREE AGCREGGSSL 1350
    SIKRTYDEHI PYTHMNGGKK NGRVLTLPRS NPS 1383
    Length:1,383
    Mass (Da):156,757
    Last modified:April 1, 1990 - v1
    Checksum:i4B919566902A944A
    GO
    Isoform Short (identifier: P15127-2) [UniParc]FASTAAdd to Basket

    Also known as: RIR-A

    The sequence of this isoform differs from the canonical sequence as follows:
         746-757: Missing.

    Show »
    Length:1,371
    Mass (Da):155,553
    Checksum:i146D5FFDA1EF415D
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei746 – 75712Missing in isoform Short. CuratedVSP_036680Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29014 mRNA. Translation: AAA41441.1.
    AF005776 Genomic DNA. Translation: AAB61414.1.
    AF005777 Genomic DNA. Translation: AAB61415.1.
    AH004882 Genomic DNA. Translation: AAB38967.1.
    AH004883 Genomic DNA. Translation: AAB38968.1.
    U80633 Genomic DNA. Translation: AAB38746.1.
    PIRiA36080.
    UniGeneiRn.9876.

    Genome annotation databases

    UCSCiRGD:2917. rat. [P15127-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29014 mRNA. Translation: AAA41441.1 .
    AF005776 Genomic DNA. Translation: AAB61414.1 .
    AF005777 Genomic DNA. Translation: AAB61415.1 .
    AH004882 Genomic DNA. Translation: AAB38967.1 .
    AH004883 Genomic DNA. Translation: AAB38968.1 .
    U80633 Genomic DNA. Translation: AAB38746.1 .
    PIRi A36080.
    UniGenei Rn.9876.

    3D structure databases

    ProteinModelPortali P15127.
    SMRi P15127. Positions 30-949, 1009-1311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P15127. 5 interactions.
    MINTi MINT-1348005.

    Chemistry

    BindingDBi P15127.
    ChEMBLi CHEMBL5486.

    PTM databases

    PhosphoSitei P15127.

    Proteomic databases

    PaxDbi P15127.
    PRIDEi P15127.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2917. rat. [P15127-1 ]

    Organism-specific databases

    RGDi 2917. Insr.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000038045.
    HOVERGENi HBG006134.
    InParanoidi P15127.
    PhylomeDBi P15127.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 5301.

    Miscellaneous databases

    NextBioi 13948910.
    PROi P15127.

    Gene expression databases

    Genevestigatori P15127.

    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

    1. "The rat insulin receptor: primary structure and conservation of tissue-specific alternative messenger RNA splicing."
      Goldstein B.J., Dudley A.L.
      Mol. Endocrinol. 4:235-244(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE SPLICING (ISOFORM SHORT).
    2. Liu Y., Tam J.W.O.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 731-756; 758-819; 969-994 AND 1119-1177.
      Strain: Sprague-Dawley.
    3. "Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2."
      Kasus-Jacobi A., Bereziat V., Perdereau D., Girard J., Burnol A.F.
      Oncogene 19:2052-2059(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB7.
    4. "Insulin and IGF-I action on insulin receptors, IGF-I receptors, and hybrid insulin/IGF-I receptors in vascular smooth muscle cells."
      Johansson G.S., Arnqvist H.J.
      Am. J. Physiol. 291:E1124-E1130(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH IGF1R.
    5. "Identification of pY19-caveolin-2 as a positive regulator of insulin-stimulated actin cytoskeleton-dependent mitogenesis."
      Kwon H., Jeong K., Pak Y.
      J. Cell. Mol. Med. 13:1549-1564(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV2.

    Entry informationi

    Entry nameiINSR_RAT
    AccessioniPrimary (citable) accession number: P15127
    Secondary accession number(s): P97681
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3