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P24062

- IGF1R_RAT

UniProt

P24062 - IGF1R_RAT

Protein

Insulin-like growth factor 1 receptor

Gene

Igf1r

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R By similarity. When present in a hybrid receptor with INSR, 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 by autophosphorylation at Tyr-1162, Tyr-1166 and Tyr-1167 on the kinase activation loop; phosphorylation at all three tyrosine residues is required for optimal kinase activity. Inhibited by MSC1609119A-1, BMS-754807, PQIP, benzimidazole pyridinone, isoquinolinedione, bis-azaindole, 3-cyanoquinoline, 2,4-bis-arylamino-1,3-pyrimidine, pyrrolopyrimidine, pyrrole-5-carboxaldehyde, picropodophyllin (PPP), tyrphostin derivatives. While most inhibitors bind to the ATP binding pocket, MSC1609119A-1 functions as allosteric inhibitor and binds close to the DFG motif and the activation loop By similarity. Dephosphorylated by PTPN1 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1034 – 10341ATPPROSITE-ProRule annotation
    Active sitei1136 – 11361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1006 – 10149ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. G-protein alpha-subunit binding Source: RGD
    3. insulin binding Source: Ensembl
    4. insulin-like growth factor-activated receptor activity Source: UniProtKB
    5. insulin-like growth factor binding Source: UniProtKB
    6. insulin receptor substrate binding Source: UniProtKB
    7. phosphatidylinositol 3-kinase binding Source: UniProtKB
    8. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. axonogenesis Source: RGD
    2. brain development Source: Ensembl
    3. establishment of cell polarity Source: RGD
    4. exocrine pancreas development Source: Ensembl
    5. immune response Source: Ensembl
    6. inactivation of MAPKK activity Source: UniProtKB
    7. insulin-like growth factor receptor signaling pathway Source: UniProtKB
    8. male sex determination Source: Ensembl
    9. mammary gland development Source: Ensembl
    10. negative regulation of apoptotic process Source: UniProtKB
    11. negative regulation of muscle cell apoptotic process Source: RGD
    12. negative regulation of protein kinase B signaling Source: Ensembl
    13. neuron projection development Source: RGD
    14. phosphatidylinositol-mediated signaling Source: Ensembl
    15. positive regulation of cell migration Source: Ensembl
    16. positive regulation of cytokinesis Source: RGD
    17. positive regulation of DNA metabolic process Source: RGD
    18. positive regulation of DNA replication Source: Ensembl
    19. positive regulation of MAPK cascade Source: Ensembl
    20. positive regulation of protein kinase B signaling Source: Ensembl
    21. positive regulation of steroid hormone biosynthetic process Source: BHF-UCL
    22. prostate gland epithelium morphogenesis Source: Ensembl
    23. protein autophosphorylation Source: UniProtKB
    24. protein heterooligomerization Source: RGD
    25. protein tetramerization Source: UniProtKB
    26. regulation of JNK cascade Source: UniProtKB
    27. response to vitamin E 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.
    ReactomeiREACT_194916. SHC-related events triggered by IGF1R.
    REACT_208985. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
    REACT_222757. IRS-related events triggered by IGF1R.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Insulin-like growth factor 1 receptor (EC:2.7.10.1)
    Alternative name(s):
    Insulin-like growth factor I receptor
    Short name:
    IGF-I receptor
    CD_antigen: CD221
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Igf1r
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi2869. Igf1r.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: RGD
    2. integral component of membrane Source: UniProtKB-KW
    3. intracellular membrane-bounded organelle Source: Ensembl
    4. neuron projection Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 737707Insulin-like growth factor 1 receptor alpha chainPRO_0000016685Add
    BLAST
    Chaini742 – 1370629Insulin-like growth factor 1 receptor beta chainPRO_0000016686Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 52By similarity
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi150 ↔ 178By similarity
    Disulfide bondi182 ↔ 205By similarity
    Disulfide bondi192 ↔ 211By similarity
    Disulfide bondi215 ↔ 224By similarity
    Disulfide bondi219 ↔ 230By similarity
    Disulfide bondi231 ↔ 239By similarity
    Disulfide bondi235 ↔ 248By similarity
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi251 ↔ 260By similarity
    Disulfide bondi264 ↔ 276By similarity
    Disulfide bondi282 ↔ 303By similarity
    Disulfide bondi307 ↔ 321By similarity
    Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi324 ↔ 328By similarity
    Disulfide bondi332 ↔ 354By similarity
    Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi456 ↔ 489By similarity
    Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi748 – 7481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi757 – 7571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi901 – 9011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence Analysis
    Modified residuei981 – 9811PhosphotyrosineBy similarity
    Modified residuei1162 – 11621Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1166 – 11661Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1167 – 11671Phosphotyrosine; by autocatalysisBy similarity
    Cross-linki1169 – 1169Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1172 – 1172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei1279 – 12791Phosphoserine; by GSK3-betaBy similarity
    Modified residuei1283 – 12831PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1166 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1162 and Tyr-1167. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1162, Tyr-1166 and Tyr-1167) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-981 is required for IRS1- and SHC1-binding. Phosphorylation of Ser-1279 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1283 By similarity. Dephosphorylated by PTPN1.By similarity
    Polyubiquitinated at Lys-1169 and Lys-1172 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation By similarity.By similarity
    Sumoylated with SUMO1.By similarity
    Controlled by regulated intramembrane proteolysis (RIP). Undergoes metalloprotease-dependent constitutive ectodomain shedding to produce a membrane-anchored 52 kDa C-Terminal fragment which is further processed by presenilin gamma-secretase to yield an intracellular 50 kDa fragment By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP24062.
    PRIDEiP24062.

    PTM databases

    PhosphoSiteiP24062.

    Expressioni

    Gene expression databases

    ArrayExpressiP24062.
    GenevestigatoriP24062.

    Interactioni

    Subunit structurei

    Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chain carries the kinase domain. Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues. Forms a hybrid receptor with INSR, 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 ARRB1 and ARRB2. Interacts with GRB10. Interacts with GNB2L1/RACK1 By similarity. Interacts with SOCS1, SOCS2 and SOCS3 By similarity. Interacts with 14-3-3 proteins By similarity. Interacts with NMD2 By similarity. Interacts with MAP3K5 By similarity. Interacts with STAT3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi247747. 2 interactions.
    STRINGi10116.ENSRNOP00000019267.

    Structurei

    3D structure databases

    ProteinModelPortaliP24062.
    SMRiP24062. Positions 31-492, 978-1291.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini742 – 936195ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini961 – 1370410CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei937 – 96024HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini490 – 610121Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini611 – 70999Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini835 – 92894Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1000 – 1275276Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi978 – 9814IRS1- and SHC1-bindingBy 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.
    GeneTreeiENSGT00750000117239.
    HOGENOMiHOG000038045.
    HOVERGENiHBG006134.
    InParanoidiP24062.
    KOiK05087.
    OMAiNRCQKMC.
    OrthoDBiEOG73RB9N.
    PhylomeDBiP24062.

    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. 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.
    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.

    P24062-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSGSGGGSP TSLWGLVFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE     50
    NCTVIEGFLH ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF 100
    PNLTVIRGWK LFYNYALVIF EMTNLKDIGL YNLRNITRGA IRIEKNADLC 150
    YLSTIDWSLI LDAVSNNYIV GNKPPKECGD LCPGTLEEKP MCEKTTINNE 200
    YNYRCWTTNR CQKMCPSVCG KRACTENNEC CHPECLGSCH TPDDNTTCVA 250
    CRHYYYKGVC VPACPPGTYR FEGWRCVDRD FCANIPNAES SDSDGFVIHD 300
    GECMQECPSG FIRNSTQSMY CIPCEGPCPK VCGDEEKKTK TIDSVTSAQM 350
    LQGCTILKGN LLINIRRGNN IASELENFMG LIEVVTGYVK IRHSHALVSL 400
    SFLKNLRLIL GEEQLEGNYS FYVLDNQNLQ QLWDWNHRNL TVRSGKMYFA 450
    FNPKLCVSEI YRMEEVTGTK GRQSKGDINT RNNGERASCE SDVLRFTSTT 500
    TWKNRIIITW HRYRPPDYRD LISFTVYYKE APFKNVTEYD GQDACGSNSW 550
    NMVDVDLPPN KEGEPGILLH GLKPWTQYAV YVKAVTLTMV ENDHIRGAKS 600
    EILYIRTNAS VPSIPLDVLS ASNSSSQLIV KWNPPTLPNG NLSYYIVRWQ 650
    RQPQDGYLFR HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC 700
    CACPKTEAEK QAEKEEAEYR KVFENFLHNS IFVPRPERRR RDVLQVANTT 750
    MSSRSRNTTV ADTYNITDPE EFETEYPFFE SRVDNKERTV ISNLRPFTLY 800
    RIDIHSCNHE AEKLGCSASN FVFARTMPAE GADDIPGPVT WEPRPENSIF 850
    LKWPEPENPN GLILMYEIKY GSQVEDQREC VSRQEYRKYG GAKLNRLNPG 900
    NYTARIQATS LSGNGSWTDP VFFYVPAKTT YENFMHLIIA LPVAILLIVG 950
    GLVIMLYVFH RKRNNSRLGN GVLYASVNPE YFSAADVYVP DEWEVAREKI 1000
    TMNRELGQGS FGMVYEGVAK GVVKDEPETR VAIKTVNEAA SMRERIEFLN 1050
    EASVMKEFNC HHVVRLLGVV SQGQPTLVIM ELMTRGDLKS YLRSLRPEVE 1100
    NNLVLIPPSL SKMIQMAGEI ADGMAYLNAN KFVHRDLAAR NCMVAEDFTV 1150
    KIGDFGMTRD IYETDYYRKG GKGLLPVRWM SPESLKDGVF TTHSDVWSFG 1200
    VVLWEIATLA EQPYQGLSNE QVLRFVMEGG LLDKPDNCPD MLFELMRMCW 1250
    QYNPKMRPSF LEIIGSIKDE MEPSFQEVSF YYSEENKPPE PEELEMELEL 1300
    EPENMESVPL DPSASSASLP LPERHSGHKA ENGPGVLVLR ASFDERQPYA 1350
    HMNGGRANER ALPLPQSSTC 1370
    Length:1,370
    Mass (Da):155,396
    Last modified:November 1, 1997 - v2
    Checksum:iA5946897A41CB145
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti985 – 9862AD → PY no nucleotide entry (PubMed:1530648)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29232 mRNA. Translation: AAA41392.1.
    M27293 mRNA. Translation: AAA41384.1.
    RefSeqiNP_434694.1. NM_052807.2.
    UniGeneiRn.10957.
    Rn.165078.

    Genome annotation databases

    EnsembliENSRNOT00000019267; ENSRNOP00000019267; ENSRNOG00000014187.
    GeneIDi25718.
    KEGGirno:25718.
    UCSCiRGD:2869. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29232 mRNA. Translation: AAA41392.1 .
    M27293 mRNA. Translation: AAA41384.1 .
    RefSeqi NP_434694.1. NM_052807.2.
    UniGenei Rn.10957.
    Rn.165078.

    3D structure databases

    ProteinModelPortali P24062.
    SMRi P24062. Positions 31-492, 978-1291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247747. 2 interactions.
    STRINGi 10116.ENSRNOP00000019267.

    Chemistry

    BindingDBi P24062.
    ChEMBLi CHEMBL1075098.

    PTM databases

    PhosphoSitei P24062.

    Proteomic databases

    PaxDbi P24062.
    PRIDEi P24062.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000019267 ; ENSRNOP00000019267 ; ENSRNOG00000014187 .
    GeneIDi 25718.
    KEGGi rno:25718.
    UCSCi RGD:2869. rat.

    Organism-specific databases

    CTDi 3480.
    RGDi 2869. Igf1r.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117239.
    HOGENOMi HOG000038045.
    HOVERGENi HBG006134.
    InParanoidi P24062.
    KOi K05087.
    OMAi NRCQKMC.
    OrthoDBi EOG73RB9N.
    PhylomeDBi P24062.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 5301.
    Reactomei REACT_194916. SHC-related events triggered by IGF1R.
    REACT_208985. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
    REACT_222757. IRS-related events triggered by IGF1R.

    Miscellaneous databases

    NextBioi 607805.
    PROi P24062.

    Gene expression databases

    ArrayExpressi P24062.
    Genevestigatori P24062.

    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. 1 hit.
    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. "Inhibition of vascular smooth muscle cell growth through antisense transcription of a rat insulin-like growth factor I receptor cDNA."
      Du J., Delafontaine P.
      Circ. Res. 76:963-972(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Developmental regulation of the rat insulin-like growth factor I receptor gene."
      Werner H., Woloschak M., Adamo M., Shen-Orr Z., Roberts C.T. Jr., Leroith D.
      Proc. Natl. Acad. Sci. U.S.A. 86:7451-7455(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-364.
      Strain: Sprague-Dawley.
    3. "A new member of the insulin receptor family, insulin receptor-related receptor, is expressed preferentially in the kidney."
      Kurachi H., Jobo K., Ohta M., Kawasaki T., Itoh N.
      Biochem. Biophys. Res. Commun. 187:934-939(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 913-1017.
    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 INSR.

    Entry informationi

    Entry nameiIGF1R_RAT
    AccessioniPrimary (citable) accession number: P24062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 145 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3