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Q60751

- IGF1R_MOUSE

UniProt

Q60751 - IGF1R_MOUSE

Protein

Insulin-like growth factor 1 receptor

Gene

Igf1r

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (11 Jan 2001)
      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-1163, Tyr-1167 and Tyr-1168 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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1034 – 10341ATPPROSITE-ProRule annotation
    Active sitei1137 – 11371Proton 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. insulin binding Source: Ensembl
    3. insulin-like growth factor-activated receptor activity Source: UniProtKB
    4. insulin-like growth factor binding Source: UniProtKB
    5. insulin receptor substrate binding Source: UniProtKB
    6. phosphatidylinositol 3-kinase binding Source: UniProtKB
    7. protein binding Source: MGI
    8. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. axonogenesis Source: Ensembl
    2. brain development Source: MGI
    3. epidermis development Source: MGI
    4. establishment of cell polarity Source: Ensembl
    5. exocrine pancreas development Source: MGI
    6. immune response Source: Ensembl
    7. inactivation of MAPKK activity Source: Ensembl
    8. insulin-like growth factor receptor signaling pathway Source: UniProtKB
    9. male sex determination Source: MGI
    10. mammary gland development Source: MGI
    11. negative regulation of MAPK cascade Source: MGI
    12. negative regulation of muscle cell apoptotic process Source: Ensembl
    13. negative regulation of protein kinase B signaling Source: MGI
    14. negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
    15. organ morphogenesis Source: MGI
    16. peptidyl-tyrosine autophosphorylation Source: MGI
    17. phosphatidylinositol-mediated signaling Source: Ensembl
    18. positive regulation of cell migration Source: Ensembl
    19. positive regulation of cytokinesis Source: Ensembl
    20. positive regulation of DNA replication Source: Ensembl
    21. positive regulation of MAPK cascade Source: MGI
    22. positive regulation of mitosis Source: MGI
    23. positive regulation of protein kinase B signaling Source: MGI
    24. positive regulation of steroid hormone biosynthetic process Source: Ensembl
    25. prostate gland epithelium morphogenesis Source: MGI
    26. protein autophosphorylation Source: UniProtKB
    27. protein heterooligomerization Source: Ensembl
    28. protein phosphorylation Source: MGI
    29. protein tetramerization Source: UniProtKB
    30. regulation of JNK cascade Source: Ensembl
    31. response to vitamin E Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.
    ReactomeiREACT_188215. IRS-related events triggered by IGF1R.
    REACT_188219. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
    REACT_188220. SHC-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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:96433. Igf1r.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: Ensembl
    2. integral component of membrane Source: MGI
    3. intracellular membrane-bounded organelle Source: Ensembl
    4. neuron projection Source: Ensembl
    5. plasma membrane Source: MGI
    6. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Deficient mice are 45% of the size of wild-type littermates at birth, and die shortly due to severe organ hypoplasia.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 737707Insulin-like growth factor 1 receptor alpha chainPRO_0000016683Add
    BLAST
    Chaini742 – 1373632Insulin-like growth factor 1 receptor beta chainPRO_0000016684Add
    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
    Glycosylationi639 – 6391N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi641 – 6411N-linked (GlcNAc...)1 Publication
    Glycosylationi748 – 7481N-linked (GlcNAc...)1 Publication
    Glycosylationi757 – 7571N-linked (GlcNAc...)1 Publication
    Glycosylationi765 – 7651N-linked (GlcNAc...)1 Publication
    Glycosylationi901 – 9011N-linked (GlcNAc...)1 Publication
    Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence Analysis
    Modified residuei981 – 9811PhosphotyrosineBy similarity
    Modified residuei1163 – 11631Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1167 – 11671Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1168 – 11681Phosphotyrosine; by autocatalysisBy similarity
    Cross-linki1170 – 1170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1173 – 1173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei1280 – 12801Phosphoserine; by GSK3-beta1 Publication
    Modified residuei1284 – 12841Phosphoserine1 Publication

    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-1167 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1163 and Tyr-1168. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1163, Tyr-1167 and Tyr-1168) 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 By similarity. Phosphorylation of Ser-1280 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1284. Dephosphorylated by PTPN1.By similarity1 Publication
    Polyubiquitinated at Lys-1170 and Lys-1173 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

    MaxQBiQ60751.
    PaxDbiQ60751.
    PRIDEiQ60751.

    PTM databases

    PhosphoSiteiQ60751.

    Expressioni

    Gene expression databases

    ArrayExpressiQ60751.
    BgeeiQ60751.
    CleanExiMM_IGF1R.
    GenevestigatoriQ60751.

    Interactioni

    Protein-protein interaction databases

    BioGridi200548. 4 interactions.
    IntActiQ60751. 2 interactions.
    MINTiMINT-219894.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60751.
    SMRiQ60751. Positions 30-653, 785-828, 848-1288.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini742 – 936195ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini961 – 1373413CytoplasmicBy similarityAdd
    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
    Domaini735 – 82995Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini835 – 92894Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1000 – 1276277Protein 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 4 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.
    InParanoidiQ60751.
    KOiK05087.
    PhylomeDBiQ60751.

    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. 4 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.

    Q60751-1 [UniParc]FASTAAdd to Basket

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    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
    DECMQECPSG 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
    RQPQDGYLYR HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC 700
    CACPKTEAEK QAEKEEAEYR KVFENFLHNS IFVPRPERRR RDVMQVANTT 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
    QNNLVLIPPS LSKMIQMAGE IADGMAYLNA NKFVHRDLAA RNCMVAEDFT 1150
    VKIGDFGMTR DIYETDYYRK GGKGLLPVRW MSPESLKDGV FTTHSDVWSF 1200
    GVVLWEIATL AEQPYQGLSN EQVLRFVMEG GLLDKPDNCP DMLFELMRMC 1250
    WQYNPKMRPS FLEIIGSIKD EMEPSFQEVS FYYSEENKPP EPEELEMELE 1300
    MEPENMESVP LDPSASSASL PLPERHSGHK AENGPGPGVL VLRASFDERQ 1350
    PYAHMNGGRA NERALPLPQS STC 1373
    Length:1,373
    Mass (Da):155,788
    Last modified:January 11, 2001 - v3
    Checksum:i5EE3B72EF101E379
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 592FL → LV in AAC52123. (PubMed:8234298)Curated
    Sequence conflicti260 – 2601C → S in AAC52123. (PubMed:8234298)Curated
    Sequence conflicti301 – 3011D → G in AAC52123. (PubMed:8234298)Curated
    Sequence conflicti306 – 3061E → V in AAC52123. (PubMed:8234298)Curated
    Sequence conflicti324 – 3241C → S in AAC52123. (PubMed:8234298)Curated
    Sequence conflicti1134 – 11341V → I in AAA40013. (PubMed:2482828)Curated
    Sequence conflicti1145 – 11451V → D in AAA40013. (PubMed:2482828)Curated
    Sequence conflicti1202 – 12021V → I in AAA40013. (PubMed:2482828)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056187 mRNA. Translation: AAC12782.1.
    U00182 mRNA. Translation: AAC52123.1.
    M33422 mRNA. Translation: AAA40013.1.
    PIRiA48805.
    JH0113.
    RefSeqiNP_034643.2. NM_010513.2.
    UniGeneiMm.275742.

    Genome annotation databases

    GeneIDi16001.
    KEGGimmu:16001.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056187 mRNA. Translation: AAC12782.1 .
    U00182 mRNA. Translation: AAC52123.1 .
    M33422 mRNA. Translation: AAA40013.1 .
    PIRi A48805.
    JH0113.
    RefSeqi NP_034643.2. NM_010513.2.
    UniGenei Mm.275742.

    3D structure databases

    ProteinModelPortali Q60751.
    SMRi Q60751. Positions 30-653, 785-828, 848-1288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200548. 4 interactions.
    IntActi Q60751. 2 interactions.
    MINTi MINT-219894.

    Chemistry

    BindingDBi Q60751.
    ChEMBLi CHEMBL5381.

    PTM databases

    PhosphoSitei Q60751.

    Proteomic databases

    MaxQBi Q60751.
    PaxDbi Q60751.
    PRIDEi Q60751.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 16001.
    KEGGi mmu:16001.

    Organism-specific databases

    CTDi 3480.
    MGIi MGI:96433. Igf1r.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000038045.
    HOVERGENi HBG006134.
    InParanoidi Q60751.
    KOi K05087.
    PhylomeDBi Q60751.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.
    Reactomei REACT_188215. IRS-related events triggered by IGF1R.
    REACT_188219. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
    REACT_188220. SHC-related events triggered by IGF1R.

    Miscellaneous databases

    ChiTaRSi IGF1R. mouse.
    NextBioi 288790.
    PROi Q60751.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60751.
    Bgeei Q60751.
    CleanExi MM_IGF1R.
    Genevestigatori Q60751.

    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. 4 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. "Cloning of cDNA for the mouse insulin-like growth factor I receptor."
      Navarro M., Garandel V., Barenton B., Bernardi H.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of cDNA for the alpha subunit of mouse insulin-like growth factor I receptor and the role of the receptor in metanephric development."
      Wada J., Liu Z.Z., Alvares K., Kumar A., Wallner E.I., Makino H., Kanwar Y.S.
      Proc. Natl. Acad. Sci. U.S.A. 90:10360-10364(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-329.
      Strain: CD-1.
      Tissue: Kidney.
    3. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
      Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
      Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1134-1203.
    4. "Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)."
      Liu J.P., Baker J., Perkins A.S., Robertson E.J., Efstratiadis A.
      Cell 75:59-72(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    5. "Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts."
      Buckley D.A., Cheng A., Kiely P.A., Tremblay M.L., O'Connor R.
      Mol. Cell. Biol. 22:1998-2010(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    6. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-748 AND ASN-901.
      Tissue: Myoblast.
    7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-639; ASN-641; ASN-757 AND ASN-765.
    8. "Serine phosphorylation of the insulin-like growth factor I (IGF-1) receptor C-terminal tail restrains kinase activity and cell growth."
      Kelly G.M., Buckley D.A., Kiely P.A., Adams D.R., O'Connor R.
      J. Biol. Chem. 287:28180-28194(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1280 AND SER-1284.

    Entry informationi

    Entry nameiIGF1R_MOUSE
    AccessioniPrimary (citable) accession number: Q60751
    Secondary accession number(s): O70438, Q62123
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3