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Reviewed, UniProtKB/Swiss-Prot P08069 (IGF1R_HUMAN)

Last modified February 9, 2010. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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:
    1- Recommended name:
            Insulin-like growth factor 1 receptor alpha chain
    2- Recommended name:
            Insulin-like growth factor 1 receptor beta chain
Gene names
Name: IGF1R
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. When present in a hybrid receptor with INSR, binds IGF1. Ref.18 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, Ref.20 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. Ref.7 Ref.10 Ref.11 Ref.12 Ref.18 Ref.20

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.12

Cofactor

Manganese.

Enzyme regulation

Autophosphorylation activates the kinase activity. Ref.9

Subunit structure

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. Ref.10 Ref.13 Ref.16 Ref.19

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Found as a hybrid receptor with INSR in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibrobasts, spleen and placenta (at protein level). Expressed in a variety of tissues. Ref.8 Ref.14 Ref.15

Post-translational modification

The cytoplasmic domain of the beta subunit is autophosphorylated on tyrosine residues in response to insulin-like growth factor I (IGF I). Ref.10 Ref.12 Ref.17 Ref.21 Ref.22 Ref.23

Phosphorylation of Tyr-980 is required for IRS1- and SHC1-binding.

Involvement in disease

Defects in IGF1R may be a cause in some cases of resistance to insulin-like growth factor 1 (IGF1 resistance) [MIM:270450]. IGF1 resistance is a gowth deficiency disorder characterized by intrauterine growth retardation and poor postnatal growth accompanied with increased plasma IGF1.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 3 fibronectin type-III domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
Transmembrane
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processanti-apoptosis

Traceable author statement. Source: ProtInc

immune response

Inferred from mutant phenotype. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: ProtInc

insulin-like growth factor receptor signaling pathway Ref.12

Inferred from direct assay. Source: UniProtKB

phosphoinositide 3-kinase cascade Ref.13

Inferred by curator. Source: UniProtKB

phosphoinositide-mediated signaling

Inferred from direct assay. Source: UniProtKB

positive regulation of DNA replication Ref.18

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of cell migration Ref.18

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement. Source: ProtInc

protein amino acid autophosphorylation Ref.10 Ref.12 Ref.17

Inferred from direct assay. Source: UniProtKB

protein tetramerization Ref.10

Inferred from direct assay. Source: UniProtKB

   Cellular componentintegral to plasma membrane Ref.12

Inferred by curator. Source: UniProtKB

microsome Ref.11

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction. Source: IntAct

insulin binding Ref.11

Inferred from physical interaction. Source: UniProtKB

insulin receptor binding Ref.11

Inferred from direct assay. Source: UniProtKB

insulin receptor substrate binding Ref.13

Inferred from physical interaction. Source: UniProtKB

insulin-like growth factor I binding Ref.11

Inferred from physical interaction. Source: UniProtKB

insulin-like growth factor receptor activity Ref.12

Inferred from direct assay. Source: UniProtKB

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoinositide 3-kinase binding Ref.13

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.7 Ref.1
Chain31 – 736706Insulin-like growth factor 1 receptor alpha chain
PRO_0000016681
Chain741 – 1367627Insulin-like growth factor 1 receptor beta chain
PRO_0000016682

Regions

Topological domain741 – 935195Extracellular Potential
Transmembrane936 – 95924 Potential
Topological domain960 – 1367408Cytoplasmic Potential
Domain488 – 606119Fibronectin type-III 1
Domain611 – 68979Fibronectin type-III 2
Domain831 – 92696Fibronectin type-III 3
Domain999 – 1274276Protein kinase
Nucleotide binding1005 – 10139ATP By similarity
Motif977 – 9804IRS1- and SHC1-binding

Sites

Active site11351Proton acceptor By similarity
Binding site10331ATP

Amino acid modifications

Modified residue9801Phosphotyrosine; by autocatalysis
Modified residue11611Phosphotyrosine; by autocatalysis By similarity
Modified residue11651Phosphotyrosine; by autocatalysis By similarity
Modified residue11661Phosphotyrosine; by autocatalysis By similarity
Modified residue13391Phosphoserine Ref.22 Ref.23
Modified residue13651Phosphoserine
Modified residue13661Phosphothreonine Ref.22
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential
Glycosylation6401N-linked (GlcNAc...) Potential
Glycosylation7471N-linked (GlcNAc...) Potential
Glycosylation7561N-linked (GlcNAc...) Potential
Glycosylation7641N-linked (GlcNAc...) Potential
Glycosylation9001N-linked (GlcNAc...) Potential
Glycosylation9131N-linked (GlcNAc...) Potential
Disulfide bond215 ↔ 224 By similarity
Disulfide bond219 ↔ 230 By similarity
Disulfide bond231 ↔ 239 By similarity
Disulfide bond235 ↔ 248 By similarity
Disulfide bond251 ↔ 260 By similarity
Disulfide bond264 ↔ 276 By similarity
Disulfide bond282 ↔ 303 By similarity
Disulfide bond307 ↔ 321 By similarity
Disulfide bond324 ↔ 328 By similarity

Natural variations

Natural variant1051V → L in a renal chromophobe sample; somatic mutation. Ref.27
VAR_041424
Natural variant1381R → Q in IGF1 resistance; has decreased IGF1R function. Ref.25
VAR_034891
Natural variant1451K → N in IGF1 resistance; has decreased IGF1R function. Ref.25
VAR_034892
Natural variant3881V → M: dbSNP rs45445894. Ref.4
VAR_018855
Natural variant4371R → H: dbSNP rs34516635. Ref.27
VAR_034893
Natural variant5111R → Q: dbSNP rs33958176.
VAR_034894
Natural variant5951R → H: dbSNP rs56248469. Ref.27
VAR_041425
Natural variant6051R → H: dbSNP rs45553041. Ref.4
VAR_018856
Natural variant7391R → Q in IGF1 resistance; leads to failure of processing of the IGF1R proreceptor to mature IGF1R. Ref.26
VAR_034895
Natural variant8081H → R: dbSNP rs34061581.
VAR_034896
Natural variant8281A → T: dbSNP rs35224135.
VAR_034897
Natural variant8571N → S: dbSNP rs45611935. Ref.27
VAR_041426
Natural variant13381A → T: dbSNP rs34102392. Ref.27
VAR_041427
Natural variant13471A → V in a lung squamous cell carcinoma sample; somatic mutation. Ref.27
VAR_041428

Experimental info

Mutagenesis9801Y → F: Reduces tyrosine phosphorylation. Abolishes interaction with IRS1 and SHC1. Does not abolish interaction with PIK3R1. Ref.13
Mutagenesis10331K → A: Kinase inactive. Abolishes tyrosine phosphorylation and abolishes interaction with IRS1, SHC1 and PIK3R1. Ref.13
Sequence conflict928 – 9292TG → R in BAG11657. Ref.3

Secondary structure

........................................................................................................................................ 1367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08069-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: AE8A735F87F745C8

FASTA1,367154,793
        10         20         30         40         50         60 
MKSGSGGGSP TSLWGLLFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE NCTVIEGYLH 

        70         80         90        100        110        120 
ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVIF 

       130        140        150        160        170        180 
EMTNLKDIGL YNLRNITRGA IRIEKNADLC YLSTVDWSLI LDAVSNNYIV GNKPPKECGD 

       190        200        210        220        230        240 
LCPGTMEEKP MCEKTTINNE YNYRCWTTNR CQKMCPSTCG KRACTENNEC CHPECLGSCS 

       250        260        270        280        290        300 
APDNDTACVA CRHYYYAGVC VPACPPNTYR FEGWRCVDRD FCANILSAES SDSEGFVIHD 

       310        320        330        340        350        360 
GECMQECPSG FIRNGSQSMY CIPCEGPCPK VCEEEKKTKT IDSVTSAQML QGCTIFKGNL 

       370        380        390        400        410        420 
LINIRRGNNI ASELENFMGL IEVVTGYVKI RHSHALVSLS FLKNLRLILG EEQLEGNYSF 

       430        440        450        460        470        480 
YVLDNQNLQQ LWDWDHRNLT IKAGKMYFAF NPKLCVSEIY RMEEVTGTKG RQSKGDINTR 

       490        500        510        520        530        540 
NNGERASCES DVLHFTSTTT SKNRIIITWH RYRPPDYRDL ISFTVYYKEA PFKNVTEYDG 

       550        560        570        580        590        600 
QDACGSNSWN MVDVDLPPNK DVEPGILLHG LKPWTQYAVY VKAVTLTMVE NDHIRGAKSE 

       610        620        630        640        650        660 
ILYIRTNASV PSIPLDVLSA SNSSSQLIVK WNPPSLPNGN LSYYIVRWQR QPQDGYLYRH 

       670        680        690        700        710        720 
NYCSKDKIPI RKYADGTIDI EEVTENPKTE VCGGEKGPCC ACPKTEAEKQ AEKEEAEYRK 

       730        740        750        760        770        780 
VFENFLHNSI FVPRPERKRR DVMQVANTTM SSRSRNTTAA DTYNITDPEE LETEYPFFES 

       790        800        810        820        830        840 
RVDNKERTVI SNLRPFTLYR IDIHSCNHEA EKLGCSASNF VFARTMPAEG ADDIPGPVTW 

       850        860        870        880        890        900 
EPRPENSIFL KWPEPENPNG LILMYEIKYG SQVEDQRECV SRQEYRKYGG AKLNRLNPGN 

       910        920        930        940        950        960 
YTARIQATSL SGNGSWTDPV FFYVQAKTGY ENFIHLIIAL PVAVLLIVGG LVIMLYVFHR 

       970        980        990       1000       1010       1020 
KRNNSRLGNG VLYASVNPEY FSAADVYVPD EWEVAREKIT MSRELGQGSF GMVYEGVAKG 

      1030       1040       1050       1060       1070       1080 
VVKDEPETRV AIKTVNEAAS MRERIEFLNE ASVMKEFNCH HVVRLLGVVS QGQPTLVIME 

      1090       1100       1110       1120       1130       1140 
LMTRGDLKSY LRSLRPEMEN NPVLAPPSLS KMIQMAGEIA DGMAYLNANK FVHRDLAARN 

      1150       1160       1170       1180       1190       1200 
CMVAEDFTVK IGDFGMTRDI YETDYYRKGG KGLLPVRWMS PESLKDGVFT TYSDVWSFGV 

      1210       1220       1230       1240       1250       1260 
VLWEIATLAE QPYQGLSNEQ VLRFVMEGGL LDKPDNCPDM LFELMRMCWQ YNPKMRPSFL 

      1270       1280       1290       1300       1310       1320 
EIISSIKEEM EPGFREVSFY YSEENKLPEP EELDLEPENM ESVPLDPSAS SSSLPLPDRH 

      1330       1340       1350       1360 
SGHKAENGPG PGVLVLRASF DERQPYAHMN GGRKNERALP LPQSSTC 

« Hide

References

« Hide 'large scale' references
[1]"Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity."
Ullrich A., Gray A., Tam A.W., Yang-Feng T., Tsubokawa M., Collins C., Henzel W., Bon T.L., Kathuria S., Chen E., Jacobs S., Francke U., Ramachandran J., Fujita-Yamaguchi Y.
EMBO J. 5:2503-2512(1986) [PubMed: 2877871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-56; 446-453; 503-524; 561-579; 668-672 AND 721-729.
Tissue: Placenta.
[2]"Insulin-like growth factor I receptor gene structure."
Abbot A.M., Bueno R., Pedrini M.T., Murray J.M., Smith R.J.
J. Biol. Chem. 267:10759-10763(1992) [PubMed: 1316909] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Nagase T., Kikuno R.F., Yamakawa H., Ohara O.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal brain.
[4]NIEHS SNPs program
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-388 AND HIS-605.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Analysis of the human type I insulin-like growth factor receptor promoter region."
Cooke D.W., Bankert L.A., Roberts C.T. Jr., Leroith D., Casella S.J.
Biochem. Biophys. Res. Commun. 177:1113-1120(1991) [PubMed: 1711844] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
[7]"Characterization of human placental insulin-like growth factor-I/insulin hybrid receptors by protein microsequencing and purification."
Kasuya J., Paz I.B., Maddux B.A., Goldfine I.D., Hefta S.A., Fujita-Yamaguchi Y.
Biochemistry 32:13531-13536(1993) [PubMed: 8257688] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-45 AND 741-750, FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
Tissue: Placenta.
[8]"A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
Lee S.-T., Strunk K.M., Spritz R.A.
Oncogene 8:3403-3410(1993) [PubMed: 8247543] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1137-1193, TISSUE SPECIFICITY.
Tissue: Melanocyte.
[9]"Substructural analysis of the insulin receptor by microsequence analyses of limited tryptic fragments isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence or presence of dithiothreitol."
Xu Q.-Y., Paxton R.J., Fujita-Yamaguchi Y.
J. Biol. Chem. 265:18673-18681(1990) [PubMed: 2211730] [Abstract]
Cited for: ENZYME REGULATION, BINDING OF MANGANESE.
Tissue: Placenta.
[10]"Interaction of the alpha beta dimers of the insulin-like growth factor I receptor is required for receptor autophosphorylation."
Tollefsen S.E., Stoszek R.M., Thompson K.
Biochemistry 30:48-54(1991) [PubMed: 1846292] [Abstract]
Cited for: FUNCTION, SUBUNIT, AUTOPHOSPHORYLATION.
[11]"Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity."
Soos M.A., Field C.E., Siddle K.
Biochem. J. 290:419-426(1993) [PubMed: 8452530] [Abstract]
Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
[12]"Role of tyrosine kinase activity in signal transduction by the insulin-like growth factor-I (IGF-I) receptor. Characterization of kinase-deficient IGF-I receptors and the action of an IGF-I-mimetic antibody (alpha IR-3)."
Kato H., Faria T.N., Stannard B., Roberts C.T. Jr., LeRoith D.
J. Biol. Chem. 268:2655-2661(1993) [PubMed: 7679099] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION.
[13]"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor."
Craparo A., O'Neill T.J., Gustafson T.A.
J. Biol. Chem. 270:15639-15643(1995) [PubMed: 7541045] [Abstract]
Cited for: INTERACTION WITH IRS1; SHC1 AND PIK3R1, MUTAGENESIS OF TYR-980 AND LYS-1033.
[14]"Insulin receptor/IGF-I receptor hybrids are widely distributed in mammalian tissues: quantification of individual receptor species by selective immunoprecipitation and immunoblotting."
Bailyes E.M., Nave B.T., Soos M.A., Orr S.R., Hayward A.C., Siddle K.
Biochem. J. 327:209-215(1997) [PubMed: 9355755] [Abstract]
Cited for: FORMATION OF A HYBRID RECEPTOR WITH INSR, TISSUE SPECIFICITY.
[15]"Distribution of insulin/insulin-like growth factor-I hybrid receptors in human tissues."
Federici M., Porzio O., Zucaro L., Fusco A., Borboni P., Lauro D., Sesti G.
Mol. Cell. Endocrinol. 129:121-126(1997) [PubMed: 9202395] [Abstract]
Cited for: FORMATION OF A HYBRID RECEPTOR WITH INSR, TISSUE SPECIFICITY.
[16]"beta-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor."
Lin F.-T., Daaka Y., Lefkowitz R.J.
J. Biol. Chem. 273:31640-31643(1998) [PubMed: 9822622] [Abstract]
Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[17]"Autophosphorylation of the insulin-like growth factor I receptor cytoplasmic domain."
Lopaczynski W., Terry C., Nissley P.
Biochem. Biophys. Res. Commun. 279:955-960(2000) [PubMed: 11162456] [Abstract]
Cited for: AUTOPHOSPHORYLATION.
[18]"Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved."
Pandini G., Frasca F., Mineo R., Sciacca L., Vigneri R., Belfiore A.
J. Biol. Chem. 277:39684-39695(2002) [PubMed: 12138094] [Abstract]
Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
[19]"{beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase."
Girnita L., Shenoy S.K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R.J., Larsson O.
J. Biol. Chem. 280:24412-24419(2005) [PubMed: 15878855] [Abstract]
Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[20]"Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant."
Slaaby R., Schaeffer L., Lautrup-Larsen I., Andersen A.S., Shaw A.C., Mathiasen I.S., Brandt J.
J. Biol. Chem. 281:25869-25874(2006) [PubMed: 16831875] [Abstract]
Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
[21]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1161; TYR-1165 AND TYR-1166, MASS SPECTROMETRY.
Tissue: Lung.
[22]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1161; TYR-1165; SER-1339 AND THR-1366, MASS SPECTROMETRY.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1339, MASS SPECTROMETRY.
[24]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1165; SER-1339; SER-1365 AND THR-1366, MASS SPECTROMETRY.
[25]"IGF-I receptor mutations resulting in intrauterine and postnatal growth retardation."
The intrauterine growth retardation (IUGR) study group
Abuzzahab M.J., Schneider A., Goddard A., Grigorescu F., Lautier C., Keller E., Kiess W., Klammt J., Kratzsch J., Osgood D., Pfaeffle R., Raile K., Seidel B., Smith R.J., Chernausek S.D.
N. Engl. J. Med. 349:2211-2222(2003) [PubMed: 14657428] [Abstract]
Cited for: VARIANTS IGF1 RESISTANCE GLN-138 AND ASN-145, CHARACTERIZATION OF VARIANTS IGF1 RESISTANCE GLN-138 AND ASN-145.
[26]"Mutation at cleavage site of insulin-like growth factor receptor in a short-stature child born with intrauterine growth retardation."
Kawashima Y., Kanzaki S., Yang F., Kinoshita T., Hanaki K., Nagaishi J., Ohtsuka Y., Hisatome I., Ninomoya H., Nanba E., Fukushima T., Takahashi S.
J. Clin. Endocrinol. Metab. 90:4679-4687(2005) [PubMed: 15928254] [Abstract]
Cited for: VARIANT IGF1 RESISTANCE GLN-739, CHARACTERIZATION OF VARIANT IGF1 RESISTANCE GLN-739.
[27]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-105; HIS-437; HIS-595; SER-857; THR-1338 AND VAL-1347.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04434 mRNA. Translation: CAA28030.1.
AB425196 mRNA. Translation: BAG11657.1. Different initiation.
AY332722 Genomic DNA. Translation: AAP81165.1.
BC113610 mRNA. Translation: AAI13611.1.
BC113612 mRNA. Translation: AAI13613.1.
M69229 Genomic DNA. Translation: AAB59399.1.
IPIIPI00027232.
PIRIGHUR1. A25690.
RefSeqNP_000866.1.
UniGeneHs.643120
Hs.653608
Hs.714012

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IGRX-ray2.60A31-492[»]
1JQHX-ray2.10A/B/C981-1286[»]
1K3AX-ray2.10A988-1286[»]
1M7NX-ray2.70A/B974-1294[»]
1P4OX-ray1.50A/B974-1294[»]
2OJ9X-ray2.00A982-1286[»]
2ZM3X-ray2.50A/B/C/D981-1286[»]
3D94X-ray2.30A986-1286[»]
3F5PX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/R/S/T981-1286[»]
3I81X-ray2.08A982-1286[»]
SMRP08069. Positions 29-926.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-476N.
IntActP08069. 12 interactions.
STRINGP08069.

PTM databases

PhosphoSiteP08069.

Proteomic databases

PeptideAtlasP08069.
PRIDEP08069.

Genome annotation databases

EnsemblENST00000268035; ENSP00000268035; ENSG00000140443; Homo sapiens. [Genome view]
GeneID3480.
KEGGhsa:3480.
UCSCuc002bul.1. human.

Organism-specific databases

CTD3480.
GeneCardsGC15P097010.
H-InvDBHIX0038072.
HGNCHGNC:5465. IGF1R.
HPACAB010268.
MIM147370. gene.
270450. phenotype.
Orphanet73273. Growth delay due to insulin-like growth factor I resistance.
PharmGKBPA29698.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04495.
HOGENOMHBG316019.
HOVERGENP08069.
InParanoidP08069.
OMATTINNEY.
OrthoDBEOG986BZ0.
PhylomeDBP08069.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBigf1_pathway. IGF1 pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.

Gene expression databases

ArrayExpressP08069.
BgeeP08069.
CleanExHS_IGF1R.
GenevestigatorP08069.
GermOnlineENSG00000140443. Homo sapiens.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR020714. Tyr_kinase_insulin_GF_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
IPR002011. Tyr_prot_kinase_rcpt_2_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
PANTHERPTHR23256:SF178. Tyr_kinase_insulin_GF_rcpt. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00041. fn3. 1 hit.
PF00757. Furin-like. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000620. Insulin_receptor. 1 hit.
SMARTSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50853. 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]
ProtoNetSearch...

Other Resources

DrugBankDB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.
DB01277. Mecasermin.
NextBio13682.
SOURCESearch...

Entry information

Entry nameIGF1R_HUMAN
AccessionPrimary (citable) accession number: P08069
Secondary accession number(s): B1B5Y2, Q14CV2, Q9UCC0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: February 9, 2010
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

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Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents