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P08069

- IGF1R_HUMAN

UniProt

P08069 - IGF1R_HUMAN

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Protein

Insulin-like growth factor 1 receptor

Gene

IGF1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.
When present in a hybrid receptor with INSR, binds IGF1. PubMed:12138094 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, PubMed:16831875 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.

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.10 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Activated by autophosphorylation at Tyr-1165, Tyr-1161 and Tyr-1166 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.11 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1033 – 10331ATP
Active sitei1135 – 11351Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1005 – 10139ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. insulin binding Source: BHF-UCL
  4. insulin-like growth factor-activated receptor activity Source: UniProtKB
  5. insulin-like growth factor binding Source: UniProtKB
  6. insulin-like growth factor I binding Source: BHF-UCL
  7. insulin receptor binding Source: BHF-UCL
  8. insulin receptor substrate binding Source: UniProtKB
  9. phosphatidylinositol 3-kinase binding Source: UniProtKB
  10. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_150139. SHC-related events triggered by IGF1R.
REACT_150203. IRS-related events triggered by IGF1R.
REACT_150359. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
SignaLinkiP08069.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:5465. IGF1R.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

GO - Cellular componenti

  1. caveola Source: Ensembl
  2. integral component of plasma membrane Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: BHF-UCL
  4. membrane Source: BHF-UCL
  5. neuron projection Source: Ensembl
  6. plasma membrane Source: Reactome
  7. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Insulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]: A disorder characterized by intrauterine growth retardation, poor postnatal growth and increased plasma IGF1 levels.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381R → Q in IGF1RES; has decreased IGF1R function. 1 Publication
VAR_034891
Natural varianti145 – 1451K → N in IGF1RES; has decreased IGF1R function. 1 Publication
VAR_034892
Natural varianti739 – 7391R → Q in IGF1RES; leads to failure of processing of the IGF1R proreceptor to mature IGF1R. 1 Publication
VAR_034895

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi980 – 9801Y → F: Reduces tyrosine phosphorylation. Abolishes interaction with IRS1 and SHC1. Does not abolish interaction with PIK3R1, nor with GRB10. 2 Publications
Mutagenesisi1033 – 10331K → A: Kinase inactive. Abolishes tyrosine phosphorylation and abolishes interaction with IRS1, SHC1 and PIK3R1. 1 Publication
Mutagenesisi1280 – 12801Y → F: No effect on GRB10-binding. 1 Publication
Mutagenesisi1281 – 12811Y → F: No effect on GRB10-binding. 1 Publication
Mutagenesisi1346 – 13461Y → F: Loss of GRB10-binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi270450. phenotype.
Orphaneti73273. Growth delay due to insulin-like growth factor I resistance.
PharmGKBiPA29698.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30302 PublicationsAdd
BLAST
Chaini31 – 736706Insulin-like growth factor 1 receptor alpha chainPRO_0000016681Add
BLAST
Chaini741 – 1367627Insulin-like growth factor 1 receptor beta chainPRO_0000016682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 521 Publication
Glycosylationi51 – 511N-linked (GlcNAc...)1 Publication
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)1 Publication
Disulfide bondi150 ↔ 1781 Publication
Disulfide bondi182 ↔ 2051 Publication
Disulfide bondi192 ↔ 2111 Publication
Disulfide bondi215 ↔ 2241 Publication
Disulfide bondi219 ↔ 2301 Publication
Disulfide bondi231 ↔ 2391 Publication
Disulfide bondi235 ↔ 2481 Publication
Glycosylationi244 – 2441N-linked (GlcNAc...)1 Publication
Disulfide bondi251 ↔ 2601 Publication
Disulfide bondi264 ↔ 2761 Publication
Disulfide bondi282 ↔ 3031 Publication
Disulfide bondi307 ↔ 3211 Publication
Glycosylationi314 – 3141N-linked (GlcNAc...)1 Publication
Disulfide bondi324 ↔ 3281 Publication
Disulfide bondi332 ↔ 3531 Publication
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi455 ↔ 4881 Publication
Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi607 – 6071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi640 – 6401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi747 – 7471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi764 – 7641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi900 – 9001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi913 – 9131N-linked (GlcNAc...)Sequence Analysis
Modified residuei980 – 9801Phosphotyrosine1 Publication
Modified residuei1161 – 11611Phosphotyrosine; by autocatalysis3 Publications
Modified residuei1165 – 11651Phosphotyrosine; by autocatalysis3 Publications
Modified residuei1166 – 11661Phosphotyrosine; by autocatalysis3 Publications
Cross-linki1168 – 1168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1171 – 1171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1278 – 12781Phosphoserine; by GSK3-betaBy similarity
Modified residuei1282 – 12821PhosphoserineBy 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-1165 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1161 and Tyr-1166. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1165, Tyr-1161 and Tyr-1166) 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-980 is required for IRS1- and SHC1-binding. Phosphorylation of Ser-1278 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1282. Dephosphorylated by PTPN1 (By similarity).By similarity
Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation.6 Publications
Sumoylated with SUMO1.1 Publication
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.1 Publication

Keywords - PTMi

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

Proteomic databases

MaxQBiP08069.
PaxDbiP08069.
PeptideAtlasiP08069.
PRIDEiP08069.

PTM databases

PhosphoSiteiP08069.

Expressioni

Tissue specificityi

Found as a hybrid receptor with INSR in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta (at protein level). Expressed in a variety of tissues. Overexpressed in tumors, including melanomas, cancers of the colon, pancreas prostate and kidney.4 Publications

Gene expression databases

BgeeiP08069.
CleanExiHS_IGF1R.
ExpressionAtlasiP08069. baseline and differential.
GenevestigatoriP08069.

Organism-specific databases

HPAiCAB010268.

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. Interacts with SOCS1, SOCS2 and SOCS3. Interacts with 14-3-3 proteins. Interacts with NMD2. Interacts with MAP3K5. Interacts with STAT3.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-475981,EBI-475981
ARHGEF12Q9NZN57EBI-475981,EBI-821440
CAMPP499133EBI-475981,EBI-6378485
CrkQ640103EBI-475981,EBI-2906540From a different organism.
CSKP412405EBI-475981,EBI-1380630
CTNNB1P352223EBI-475981,EBI-491549
IGF1P050195EBI-475981,EBI-7902275
INSP013174EBI-475981,EBI-3989070From a different organism.
LEF1Q9UJU25EBI-475981,EBI-926131
MDM2Q009872EBI-475981,EBI-389668
PIK3R1P279864EBI-475981,EBI-79464
PTPN1P180313EBI-475981,EBI-968788
PTPN11Q061243EBI-475981,EBI-297779
SHC1P29353-22EBI-475981,EBI-1000553
TAGLNQ019952EBI-475981,EBI-1054248

Protein-protein interaction databases

BioGridi109701. 51 interactions.
DIPiDIP-476N.
IntActiP08069. 42 interactions.
MINTiMINT-85902.
STRINGi9606.ENSP00000268035.

Structurei

Secondary structure

1
1367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 415
Helixi43 – 497
Beta strandi53 – 575
Beta strandi59 – 657
Beta strandi68 – 703
Beta strandi80 – 834
Beta strandi85 – 928
Helixi96 – 983
Beta strandi115 – 1217
Beta strandi138 – 1447
Helixi157 – 1604
Helixi164 – 1663
Beta strandi168 – 1714
Helixi175 – 1784
Turni183 – 1886
Beta strandi194 – 1996
Beta strandi201 – 2033
Beta strandi205 – 2095
Helixi217 – 2193
Beta strandi235 – 2417
Beta strandi247 – 2559
Beta strandi257 – 2637
Beta strandi269 – 2713
Turni272 – 2743
Beta strandi275 – 2773
Helixi279 – 2835
Beta strandi297 – 2993
Beta strandi302 – 3065
Beta strandi311 – 3155
Beta strandi321 – 3233
Beta strandi325 – 3273
Beta strandi331 – 34111
Helixi345 – 3473
Turni349 – 3524
Beta strandi354 – 3629
Helixi375 – 3784
Beta strandi383 – 3864
Beta strandi388 – 3925
Turni415 – 4173
Beta strandi418 – 4236
Turni434 – 4363
Beta strandi440 – 4434
Beta strandi445 – 4517
Helixi456 – 46611
Beta strandi474 – 4774
Turni479 – 4813
Beta strandi980 – 9823
Helixi983 – 9853
Turni990 – 9923
Helixi996 – 9983
Beta strandi999 – 10079
Beta strandi1009 – 102214
Beta strandi1025 – 103410
Beta strandi1037 – 10393
Helixi1041 – 105313
Helixi1054 – 10563
Beta strandi1065 – 10695
Beta strandi1071 – 10744
Beta strandi1076 – 10805
Helixi1087 – 110014
Helixi1109 – 112820
Helixi1138 – 11403
Beta strandi1141 – 11433
Beta strandi1149 – 11513
Helixi1155 – 11573
Helixi1159 – 11646
Helixi1168 – 11703
Beta strandi1171 – 11744
Helixi1176 – 11783
Helixi1181 – 11866
Helixi1191 – 120717
Turni1212 – 12154
Helixi1218 – 12269
Helixi1239 – 124810
Helixi1253 – 12553
Helixi1259 – 12668
Helixi1267 – 12693
Helixi1274 – 12774
Turni1279 – 12813
Turni1283 – 12853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IGRX-ray2.60A31-492[»]
1JQHX-ray2.10A/B/C979-1286[»]
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[»]
3LVPX-ray3.00A/B/C/D951-1286[»]
3LW0X-ray1.79A/B/C/D983-1286[»]
3NW5X-ray2.14A982-1286[»]
3NW6X-ray2.20A982-1286[»]
3NW7X-ray2.11A982-1286[»]
3O23X-ray2.10A982-1286[»]
3QQUX-ray2.90A/B/C/D988-1286[»]
ProteinModelPortaliP08069.
SMRiP08069. Positions 30-924, 957-1317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08069.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini741 – 935195ExtracellularSequence AnalysisAdd
BLAST
Topological domaini960 – 1367408CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei936 – 95924HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini491 – 609119Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini610 – 70899Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini735 – 82894Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini834 – 92794Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini999 – 1274276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi977 – 9804IRS1- and SHC1-binding

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.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP08069.
KOiK05087.
OMAiNRCQKMC.
OrthoDBiEOG73RB9N.
PhylomeDBiP08069.
TreeFamiTF351636.

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.

P08069 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MKSGSGGGSP TSLWGLLFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE
60 70 80 90 100
NCTVIEGYLH ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF
110 120 130 140 150
PNLTVIRGWK LFYNYALVIF EMTNLKDIGL YNLRNITRGA IRIEKNADLC
160 170 180 190 200
YLSTVDWSLI LDAVSNNYIV GNKPPKECGD LCPGTMEEKP MCEKTTINNE
210 220 230 240 250
YNYRCWTTNR CQKMCPSTCG KRACTENNEC CHPECLGSCS APDNDTACVA
260 270 280 290 300
CRHYYYAGVC VPACPPNTYR FEGWRCVDRD FCANILSAES SDSEGFVIHD
310 320 330 340 350
GECMQECPSG FIRNGSQSMY CIPCEGPCPK VCEEEKKTKT IDSVTSAQML
360 370 380 390 400
QGCTIFKGNL LINIRRGNNI ASELENFMGL IEVVTGYVKI RHSHALVSLS
410 420 430 440 450
FLKNLRLILG EEQLEGNYSF YVLDNQNLQQ LWDWDHRNLT IKAGKMYFAF
460 470 480 490 500
NPKLCVSEIY RMEEVTGTKG RQSKGDINTR NNGERASCES DVLHFTSTTT
510 520 530 540 550
SKNRIIITWH RYRPPDYRDL ISFTVYYKEA PFKNVTEYDG QDACGSNSWN
560 570 580 590 600
MVDVDLPPNK DVEPGILLHG LKPWTQYAVY VKAVTLTMVE NDHIRGAKSE
610 620 630 640 650
ILYIRTNASV PSIPLDVLSA SNSSSQLIVK WNPPSLPNGN LSYYIVRWQR
660 670 680 690 700
QPQDGYLYRH NYCSKDKIPI RKYADGTIDI EEVTENPKTE VCGGEKGPCC
710 720 730 740 750
ACPKTEAEKQ AEKEEAEYRK VFENFLHNSI FVPRPERKRR DVMQVANTTM
760 770 780 790 800
SSRSRNTTAA DTYNITDPEE LETEYPFFES RVDNKERTVI SNLRPFTLYR
810 820 830 840 850
IDIHSCNHEA EKLGCSASNF VFARTMPAEG ADDIPGPVTW EPRPENSIFL
860 870 880 890 900
KWPEPENPNG LILMYEIKYG SQVEDQRECV SRQEYRKYGG AKLNRLNPGN
910 920 930 940 950
YTARIQATSL SGNGSWTDPV FFYVQAKTGY ENFIHLIIAL PVAVLLIVGG
960 970 980 990 1000
LVIMLYVFHR KRNNSRLGNG VLYASVNPEY FSAADVYVPD EWEVAREKIT
1010 1020 1030 1040 1050
MSRELGQGSF GMVYEGVAKG VVKDEPETRV AIKTVNEAAS MRERIEFLNE
1060 1070 1080 1090 1100
ASVMKEFNCH HVVRLLGVVS QGQPTLVIME LMTRGDLKSY LRSLRPEMEN
1110 1120 1130 1140 1150
NPVLAPPSLS KMIQMAGEIA DGMAYLNANK FVHRDLAARN CMVAEDFTVK
1160 1170 1180 1190 1200
IGDFGMTRDI YETDYYRKGG KGLLPVRWMS PESLKDGVFT TYSDVWSFGV
1210 1220 1230 1240 1250
VLWEIATLAE QPYQGLSNEQ VLRFVMEGGL LDKPDNCPDM LFELMRMCWQ
1260 1270 1280 1290 1300
YNPKMRPSFL EIISSIKEEM EPGFREVSFY YSEENKLPEP EELDLEPENM
1310 1320 1330 1340 1350
ESVPLDPSAS SSSLPLPDRH SGHKAENGPG PGVLVLRASF DERQPYAHMN
1360
GGRKNERALP LPQSSTC
Length:1,367
Mass (Da):154,793
Last modified:August 1, 1988 - v1
Checksum:iAE8A735F87F745C8
GO

Sequence cautioni

The sequence BAG11657.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti928 – 9292TG → R in BAG11657. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051V → L in a renal chromophobe sample; somatic mutation. 1 Publication
VAR_041424
Natural varianti138 – 1381R → Q in IGF1RES; has decreased IGF1R function. 1 Publication
VAR_034891
Natural varianti145 – 1451K → N in IGF1RES; has decreased IGF1R function. 1 Publication
VAR_034892
Natural varianti388 – 3881V → M.1 Publication
Corresponds to variant rs45445894 [ dbSNP | Ensembl ].
VAR_018855
Natural varianti437 – 4371R → H.1 Publication
Corresponds to variant rs34516635 [ dbSNP | Ensembl ].
VAR_034893
Natural varianti511 – 5111R → Q.
Corresponds to variant rs33958176 [ dbSNP | Ensembl ].
VAR_034894
Natural varianti595 – 5951R → H.1 Publication
Corresponds to variant rs56248469 [ dbSNP | Ensembl ].
VAR_041425
Natural varianti605 – 6051R → H.1 Publication
Corresponds to variant rs45553041 [ dbSNP | Ensembl ].
VAR_018856
Natural varianti739 – 7391R → Q in IGF1RES; leads to failure of processing of the IGF1R proreceptor to mature IGF1R. 1 Publication
VAR_034895
Natural varianti808 – 8081H → R.
Corresponds to variant rs34061581 [ dbSNP | Ensembl ].
VAR_034896
Natural varianti828 – 8281A → T.
Corresponds to variant rs35224135 [ dbSNP | Ensembl ].
VAR_034897
Natural varianti857 – 8571N → S.1 Publication
Corresponds to variant rs45611935 [ dbSNP | Ensembl ].
VAR_041426
Natural varianti1338 – 13381A → T.1 Publication
Corresponds to variant rs34102392 [ dbSNP | Ensembl ].
VAR_041427
Natural varianti1347 – 13471A → V in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_041428

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04434 mRNA. Translation: CAA28030.1.
AB425196 mRNA. Translation: BAG11657.1. Different initiation.
AY332722 Genomic DNA. Translation: AAP81165.1.
AC055807 Genomic DNA. No translation available.
AC069029 Genomic DNA. No translation available.
AC118658 Genomic DNA. No translation available.
AC118660 Genomic DNA. No translation available.
BC113610 mRNA. Translation: AAI13611.1.
BC113612 mRNA. Translation: AAI13613.1.
M69229 Genomic DNA. Translation: AAB59399.1.
CCDSiCCDS10378.1.
PIRiA25690. IGHUR1.
RefSeqiNP_000866.1. NM_000875.4.
NP_001278787.1. NM_001291858.1.
UniGeneiHs.643120.
Hs.714012.

Genome annotation databases

EnsembliENST00000268035; ENSP00000268035; ENSG00000140443.
GeneIDi3480.
KEGGihsa:3480.
UCSCiuc002bul.3. human.

Polymorphism databases

DMDMi124240.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

IGF-1 receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04434 mRNA. Translation: CAA28030.1 .
AB425196 mRNA. Translation: BAG11657.1 . Different initiation.
AY332722 Genomic DNA. Translation: AAP81165.1 .
AC055807 Genomic DNA. No translation available.
AC069029 Genomic DNA. No translation available.
AC118658 Genomic DNA. No translation available.
AC118660 Genomic DNA. No translation available.
BC113610 mRNA. Translation: AAI13611.1 .
BC113612 mRNA. Translation: AAI13613.1 .
M69229 Genomic DNA. Translation: AAB59399.1 .
CCDSi CCDS10378.1.
PIRi A25690. IGHUR1.
RefSeqi NP_000866.1. NM_000875.4.
NP_001278787.1. NM_001291858.1.
UniGenei Hs.643120.
Hs.714012.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IGR X-ray 2.60 A 31-492 [» ]
1JQH X-ray 2.10 A/B/C 979-1286 [» ]
1K3A X-ray 2.10 A 988-1286 [» ]
1M7N X-ray 2.70 A/B 974-1294 [» ]
1P4O X-ray 1.50 A/B 974-1294 [» ]
2OJ9 X-ray 2.00 A 982-1286 [» ]
2ZM3 X-ray 2.50 A/B/C/D 981-1286 [» ]
3D94 X-ray 2.30 A 986-1286 [» ]
3F5P X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L/M/R/S/T 981-1286 [» ]
3I81 X-ray 2.08 A 982-1286 [» ]
3LVP X-ray 3.00 A/B/C/D 951-1286 [» ]
3LW0 X-ray 1.79 A/B/C/D 983-1286 [» ]
3NW5 X-ray 2.14 A 982-1286 [» ]
3NW6 X-ray 2.20 A 982-1286 [» ]
3NW7 X-ray 2.11 A 982-1286 [» ]
3O23 X-ray 2.10 A 982-1286 [» ]
3QQU X-ray 2.90 A/B/C/D 988-1286 [» ]
ProteinModelPortali P08069.
SMRi P08069. Positions 30-924, 957-1317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109701. 51 interactions.
DIPi DIP-476N.
IntActi P08069. 42 interactions.
MINTi MINT-85902.
STRINGi 9606.ENSP00000268035.

Chemistry

BindingDBi P08069.
ChEMBLi CHEMBL1957.
DrugBanki DB00071. "Insulin.
DB00047. Insulin Glargine.
DB00046. Insulin Lispro.
DB00030. Insulin Regular.
DB01277. Mecasermin.
GuidetoPHARMACOLOGYi 1801.

PTM databases

PhosphoSitei P08069.

Polymorphism databases

DMDMi 124240.

Proteomic databases

MaxQBi P08069.
PaxDbi P08069.
PeptideAtlasi P08069.
PRIDEi P08069.

Protocols and materials databases

DNASUi 3480.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268035 ; ENSP00000268035 ; ENSG00000140443 .
GeneIDi 3480.
KEGGi hsa:3480.
UCSCi uc002bul.3. human.

Organism-specific databases

CTDi 3480.
GeneCardsi GC15P099192.
HGNCi HGNC:5465. IGF1R.
HPAi CAB010268.
MIMi 147370. gene.
270450. phenotype.
neXtProti NX_P08069.
Orphaneti 73273. Growth delay due to insulin-like growth factor I resistance.
PharmGKBi PA29698.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000038045.
HOVERGENi HBG006134.
InParanoidi P08069.
KOi K05087.
OMAi NRCQKMC.
OrthoDBi EOG73RB9N.
PhylomeDBi P08069.
TreeFami TF351636.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_150139. SHC-related events triggered by IGF1R.
REACT_150203. IRS-related events triggered by IGF1R.
REACT_150359. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
SignaLinki P08069.

Miscellaneous databases

ChiTaRSi IGF1R. human.
EvolutionaryTracei P08069.
GeneWikii Insulin-like_growth_factor_1_receptor.
GenomeRNAii 3480.
NextBioi 13682.
PROi P08069.
SOURCEi Search...

Gene expression databases

Bgeei P08069.
CleanExi HS_IGF1R.
ExpressionAtlasi P08069. baseline and differential.
Genevestigatori P08069.

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

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-45 AND 741-750, FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
    Tissue: Placenta.
  9. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1137-1193, TISSUE SPECIFICITY.
    Tissue: Melanocyte.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRS1; SHC1 AND PIK3R1, MUTAGENESIS OF TYR-980 AND LYS-1033, PHOSPHORYLATION AT TYR-980.
  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] [Europe PMC] [Abstract]
    Cited for: FORMATION OF A HYBRID RECEPTOR WITH INSR, TISSUE SPECIFICITY.
  15. "14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor."
    Furlanetto R.W., Dey B.R., Lopaczynski W., Nissley S.P.
    Biochem. J. 327:765-771(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3 PROTEINS.
  16. "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] [Europe PMC] [Abstract]
    Cited for: FORMATION OF A HYBRID RECEPTOR WITH INSR, TISSUE SPECIFICITY.
  17. "Interaction of human suppressor of cytokine signaling (SOCS)-2 with the insulin-like growth factor-I receptor."
    Dey B.R., Spence S.L., Nissley P., Furlanetto R.W.
    J. Biol. Chem. 273:24095-24101(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SOCS1 AND SOCS2.
  18. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1 AND ARRB2.
  19. "The IGF-I receptor in cancer research."
    Baserga R.
    Exp. Cell Res. 253:1-6(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CANCER.
  20. "Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
    Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
    Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB10, MUTAGENESIS OF TYR-980; TYR-1280; TYR-1281 AND TYR-1346.
  21. "Suppressor of cytokine signaling (SOCS)-3 protein interacts with the insulin-like growth factor-I receptor."
    Dey B.R., Furlanetto R.W., Nissley P.
    Biochem. Biophys. Res. Commun. 278:38-43(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SOCS3.
  22. "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] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  23. "Mechanism of STAT3 activation by insulin-like growth factor I receptor."
    Zong C.S., Chan J., Levy D.E., Horvath C., Sadowski H.B., Wang L.H.
    J. Biol. Chem. 275:15099-15105(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF STAT3.
  24. "Expression of the type 1 insulin-like growth factor receptor is up-regulated in primary prostate cancer and commonly persists in metastatic disease."
    Hellawell G.O., Turner G.D., Davies D.R., Poulsom R., Brewster S.F., Macaulay V.M.
    Cancer Res. 62:2942-2950(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  25. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
  26. "RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting protein, modulates IGF-I-dependent integrin signaling and promotes cell spreading and contact with extracellular matrix."
    Hermanto U., Zong C.S., Li W., Wang L.H.
    Mol. Cell. Biol. 22:2345-2365(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  27. "Type 1 insulin-like growth factor receptor (IGF-IR) signaling inhibits apoptosis signal-regulating kinase 1 (ASK1)."
    Galvan V., Logvinova A., Sperandio S., Ichijo H., Bredesen D.E.
    J. Biol. Chem. 278:13325-13332(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP3K5.
  28. "Mdm2-dependent ubiquitination and degradation of the insulin-like growth factor 1 receptor."
    Girnita L., Girnita A., Larsson O.
    Proc. Natl. Acad. Sci. U.S.A. 100:8247-8252(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MDM2, INTERACTION WITH MDM2.
  29. "Cyclolignans as inhibitors of the insulin-like growth factor-1 receptor and malignant cell growth."
    Girnita A., Girnita L., del Prete F., Bartolazzi A., Larsson O., Axelson M.
    Cancer Res. 64:236-242(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  30. "{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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1 AND ARRB2.
  31. "JAK/STAT3 pathway is involved in survival of neurons in response to insulin-like growth factor and negatively regulated by suppressor of cytokine signaling-3."
    Yadav A., Kalita A., Dhillon S., Banerjee K.
    J. Biol. Chem. 280:31830-31840(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT3.
  32. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.
  33. "The insulin-like growth factor 1 (IGF-1) receptor is a substrate for gamma-secretase-mediated intramembrane proteolysis."
    McElroy B., Powell J.C., McCarthy J.V.
    Biochem. Biophys. Res. Commun. 358:1136-1141(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  34. "The insulin-like growth factor 1 receptor in cancer: old focus, new future."
    Hartog H., Wesseling J., Boezen H.M., van der Graaf W.T.
    Eur. J. Cancer 43:1895-1904(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON IGF1R IN CANCER.
  35. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
    Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
    PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  38. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  39. "Polyubiquitination of insulin-like growth factor I receptor (IGF-IR) activation loop promotes antibody-induced receptor internalization and down-regulation."
    Mao Y., Shang Y., Pham V.C., Ernst J.A., Lill J.R., Scales S.J., Zha J.
    J. Biol. Chem. 286:41852-41861(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-1168 AND LYS-1171.
  40. "Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor."
    Garrett T.P., McKern N.M., Lou M., Frenkel M.J., Bentley J.D., Lovrecz G.O., Elleman T.C., Cosgrove L.J., Ward C.W.
    Nature 394:395-399(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-492, DISULFIDE BONDS, GLYCOSYLATION AT ASN-51; ASN-135; ASN-244 AND ASN-314.
  41. "Structure and autoregulation of the insulin-like growth factor 1 receptor kinase."
    Favelyukis S., Till J.H., Hubbard S.R., Miller W.T.
    Nat. Struct. Biol. 8:1058-1063(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 988-1286 IN COMPLEX WITH AMP-PCP AND PEPTIDE SUBSTRATE, CATALYTIC ACTIVITY, ACTIVE SITE, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166.
  42. "Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation."
    Pautsch A., Zoephel A., Ahorn H., Spevak W., Hauptmann R., Nar H.
    Structure 9:955-965(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 981-1286 IN COMPLEX WITH ANP, AUTOPHOSPHORYLATION, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
  43. "Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity."
    Munshi S., Kornienko M., Hall D.L., Reid J.C., Waxman L., Stirdivant S.M., Darke P.L., Kuo L.C.
    J. Biol. Chem. 277:38797-38802(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 974-1294.
  44. "Structure of apo, unactivated insulin-like growth factor-1 receptor kinase at 1.5 A resolution."
    Munshi S., Hall D.L., Kornienko M., Darke P.L., Kuo L.C.
    Acta Crystallogr. D 59:1725-1730(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 974-1294.
  45. "Discovery and initial SAR of 3-(1H-benzo[d]imidazol-2-yl)pyridin-2(1H)-ones as inhibitors of insulin-like growth factor 1-receptor (IGF-1R)."
    Velaparthi U., Wittman M., Liu P., Stoffan K., Zimmermann K., Sang X., Carboni J., Li A., Attar R., Gottardis M., Greer A., Chang C.Y., Jacobsen B.L., Sack J.S., Sun Y., Langley D.R., Balasubramanian B., Vyas D.
    Bioorg. Med. Chem. Lett. 17:2317-2321(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 982-1286 IN COMPLEX WITH BENZIMIDAZOLE PYRIDINONE INHIBITOR, CATALYTIC ACTIVITY, ENZYME REGULATION.
  46. "Lead identification to generate isoquinolinedione inhibitors of insulin-like growth factor receptor (IGF-1R) for potential use in cancer treatment."
    Mayer S.C., Banker A.L., Boschelli F., Di L., Johnson M., Kenny C.H., Krishnamurthy G., Kutterer K., Moy F., Petusky S., Ravi M., Tkach D., Tsou H.R., Xu W.
    Bioorg. Med. Chem. Lett. 18:3641-3645(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 981-1286, PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166.
  47. "Small-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptor."
    Wu J., Li W., Craddock B.P., Foreman K.W., Mulvihill M.J., Ji Q.S., Miller W.T., Hubbard S.R.
    EMBO J. 27:1985-1994(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 986-1286 IN COMPLEX WITH INHIBITOR PQIP, SUBUNIT, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, ACTIVE SITE, ENZYME REGULATION.
  48. "Lead identification to generate 3-cyanoquinoline inhibitors of insulin-like growth factor receptor (IGF-1R) for potential use in cancer treatment."
    Miller L.M., Mayer S.C., Berger D.M., Boschelli D.H., Boschelli F., Di L., Du X., Dutia M., Floyd M.B., Johnson M., Kenny C.H., Krishnamurthy G., Moy F., Petusky S., Tkach D., Torres N., Wu B., Xu W.
    Bioorg. Med. Chem. Lett. 19:62-66(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 981-1286 IN COMPLEX WITH 3-CYANOQUINOLINE INHIBITOR, CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166.
  49. Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 982-1286 IN COMPLEX WITH BMS-754807, CATALYTIC ACTIVITY, ENZYME REGULATION.
  50. Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 983-1286 IN COMPLEX WITH MSC1609119A-1, CATALYTIC ACTIVITY, ENZYME REGULATION.
  51. "Proline isosteres in a series of 2,4-disubstituted pyrrolo[1,2-f][1,2,4]triazine inhibitors of IGF-1R kinase and IR kinase."
    Sampognaro A.J., Wittman M.D., Carboni J.M., Chang C., Greer A.F., Hurlburt W.W., Sack J.S., Vyas D.M.
    Bioorg. Med. Chem. Lett. 20:5027-5030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 982-1286 IN COMPLEXES WITH INHIBITORS, CATALYTIC ACTIVITY, ENZYME REGULATION.
  52. Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 951-1286 IN COMPLEX WITH BIS-AZAINDOLE INHIBITOR, AUTOPHOSPHORYLATION, ENZYME REGULATION.
  53. "Discovery of the first non-ATP competitive IGF-1R kinase inhibitors: advantages in comparison with competitive inhibitors."
    Lesuisse D., Mauger J., Nemecek C., Maignan S., Boiziau J., Harlow G., Hittinger A., Ruf S., Strobel H., Nair A., Ritter K., Malleron J.L., Dagallier A., El-Ahmad Y., Guilloteau J.P., Guizani H., Bouchard H., Venot C.
    Bioorg. Med. Chem. Lett. 21:2224-2228(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 982-1286 IN COMPLEX WITH HYDANTOIN DERIVATIVE, CATALYTIC ACTIVITY, ENZYME REGULATION.
  54. Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 988-1286 IN COMPLEX WITH 2,4-BIS-ARYLAMINO-1,3-PYRIMIDINE INHIBITOR, CATALYTIC ACTIVITY, ENZYME REGULATION.
  55. Cited for: VARIANTS IGF1RES GLN-138 AND ASN-145, CHARACTERIZATION OF VARIANTS IGF1RES GLN-138 AND ASN-145.
  56. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT IGF1RES GLN-739, CHARACTERIZATION OF VARIANT IGF1RES GLN-739.
  57. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-105; HIS-437; HIS-595; SER-857; THR-1338 AND VAL-1347.

Entry informationi

Entry nameiIGF1R_HUMAN
AccessioniPrimary (citable) accession number: P08069
Secondary accession number(s): B1B5Y2, Q14CV2, Q9UCC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 29, 2014
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3