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P24062

- IGF1R_RAT

UniProt

P24062 - IGF1R_RAT

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Protein

Insulin-like growth factor 1 receptor

Gene

Igf1r

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R By similarity. When present in a hybrid receptor with INSR, binds IGF1 By similarity.By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by autophosphorylation at Tyr-1162, Tyr-1166 and Tyr-1167 on the kinase activation loop; phosphorylation at all three tyrosine residues is required for optimal kinase activity. Inhibited by MSC1609119A-1, BMS-754807, PQIP, benzimidazole pyridinone, isoquinolinedione, bis-azaindole, 3-cyanoquinoline, 2,4-bis-arylamino-1,3-pyrimidine, pyrrolopyrimidine, pyrrole-5-carboxaldehyde, picropodophyllin (PPP), tyrphostin derivatives. While most inhibitors bind to the ATP binding pocket, MSC1609119A-1 functions as allosteric inhibitor and binds close to the DFG motif and the activation loop By similarity. Dephosphorylated by PTPN1 By similarity.By similarity

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. axonogenesis Source: RGD
  2. brain development Source: Ensembl
  3. epidermis development Source: Ensembl
  4. establishment of cell polarity Source: RGD
  5. exocrine pancreas development Source: Ensembl
  6. immune response Source: Ensembl
  7. inactivation of MAPKK activity Source: UniProtKB
  8. insulin-like growth factor receptor signaling pathway Source: UniProtKB
  9. male sex determination Source: Ensembl
  10. mammary gland development Source: Ensembl
  11. negative regulation of apoptotic process Source: UniProtKB
  12. negative regulation of muscle cell apoptotic process Source: RGD
  13. negative regulation of protein kinase B signaling Source: Ensembl
  14. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  15. neuron projection development Source: RGD
  16. peptidyl-tyrosine autophosphorylation Source: Ensembl
  17. phosphatidylinositol-mediated signaling Source: Ensembl
  18. positive regulation of cell migration Source: Ensembl
  19. positive regulation of cytokinesis Source: RGD
  20. positive regulation of DNA metabolic process Source: RGD
  21. positive regulation of DNA replication Source: Ensembl
  22. positive regulation of MAPK cascade Source: Ensembl
  23. positive regulation of mitosis Source: Ensembl
  24. positive regulation of protein kinase B signaling Source: Ensembl
  25. positive regulation of steroid hormone biosynthetic process Source: BHF-UCL
  26. prostate gland epithelium morphogenesis Source: Ensembl
  27. protein autophosphorylation Source: UniProtKB
  28. protein heterooligomerization Source: RGD
  29. protein tetramerization Source: UniProtKB
  30. regulation of JNK cascade Source: UniProtKB
  31. response to vitamin E Source: RGD
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. 5301.
ReactomeiREACT_194916. SHC-related events triggered by IGF1R.
REACT_208985. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
REACT_222757. IRS-related events triggered by IGF1R.

Names & Taxonomyi

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

Organism-specific databases

RGDi2869. Igf1r.

Subcellular locationi

GO - Cellular componenti

  1. caveola Source: RGD
  2. integral component of membrane Source: UniProtKB-KW
  3. intracellular membrane-bounded organelle Source: Ensembl
  4. neuron projection Source: RGD
  5. receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

PaxDbiP24062.
PRIDEiP24062.

PTM databases

PhosphoSiteiP24062.

Expressioni

Gene expression databases

GenevestigatoriP24062.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chain carries the kinase domain. Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues. Forms a hybrid receptor with INSR, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts with ARRB1 and ARRB2. Interacts with GRB10. Interacts with GNB2L1/RACK1 By similarity. Interacts with SOCS1, SOCS2 and SOCS3 By similarity. Interacts with 14-3-3 proteins By similarity. Interacts with NMD2 By similarity. Interacts with MAP3K5 By similarity. Interacts with STAT3 By similarity.By similarity

Protein-protein interaction databases

BioGridi247747. 2 interactions.
STRINGi10116.ENSRNOP00000019267.

Structurei

3D structure databases

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

Topological domain

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

Transmembrane

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

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi978 – 9814IRS1- and SHC1-bindingBy similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP24062.
KOiK05087.
OMAiNRCQKMC.
OrthoDBiEOG73RB9N.
PhylomeDBiP24062.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000620. Insulin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24062-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKSGSGGGSP TSLWGLVFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE
60 70 80 90 100
NCTVIEGFLH ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF
110 120 130 140 150
PNLTVIRGWK LFYNYALVIF EMTNLKDIGL YNLRNITRGA IRIEKNADLC
160 170 180 190 200
YLSTIDWSLI LDAVSNNYIV GNKPPKECGD LCPGTLEEKP MCEKTTINNE
210 220 230 240 250
YNYRCWTTNR CQKMCPSVCG KRACTENNEC CHPECLGSCH TPDDNTTCVA
260 270 280 290 300
CRHYYYKGVC VPACPPGTYR FEGWRCVDRD FCANIPNAES SDSDGFVIHD
310 320 330 340 350
GECMQECPSG FIRNSTQSMY CIPCEGPCPK VCGDEEKKTK TIDSVTSAQM
360 370 380 390 400
LQGCTILKGN LLINIRRGNN IASELENFMG LIEVVTGYVK IRHSHALVSL
410 420 430 440 450
SFLKNLRLIL GEEQLEGNYS FYVLDNQNLQ QLWDWNHRNL TVRSGKMYFA
460 470 480 490 500
FNPKLCVSEI YRMEEVTGTK GRQSKGDINT RNNGERASCE SDVLRFTSTT
510 520 530 540 550
TWKNRIIITW HRYRPPDYRD LISFTVYYKE APFKNVTEYD GQDACGSNSW
560 570 580 590 600
NMVDVDLPPN KEGEPGILLH GLKPWTQYAV YVKAVTLTMV ENDHIRGAKS
610 620 630 640 650
EILYIRTNAS VPSIPLDVLS ASNSSSQLIV KWNPPTLPNG NLSYYIVRWQ
660 670 680 690 700
RQPQDGYLFR HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC
710 720 730 740 750
CACPKTEAEK QAEKEEAEYR KVFENFLHNS IFVPRPERRR RDVLQVANTT
760 770 780 790 800
MSSRSRNTTV ADTYNITDPE EFETEYPFFE SRVDNKERTV ISNLRPFTLY
810 820 830 840 850
RIDIHSCNHE AEKLGCSASN FVFARTMPAE GADDIPGPVT WEPRPENSIF
860 870 880 890 900
LKWPEPENPN GLILMYEIKY GSQVEDQREC VSRQEYRKYG GAKLNRLNPG
910 920 930 940 950
NYTARIQATS LSGNGSWTDP VFFYVPAKTT YENFMHLIIA LPVAILLIVG
960 970 980 990 1000
GLVIMLYVFH RKRNNSRLGN GVLYASVNPE YFSAADVYVP DEWEVAREKI
1010 1020 1030 1040 1050
TMNRELGQGS FGMVYEGVAK GVVKDEPETR VAIKTVNEAA SMRERIEFLN
1060 1070 1080 1090 1100
EASVMKEFNC HHVVRLLGVV SQGQPTLVIM ELMTRGDLKS YLRSLRPEVE
1110 1120 1130 1140 1150
NNLVLIPPSL SKMIQMAGEI ADGMAYLNAN KFVHRDLAAR NCMVAEDFTV
1160 1170 1180 1190 1200
KIGDFGMTRD IYETDYYRKG GKGLLPVRWM SPESLKDGVF TTHSDVWSFG
1210 1220 1230 1240 1250
VVLWEIATLA EQPYQGLSNE QVLRFVMEGG LLDKPDNCPD MLFELMRMCW
1260 1270 1280 1290 1300
QYNPKMRPSF LEIIGSIKDE MEPSFQEVSF YYSEENKPPE PEELEMELEL
1310 1320 1330 1340 1350
EPENMESVPL DPSASSASLP LPERHSGHKA ENGPGVLVLR ASFDERQPYA
1360 1370
HMNGGRANER ALPLPQSSTC
Length:1,370
Mass (Da):155,396
Last modified:November 1, 1997 - v2
Checksum:iA5946897A41CB145
GO

Experimental Info

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

Sequence databases

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

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 247747. 2 interactions.
STRINGi 10116.ENSRNOP00000019267.

Chemistry

BindingDBi P24062.
ChEMBLi CHEMBL1075098.

PTM databases

PhosphoSitei P24062.

Proteomic databases

PaxDbi P24062.
PRIDEi P24062.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 3480.
RGDi 2869. Igf1r.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000038045.
HOVERGENi HBG006134.
InParanoidi P24062.
KOi K05087.
OMAi NRCQKMC.
OrthoDBi EOG73RB9N.
PhylomeDBi P24062.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 607805.
PROi P24062.

Gene expression databases

Genevestigatori P24062.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProi IPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view ]
Pfami PF00041. fn3. 1 hit.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view ]
PIRSFi PIRSF000620. Insulin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Inhibition of vascular smooth muscle cell growth through antisense transcription of a rat insulin-like growth factor I receptor cDNA."
    Du J., Delafontaine P.
    Circ. Res. 76:963-972(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Developmental regulation of the rat insulin-like growth factor I receptor gene."
    Werner H., Woloschak M., Adamo M., Shen-Orr Z., Roberts C.T. Jr., Leroith D.
    Proc. Natl. Acad. Sci. U.S.A. 86:7451-7455(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-364.
    Strain: Sprague-Dawley.
  3. "A new member of the insulin receptor family, insulin receptor-related receptor, is expressed preferentially in the kidney."
    Kurachi H., Jobo K., Ohta M., Kawasaki T., Itoh N.
    Biochem. Biophys. Res. Commun. 187:934-939(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 913-1017.
  4. "Insulin and IGF-I action on insulin receptors, IGF-I receptors, and hybrid insulin/IGF-I receptors in vascular smooth muscle cells."
    Johansson G.S., Arnqvist H.J.
    Am. J. Physiol. 291:E1124-E1130(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FORMATION OF A HYBRID RECEPTOR WITH INSR.

Entry informationi

Entry nameiIGF1R_RAT
AccessioniPrimary (citable) accession number: P24062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3