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Q60751 (IGF1R_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Gene names
Name:Igf1r
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

Activated by autophosphorylation at Tyr-1163, Tyr-1167 and Tyr-1168 on the kinase activation loop; phosphorylation at all three tyrosine residues is required for optimal kinase activity. Inhibited by MSC1609119A-1, BMS-754807, PQIP, benzimidazole pyridinone, isoquinolinedione, bis-azaindole, 3-cyanoquinoline, 2,4-bis-arylamino-1,3-pyrimidine, pyrrolopyrimidine, pyrrole-5-carboxaldehyde, picropodophyllin (PPP), tyrphostin derivatives. While most inhibitors bind to the ATP binding pocket, MSC1609119A-1 functions as allosteric inhibitor and binds close to the DFG motif and the activation loop By similarity. Ref.5

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1167 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1163 and Tyr-1168. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1163, Tyr-1167 and Tyr-1168) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-981 is required for IRS1- and SHC1-binding By similarity. Phosphorylation of Ser-1280 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1284. Dephosphorylated by PTPN1. Ref.8

Polyubiquitinated at Lys-1170 and Lys-1173 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation By similarity.

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.

Disruption phenotype

Deficient mice are 45% of the size of wild-type littermates at birth, and die shortly due to severe organ hypoplasia. Ref.4

Sequence similarities

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

Contains 4 fibronectin type-III domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from mutant phenotype PubMed 12904469. Source: MGI

epidermis development

Inferred from mutant phenotype PubMed 23906066. Source: MGI

establishment of cell polarity

Inferred from electronic annotation. Source: Ensembl

exocrine pancreas development

Inferred from mutant phenotype PubMed 12101187. Source: MGI

immune response

Inferred from electronic annotation. Source: Ensembl

inactivation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

insulin-like growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

male sex determination

Inferred from mutant phenotype PubMed 14628051. Source: MGI

mammary gland development

Inferred from mutant phenotype PubMed 17662267. Source: MGI

negative regulation of MAPK cascade

Inferred from mutant phenotype PubMed 18451178. Source: MGI

negative regulation of muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 18451178. Source: MGI

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 23906066. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 12101187. Source: MGI

peptidyl-tyrosine autophosphorylation

Inferred from direct assay PubMed 10100151. Source: MGI

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 18451178. Source: MGI

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokinesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from mutant phenotype PubMed 23906066. Source: MGI

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 18451178. Source: MGI

positive regulation of steroid hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

prostate gland epithelium morphogenesis

Inferred from mutant phenotype PubMed 18451178. Source: MGI

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 18216249. Source: MGI

protein tetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from direct assay PubMed 7931420. Source: MGI

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 18451178. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

insulin binding

Inferred from electronic annotation. Source: Ensembl

insulin receptor substrate binding

Inferred from sequence or structural similarity. Source: UniProtKB

insulin-like growth factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

insulin-like growth factor-activated receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12771153PubMed 12917015. Source: MGI

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 737707Insulin-like growth factor 1 receptor alpha chain
PRO_0000016683
Chain742 – 1373632Insulin-like growth factor 1 receptor beta chain
PRO_0000016684

Regions

Topological domain742 – 936195Extracellular Potential
Transmembrane937 – 96024Helical; Potential
Topological domain961 – 1373413Cytoplasmic By similarity
Domain490 – 610121Fibronectin type-III 1
Domain611 – 70999Fibronectin type-III 2
Domain735 – 82995Fibronectin type-III 3
Domain835 – 92894Fibronectin type-III 4
Domain1000 – 1276277Protein kinase
Nucleotide binding1006 – 10149ATP By similarity
Motif978 – 9814IRS1- and SHC1-binding By similarity

Sites

Active site11371Proton acceptor By similarity
Binding site10341ATP By similarity

Amino acid modifications

Modified residue9811Phosphotyrosine By similarity
Modified residue11631Phosphotyrosine; by autocatalysis By similarity
Modified residue11671Phosphotyrosine; by autocatalysis By similarity
Modified residue11681Phosphotyrosine; by autocatalysis By similarity
Modified residue12801Phosphoserine; by GSK3-beta Ref.8
Modified residue12841Phosphoserine Ref.8
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation5351N-linked (GlcNAc...) Potential
Glycosylation6081N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Glycosylation6391N-linked (GlcNAc...); atypical Ref.7
Glycosylation6411N-linked (GlcNAc...) Ref.7
Glycosylation7481N-linked (GlcNAc...) Ref.6
Glycosylation7571N-linked (GlcNAc...) Ref.7
Glycosylation7651N-linked (GlcNAc...) Ref.7
Glycosylation9011N-linked (GlcNAc...) Ref.6
Glycosylation9141N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 52 By similarity
Disulfide bond150 ↔ 178 By similarity
Disulfide bond182 ↔ 205 By similarity
Disulfide bond192 ↔ 211 By similarity
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
Disulfide bond332 ↔ 354 By similarity
Disulfide bond456 ↔ 489 By similarity
Cross-link1170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict58 – 592FL → LV in AAC52123. Ref.2
Sequence conflict2601C → S in AAC52123. Ref.2
Sequence conflict3011D → G in AAC52123. Ref.2
Sequence conflict3061E → V in AAC52123. Ref.2
Sequence conflict3241C → S in AAC52123. Ref.2
Sequence conflict11341V → I in AAA40013. Ref.3
Sequence conflict11451V → D in AAA40013. Ref.3
Sequence conflict12021V → I in AAA40013. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q60751 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 5EE3B72EF101E379

FASTA1,373155,788
        10         20         30         40         50         60 
MKSGSGGGSP TSLWGLVFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE NCTVIEGFLH 

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

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

       190        200        210        220        230        240 
LCPGTLEEKP MCEKTTINNE YNYRCWTTNR CQKMCPSVCG KRACTENNEC CHPECLGSCH 

       250        260        270        280        290        300 
TPDDNTTCVA CRHYYYKGVC VPACPPGTYR FEGWRCVDRD FCANIPNAES SDSDGFVIHD 

       310        320        330        340        350        360 
DECMQECPSG FIRNSTQSMY CIPCEGPCPK VCGDEEKKTK TIDSVTSAQM LQGCTILKGN 

       370        380        390        400        410        420 
LLINIRRGNN IASELENFMG LIEVVTGYVK IRHSHALVSL SFLKNLRLIL GEEQLEGNYS 

       430        440        450        460        470        480 
FYVLDNQNLQ QLWDWNHRNL TVRSGKMYFA FNPKLCVSEI YRMEEVTGTK GRQSKGDINT 

       490        500        510        520        530        540 
RNNGERASCE SDVLRFTSTT TWKNRIIITW HRYRPPDYRD LISFTVYYKE APFKNVTEYD 

       550        560        570        580        590        600 
GQDACGSNSW NMVDVDLPPN KEGEPGILLH GLKPWTQYAV YVKAVTLTMV ENDHIRGAKS 

       610        620        630        640        650        660 
EILYIRTNAS VPSIPLDVLS ASNSSSQLIV KWNPPTLPNG NLSYYIVRWQ RQPQDGYLYR 

       670        680        690        700        710        720 
HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC CACPKTEAEK QAEKEEAEYR 

       730        740        750        760        770        780 
KVFENFLHNS IFVPRPERRR RDVMQVANTT MSSRSRNTTV ADTYNITDPE EFETEYPFFE 

       790        800        810        820        830        840 
SRVDNKERTV ISNLRPFTLY RIDIHSCNHE AEKLGCSASN FVFARTMPAE GADDIPGPVT 

       850        860        870        880        890        900 
WEPRPENSIF LKWPEPENPN GLILMYEIKY GSQVEDQREC VSRQEYRKYG GAKLNRLNPG 

       910        920        930        940        950        960 
NYTARIQATS LSGNGSWTDP VFFYVPAKTT YENFMHLIIA LPVAILLIVG GLVIMLYVFH 

       970        980        990       1000       1010       1020 
RKRNNSRLGN GVLYASVNPE YFSAADVYVP DEWEVAREKI TMNRELGQGS FGMVYEGVAK 

      1030       1040       1050       1060       1070       1080 
GVVKDEPETR VAIKTVNEAA SMRERIEFLN EASVMKEFNC HHVVRLLGVV SQGQPTLVIM 

      1090       1100       1110       1120       1130       1140 
ELMTRGDLKS YLRSLRPEVE QNNLVLIPPS LSKMIQMAGE IADGMAYLNA NKFVHRDLAA 

      1150       1160       1170       1180       1190       1200 
RNCMVAEDFT VKIGDFGMTR DIYETDYYRK GGKGLLPVRW MSPESLKDGV FTTHSDVWSF 

      1210       1220       1230       1240       1250       1260 
GVVLWEIATL AEQPYQGLSN EQVLRFVMEG GLLDKPDNCP DMLFELMRMC WQYNPKMRPS 

      1270       1280       1290       1300       1310       1320 
FLEIIGSIKD EMEPSFQEVS FYYSEENKPP EPEELEMELE MEPENMESVP LDPSASSASL 

      1330       1340       1350       1360       1370 
PLPERHSGHK AENGPGPGVL VLRASFDERQ PYAHMNGGRA NERALPLPQS STC 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF056187 mRNA. Translation: AAC12782.1.
U00182 mRNA. Translation: AAC52123.1.
M33422 mRNA. Translation: AAA40013.1.
PIRA48805.
JH0113.
RefSeqNP_034643.2. NM_010513.2.
UniGeneMm.275742.

3D structure databases

ProteinModelPortalQ60751.
SMRQ60751. Positions 30-653, 785-828, 848-1288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200548. 4 interactions.
IntActQ60751. 2 interactions.
MINTMINT-219894.

Chemistry

BindingDBQ60751.
ChEMBLCHEMBL5381.

PTM databases

PhosphoSiteQ60751.

Proteomic databases

MaxQBQ60751.
PaxDbQ60751.
PRIDEQ60751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16001.
KEGGmmu:16001.

Organism-specific databases

CTD3480.
MGIMGI:96433. Igf1r.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000038045.
HOVERGENHBG006134.
InParanoidQ60751.
KOK05087.
PhylomeDBQ60751.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressQ60751.
BgeeQ60751.
CleanExMM_IGF1R.
GenevestigatorQ60751.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProIPR000494. 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]
PfamPF00041. fn3. 1 hit.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000620. Insulin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

ChiTaRSIGF1R. mouse.
NextBio288790.
PROQ60751.
SOURCESearch...

Entry information

Entry nameIGF1R_MOUSE
AccessionPrimary (citable) accession number: Q60751
Secondary accession number(s): O70438, Q62123
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot