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Protein

Insulin-like growth factor 1 receptor

Gene

Igf1r

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity). When present in a hybrid receptor with INSR, binds IGF1 (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1034ATPPROSITE-ProRule annotation1
Active sitei1137Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1006 – 1014ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • adrenal gland development Source: CACAO
  • animal organ morphogenesis Source: MGI
  • brain development Source: MGI
  • cellular response to glucose stimulus Source: MGI
  • cellular response to insulin stimulus Source: MGI
  • epidermis development Source: MGI
  • exocrine pancreas development Source: MGI
  • immune response Source: MGI
  • inactivation of MAPKK activity Source: MGI
  • insulin-like growth factor receptor signaling pathway Source: UniProtKB
  • male sex determination Source: MGI
  • mammary gland development Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of MAPK cascade Source: MGI
  • negative regulation of protein kinase B signaling Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • peptidyl-tyrosine autophosphorylation Source: MGI
  • phosphatidylinositol-mediated signaling Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of DNA replication Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of meiotic cell cycle Source: CACAO
  • positive regulation of mitotic nuclear division Source: MGI
  • positive regulation of protein kinase B signaling Source: MGI
  • positive regulation of transcription, DNA-templated Source: CACAO
  • prostate gland epithelium morphogenesis Source: MGI
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: MGI
  • protein tetramerization Source: UniProtKB
  • regulation of JNK cascade Source: MGI
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. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor 1 receptor (EC:2.7.10.1)
Alternative name(s):
Insulin-like growth factor I receptor
Short name:
IGF-I receptor
CD_antigen: CD221
Cleaved into the following 2 chains:
Gene namesi
Name:Igf1r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96433. Igf1r.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini742 – 936ExtracellularSequence analysisAdd BLAST195
Transmembranei937 – 960HelicalSequence analysisAdd BLAST24
Topological domaini961 – 1373CytoplasmicBy similarityAdd BLAST413

GO - Cellular componenti

  • alphav-beta3 integrin-IGF-1-IGF1R complex Source: MGI
  • integral component of membrane Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
  • T-tubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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

Chemistry databases

ChEMBLiCHEMBL5381.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001668331 – 737Insulin-like growth factor 1 receptor alpha chainAdd BLAST707
ChainiPRO_0000016684742 – 1373Insulin-like growth factor 1 receptor beta chainAdd BLAST632

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 52By similarity
Glycosylationi51N-linked (GlcNAc...)Sequence analysis1
Glycosylationi102N-linked (GlcNAc...)Sequence analysis1
Glycosylationi135N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi245N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi251 ↔ 260By similarity
Disulfide bondi264 ↔ 276By similarity
Disulfide bondi282 ↔ 303By similarity
Disulfide bondi307 ↔ 321By similarity
Glycosylationi314N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi324 ↔ 328By similarity
Disulfide bondi332 ↔ 354By similarity
Glycosylationi418N-linked (GlcNAc...)Sequence analysis1
Glycosylationi439N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi456 ↔ 489By similarity
Glycosylationi535N-linked (GlcNAc...)Sequence analysis1
Glycosylationi608N-linked (GlcNAc...)Sequence analysis1
Glycosylationi623N-linked (GlcNAc...)Sequence analysis1
Glycosylationi639N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi641N-linked (GlcNAc...)1 Publication1
Glycosylationi748N-linked (GlcNAc...)1 Publication1
Glycosylationi757N-linked (GlcNAc...)1 Publication1
Glycosylationi765N-linked (GlcNAc...)1 Publication1
Glycosylationi901N-linked (GlcNAc...)1 Publication1
Glycosylationi914N-linked (GlcNAc...)Sequence analysis1
Modified residuei1163Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1167Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1168Phosphotyrosine; by autocatalysisBy similarity1
Cross-linki1170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1280Phosphoserine; by GSK3-beta1 Publication1
Modified residuei1284Phosphoserine1 Publication1

Post-translational modificationi

Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1167 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1163 and Tyr-1168. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1163, Tyr-1167 and Tyr-1168) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-981 is required for IRS1- and SHC1-binding (By similarity). Phosphorylation of Ser-1280 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1284. Dephosphorylated by PTPN1.By similarity1 Publication
Polyubiquitinated at Lys-1170 and Lys-1173 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation (By similarity).By similarity
Sumoylated with SUMO1.By similarity
Controlled by regulated intramembrane proteolysis (RIP). Undergoes metalloprotease-dependent constitutive ectodomain shedding to produce a membrane-anchored 52 kDa C-Terminal fragment which is further processed by presenilin gamma-secretase to yield an intracellular 50 kDa fragment (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiQ60751.
PaxDbiQ60751.
PeptideAtlasiQ60751.
PRIDEiQ60751.

PTM databases

iPTMnetiQ60751.
PhosphoSitePlusiQ60751.

Expressioni

Gene expression databases

BgeeiENSMUSG00000005533.
CleanExiMM_IGF1R.

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 RACK1. Interacts with SOCS1, SOCS2 and SOCS3. Interacts with 14-3-3 proteins. Interacts with NMD2. Interacts with MAP3K5. Interacts with STAT3. Found in a ternary complex with IGF1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200548. 6 interactors.
IntActiQ60751. 2 interactors.
MINTiMINT-219894.
STRINGi10090.ENSMUSP00000005671.

Chemistry databases

BindingDBiQ60751.

Structurei

3D structure databases

ProteinModelPortaliQ60751.
SMRiQ60751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini490 – 610Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST121
Domaini611 – 709Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST99
Domaini735 – 829Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST95
Domaini835 – 928Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST94
Domaini1000 – 1276Protein kinasePROSITE-ProRule annotationAdd BLAST277

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi978 – 981IRS1- and SHC1-bindingBy similarity4

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

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiQ60751.
KOiK05087.
PhylomeDBiQ60751.

Family and domain databases

CDDicd00063. FN3. 3 hits.
Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
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]
PfamiPF00757. 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.
SSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60751-1 [UniParc]FASTAAdd to basket

« 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
DECMQECPSG 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
RQPQDGYLYR HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC
710 720 730 740 750
CACPKTEAEK QAEKEEAEYR KVFENFLHNS IFVPRPERRR RDVMQVANTT
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
QNNLVLIPPS LSKMIQMAGE IADGMAYLNA NKFVHRDLAA RNCMVAEDFT
1160 1170 1180 1190 1200
VKIGDFGMTR DIYETDYYRK GGKGLLPVRW MSPESLKDGV FTTHSDVWSF
1210 1220 1230 1240 1250
GVVLWEIATL AEQPYQGLSN EQVLRFVMEG GLLDKPDNCP DMLFELMRMC
1260 1270 1280 1290 1300
WQYNPKMRPS FLEIIGSIKD EMEPSFQEVS FYYSEENKPP EPEELEMELE
1310 1320 1330 1340 1350
MEPENMESVP LDPSASSASL PLPERHSGHK AENGPGPGVL VLRASFDERQ
1360 1370
PYAHMNGGRA NERALPLPQS STC
Length:1,373
Mass (Da):155,788
Last modified:January 11, 2001 - v3
Checksum:i5EE3B72EF101E379
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58 – 59FL → LV in AAC52123 (PubMed:8234298).Curated2
Sequence conflicti260C → S in AAC52123 (PubMed:8234298).Curated1
Sequence conflicti301D → G in AAC52123 (PubMed:8234298).Curated1
Sequence conflicti306E → V in AAC52123 (PubMed:8234298).Curated1
Sequence conflicti324C → S in AAC52123 (PubMed:8234298).Curated1
Sequence conflicti1134V → I in AAA40013 (PubMed:2482828).Curated1
Sequence conflicti1145V → D in AAA40013 (PubMed:2482828).Curated1
Sequence conflicti1202V → I in AAA40013 (PubMed:2482828).Curated1

Sequence databases

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

Genome annotation databases

GeneIDi16001.
KEGGimmu:16001.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ60751.
SMRiQ60751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200548. 6 interactors.
IntActiQ60751. 2 interactors.
MINTiMINT-219894.
STRINGi10090.ENSMUSP00000005671.

Chemistry databases

BindingDBiQ60751.
ChEMBLiCHEMBL5381.

PTM databases

iPTMnetiQ60751.
PhosphoSitePlusiQ60751.

Proteomic databases

MaxQBiQ60751.
PaxDbiQ60751.
PeptideAtlasiQ60751.
PRIDEiQ60751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16001.
KEGGimmu:16001.

Organism-specific databases

CTDi3480.
MGIiMGI:96433. Igf1r.

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiQ60751.
KOiK05087.
PhylomeDBiQ60751.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Miscellaneous databases

ChiTaRSiIgf1r. mouse.
PROiQ60751.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005533.
CleanExiMM_IGF1R.

Family and domain databases

CDDicd00063. FN3. 3 hits.
Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
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]
PfamiPF00757. 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.
SSF52058. SSF52058. 2 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]
ProtoNetiSearch...

Entry informationi

Entry nameiIGF1R_MOUSE
AccessioniPrimary (citable) accession number: Q60751
Secondary accession number(s): O70438, Q62123
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.