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Q60751

- IGF1R_MOUSE

UniProt

Q60751 - IGF1R_MOUSE

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Protein

Insulin-like growth factor 1 receptor

Gene

Igf1r

Organism
Mus musculus (Mouse)
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 (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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1034 – 10341ATPPROSITE-ProRule annotation
Active sitei1137 – 11371Proton 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. insulin binding Source: Ensembl
  3. insulin-like growth factor-activated receptor activity Source: UniProtKB
  4. insulin-like growth factor binding Source: UniProtKB
  5. insulin receptor substrate binding Source: UniProtKB
  6. phosphatidylinositol 3-kinase binding Source: UniProtKB
  7. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. brain development Source: MGI
  3. epidermis development Source: MGI
  4. establishment of cell polarity Source: Ensembl
  5. exocrine pancreas development Source: MGI
  6. immune response Source: Ensembl
  7. inactivation of MAPKK activity Source: Ensembl
  8. insulin-like growth factor receptor signaling pathway Source: UniProtKB
  9. male sex determination Source: MGI
  10. mammary gland development Source: MGI
  11. negative regulation of MAPK cascade Source: MGI
  12. negative regulation of muscle cell apoptotic process Source: Ensembl
  13. negative regulation of protein kinase B signaling Source: MGI
  14. negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  15. organ morphogenesis Source: MGI
  16. peptidyl-tyrosine autophosphorylation Source: MGI
  17. phosphatidylinositol-mediated signaling Source: Ensembl
  18. positive regulation of cell migration Source: Ensembl
  19. positive regulation of cytokinesis Source: Ensembl
  20. positive regulation of DNA replication Source: Ensembl
  21. positive regulation of MAPK cascade Source: MGI
  22. positive regulation of mitosis Source: MGI
  23. positive regulation of protein kinase B signaling Source: MGI
  24. positive regulation of steroid hormone biosynthetic process Source: Ensembl
  25. prostate gland epithelium morphogenesis Source: MGI
  26. protein autophosphorylation Source: UniProtKB
  27. protein heterooligomerization Source: Ensembl
  28. protein phosphorylation Source: MGI
  29. protein tetramerization Source: UniProtKB
  30. regulation of JNK cascade Source: Ensembl
  31. response to vitamin E Source: Ensembl
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.
ReactomeiREACT_188215. IRS-related events triggered by IGF1R.
REACT_188219. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
REACT_188220. SHC-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:96433. Igf1r.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini742 – 936195ExtracellularSequence AnalysisAdd
BLAST
Transmembranei937 – 96024HelicalSequence AnalysisAdd
BLAST
Topological domaini961 – 1373413CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. caveola Source: Ensembl
  2. integral component of membrane Source: MGI
  3. intracellular membrane-bounded organelle Source: Ensembl
  4. neuron projection Source: Ensembl
  5. plasma membrane Source: MGI
  6. receptor complex 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 737707Insulin-like growth factor 1 receptor alpha chainPRO_0000016683Add
BLAST
Chaini742 – 1373632Insulin-like growth factor 1 receptor beta chainPRO_0000016684Add
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
Glycosylationi639 – 6391N-linked (GlcNAc...); atypical1 Publication
Glycosylationi641 – 6411N-linked (GlcNAc...)1 Publication
Glycosylationi748 – 7481N-linked (GlcNAc...)1 Publication
Glycosylationi757 – 7571N-linked (GlcNAc...)1 Publication
Glycosylationi765 – 7651N-linked (GlcNAc...)1 Publication
Glycosylationi901 – 9011N-linked (GlcNAc...)1 Publication
Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence Analysis
Modified residuei981 – 9811PhosphotyrosineBy similarity
Modified residuei1163 – 11631Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1167 – 11671Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1168 – 11681Phosphotyrosine; by autocatalysisBy similarity
Cross-linki1170 – 1170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1173 – 1173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1280 – 12801Phosphoserine; by GSK3-beta1 Publication
Modified residuei1284 – 12841Phosphoserine1 Publication

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.
PRIDEiQ60751.

PTM databases

PhosphoSiteiQ60751.

Expressioni

Gene expression databases

BgeeiQ60751.
CleanExiMM_IGF1R.
ExpressionAtlasiQ60751. baseline and differential.
GenevestigatoriQ60751.

Interactioni

Protein-protein interaction databases

BioGridi200548. 4 interactions.
IntActiQ60751. 2 interactions.
MINTiMINT-219894.

Structurei

3D structure databases

ProteinModelPortaliQ60751.
SMRiQ60751. Positions 30-653, 785-828, 848-1288.
ModBaseiSearch...
MobiDBiSearch...

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
Domaini735 – 82995Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini835 – 92894Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1000 – 1276277Protein 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 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.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiQ60751.
KOiK05087.
PhylomeDBiQ60751.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 592FL → LV in AAC52123. (PubMed:8234298)Curated
Sequence conflicti260 – 2601C → S in AAC52123. (PubMed:8234298)Curated
Sequence conflicti301 – 3011D → G in AAC52123. (PubMed:8234298)Curated
Sequence conflicti306 – 3061E → V in AAC52123. (PubMed:8234298)Curated
Sequence conflicti324 – 3241C → S in AAC52123. (PubMed:8234298)Curated
Sequence conflicti1134 – 11341V → I in AAA40013. (PubMed:2482828)Curated
Sequence conflicti1145 – 11451V → D in AAA40013. (PubMed:2482828)Curated
Sequence conflicti1202 – 12021V → I in AAA40013. (PubMed:2482828)Curated

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 .
PIRi A48805.
JH0113.
RefSeqi NP_034643.2. NM_010513.2.
UniGenei Mm.275742.

3D structure databases

ProteinModelPortali Q60751.
SMRi Q60751. Positions 30-653, 785-828, 848-1288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200548. 4 interactions.
IntActi Q60751. 2 interactions.
MINTi MINT-219894.

Chemistry

BindingDBi Q60751.
ChEMBLi CHEMBL5381.

PTM databases

PhosphoSitei Q60751.

Proteomic databases

MaxQBi Q60751.
PaxDbi Q60751.
PRIDEi Q60751.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16001.
KEGGi mmu:16001.

Organism-specific databases

CTDi 3480.
MGIi MGI:96433. Igf1r.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000038045.
HOVERGENi HBG006134.
InParanoidi Q60751.
KOi K05087.
PhylomeDBi Q60751.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_188215. IRS-related events triggered by IGF1R.
REACT_188219. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
REACT_188220. SHC-related events triggered by IGF1R.

Miscellaneous databases

ChiTaRSi Igf1r. mouse.
NextBioi 288790.
PROi Q60751.
SOURCEi Search...

Gene expression databases

Bgeei Q60751.
CleanExi MM_IGF1R.
ExpressionAtlasi Q60751. baseline and differential.
Genevestigatori Q60751.

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. "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.

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 26, 2014
This is version 153 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

External Data

Dasty 3