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Insulin receptor substrate 1 (IRS-1)

 IRS1_MOUSE              Reviewed;        1233 AA.
P35569;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Insulin receptor substrate 1;
Short=IRS-1;
Name=Irs1; Synonyms=Irs-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8167159; DOI=10.1016/0167-4889(94)90261-5;
Araki E., Haag B.L. III, Kahn C.R.;
"Cloning of the mouse insulin receptor substrate-1 (IRS-1) gene and
complete sequence of mouse IRS-1.";
Biochim. Biophys. Acta 1221:353-356(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8448209; DOI=10.1016/0167-4781(93)90222-Y;
Keller S.R., Aebersold R., Garner C.W., Lienhard G.E.;
"The insulin-elicited 160 kDa phosphotyrosine protein in mouse
adipocytes is an insulin receptor substrate 1: identification by
cloning.";
Biochim. Biophys. Acta 1172:323-326(1993).
[3]
INTERACTION WITH FER.
PubMed=11006284; DOI=10.1074/jbc.M006665200;
Iwanishi M., Czech M.P., Cherniack A.D.;
"The protein-tyrosine kinase fer associates with signaling complexes
containing insulin receptor substrate-1 and phosphatidylinositol 3-
kinase.";
J. Biol. Chem. 275:38995-39000(2000).
[4]
INTERACTION WITH PHIP.
PubMed=11018022; DOI=10.1074/jbc.C000611200;
Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
"Cloning and characterization of PHIP, a novel insulin receptor
substrate-1 pleckstrin homology domain interacting protein.";
J. Biol. Chem. 275:40492-40497(2000).
[5]
TISSUE SPECIFICITY.
PubMed=10749573; DOI=10.1172/JCI9017;
Ogata N., Chikazu D., Kubota N., Terauchi Y., Tobe K., Azuma Y.,
Ohta T., Kadowaki T., Nakamura K., Kawaguchi H.;
"Insulin receptor substrate-1 in osteoblast is indispensable for
maintaining bone turnover.";
J. Clin. Invest. 105:935-943(2000).
[6]
PHOSPHORYLATION AT SER-789.
PubMed=11598104; DOI=10.1074/jbc.C100483200;
Jakobsen S.N., Hardie D.G., Morrice N., Tornqvist H.E.;
"5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in
mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide
riboside.";
J. Biol. Chem. 276:46912-46916(2001).
[7]
INTERACTION WITH UBTF AND PIK3CA, AND EFFECT ON CELL AND BODY SIZE.
PubMed=15197263; DOI=10.1073/pnas.0403328101;
Drakas R., Tu X., Baserga R.;
"Control of cell size through phosphorylation of upstream binding
factor 1 by nuclear phosphatidylinositol 3-kinase.";
Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004).
[8]
PHOSPHORYLATION AT SER-632.
PubMed=16098829; DOI=10.1016/j.cmet.2005.06.011;
Furukawa N., Ongusaha P., Jahng W.J., Araki K., Choi C.S., Kim H.J.,
Lee Y.H., Kaibuchi K., Kahn B.B., Masuzaki H., Kim J.K., Lee S.W.,
Kim Y.B.;
"Role of Rho-kinase in regulation of insulin action and glucose
homeostasis.";
Cell Metab. 2:119-129(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 AND SER-1097, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-414; SER-887;
SER-1096 AND SER-1097, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
INTERACTION WITH EIF2AK2.
PubMed=22948222; DOI=10.1210/en.2012-1400;
Carvalho-Filho M.A., Carvalho B.M., Oliveira A.G., Guadagnini D.,
Ueno M., Dias M.M., Tsukumo D.M., Hirabara S.M., Reis L.F., Curi R.,
Carvalheira J.B., Saad M.J.;
"Double-stranded RNA-activated protein kinase is a key modulator of
insulin sensitivity in physiological conditions and in obesity in
mice.";
Endocrinology 153:5261-5274(2012).
-!- FUNCTION: May mediate the control of various cellular processes by
insulin. When phosphorylated by the insulin receptor binds
specifically to various cellular proteins containing SH2 domains
such as phosphatidylinositol 3-kinase p85 subunit or GRB2.
Activates phosphatidylinositol 3-kinase when bound to the
regulatory p85 subunit (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts (via phosphorylated YXXM motifs) with PIK3R1
(By similarity). Interacts with ROCK1 (By similarity). Interacts
with GRB2 (By similarity). Interacts with SOCS7 (By similarity).
Interacts (via IRS-type PTB domain) with IGF1R and INSR (via the
tyrosine-phosphorylated NPXY motif) (By similarity). Interacts
with UBTF and PIK3CA. Interacts (via PH domain) with PHIP.
Interacts with FER. Interacts with ALK (By similarity). Interacts
with EIF2AK2/PKR. {ECO:0000250, ECO:0000269|PubMed:11006284,
ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:15197263,
ECO:0000269|PubMed:22948222}.
-!- INTERACTION:
Q03963:Eif2ak2; NbExp=2; IntAct=EBI-400825, EBI-2603444;
P26450:Pik3r1; NbExp=2; IntAct=EBI-400825, EBI-641764;
Q13625-2:TP53BP2 (xeno); NbExp=2; IntAct=EBI-400825, EBI-287091;
Q1XH17:Trim72; NbExp=4; IntAct=EBI-400825, EBI-16034016;
-!- TISSUE SPECIFICITY: Expressed in osteoblasts, but not in
osteoclasts. {ECO:0000269|PubMed:10749573}.
-!- PTM: Serine phosphorylation of IRS1 is a mechanism for insulin
resistance. Ser-307 phosphorylation inhibits insulin action
through disruption of IRS1 interaction with the insulin receptor
(By similarity). Phosphorylation of Tyr-891 is required for GRB2-
binding (By similarity). Phosphorylated by ALK. Phosphorylated at
Ser-265, Ser-302, Ser-632 and Ser-1097 by RPS6KB1; phosphorylation
induces accelerated degradation of IRS1 (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated by the Cul7-RING(FBXW8) complex in a mTOR-
dependent manner, leading to its degradation: the Cul7-RING(FBXW8)
complex recognizes and binds IRS1 previously phosphorylated by S6
kinase (RPS6KB1 or RPS6KB2). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; L24563; AAA39335.1; -; mRNA.
EMBL; X69722; CAA49378.1; -; mRNA.
PIR; S30185; S30185.
RefSeq; NP_034700.2; NM_010570.4.
UniGene; Mm.4952; -.
PDB; 1AYB; X-ray; 3.00 A; P=887-898.
PDB; 5AXI; X-ray; 2.50 A; E=606-610.
PDBsum; 1AYB; -.
PDBsum; 5AXI; -.
ProteinModelPortal; P35569; -.
SMR; P35569; -.
BioGrid; 200788; 13.
DIP; DIP-32456N; -.
IntAct; P35569; 51.
MINT; MINT-1540686; -.
STRING; 10090.ENSMUSP00000063795; -.
iPTMnet; P35569; -.
PhosphoSitePlus; P35569; -.
SwissPalm; P35569; -.
MaxQB; P35569; -.
PaxDb; P35569; -.
PeptideAtlas; P35569; -.
PRIDE; P35569; -.
GeneID; 16367; -.
KEGG; mmu:16367; -.
CTD; 3667; -.
MGI; MGI:99454; Irs1.
eggNOG; ENOG410IXEK; Eukaryota.
eggNOG; ENOG410Z9EP; LUCA.
HOGENOM; HOG000113103; -.
HOVERGEN; HBG000542; -.
InParanoid; P35569; -.
KO; K16172; -.
PhylomeDB; P35569; -.
Reactome; R-MMU-198203; PI3K/AKT activation.
Reactome; R-MMU-2586551; Signaling by Leptin.
ChiTaRS; Irs1; mouse.
EvolutionaryTrace; P35569; -.
PRO; PR:P35569; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_IRS1; -.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0036064; C:ciliary basal body; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:MGI.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IDA:MGI.
GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; ISO:MGI.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; IMP:MGI.
GO; GO:0030879; P:mammary gland development; IGI:MGI.
GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; ISO:MGI.
GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0032868; P:response to insulin; ISO:MGI.
CDD; cd01204; PTB_IRS; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR002404; IRS_PTB.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
Pfam; PF02174; IRS; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00628; INSULINRSI.
SMART; SM00233; PH; 1.
SMART; SM00310; PTBI; 1.
SUPFAM; SSF50729; SSF50729; 2.
PROSITE; PS51064; IRS_PTB; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
Repeat; Transducer; Ubl conjugation.
CHAIN 1 1233 Insulin receptor substrate 1.
/FTId=PRO_0000084237.
DOMAIN 12 115 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 155 259 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
REGION 3 133 Mediates interaction with PHIP.
{ECO:0000250}.
REGION 891 893 GRB2-binding. {ECO:0000250}.
MOTIF 460 463 YXXM motif 1.
MOTIF 546 549 YXXM motif 2.
MOTIF 608 611 YXXM motif 3.
MOTIF 628 631 YXXM motif 4.
MOTIF 658 661 YXXM motif 5.
MOTIF 727 730 YXXM motif 6.
MOTIF 935 938 YXXM motif 7.
MOTIF 983 986 YXXM motif 8.
MOTIF 1006 1009 YXXM motif 9.
COMPBIAS 675 680 Poly-Ser.
COMPBIAS 872 877 Poly-Gln.
COMPBIAS 1119 1128 Poly-Gly.
COMPBIAS 1194 1198 Poly-Pro.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 99 99 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 265 265 Phosphoserine; by RPS6KB1.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 302 302 Phosphoserine; by RPS6KB1.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 307 307 Phosphoserine; by IKKB, MAPK8 and
RPS6KB1. {ECO:0000250|UniProtKB:P35568}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 448 448 Phosphothreonine.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 460 460 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 522 522 Phosphoserine; by RPS6KB1.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 608 608 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 628 628 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 632 632 Phosphoserine; by RPS6KB1 and ROCK2.
{ECO:0000305|PubMed:16098829}.
MOD_RES 658 658 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 789 789 Phosphoserine; by AMPK and SIK2.
{ECO:0000269|PubMed:11598104}.
MOD_RES 887 887 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 891 891 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 935 935 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 983 983 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 1096 1096 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1097 1097 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1173 1173 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35570}.
MOD_RES 1220 1220 Phosphotyrosine; by INSR.
{ECO:0000250|UniProtKB:P35570}.
CONFLICT 1038 1039 Missing (in Ref. 2). {ECO:0000305}.
CONFLICT 1182 1182 H -> R (in Ref. 2; CAA49378).
{ECO:0000305}.
SEQUENCE 1233 AA; 130723 MW; C0E9B2D890DADD87 CRC64;
MASPPDTDGF SDVRKVGYLR KPKSMHKRFF VLRAASEAGG PARLEYYENE KKWRHKSSAP
KRSIPLESCF NINKRADSKN KHLVALYTRD EHFAIAADSE AEQDSWYQAL LQLHNRAKAH
HDGAGGGCGG SCSGSSGVGE AGEDLSYDTG PGPAFKEVWQ VILKPKGLGQ TKNLIGIYRL
CLTSKTISFV KLNSEAAAVV LQLMNIRRCG HSENFFFIEV GRSAVTGPGE FWMQVDDSVV
AQNMHETILE AMRAMSDEFR PRSKSQSSSS CSNPISVPLR RHHLNNPPPS QVGLTRRSRT
ESITATSPAS MVGGKPGSFR VRASSDGEGT MSRPASVDGS PVSPSTNRTH AHRHRGSSRL
HPPLNHSRSI PMPSSRCSPS ATSPVSLSSS STSGHGSTSD CLFPRRSSAS VSGSPSDGGF
ISSDEYGSSP CDFRSSFRSV TPDSLGHTPP ARGEEELSNY ICMGGKGAST LAAPNGHYIL
SRGGNGHRYI PGANLGTSPA LPGDEAAGAA DLDNRFRKRT HSAGTSPTIS HQKTPSQSSV
ASIEEYTEMM PAAYPPGGGS GGRLPGYRHS AFVPTHSYPE EGLEMHHLER RGGHHRPDTS
NLHTDDGYMP MSPGVAPVPS NRKGNGDYMP MSPKSVSAPQ QIINPIRRHP QRVDPNGYMM
MSPSGSCSPD IGGGSSSSSS ISAAPSGSSY GKPWTNGVGG HHTHALPHAK PPVESGGGKL
LPCTGDYMNM SPVGDSNTSS PSECYYGPED PQHKPVLSYY SLPRSFKHTQ RPGEPEEGAR
HQHLRLSSSS GRLRYTATAE DSSSSTSSDS LGGGYCGARP ESSLTHPHHH VLQPHLPRKV
DTAAQTNSRL ARPTRLSLGD PKASTLPRVR EQQQQQQSSL HPPEPKSPGE YVNIEFGSGQ
PGYLAGPATS RSSPSVRCPP QLHPAPREET GSEEYMNMDL GPGRRATWQE SGGVELGRIG
PAPPGSATVC RPTRSVPNSR GDYMTMQIGC PRQSYVDTSP VAPVSYADMR TGIAAEKASL
PRPTGAAPPP SSTASSSASV TPQGATAEQA THSSLLGGPQ GPGGMSAFTR VNLSPNHNQS
AKVIRADTQG CRRRHSSETF SAPTRAGNTV PFGAGAAVGG SGGGGGGGSE DVKRHSSASF
ENVWLRPGDL GGVSKESAPV CGAAGGLEKS LNYIDLDLAK EHSQDCPSQQ QSLPPPPPHQ
PLGSNEGNSP RRSSEDLSNY ASISFQKQPE DRQ


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