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Insulin receptor substrate 1 (IRS-1) (pp185)

 IRS1_RAT                Reviewed;        1235 AA.
P35570;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
28-MAR-2018, entry version 154.
RecName: Full=Insulin receptor substrate 1;
Short=IRS-1;
AltName: Full=pp185;
Name=Irs1; Synonyms=Irs-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1648180; DOI=10.1038/352073a0;
Sun X.-J., Rothenberg P.L., Kahn C.R., Backer J.M., Araki E.,
Wilden P.A., Cahill D.A., Goldstein B.J., White M.F.;
"Structure of the insulin receptor substrate IRS-1 defines a unique
signal transduction protein.";
Nature 352:73-77(1991).
[2]
PROTEIN SEQUENCE OF 44-51; 173-178; 223-243; 489-506; 635-646; 932-947
AND 1098-1106.
PubMed=2022647;
Rothenberg P.L., Lane W.S., Karasik A., Backer J.M., White M.F.,
Kahn C.R.;
"Purification and partial sequence analysis of pp185, the major
cellular substrate of the insulin receptor tyrosine kinase.";
J. Biol. Chem. 266:8302-8311(1991).
[3]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH PIK3R1.
PubMed=1380456;
Backer J.M., Myers M.G. Jr., Shoelson S.E., Chin D.J., Sun X.-J.,
Miralpeix M., Hu P., Margolis B., Skolnik E.Y., Schlessinger J.,
White M.F.;
"Phosphatidylinositol 3'-kinase is activated by association with IRS-1
during insulin stimulation.";
EMBO J. 11:3469-3479(1992).
[4]
INTERACTION WITH GRB2.
PubMed=8491186;
Skolnik E.Y., Lee C.-H., Batzer A.G., Vicentini L.M., Zhou M.,
Daly R.J., Myers M.J. Jr., Backer J.M., Ullrich A., White M.F.,
Schlessinger J.;
"The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-
phosphorylated IRS1 and Shc: implications for insulin control of ras
signalling.";
EMBO J. 12:1929-1936(1993).
[5]
PHOSPHORYLATION AT TYR-460; TYR-608; TYR-628; TYR-895; TYR-939;
TYR-987; TYR-1172 AND TYR-1222.
PubMed=7504175; DOI=10.1128/MCB.13.12.7418;
Sun X.-J., Crimmins D.L., Myers M.G. Jr., Miralpeix M., White M.F.;
"Pleiotropic insulin signals are engaged by multisite phosphorylation
of IRS-1.";
Mol. Cell. Biol. 13:7418-7428(1993).
[6]
PHOSPHORYLATION AT SER-99 AND THR-502.
PubMed=8349691;
Tanasijevic M.J., Myers M.G. Jr., Thoma R.S., Crimmins D.L.,
White M.F., Sacks D.B.;
"Phosphorylation of the insulin receptor substrate IRS-1 by casein
kinase II.";
J. Biol. Chem. 268:18157-18166(1993).
[7]
INTERACTION WITH PHIP, AND MUTAGENESIS OF TRP-106.
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).
[8]
PHOSPHORYLATION AT SER-307.
PubMed=11606564; DOI=10.1074/jbc.M101521200;
Aguirre V., Werner E.D., Giraud J., Lee Y.H., Shoelson S.E.,
White M.F.;
"Phosphorylation of Ser307 in insulin receptor substrate-1 blocks
interactions with the insulin receptor and inhibits insulin action.";
J. Biol. Chem. 277:1531-1537(2002).
[9]
PHOSPHORYLATION AT SER-789.
PubMed=12006586; DOI=10.1074/jbc.M201494200;
Qiao L.Y., Zhande R., Jetton T.L., Zhou G., Sun X.-J.;
"In vivo phosphorylation of insulin receptor substrate 1 at serine 789
by a novel serine kinase in insulin-resistant rodents.";
J. Biol. Chem. 277:26530-26539(2002).
[10]
INTERACTION WITH ROCK1, AND PHOSPHORYLATION.
PubMed=11739394; DOI=10.1074/jbc.M110508200;
Begum N., Sandu O.A., Ito M., Lohmann S.M., Smolenski A.;
"Active Rho kinase (ROK-alpha) associates with insulin receptor
substrate-1 and inhibits insulin signaling in vascular smooth muscle
cells.";
J. Biol. Chem. 277:6214-6222(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-343; THR-441;
THR-448 AND SER-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(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. {ECO:0000269|PubMed:1380456}.
-!- SUBUNIT: 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,
FER and PIK3CA (By similarity). Interacts (via phosphorylated YXXM
motifs) with PIK3R1. Interacts with ROCK1. Interacts (via PH
domain) with PHIP. Interacts with GRB2. Interacts with ALK (By
similarity). Interacts with EIF2AK2/PKR (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P39688:Fyn (xeno); NbExp=4; IntAct=EBI-520230, EBI-524514;
P62993:GRB2 (xeno); NbExp=5; IntAct=EBI-520230, EBI-401755;
P06213:INSR (xeno); NbExp=5; IntAct=EBI-520230, EBI-475899;
Q9EPH8:Pabpc1; NbExp=2; IntAct=EBI-520230, EBI-919825;
Q8VDD9:Phip (xeno); NbExp=2; IntAct=EBI-520230, EBI-1369766;
P27986:PIK3R1 (xeno); NbExp=2; IntAct=EBI-520230, EBI-79464;
Q63787:Pik3r1; NbExp=3; IntAct=EBI-520230, EBI-518443;
Q04759:PRKCQ (xeno); NbExp=2; IntAct=EBI-520230, EBI-374762;
P18031:PTPN1 (xeno); NbExp=3; IntAct=EBI-520230, EBI-968788;
Q06124:PTPN11 (xeno); NbExp=3; IntAct=EBI-520230, EBI-297779;
Q13625-2:TP53BP2 (xeno); NbExp=4; IntAct=EBI-520230, EBI-287091;
-!- 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,
and Ser-789 phosphorylation is increased in the liver of insulin-
resistant rats. Phosphorylation of Tyr-895 is required for GRB2-
binding. Phosphorylated by ALK. Phosphorylated at Ser-265, Ser-
302, Ser-632 and Ser-1100 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; X58375; CAA41264.1; -; mRNA.
PIR; S16948; S16948.
RefSeq; NP_037101.1; NM_012969.1.
UniGene; Rn.10476; -.
PDB; 5WRK; X-ray; 2.62 A; P=607-614.
PDB; 5WRL; X-ray; 3.10 A; P=627-634.
PDB; 5WRM; X-ray; 2.60 A; P=657-664.
PDBsum; 5WRK; -.
PDBsum; 5WRL; -.
PDBsum; 5WRM; -.
ProteinModelPortal; P35570; -.
SMR; P35570; -.
BioGrid; 247500; 13.
CORUM; P35570; -.
DIP; DIP-664N; -.
ELM; P35570; -.
IntAct; P35570; 25.
MINT; P35570; -.
STRING; 10116.ENSRNOP00000019579; -.
BindingDB; P35570; -.
ChEMBL; CHEMBL1163110; -.
iPTMnet; P35570; -.
PhosphoSitePlus; P35570; -.
PaxDb; P35570; -.
PRIDE; P35570; -.
GeneID; 25467; -.
KEGG; rno:25467; -.
UCSC; RGD:2922; rat.
CTD; 3667; -.
RGD; 2922; Irs1.
eggNOG; ENOG410IXEK; Eukaryota.
eggNOG; ENOG410Z9EP; LUCA.
HOGENOM; HOG000113103; -.
HOVERGEN; HBG000542; -.
InParanoid; P35570; -.
KO; K16172; -.
PhylomeDB; P35570; -.
PRO; PR:P35570; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005901; C:caveola; ISO:RGD.
GO; GO:0036064; C:ciliary basal body; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005899; C:insulin receptor complex; IMP:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005158; F:insulin receptor binding; IMP:RGD.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IMP:BHF-UCL.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:1904385; P:cellular response to angiotensin; IDA:RGD.
GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
GO; GO:0071478; P:cellular response to radiation; IEP:RGD.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; ISO:RGD.
GO; GO:0030879; P:mammary gland development; ISO:RGD.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0090275; P:negative regulation of somatostatin secretion; IMP:BHF-UCL.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:RGD.
GO; GO:0070094; P:positive regulation of glucagon secretion; IMP:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; ISO:RGD.
GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:RGD.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:RGD.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0031000; P:response to caffeine; IDA:RGD.
GO; GO:0032868; P:response to insulin; ISO:RGD.
GO; GO:0043434; P:response to peptide hormone; IDA:UniProtKB.
CDD; cd01204; PTB_IRS; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR002404; IRS_PTB.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF02174; IRS; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00628; INSULINRSI.
SMART; SM00233; PH; 1.
SMART; SM00310; PTBI; 1.
PROSITE; PS51064; IRS_PTB; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Phosphoprotein; Reference proteome; Repeat; Transducer;
Ubl conjugation.
CHAIN 1 1235 Insulin receptor substrate 1.
/FTId=PRO_0000084238.
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:0000269|PubMed:11018022}.
REGION 895 897 GRB2-binding.
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 939 942 YXXM motif 7.
MOTIF 987 990 YXXM motif 8.
MOTIF 1010 1013 YXXM motif 9.
COMPBIAS 872 881 Poly-Gln.
COMPBIAS 1196 1200 Poly-Pro.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 99 99 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8349691}.
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:0000250|UniProtKB:P35569}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000250|UniProtKB:P35569}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000250|UniProtKB:P35569}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 448 448 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 460 460 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 502 502 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:8349691}.
MOD_RES 522 522 Phosphoserine; by RPS6KB1.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 608 608 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 628 628 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 632 632 Phosphoserine; by RPS6KB1 and ROCK2.
{ECO:0000250|UniProtKB:P35569}.
MOD_RES 658 658 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 789 789 Phosphoserine; by AMPK and SIK2.
{ECO:0000269|PubMed:12006586}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 895 895 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 939 939 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 987 987 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 1099 1099 Phosphoserine.
{ECO:0000250|UniProtKB:P35569}.
MOD_RES 1100 1100 Phosphoserine; by RPS6KB1.
{ECO:0000250|UniProtKB:P35568}.
MOD_RES 1172 1172 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MOD_RES 1222 1222 Phosphotyrosine; by INSR.
{ECO:0000269|PubMed:7504175}.
MUTAGEN 106 106 W->A: Loss of interaction with PHIP.
{ECO:0000269|PubMed:11018022}.
CONFLICT 1098 1098 H -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 1235 AA; 131178 MW; A274BC7540CA85C5 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 PRTKSQSSSS CSNPISVPLR RHHLNNPPPS QVGLTRRSRT
ESITATSPAS MVGGKPGSFR VRASSDGEGT MSRPASVDGS PVSPSTNRTH AHRHRGSSRL
HPPLNHSRSI PMPSSRCSPS ATSPVSLSSS STSGHGSTSD CLFPRRSSAS VSGSPSDGGF
ISSDEYGSSP CDFRSSFRSV TPDSLGHTPP ARGEEELSNY ICMGGKGAST LTAPNGHYIL
SRGGNGHRYI PGATMGTSPA LTGDEAAGAA DLDNRFRKRT HSAGTSPTIS HQKTPSQSSV
VSIEEYTEMM PAAYPPGGGS GGRLPGYRHS AFVPTHSYPE EGLEMHHLER RGGHHRPDSS
NLHTDDGYMP MSPGVAPVPS NRKGNGDYMP MSPKSVSAPQ QIINPIRRHP QRVDPNGYMM
MSPSGSCSPD IGGGSCSSSS ISAAPSGSSY GKPWTNGVGG HHTHALPHAK PPVESGGGKL
LPCTGDYMNM SPVGDSNTSS PSECYYGPED PQHKPVLSYY SLPRSFKHTQ RPGEPEEGAR
HQHLRLSSSS GRLRYTATAE DSSSSTSSDS LGGGYCGARP ESSVTHPHHH ALQPHLPRKV
DTAAQTNSRL ARPTRLSLGD PKASTLPRVR EQQQQQQQQQ QSSLHPPEPK SPGEYVNIEF
GSGQPGYLAG PATSRSSPSV RCLPQLHPAP REETGSEEYM NMDLGPGRRA TWQESGGVEL
GRVGPAPPGA ASICRPTRSV PNSRGDYMTM QIGCPRQSYV DTSPVAPVSY ADMRTGIAAE
KVSLPRTTGA APPPSSTASA SASVTPQGAA EQAAHSSLLG GPQGPGGMSA FTRVNLSPNH
NQSAKVIRAD TQGCRRRHSS ETFSAPTRAA NTVSFGAGAA GGGSGGGSED VKRHSSASFE
NVWLRPGDLG GASKESAPGC GAAGGLEKSL NYIDLDLVKD VKQHPQDCPS QQQSLPPPPP
HQPLGSNEGS SPRRSSEDLS TYASINFQKQ PEDRQ


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