ID   IRS1_MOUSE              Reviewed;        1233 AA.
AC   P35569;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Insulin receptor substrate 1;
DE            Short=IRS-1;
GN   Name=Irs1; Synonyms=Irs-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8167159; DOI=10.1016/0167-4889(94)90261-5;
RA   Araki E., Haag B.L. III, Kahn C.R.;
RT   "Cloning of the mouse insulin receptor substrate-1 (IRS-1) gene and
RT   complete sequence of mouse IRS-1.";
RL   Biochim. Biophys. Acta 1221:353-356(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8448209; DOI=10.1016/0167-4781(93)90222-y;
RA   Keller S.R., Aebersold R., Garner C.W., Lienhard G.E.;
RT   "The insulin-elicited 160 kDa phosphotyrosine protein in mouse adipocytes
RT   is an insulin receptor substrate 1: identification by cloning.";
RL   Biochim. Biophys. Acta 1172:323-326(1993).
RN   [3]
RP   INTERACTION WITH FER.
RX   PubMed=11006284; DOI=10.1074/jbc.m006665200;
RA   Iwanishi M., Czech M.P., Cherniack A.D.;
RT   "The protein-tyrosine kinase fer associates with signaling complexes
RT   containing insulin receptor substrate-1 and phosphatidylinositol 3-
RT   kinase.";
RL   J. Biol. Chem. 275:38995-39000(2000).
RN   [4]
RP   INTERACTION WITH PHIP.
RX   PubMed=11018022; DOI=10.1074/jbc.c000611200;
RA   Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT   "Cloning and characterization of PHIP, a novel insulin receptor substrate-1
RT   pleckstrin homology domain interacting protein.";
RL   J. Biol. Chem. 275:40492-40497(2000).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=10749573; DOI=10.1172/jci9017;
RA   Ogata N., Chikazu D., Kubota N., Terauchi Y., Tobe K., Azuma Y., Ohta T.,
RA   Kadowaki T., Nakamura K., Kawaguchi H.;
RT   "Insulin receptor substrate-1 in osteoblast is indispensable for
RT   maintaining bone turnover.";
RL   J. Clin. Invest. 105:935-943(2000).
RN   [6]
RP   PHOSPHORYLATION AT SER-789.
RX   PubMed=11598104; DOI=10.1074/jbc.c100483200;
RA   Jakobsen S.N., Hardie D.G., Morrice N., Tornqvist H.E.;
RT   "5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse
RT   C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside.";
RL   J. Biol. Chem. 276:46912-46916(2001).
RN   [7]
RP   INTERACTION WITH UBTF AND PIK3CA, AND EFFECT ON CELL AND BODY SIZE.
RX   PubMed=15197263; DOI=10.1073/pnas.0403328101;
RA   Drakas R., Tu X., Baserga R.;
RT   "Control of cell size through phosphorylation of upstream binding factor 1
RT   by nuclear phosphatidylinositol 3-kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004).
RN   [8]
RP   PHOSPHORYLATION AT SER-632.
RX   PubMed=16098829; DOI=10.1016/j.cmet.2005.06.011;
RA   Furukawa N., Ongusaha P., Jahng W.J., Araki K., Choi C.S., Kim H.J.,
RA   Lee Y.H., Kaibuchi K., Kahn B.B., Masuzaki H., Kim J.K., Lee S.W.,
RA   Kim Y.B.;
RT   "Role of Rho-kinase in regulation of insulin action and glucose
RT   homeostasis.";
RL   Cell Metab. 2:119-129(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 AND SER-1097, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-414; SER-887;
RP   SER-1096 AND SER-1097, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC   Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   INTERACTION WITH EIF2AK2.
RX   PubMed=22948222; DOI=10.1210/en.2012-1400;
RA   Carvalho-Filho M.A., Carvalho B.M., Oliveira A.G., Guadagnini D., Ueno M.,
RA   Dias M.M., Tsukumo D.M., Hirabara S.M., Reis L.F., Curi R.,
RA   Carvalheira J.B., Saad M.J.;
RT   "Double-stranded RNA-activated protein kinase is a key modulator of insulin
RT   sensitivity in physiological conditions and in obesity in mice.";
RL   Endocrinology 153:5261-5274(2012).
RN   [12]
RP   PHOSPHORYLATION AT SER-612.
RX   PubMed=24187137; DOI=10.1074/jbc.m113.500736;
RA   Seldin M.M., Lei X., Tan S.Y., Stanson K.P., Wei Z., Wong G.W.;
RT   "Skeletal muscle-derived myonectin activates the mammalian target of
RT   rapamycin (mTOR) pathway to suppress autophagy in liver.";
RL   J. Biol. Chem. 288:36073-36082(2013).
RN   [13]
RP   INTERACTION WITH GKAP1, AND PHOSPHORYLATION.
RX   PubMed=25586176; DOI=10.1074/jbc.m114.624759;
RA   Ando Y., Shinozawa Y., Iijima Y., Yu B.C., Sone M., Ooi Y., Watanaka Y.,
RA   Chida K., Hakuno F., Takahashi S.;
RT   "Tumor necrosis factor (TNF)-alpha-induced repression of GKAP42 protein
RT   levels through cGMP-dependent kinase (cGK)-Ialpha causes insulin resistance
RT   in 3T3-L1 adipocytes.";
RL   J. Biol. Chem. 290:5881-5892(2015).
RN   [14]
RP   INTERACTION WITH DGKZ, AND IDENTIFICATION IN A COMPLEX WITH DGKZ AND
RP   PIP5K1A.
RX   PubMed=27739494; DOI=10.1038/srep35438;
RA   Liu T., Yu B., Kakino M., Fujimoto H., Ando Y., Hakuno F., Takahashi S.I.;
RT   "A novel IRS-1-associated protein, DGKzeta regulates GLUT4 translocation in
RT   3T3-L1 adipocytes.";
RL   Sci. Rep. 6:35438-35438(2016).
CC   -!- FUNCTION: May mediate the control of various cellular processes by
CC       insulin. When phosphorylated by the insulin receptor binds specifically
CC       to various cellular proteins containing SH2 domains such as
CC       phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates
CC       phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via phosphorylated YXXM motifs) with PIK3R1 (By
CC       similarity). Interacts with ROCK1 (By similarity). Interacts with GRB2
CC       (By similarity). Interacts with SOCS7 (By similarity). Interacts (via
CC       IRS-type PTB domain) with IGF1R and INSR (via the tyrosine-
CC       phosphorylated NPXY motif) (By similarity). Interacts with UBTF and
CC       PIK3CA (PubMed:15197263). Interacts (via PH domain) with PHIP
CC       (PubMed:11018022). Interacts with FER (PubMed:11006284). Interacts with
CC       ALK (By similarity). Interacts with EIF2AK2/PKR (PubMed:22948222).
CC       Interacts with GKAP1 (PubMed:25586176). Interacts with DGKZ in the
CC       absence of insulin; insulin stimulation decreases this interaction
CC       (PubMed:27739494). Found in a ternary complex with DGKZ and PIP5K1A in
CC       the absence of insulin stimulation (PubMed:27739494). Interacts with
CC       SQSTM1; the interaction is disrupted by the presence of tensin TNS2 (By
CC       similarity). {ECO:0000250|UniProtKB:P35568,
CC       ECO:0000250|UniProtKB:P35570, ECO:0000269|PubMed:11006284,
CC       ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:15197263,
CC       ECO:0000269|PubMed:22948222, ECO:0000269|PubMed:25586176,
CC       ECO:0000269|PubMed:27739494}.
CC   -!- INTERACTION:
CC       P35569; Q03963: Eif2ak2; NbExp=2; IntAct=EBI-400825, EBI-2603444;
CC       P35569; P26450: Pik3r1; NbExp=3; IntAct=EBI-400825, EBI-641764;
CC       P35569; Q1XH17: Trim72; NbExp=4; IntAct=EBI-400825, EBI-16034016;
CC       P35569; Q13625-2: TP53BP2; Xeno; NbExp=2; IntAct=EBI-400825, EBI-287091;
CC   -!- TISSUE SPECIFICITY: Expressed in osteoblasts, but not in osteoclasts.
CC       {ECO:0000269|PubMed:10749573}.
CC   -!- PTM: Serine phosphorylation of IRS1 is a mechanism for insulin
CC       resistance. Ser-307 phosphorylation inhibits insulin action through
CC       disruption of IRS1 interaction with the insulin receptor (By
CC       similarity). Phosphorylation of Tyr-891 is required for GRB2-binding
CC       (By similarity). Phosphorylated by ALK. Phosphorylated at Ser-265, Ser-
CC       302, Ser-632 and Ser-1097 by RPS6KB1; phosphorylation induces
CC       accelerated degradation of IRS1 (By similarity). Phosphorylated on
CC       tyrosine residues in response to insulin (PubMed:25586176). In skeletal
CC       muscles, dephosphorylated on Tyr-608 by TNS2 under anabolic conditions;
CC       dephosphorylation results in the proteasomal degradation of IRS1 (By
CC       similarity). {ECO:0000250|UniProtKB:P35568,
CC       ECO:0000250|UniProtKB:P35570, ECO:0000269|PubMed:25586176}.
CC   -!- PTM: Ubiquitinated by the Cul7-RING(FBXW8) complex in a mTOR-dependent
CC       manner, leading to its degradation: the Cul7-RING(FBXW8) complex
CC       recognizes and binds IRS1 previously phosphorylated by S6 kinase
CC       (RPS6KB1 or RPS6KB2). {ECO:0000250}.
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DR   EMBL; L24563; AAA39335.1; -; mRNA.
DR   EMBL; X69722; CAA49378.1; -; mRNA.
DR   PIR; S30185; S30185.
DR   RefSeq; NP_034700.2; NM_010570.4.
DR   PDB; 1AYB; X-ray; 3.00 A; P=887-898.
DR   PDB; 5AXI; X-ray; 2.50 A; E=606-610.
DR   PDBsum; 1AYB; -.
DR   PDBsum; 5AXI; -.
DR   AlphaFoldDB; P35569; -.
DR   BMRB; P35569; -.
DR   SMR; P35569; -.
DR   BioGRID; 200788; 22.
DR   CORUM; P35569; -.
DR   DIP; DIP-32456N; -.
DR   IntAct; P35569; 51.
DR   MINT; P35569; -.
DR   STRING; 10090.ENSMUSP00000063795; -.
DR   GlyGen; P35569; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P35569; -.
DR   PhosphoSitePlus; P35569; -.
DR   SwissPalm; P35569; -.
DR   jPOST; P35569; -.
DR   MaxQB; P35569; -.
DR   PaxDb; 10090-ENSMUSP00000063795; -.
DR   PeptideAtlas; P35569; -.
DR   ProteomicsDB; 269333; -.
DR   Pumba; P35569; -.
DR   DNASU; 16367; -.
DR   GeneID; 16367; -.
DR   KEGG; mmu:16367; -.
DR   AGR; MGI:99454; -.
DR   CTD; 3667; -.
DR   MGI; MGI:99454; Irs1.
DR   eggNOG; ENOG502QUNU; Eukaryota.
DR   InParanoid; P35569; -.
DR   OrthoDB; 4212441at2759; -.
DR   PhylomeDB; P35569; -.
DR   Reactome; R-MMU-109704; PI3K Cascade.
DR   Reactome; R-MMU-112399; IRS-mediated signalling.
DR   Reactome; R-MMU-112412; SOS-mediated signalling.
DR   Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR   Reactome; R-MMU-198203; PI3K/AKT activation.
DR   Reactome; R-MMU-201556; Signaling by ALK.
DR   Reactome; R-MMU-2428928; IRS-related events triggered by IGF1R.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-MMU-74713; IRS activation.
DR   Reactome; R-MMU-74749; Signal attenuation.
DR   BioGRID-ORCS; 16367; 6 hits in 76 CRISPR screens.
DR   ChiTaRS; Irs1; mouse.
DR   EvolutionaryTrace; P35569; -.
DR   PRO; PR:P35569; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P35569; Protein.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005899; C:insulin receptor complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0141038; F:phosphatidylinositol 3-kinase activator activity; IMP:MGI.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:MGI.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:MGI.
DR   GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:MGI.
DR   GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0071398; P:cellular response to fatty acid; IMP:ARUK-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0010631; P:epithelial cell migration; IGI:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IMP:MGI.
DR   GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0090275; P:negative regulation of somatostatin secretion; ISO:MGI.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:MGI.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IGI:MGI.
DR   GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISO:MGI.
DR   GO; GO:0070094; P:positive regulation of glucagon secretion; ISO:MGI.
DR   GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR   GO; GO:0010907; P:positive regulation of glucose metabolic process; ISO:MGI.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO:MGI.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:MGI.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR   GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0031000; P:response to caffeine; ISO:MGI.
DR   GO; GO:0032868; P:response to insulin; ISO:MGI.
DR   CDD; cd01257; PH_IRS; 1.
DR   CDD; cd01204; PTB_IRS; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR039011; IRS.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR10614; INSULIN RECEPTOR SUBSTRATE; 1.
DR   PANTHER; PTHR10614:SF11; INSULIN RECEPTOR SUBSTRATE 1; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00628; INSULINRSI.
DR   SMART; SM01244; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Reference proteome; Repeat; Transducer;
KW   Ubl conjugation.
FT   CHAIN           1..1233
FT                   /note="Insulin receptor substrate 1"
FT                   /id="PRO_0000084237"
FT   DOMAIN          12..115
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          155..259
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          3..133
FT                   /note="Mediates interaction with PHIP"
FT                   /evidence="ECO:0000250"
FT   REGION          257..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..893
FT                   /note="GRB2-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1015..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           460..463
FT                   /note="YXXM motif 1"
FT   MOTIF           546..549
FT                   /note="YXXM motif 2"
FT   MOTIF           608..611
FT                   /note="YXXM motif 3"
FT   MOTIF           628..631
FT                   /note="YXXM motif 4"
FT   MOTIF           658..661
FT                   /note="YXXM motif 5"
FT   MOTIF           727..730
FT                   /note="YXXM motif 6"
FT   MOTIF           935..938
FT                   /note="YXXM motif 7"
FT   MOTIF           983..986
FT                   /note="YXXM motif 8"
FT   MOTIF           1006..1009
FT                   /note="YXXM motif 9"
FT   COMPBIAS        261..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..783
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         99
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         265
FT                   /note="Phosphoserine; by RPS6KB1"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         302
FT                   /note="Phosphoserine; by RPS6KB1"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         307
FT                   /note="Phosphoserine; by IKKB, MAPK8 and RPS6KB1"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         441
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         448
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         460
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         522
FT                   /note="Phosphoserine; by RPS6KB1"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         608
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:24187137"
FT   MOD_RES         628
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         632
FT                   /note="Phosphoserine; by RPS6KB1 and ROCK2"
FT                   /evidence="ECO:0000305|PubMed:16098829"
FT   MOD_RES         658
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         789
FT                   /note="Phosphoserine; by AMPK and SIK2"
FT                   /evidence="ECO:0000269|PubMed:11598104"
FT   MOD_RES         887
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         891
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         935
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35568"
FT   MOD_RES         983
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         1096
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1097
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1173
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   MOD_RES         1220
FT                   /note="Phosphotyrosine; by INSR"
FT                   /evidence="ECO:0000250|UniProtKB:P35570"
FT   CONFLICT        1038..1039
FT                   /note="Missing (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1182
FT                   /note="H -> R (in Ref. 2; CAA49378)"
FT                   /evidence="ECO:0000305"
SQ   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
//