ID   PIG2_YEAST              Reviewed;         538 AA.
AC   P40187; D6VVN7; E9P960;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=GSY2-interacting protein PIG2;
GN   Name=PIG2; OrderedLocusNames=YIL045W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=9046081;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<1::aid-yea49>3.0.co;2-f;
RA   Cheng C., Huang D., Roach P.J.;
RT   "Yeast PIG genes: PIG1 encodes a putative type 1 phosphatase subunit that
RT   interacts with the yeast glycogen synthase Gsy2p.";
RL   Yeast 13:1-8(1997).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-196, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-304, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Interacts with glycogen synthase 2 (GSY2); possibly also
CC       interacts with phosphatase 1 (GLC7).
CC   -!- MISCELLANEOUS: Present with 996 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z46861; CAA86906.1; -; Genomic_DNA.
DR   EMBL; AY723830; AAU09747.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08503.1; -; Genomic_DNA.
DR   PIR; S49933; S49933.
DR   RefSeq; NP_012219.3; NM_001179395.3.
DR   AlphaFoldDB; P40187; -.
DR   SMR; P40187; -.
DR   BioGRID; 34945; 65.
DR   DIP; DIP-5191N; -.
DR   IntAct; P40187; 14.
DR   MINT; P40187; -.
DR   STRING; 4932.YIL045W; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   iPTMnet; P40187; -.
DR   MaxQB; P40187; -.
DR   PaxDb; 4932-YIL045W; -.
DR   PeptideAtlas; P40187; -.
DR   EnsemblFungi; YIL045W_mRNA; YIL045W; YIL045W.
DR   GeneID; 854766; -.
DR   KEGG; sce:YIL045W; -.
DR   AGR; SGD:S000001307; -.
DR   SGD; S000001307; PIG2.
DR   VEuPathDB; FungiDB:YIL045W; -.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000174300; -.
DR   HOGENOM; CLU_017894_0_0_1; -.
DR   InParanoid; P40187; -.
DR   OMA; NEYGDTW; -.
DR   OrthoDB; 1334368at2759; -.
DR   BioCyc; YEAST:G3O-31316-MONOMER; -.
DR   Reactome; R-SCE-3322077; Glycogen synthesis.
DR   BioGRID-ORCS; 854766; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40187; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40187; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; ISA:SGD.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IPI:SGD.
DR   Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   InterPro; IPR016717; Gip2/Pig2.
DR   PANTHER; PTHR12307; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR12307:SF36; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 3D; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   PIRSF; PIRSF018234; PPase_interacting; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..538
FT                   /note="GSY2-interacting protein PIG2"
FT                   /id="PRO_0000071522"
FT   DOMAIN          384..508
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        537
FT                   /note="F -> L (in Ref. 3; AAU09747)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   538 AA;  61938 MW;  73ED8F5CC6692172 CRC64;
     MATTTQPQNI LMDEPLNLPN NSAHNNNYGN INANIRTFAG MSMHMHPARL NSLEFLHKPR
     RLSNVKLHRL PQDELQRNTD MNKGMYFNGK QVHAHHPFIN SGANFNAHHQ DVSKLGEEED
     EISPLSHDNF QYESEENGNP SPPIYKKSGE LVKSSLKRRS KSLPITPKSI FNKTGSKSKH
     VNLDHVDTRL LQRSKSVHFD RVLPIKLFNE NEKPIDVGKQ MVQQDVLNFK HKPLTRLSAL
     NGGSDSVPIE DLLSENNQNE YGDTWLQNPK GVFLFGTNSN NRRNKKKKFK LSDDDSDIEN
     DNDSDDAINR LVRQQDKDQA HLAHGLKNLL INDDDDYLET RTNSAKSGAN LFIGNSKRIV
     GLYNKNFPIL SDRNRKSLKL NIFLNLSRGR PVFLQEITLL TGFHNMVIIG KVFVKNIYFD
     KKIIVRYTWD AWRTFHESEC VYFSNANGIL PGSNMDIFKF SIDDIHNPND KDSNISQLEF
     CIQYLTWGVD RSRKEYWDNN DSANYKIDVV TNETRTGPTT DVNDNYEMKH SLFRNPFH
//