PIG2_YEAST
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 03-AUG-2022, entry version 158.
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; 59.
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; P40187; -.
DR PRIDE; P40187; -.
DR EnsemblFungi; YIL045W_mRNA; YIL045W; YIL045W.
DR GeneID; 854766; -.
DR KEGG; sce:YIL045W; -.
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; INSGANF; -.
DR BioCyc; YEAST:G3O-31316-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
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; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR InterPro; IPR016717; Gip2/Pig2.
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
