GIP2_YEAST
ID GIP2_YEAST Reviewed; 548 AA.
AC P40036; D3DLV7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=GLC7-interacting protein 2;
GN Name=GIP2; OrderedLocusNames=YER054C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 INTERACTION WITH GLC7.
RA Tu J., Song W., Carslon R.;
RL Unpublished observations (MAR-1996).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; THR-52; SER-155 AND
RP SER-221, AND 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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBUNIT: Interacts with phosphatase 1 (GLC7). {ECO:0000269|Ref.3}.
CC -!- INTERACTION:
CC P40036; P40073: SHO1; NbExp=2; IntAct=EBI-7612, EBI-18140;
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18813; AAB64590.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07711.1; -; Genomic_DNA.
DR PIR; S50557; S50557.
DR RefSeq; NP_010974.1; NM_001178945.1.
DR AlphaFoldDB; P40036; -.
DR BioGRID; 36794; 69.
DR DIP; DIP-2376N; -.
DR IntAct; P40036; 16.
DR MINT; P40036; -.
DR STRING; 4932.YER054C; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; P40036; -.
DR MaxQB; P40036; -.
DR PaxDb; P40036; -.
DR PRIDE; P40036; -.
DR EnsemblFungi; YER054C_mRNA; YER054C; YER054C.
DR GeneID; 856781; -.
DR KEGG; sce:YER054C; -.
DR SGD; S000000856; GIP2.
DR VEuPathDB; FungiDB:YER054C; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000174300; -.
DR HOGENOM; CLU_017894_0_0_1; -.
DR InParanoid; P40036; -.
DR OMA; KSKRFQN; -.
DR BioCyc; YEAST:G3O-30232-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR PRO; PR:P40036; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40036; protein.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:SGD.
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; IDA:SGD.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:SGD.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
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..548
FT /note="GLC7-interacting protein 2"
FT /id="PRO_0000071521"
FT DOMAIN 419..534
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 548 AA; 62319 MW; B28EE5241989A9BF CRC64;
MYIKAEQKPQ QFERKNEKLD RNKNQQLPDL ETDFKGYRVN SDLYNKERDG STEETLNSLK
FLHKPQRVTQ MRANRFPEEE VQRNTDLNKR IFSAGNDENV DNESGWSKIA AAKNHTSVES
LNGSTRPPFK IELPPLSPKS TVPKSFQAEY PEAKSPGNDM NFEYDEEILI PFAPPVYKKS
GELLKSSLKR RSKSLPTTPG IRSGNGVQAR DGSPMLIRSK SVHFDQAAPV KYFAEDESPI
NVNKTEQHDN CLSFKHKPVN LMVDPEEETK MLSSGLETTS IDDDLTTVAP KGFAHPAKIS
NPNNGKGTNN TKLRKSKRFQ NLLKNRTDMP PSKSNKKFVN GGGAHEISDR NSKNYHVVGL
YSKNFPILSN KNPKSLKLNI FINLSQNKKV FLQELSLYIH RDNNYFSNSS SFYNIPNSHN
GNDCNGVAKG YNAGCTRLIA GRILVKNIFY DKRVVVRYTW DSWRTTHEVE CVYISDGDGI
LPGTNMDIFH FIIDDVSKVD PRGKLEFCIH YSTRNDYERE EYWDNNNGNN YKVDVVMDGF
NDPFAAAA
