GIP3_YEAST
ID GIP3_YEAST Reviewed; 1276 AA.
AC Q03016; D6W3N1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=GLC7-interacting protein 3;
GN Name=GIP3; OrderedLocusNames=YPL137C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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-143; SER-260; THR-264 AND
RP SER-269, AND IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-99 AND SER-103, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-99 AND SER-103, 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 -!- SUBUNIT: Interacts with phosphatase 1 (GLC7).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GIP3/HER1 family. {ECO:0000305}.
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DR EMBL; U43703; AAB68223.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11297.1; -; Genomic_DNA.
DR PIR; S69048; S69048.
DR RefSeq; NP_015188.1; NM_001183951.1.
DR AlphaFoldDB; Q03016; -.
DR BioGRID; 36045; 77.
DR IntAct; Q03016; 8.
DR MINT; Q03016; -.
DR STRING; 4932.YPL137C; -.
DR iPTMnet; Q03016; -.
DR MaxQB; Q03016; -.
DR PaxDb; Q03016; -.
DR PRIDE; Q03016; -.
DR EnsemblFungi; YPL137C_mRNA; YPL137C; YPL137C.
DR GeneID; 855967; -.
DR KEGG; sce:YPL137C; -.
DR SGD; S000006058; GIP3.
DR VEuPathDB; FungiDB:YPL137C; -.
DR eggNOG; ENOG502QYHN; Eukaryota.
DR GeneTree; ENSGT00940000176518; -.
DR HOGENOM; CLU_007231_0_0_1; -.
DR InParanoid; Q03016; -.
DR OMA; WLYKGKS; -.
DR BioCyc; YEAST:G3O-34035-MON; -.
DR PRO; PR:Q03016; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03016; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:SGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:SGD.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Phosphoprotein; Reference proteome.
FT CHAIN 1..1276
FT /note="GLC7-interacting protein 3"
FT /id="PRO_0000238623"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 264
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 1276 AA; 140891 MW; 32F84A311C92699A CRC64;
MITNTEFDVP VDWLYKGKSR RKTNTKPSRP STSPASSSST SSSKNGDNST SGNRSSNDKP
RARSSSVSNA ALCNTEKPDL KRNDGNTSAS DTDNIPLLTP INSGNRSDSA DIDNPATVDA
IDLIDNDDNG SSTQFVRKKR STSISNAVVS SKPRLASSAI NATASSSVGK GKHPPISSPS
NATLKRSNST SGEKTKRSIF GSLFSKRSTS SSASTAKKPL PVVNTSTTEN ESGGIKAVAT
PDPRVKEISS PMRGVAPTAS KPQTPILPSP ALAVKDLSTV SLKRVSFAVD KFESDPPQQL
PSRTPKKGNI LIPDDMISEV PSISVGISSS NQSAKSTNSN IKGPLYTKKS KEYILALENQ
KLALREAAKH QQEAHFAANR IAFEVANFKT ASDAGGKLTE KSSEGTITKQ REEVSPPNVE
ADRELENNKL AENLSKAGID KPIHMHEHYF KEPDQDKYQD GHSIENNEVT LDVIYTRCCH
LREILPIPST LRQVKDKTAP LQILKFLNPK PTLIDILSFC DFITIAPIHT IVFDNVALNQ
DMFRIIISAL VNSTVLDKLS LRNVRIDQDG WKLLCKFLLL NKSLNKLDIS QTKIKSDLAE
SLYRHNMDWN LFTDVLSQRS HKPIEELLFN GIQFSKIPYS CFARLLTSFA TQKNFPESGI
RLGLAGATTS NISQDCLKFI FNWMSQYNVQ GVDLAFNDLS TMIKPMVGKL SALSYDNLRY
FILNSTNIST SYDLALLLKY LSKLPNLIFL DLSNLSQCFP DILPYMYKYL PRFPNLKRIH
LDSNNLTLKE LAVVCNILIK CKSLSHVSMT NQNVENFYLM NGTDSPVQQT NTDGDLDSSS
TLDVKGQFAK NSFSSTLYAF ARDSPNLIGL DFDYDLISEE IQSRIALCLM RNMKRTMDST
FQLDELDSQD DLLFDGSLVT MTAESVLEKL NLLSDKSTKV KKDTTKRYLL KKYIEKFHIL
HHNVQHTIDT MFEKRKSGEL PLQEKENLVR LLLLEQNLCN ILELFSHNPN LNDVLGSSRD
DSKESVDSSE DSKLPALKHV ESGYHVPEEK IQPENDVITA RPHLMATDSG KTIDVFTGKP
LVFKHTSSST SVGCKKQEEE EGELHKWGFF VQQQRSLYPE NESTRQTPFA SGDTPINTET
AGKSTSSPSV STSNNETATT SLFSPANPKI LPKIPSGAVL RSAIMKAKGI DSIDDLIQNV
NSNNIELENI YGESIQNSAS TFTPGVDSDV SAPNTDKGSV ETLPAVSTDD PNCEVKVTAT
YDKLLNNLSM ERSIRL
