YG3A_YEAST
ID YG3A_YEAST Reviewed; 816 AA.
AC P53278; D6VUR2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Uncharacterized protein YGR130C;
GN OrderedLocusNames=YGR130C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-347, AND
RP 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND THR-809, 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).
RN [7]
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).
RN [8]
RP PYROPHOSPHORYLATION.
RX PubMed=15604408; DOI=10.1126/science.1103344;
RA Saiardi A., Bhandari R., Resnick A.C., Snowman A.M., Snyder S.H.;
RT "Phosphorylation of proteins by inositol pyrophosphates.";
RL Science 306:2101-2105(2004).
RN [9]
RP PYROPHOSPHORYLATION.
RX PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT "Protein pyrophosphorylation by inositol pyrophosphates is a
RT posttranslational event.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) (PubMed:15604408). Serine pyrophosphorylation is achieved by
CC Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC (PubMed:15604408, PubMed:17873058). {ECO:0000269|PubMed:15604408,
CC ECO:0000269|PubMed:17873058}.
CC -!- MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72915; CAA97143.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08223.1; -; Genomic_DNA.
DR PIR; S64439; S64439.
DR RefSeq; NP_011646.1; NM_001181259.1.
DR AlphaFoldDB; P53278; -.
DR SMR; P53278; -.
DR BioGRID; 33378; 188.
DR DIP; DIP-3006N; -.
DR IntAct; P53278; 57.
DR MINT; P53278; -.
DR STRING; 4932.YGR130C; -.
DR iPTMnet; P53278; -.
DR MaxQB; P53278; -.
DR PaxDb; P53278; -.
DR PRIDE; P53278; -.
DR EnsemblFungi; YGR130C_mRNA; YGR130C; YGR130C.
DR GeneID; 853031; -.
DR KEGG; sce:YGR130C; -.
DR SGD; S000003362; YGR130C.
DR VEuPathDB; FungiDB:YGR130C; -.
DR eggNOG; ENOG502RJFX; Eukaryota.
DR HOGENOM; CLU_018313_0_0_1; -.
DR InParanoid; P53278; -.
DR OMA; TEEEIMY; -.
DR BioCyc; YEAST:G3O-30836-MON; -.
DR PRO; PR:P53278; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53278; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032126; C:eisosome; IDA:SGD.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..816
FT /note="Uncharacterized protein YGR130C"
FT /id="PRO_0000202822"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 809
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 816 AA; 92698 MW; D482327C9274C026 CRC64;
MLFNINRQED DPFTQLINQS SANTQNQQAH QQESPYQFLQ KVVSNEPKGK EEWVSPFRQD
ALANRQNNRA YGEDAKNRKF PTVSATSAYS KQQPKDLGYK NIPKNAKRAK DIRFPTYLTQ
NEERQYQLLT ELELKEKHLK YLKKCQKITD LTKDEKDDTD TTTSSSTSTS SSSSSSSSSS
SSSSSDEGDV TSTTTSEATE ATADTATTTT TTTSTSTTST STTNAVENSA DEATSVEEEH
EDKVSESTSI GKGTADSAQI NVAEPISSEN GVLEPRTTDQ SGGSKSGVVP TDEQKEEKSD
VKKVNPPSGE EKKEVEAEGD AEEETEQSSA EESAERTSTP ETSEPESEED ESPIDPSKAP
KVPFQEPSRK ERTGIFALWK SPTSSSTQKS KTAAPSNPVA TPENPELIVK TKEHGYLSKA
VYDKINYDEK IHQAWLADLR AKEKDKYDAK NKEYKEKLQD LQNQIDEIEN SMKAMREETS
EKIEVSKNRL VKKIIDVNAE HNNKKLMILK DTENMKNQKL QEKNEVLDKQ TNVKSEIDDL
NNEKTNVQKE FNDWTTNLSN LSQQLDAQIF KINQINLKQG KVQNEIDNLE KKKEDLVTQT
EENKKLHEKN VQVLESVENK EYLPQINDID NQISSLLNEV TIIKQENANE KTQLSAITKR
LEDERRAHEE QLKLEAEERK RKEENLLEKQ RQELEEQAHQ AQLDHEQQIT QVKQTYNDQL
TELQDKLATE EKELEAVKRE RTRLQAEKAI EEQTRQKNAD EALKQEILSR QHKQAEGIHA
AENHKIPNDR SQKNTSVLPK DDSLYEYHTE EDVMYA
