RUP1_YEAST
ID RUP1_YEAST Reviewed; 671 AA.
AC Q12242; D6W2J5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=UBA domain-containing protein RUP1;
GN Name=RUP1; OrderedLocusNames=YOR138C; ORFNames=YOR3332c;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH RSP5 AND UBP2.
RX PubMed=15933713; DOI=10.1038/sj.emboj.7600710;
RA Kee Y., Lyon N., Huibregtse J.M.;
RT "The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2
RT deubiquitinating enzyme.";
RL EMBO J. 24:2414-2424(2005).
RN [8]
RP FUNCTION.
RX PubMed=17028178; DOI=10.1074/jbc.m608756200;
RA Kee Y., Munoz W., Lyon N., Huibregtse J.M.;
RT "The Ubp2 deubiquitinating enzyme modulates Rsp5-dependent K63-linked
RT polyubiquitin conjugates in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 281:36724-36731(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, 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 [10]
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 [11]
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 -!- FUNCTION: Modulates the activity of the RSP5 HECT ubiquitin-protein
CC ligase through its mediation of the interaction between RSP5 and the
CC deubiquitinase UBP2. Involved in regulation of cell wall homeostasis.
CC {ECO:0000269|PubMed:15933713, ECO:0000269|PubMed:17028178}.
CC -!- SUBUNIT: Forms a ternary complex with RSP5 and UBP2.
CC -!- INTERACTION:
CC Q12242; Q01476: UBP2; NbExp=3; IntAct=EBI-38794, EBI-19826;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X94335; CAA64056.1; -; Genomic_DNA.
DR EMBL; Z75046; CAA99337.1; -; Genomic_DNA.
DR EMBL; AY692617; AAT92636.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10911.1; -; Genomic_DNA.
DR PIR; S61693; S61693.
DR RefSeq; NP_014781.1; NM_001183557.1.
DR AlphaFoldDB; Q12242; -.
DR SMR; Q12242; -.
DR BioGRID; 34533; 69.
DR DIP; DIP-1986N; -.
DR IntAct; Q12242; 6.
DR MINT; Q12242; -.
DR STRING; 4932.YOR138C; -.
DR iPTMnet; Q12242; -.
DR MaxQB; Q12242; -.
DR PaxDb; Q12242; -.
DR PRIDE; Q12242; -.
DR EnsemblFungi; YOR138C_mRNA; YOR138C; YOR138C.
DR GeneID; 854306; -.
DR KEGG; sce:YOR138C; -.
DR SGD; S000005664; RUP1.
DR VEuPathDB; FungiDB:YOR138C; -.
DR eggNOG; ENOG502S0Z0; Eukaryota.
DR HOGENOM; CLU_028632_0_0_1; -.
DR InParanoid; Q12242; -.
DR OMA; PLEFYPQ; -.
DR BioCyc; YEAST:G3O-33660-MON; -.
DR PRO; PR:Q12242; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12242; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:SGD.
DR GO; GO:0016579; P:protein deubiquitination; IMP:SGD.
DR CDD; cd14307; UBA_RUP1p; 1.
DR InterPro; IPR041970; Rup1_UBA.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..671
FT /note="UBA domain-containing protein RUP1"
FT /id="PRO_0000269644"
FT DOMAIN 1..41
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 68..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..501
FT /evidence="ECO:0000255"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 671 AA; 75361 MW; 69E950C4537597FB CRC64;
MMDNQAVKSL LEMGIPHEVA VDALQRTGGN LEAAVNFIFS NELPEQAEMG EENDGSQPRI
SENKIVAGTK PCDVPNNGDQ DIDMPDVSGV DVDYDDDEDI TDERSGSNST SGCRVTAQNY
DRYSISETSI PPPSYSIVQH NEFKSNVGDP TVVLPLPLNS LIESYFGLFA LLTAVYFPHV
FLKPDFKDLN YRADWFKGSS FTEPKYRLAY CEAEDGSTTS EIVLASGPNE GLQPHLLWQL
QKLISVVNTR KCERAFVSAK VFTSSLEPQL RSKLADSEHL YEVLPAFIKS LAVDLEMCPG
IRDRETRSLF ISSALHTPNK NEPPMETFLS LFHFLPEEYD SNLYKMFNVL LYPEEEEEEE
DVIRGGEQEE ARYVEPENTL KEVAPVLTIL FNELETNTES VSLPNGVDIP LEFYPQLYTK
QCKDQLIRHI ISKRKQARTR SRCLLQEINE LKSYQGKNIS TILESTLAYL QTIPDDANNE
AAKQIASLKD TLNSARAAKM EEYKDLASKL HGEWNLSHPE THIINTAKQL GLIENPYILT
MAALSPYSYF IRSRNGAWSW IQSNTLGTEF KVKKCSSPSV VQEAIKHGTK YASETPLMFI
YCEEGKIPTE EVVAEALKSN SGCLKFAEDD QNSLKTLRSQ FFDGMGDPEQ ATNNINNGND
NDNDDDIDSD N
