RHC31_YEAST
ID RHC31_YEAST Reviewed; 347 AA.
AC Q06624; D6W4I0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=DNA damage tolerance protein RHC31;
DE AltName: Full=RAD31 homolog;
GN Name=AOS1; Synonyms=RHC31; OrderedLocusNames=YPR180W; ORFNames=P9705.5;
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 CHARACTERIZATION.
RX PubMed=9092625; DOI=10.1093/nar/25.6.1162;
RA Shayeghi M., Doe C.L., Tavassoli M., Watts F.Z.;
RT "Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene
RT required for DNA damage tolerance.";
RL Nucleic Acids Res. 25:1162-1169(1997).
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 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: Could be involved in a ubiquitin-related process important
CC for DNA damage tolerance.
CC -!- INTERACTION:
CC Q06624; P52488: UBA2; NbExp=3; IntAct=EBI-15107, EBI-19710;
CC -!- MISCELLANEOUS: Present with 7430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U25842; AAB68113.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11596.1; -; Genomic_DNA.
DR PIR; S59837; S59837.
DR RefSeq; NP_015506.1; NM_001184277.1.
DR AlphaFoldDB; Q06624; -.
DR SMR; Q06624; -.
DR BioGRID; 36352; 224.
DR ComplexPortal; CPX-3238; SUMO activating enzyme complex.
DR DIP; DIP-2338N; -.
DR IntAct; Q06624; 18.
DR MINT; Q06624; -.
DR STRING; 4932.YPR180W; -.
DR iPTMnet; Q06624; -.
DR MaxQB; Q06624; -.
DR PaxDb; Q06624; -.
DR PRIDE; Q06624; -.
DR EnsemblFungi; YPR180W_mRNA; YPR180W; YPR180W.
DR GeneID; 856310; -.
DR KEGG; sce:YPR180W; -.
DR SGD; S000006384; AOS1.
DR VEuPathDB; FungiDB:YPR180W; -.
DR eggNOG; KOG2014; Eukaryota.
DR GeneTree; ENSGT00960000189260; -.
DR HOGENOM; CLU_002556_4_1_1; -.
DR InParanoid; Q06624; -.
DR OMA; TDVWGTF; -.
DR BioCyc; YEAST:G3O-34305-MON; -.
DR Reactome; R-SCE-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-SCE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR PRO; PR:Q06624; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06624; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IPI:SGD.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW DNA damage; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..347
FT /note="DNA damage tolerance protein RHC31"
FT /id="PRO_0000194975"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219"
SQ SEQUENCE 347 AA; 39273 MW; 1ADB7B817BA27F3E CRC64;
MDMKVEKLSE DEIALYDRQI RLWGMTAQAN MRSAKVLLIN LGAIGSEITK SIVLSGIGHL
TILDGHMVTE EDLGSQFFIG SEDVGQWKID ATKERIQDLN PRIELNFDKQ DLQEKDEEFF
QQFDLVVATE MQIDEAIKIN TLTRKLNIPL YVAGSNGLFA YVFIDLIEFI SEDEKLQSVR
PTTVGPISSN RSIIEVTTRK DEEDEKKTYE RIKTKNCYRP LNEVLSTATL KEKMTQRQLK
RVTSILPLTL SLLQYGLNQK GKAISFEQMK RDAAVWCENL GVPATVVKDD YIQQFIKQKG
IEFAPVAAII GGAVAQDVIN ILGKRLSPLN NFIVFDGITL DMPLFEF
