SHU2_YEAST
ID SHU2_YEAST Reviewed; 223 AA.
AC P38957; D6VS64;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Suppressor of hydroxyurea sensitivity protein 2;
GN Name=SHU2; OrderedLocusNames=YDR078C; ORFNames=D4436;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [4]
RP FUNCTION.
RX PubMed=12972632; DOI=10.1073/pnas.2035018100;
RA Huang M.-E., Rio A.-G., Nicolas A., Kolodner R.D.;
RT "A genomewide screen in Saccharomyces cerevisiae for genes that suppress
RT the accumulation of mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11529-11534(2003).
RN [5]
RP IDENTIFICATION IN THE SHU COMPLEX, AND FUNCTION.
RX PubMed=15654096; DOI=10.1534/genetics.104.036764;
RA Shor E., Weinstein J., Rothstein R.;
RT "A genetic screen for top3 suppressors in Saccharomyces cerevisiae
RT identifies SHU1, SHU2, PSY3 and CSM2: four genes involved in error-free DNA
RT repair.";
RL Genetics 169:1275-1289(2005).
RN [6]
RP FUNCTION.
RX PubMed=17671161; DOI=10.1091/mbc.e07-05-0490;
RA Mankouri H.W., Ngo H.P., Hickson I.D.;
RT "Shu proteins promote the formation of homologous recombination
RT intermediates that are processed by Sgs1-Rmi1-Top3.";
RL Mol. Biol. Cell 18:4062-4073(2007).
RN [7]
RP IDENTIFICATION IN THE SHU COMPLEX, AND FUNCTION.
RX PubMed=19496932; DOI=10.1111/j.1365-2958.2009.06748.x;
RA Ball L.G., Zhang K., Cobb J.A., Boone C., Xiao W.;
RT "The yeast Shu complex couples error-free post-replication repair to
RT homologous recombination.";
RL Mol. Microbiol. 73:89-102(2009).
CC -!- FUNCTION: Plays a role in a RAD51/RAD54-dependent homologous
CC recombination repair (HRR) pathway to repair MMS-induced lesions during
CC S-phase. Required for error-free repair of spontaneous and induced DNA
CC lesions to protect the genome from mutation.
CC {ECO:0000269|PubMed:12972632, ECO:0000269|PubMed:15654096,
CC ECO:0000269|PubMed:17671161, ECO:0000269|PubMed:19496932}.
CC -!- SUBUNIT: Component of the SHU complex composed of at least CSM2, PSY3,
CC SHU1 and SHU2. {ECO:0000269|PubMed:15654096,
CC ECO:0000269|PubMed:19496932}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHU2 family. {ECO:0000305}.
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DR EMBL; Z46796; CAA86800.1; -; Genomic_DNA.
DR EMBL; X82086; CAA57605.1; -; Genomic_DNA.
DR EMBL; Z74374; CAA98897.1; -; Genomic_DNA.
DR EMBL; AY557677; AAS56003.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11924.1; -; Genomic_DNA.
DR PIR; S48765; S48765.
DR RefSeq; NP_010363.1; NM_001180386.1.
DR PDB; 5XYN; X-ray; 3.30 A; D=1-223.
DR PDBsum; 5XYN; -.
DR AlphaFoldDB; P38957; -.
DR SMR; P38957; -.
DR BioGRID; 32133; 46.
DR ComplexPortal; CPX-3087; Shu complex.
DR DIP; DIP-1370N; -.
DR IntAct; P38957; 6.
DR MINT; P38957; -.
DR STRING; 4932.YDR078C; -.
DR PaxDb; P38957; -.
DR EnsemblFungi; YDR078C_mRNA; YDR078C; YDR078C.
DR GeneID; 851650; -.
DR KEGG; sce:YDR078C; -.
DR SGD; S000002485; SHU2.
DR VEuPathDB; FungiDB:YDR078C; -.
DR eggNOG; ENOG502S0XB; Eukaryota.
DR HOGENOM; CLU_1115918_0_0_1; -.
DR InParanoid; P38957; -.
DR OMA; WLKLHLN; -.
DR BioCyc; YEAST:G3O-29683-MON; -.
DR PRO; PR:P38957; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38957; protein.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097196; C:Shu complex; IDA:SGD.
DR GO; GO:0035861; C:site of double-strand break; IMP:SGD.
DR GO; GO:0000730; P:DNA recombinase assembly; IMP:SGD.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IC:ComplexPortal.
DR GO; GO:0070987; P:error-free translesion synthesis; IC:SGD.
DR GO; GO:0043007; P:maintenance of rDNA; IGI:SGD.
DR GO; GO:1903112; P:positive regulation of single-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..223
FT /note="Suppressor of hydroxyurea sensitivity protein 2"
FT /id="PRO_0000202593"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5XYN"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:5XYN"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:5XYN"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5XYN"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:5XYN"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5XYN"
SQ SEQUENCE 223 AA; 26123 MW; A02B8EBF38FC4423 CRC64;
MSKDVIEYSK LFAKLVNTND DTKLDDTIAS FLYYMFPREL FIRAISLLES SDMFIYILDR
VHNKEGNEHT SLIDVLVDEF YKGSSNSLLE YRLIVKDTND GAPPILVDIA HWFCSCEEFC
KYFHEALEKT DEKEELHDVL INEVDDHLQF SDDRFAQLDP HSLSKQWYFK FDKVCCSHLL
AFSILLRSSI NVLKFFTVNS NKVFVIAIDN IDEWLNLHIN IVE
