SLD2_YEAST
ID SLD2_YEAST Reviewed; 453 AA.
AC P34252; D6VXH9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DNA replication regulator SLD2;
DE AltName: Full=DNA replication and checkpoint protein 1;
GN Name=SLD2; Synonyms=DRC1; OrderedLocusNames=YKL108W; ORFNames=YKL463;
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 204508 / S288c;
RX PubMed=8109175; DOI=10.1002/yea.320091113;
RA Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H.,
RA Bolotin-Fukuhara M., Sor F.;
RT "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of
RT Saccharomyces cerevisiae suggests the presence of a second aspartate
RT aminotransferase gene in yeast.";
RL Yeast 9:1259-1265(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 FUNCTION, AND INTERACTION WITH DPB11.
RX PubMed=9742127; DOI=10.1128/mcb.18.10.6102;
RA Kamimura Y., Masumoto H., Sugino A., Araki H.;
RT "Sld2, which interacts with Dpb11 in Saccharomyces cerevisiae, is required
RT for chromosomal DNA replication.";
RL Mol. Cell. Biol. 18:6102-6109(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH DPB11.
RX PubMed=10097122; DOI=10.1073/pnas.96.7.3824;
RA Wang H., Elledge S.J.;
RT "DRC1, DNA replication and checkpoint protein 1, functions with DPB11 to
RT control DNA replication and the S-phase checkpoint in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3824-3829(1999).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION BY CDC28.
RX PubMed=11807498; DOI=10.1038/nature713;
RA Masumoto H., Muramatsu S., Kamimura Y., Araki H.;
RT "S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA
RT replication in budding yeast.";
RL Nature 415:651-655(2002).
RN [7]
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 [8]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [9]
RP INTERACTION WITH DPB11, PHOSPHORYLATION AT THR-84, AND MUTAGENESIS OF
RP THR-84; SER-100; SER-208 AND THR-241.
RX PubMed=16619031; DOI=10.1038/sj.emboj.7601075;
RA Tak Y.-S., Tanaka Y., Endo S., Kamimura Y., Araki H.;
RT "A CDK-catalysed regulatory phosphorylation for formation of the DNA
RT replication complex Sld2-Dpb11.";
RL EMBO J. 25:1987-1996(2006).
RN [10]
RP DEPHOSPHORYLATION BY CDC14.
RX PubMed=17116692; DOI=10.1128/mcb.01069-06;
RA Bloom J., Cross F.R.;
RT "Novel role for Cdc14 sequestration: Cdc14 dephosphorylates factors that
RT promote DNA replication.";
RL Mol. Cell. Biol. 27:842-853(2007).
CC -!- FUNCTION: Has a role in the initiation of DNA replication. Required at
CC S-phase checkpoint. Also required for the proper activation of RAD53 in
CC response to DNA damage and replication blocks.
CC {ECO:0000269|PubMed:10097122, ECO:0000269|PubMed:11807498,
CC ECO:0000269|PubMed:9742127}.
CC -!- SUBUNIT: Interacts with DPB11. {ECO:0000269|PubMed:10097122,
CC ECO:0000269|PubMed:16619031, ECO:0000269|PubMed:9742127}.
CC -!- INTERACTION:
CC P34252; P47027: DPB11; NbExp=9; IntAct=EBI-26824, EBI-25984;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDC28 at the onset of S-phase. This
CC phosphorylation, specifically phosphorylation of Thr-84 promotes
CC interaction with DPB11 leading to DNA replication. Dephosphorylated by
CC CDC14. {ECO:0000269|PubMed:11807498, ECO:0000269|PubMed:14574415,
CC ECO:0000269|PubMed:16619031}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLD2 family. {ECO:0000305}.
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DR EMBL; X71133; CAA50449.1; -; Genomic_DNA.
DR EMBL; Z28108; CAA81948.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09049.1; -; Genomic_DNA.
DR PIR; S37935; S37935.
DR RefSeq; NP_012814.1; NM_001179674.1.
DR AlphaFoldDB; P34252; -.
DR SMR; P34252; -.
DR BioGRID; 34025; 58.
DR ComplexPortal; CPX-1188; DPB11-SLD3-SLD2 DNA replication complex.
DR DIP; DIP-5880N; -.
DR IntAct; P34252; 21.
DR MINT; P34252; -.
DR STRING; 4932.YKL108W; -.
DR iPTMnet; P34252; -.
DR MaxQB; P34252; -.
DR PaxDb; P34252; -.
DR PRIDE; P34252; -.
DR EnsemblFungi; YKL108W_mRNA; YKL108W; YKL108W.
DR GeneID; 853752; -.
DR KEGG; sce:YKL108W; -.
DR SGD; S000001591; SLD2.
DR VEuPathDB; FungiDB:YKL108W; -.
DR eggNOG; ENOG502SCF7; Eukaryota.
DR HOGENOM; CLU_057728_0_0_1; -.
DR InParanoid; P34252; -.
DR OMA; GPTPQIY; -.
DR BioCyc; YEAST:G3O-31894-MON; -.
DR PRO; PR:P34252; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34252; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IGI:SGD.
DR GO; GO:0071163; P:DNA replication preinitiation complex assembly; IMP:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:SGD.
DR GO; GO:1902977; P:mitotic DNA replication preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:SGD.
DR GO; GO:1903466; P:regulation of mitotic DNA replication initiation; IC:ComplexPortal.
DR InterPro; IPR021110; DNA_rep_checkpnt_protein.
DR InterPro; IPR040203; Sld2.
DR PANTHER; PTHR28124; PTHR28124; 1.
DR Pfam; PF11719; Drc1-Sld2; 2.
PE 1: Evidence at protein level;
KW Cell cycle; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..453
FT /note="DNA replication regulator SLD2"
FT /id="PRO_0000071952"
FT REGION 284..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..453
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16619031"
FT MUTAGEN 84
FT /note="T->A: No interaction with DPB11."
FT /evidence="ECO:0000269|PubMed:16619031"
FT MUTAGEN 100
FT /note="S->A: No interaction with DPB11."
FT /evidence="ECO:0000269|PubMed:16619031"
FT MUTAGEN 208
FT /note="S->A: Normal interaction with DPB11."
FT /evidence="ECO:0000269|PubMed:16619031"
FT MUTAGEN 241
FT /note="T->A: Reduced interaction with DPB11."
FT /evidence="ECO:0000269|PubMed:16619031"
SQ SEQUENCE 453 AA; 52272 MW; 52B2969C97AAEAC8 CRC64;
MYSFELDKLK IELKTWEHDF IDKNKREPTR DDIKSLRTVR QMYKQYSTLK KKQSLQRQKV
DTQESVELPA HKKDHDEVVE IGPTPQVYGK AISIFDMNLS PIKPIYMTFT NNIDVNNDNS
KTISNESSPR KTILLKSSPA DRTLVAEPIS SVKRQLNFQM LNASSTRTPT SSPCKNRNGK
LVEIKKCSPT INPPLESGKP SGYYGPNSPL KLDEENIHLN ISLNSSTKRR LQIAYPSLQK
TPSKDQADIS TSFSPSPLIR RPLTKSLIEL AREHTEIVKE FGVLQEEDIE EEEEGEEGEN
GYDEKNHEDD FGLEDELIRP KVVKDIFQED DDNDDSQARE DTFIRKRPKR RKVIRRLRDN
DPETETAGFE RDVHKELVKL KRRKVAEFLG STSQISDTEF EHDPEASSGV VSSEQKPTAK
RKGRKKYNLV SNNFRRLKLP KKNRFSNGRW GRR
