DPB11_YEAST
ID DPB11_YEAST Reviewed; 764 AA.
AC P47027; D6VW94; Q05712;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=DNA replication regulator DPB11;
GN Name=DPB11; OrderedLocusNames=YJL090C; ORFNames=J0918;
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], AND FUNCTION.
RC STRAIN=SK1;
RX PubMed=8524850; DOI=10.1073/pnas.92.25.11791;
RA Araki H., Leem S.-H., Phongdara A., Sugino A.;
RT "Dpb11, which interacts with DNA polymerase II(epsilon) in Saccharomyces
RT cerevisiae, has a dual role in S-phase progression and at a cell cycle
RT checkpoint.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11791-11795(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH SLD2.
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 SUBCELLULAR LOCATION.
RX PubMed=12730134; DOI=10.1101/gad.1065903;
RA Takayama Y., Kamimura Y., Okawa M., Muramatsu S., Sugino A., Araki H.;
RT "GINS, a novel multiprotein complex required for chromosomal DNA
RT replication in budding yeast.";
RL Genes Dev. 17:1153-1165(2003).
RN [7]
RP INTERACTION WITH SLD2.
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 [8]
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 [9]
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).
CC -!- FUNCTION: Has a role in the initiation of DNA replication. Required at
CC S-phase checkpoint. Required for the association of PSF1 with origins.
CC Also required for the proper activation of RAD53 in response to DNA
CC damage and replication blocks. Multicopy suppressor of DPB2 mutation.
CC Overexpression restores the growth defect conferred by POL2 mutation.
CC {ECO:0000269|PubMed:10097122, ECO:0000269|PubMed:12730134,
CC ECO:0000269|PubMed:8524850}.
CC -!- SUBUNIT: Interacts with SLD2. {ECO:0000269|PubMed:10097122,
CC ECO:0000269|PubMed:9742127}.
CC -!- INTERACTION:
CC P47027; Q04377: LCD1; NbExp=7; IntAct=EBI-25984, EBI-35652;
CC P47027; P38111: MEC1; NbExp=3; IntAct=EBI-25984, EBI-6668;
CC P47027; P14737: RAD9; NbExp=13; IntAct=EBI-25984, EBI-14788;
CC P47027; P34252: SLD2; NbExp=9; IntAct=EBI-25984, EBI-26824;
CC P47027; P53135: SLD3; NbExp=9; IntAct=EBI-25984, EBI-23925;
CC P47027; Q12098: SLX4; NbExp=2; IntAct=EBI-25984, EBI-37788;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730134}.
CC -!- MISCELLANEOUS: Present with 540 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D42168; BAA07725.2; -; Genomic_DNA.
DR EMBL; X83502; CAA58477.1; -; Genomic_DNA.
DR EMBL; Z49365; CAA89383.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08710.1; -; Genomic_DNA.
DR PIR; S56017; S56017.
DR RefSeq; NP_012445.1; NM_001181523.1.
DR AlphaFoldDB; P47027; -.
DR BioGRID; 33667; 587.
DR ComplexPortal; CPX-1188; DPB11-SLD3-SLD2 DNA replication complex.
DR DIP; DIP-5037N; -.
DR IntAct; P47027; 17.
DR MINT; P47027; -.
DR STRING; 4932.YJL090C; -.
DR iPTMnet; P47027; -.
DR MaxQB; P47027; -.
DR PaxDb; P47027; -.
DR PRIDE; P47027; -.
DR EnsemblFungi; YJL090C_mRNA; YJL090C; YJL090C.
DR GeneID; 853355; -.
DR KEGG; sce:YJL090C; -.
DR SGD; S000003626; DPB11.
DR VEuPathDB; FungiDB:YJL090C; -.
DR eggNOG; KOG1929; Eukaryota.
DR HOGENOM; CLU_020751_0_0_1; -.
DR InParanoid; P47027; -.
DR OMA; CLHYKKL; -.
DR BioCyc; YEAST:G3O-31545-MON; -.
DR PRO; PR:P47027; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47027; protein.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IMP:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
DR GO; GO:0070182; F:DNA polymerase binding; IDA:SGD.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0007533; P:mating type switching; IMP:SGD.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IGI:SGD.
DR GO; GO:1902597; P:positive regulation of DNA replication origin binding; IMP:SGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:SGD.
DR GO; GO:0000725; P:recombinational repair; IDA:SGD.
DR GO; GO:1903466; P:regulation of mitotic DNA replication initiation; IC:ComplexPortal.
DR Gene3D; 3.40.50.10190; -; 4.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SMART; SM00292; BRCT; 3.
DR SUPFAM; SSF52113; SSF52113; 4.
DR PROSITE; PS50172; BRCT; 3.
PE 1: Evidence at protein level;
KW Cell cycle; DNA replication; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..764
FT /note="DNA replication regulator DPB11"
FT /id="PRO_0000079989"
FT DOMAIN 1..99
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 129..220
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 322..418
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 651..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 72
FT /note="Q -> K (in Ref. 1; BAA07725)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..296
FT /note="QQ -> HR (in Ref. 1; BAA07725)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="C -> Y (in Ref. 1; BAA07725)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="Y -> C (in Ref. 1; BAA07725)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="R -> K (in Ref. 1; BAA07725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 87241 MW; 79B3A9BC7815E440 CRC64;
MKPFQGITFC PTAINNEILA KKISKKIIKL GGIFSKDLTR QVNVLVVGST TNTNKFKFAV
KHRFDIIFID IQAIDDIYQL WLSGENILPD SNTATMTGST YEMLKILYRR FSFKYLHNFN
IFIGRITDTN ITSIDSLVRS IKKLGCSSYN YQNFVIKDTS SHNDDDDQGQ NGQISIFVTD
TLLGARVNAA IEQNIPIVHF KWILDCQKRS ALLPYDPYYL LPNIKDLPYD SIGSNSCDCW
DKINTTFPTN IDAQSSLQRQ QSSSTLTPSL PKTSSLLNKF KPKGEKIWDK AMSLQQHSKT
NFSVLGQSPL SINNKQEDLS DNSTLIFKNC AFIIHHIFPG NHRSILTKIV VQNGGKIETS
YLSGIYDHSY YIIPSNKALD SFNDLPEIID DNDGIVTEFF IERCLYYQKL LHPIDLWSKP
FLSTIEFQVS SSSKLLHHEF SSSPFLNVTI TGFSGVELLH LTKVLNLLKP MGINYVEYLN
KSTDILLINL AALPSIPKTH PLWSNEFSDL FTQFCINNNN DDPGDNNRKD FQNNSILRNS
MKRKIEYIKK FHSIPVVTPA FIFKLLSAAS GENNEIFLNN IKWCIICPRG HKDDFKCKIK
KPYYTSISSE KKYQNNDPKI DKTILLKRNN SSLSEHSMKD TKNELLQKIR ETDSGRKKRS
VSSSIMDVSS ERQMPDTKRI KLESLPKNFV PKQIKRTTSW GTIMSENVPT EQPTAISNPE
EIPRTEEVSH TQVTYGSIQD KKRTASLEKP MRRQTRNQTK ELDS
