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Protein

DDK kinase regulatory subunit DBF4

Gene

DBF4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-dependent kinase (DDK), which is involved in cell cycle regulation of premitotic and premeiotic chromosome replication and in chromosome segregation. DDK plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7 to MCM2 and to origins of replication. DDK has also postreplicative functions in meiosis. DDK phosphorylates the meiosis-specific double-strand break protein MER2 for initiation of meiotic recombination. Interacts with CDC5 during meiosis to promote double-strand breaks and monopolar spindle orientation. Inhibits CDC5 activity during mitosis through direct binding to its PBD.12 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri654 – 70350DBF4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA replication origin binding Source: SGD
  • protein serine/threonine kinase activator activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB-KW
  • DNA replication initiation Source: SGD
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of exit from mitosis Source: SGD
  • positive regulation of meiosis I Source: SGD
  • positive regulation of protein kinase activity Source: SGD
  • premeiotic DNA replication Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, DNA replication, Meiosis, Mitosis

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29662-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DDK kinase regulatory subunit DBF4
Alternative name(s):
Dumbbell forming protein 4
Gene namesi
Name:DBF4
Synonyms:DNA52
Ordered Locus Names:YDR052C
ORF Names:D4205, YD9609.07C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR052C.
SGDiS000002459. DBF4.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: SGD
  • Dbf4-dependent protein kinase complex Source: SGD
  • nucleus Source: GOC
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831R → A or E: Defective for interaction with CDC5. 1 Publication
Mutagenesisi84 – 841S → A: No effect. 1 Publication
Mutagenesisi85 – 851I → A: Defective for interaction with CDC5. 1 Publication
Mutagenesisi86 – 861E → K: No effect. 1 Publication
Mutagenesisi87 – 871G → A: Defective for interaction with CDC5. 1 Publication
Mutagenesisi88 – 881A → V: Defective for interaction with CDC5. 1 Publication
Mutagenesisi661 – 6611C → A in DBF4-AAHH; weakens interaction with ARS1 origin DNA and MCM2, but not other known ligands; when associated with A-664. 1 Publication
Mutagenesisi664 – 6641C → A in DBF4-AAHH; weakens interaction with ARS1 origin DNA and MCM2, but not other known ligands; when associated with A-661. 1 Publication
Mutagenesisi674 – 6741H → A in DBF4-CCAA; weakens interaction with ARS1 origin DNA and MCM2, but not other known ligands; when associated with A-680. 1 Publication
Mutagenesisi680 – 6801H → A: Weakens interaction with ARS1 origin DNA and MCM2, but not other known ligands. In DBF4-CCAA; weakens interaction with ARS1 origin DNA and MCM2, but not other known ligands; when associated with A-674. 1 Publication
Mutagenesisi680 – 6801H → C: Weakens interaction with ARS1 origin DNA and MCM2, but not other known ligands. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 704704DDK kinase regulatory subunit DBF4PRO_0000079791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources
Modified residuei623 – 6231PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDC7 and by CDC5.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32325.

PTM databases

iPTMnetiP32325.

Expressioni

Inductioni

Cell cycle-regulated. Protein levels increase as cells begin S phase and remain high through late mitosis.2 Publications

Interactioni

Subunit structurei

Heterodimer with CDC7 to form the DBF4-dependent kinase (DDK) complex. Interacts (via PBD-binding motif) with CDC5 (via POLO box domains). Interacts (via N-terminus) with ORC2, ORC3 and RAD53. Binds to ARS1 origin DNA.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC7P062438EBI-5575,EBI-4451

Protein-protein interaction databases

BioGridi32106. 130 interactions.
DIPiDIP-2290N.
IntActiP32325. 4 interactions.
MINTiMINT-364128.

Structurei

Secondary structure

1
704
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 12318Combined sources
Beta strandi125 – 1284Combined sources
Helixi138 – 15720Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi172 – 1776Combined sources
Helixi179 – 1846Combined sources
Helixi190 – 1967Combined sources
Beta strandi200 – 2034Combined sources
Helixi204 – 21310Combined sources
Helixi218 – 2214Combined sources
Helixi233 – 2419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQ0X-ray2.70A/B/C/D/E/F/G/H/I/J120-250[»]
3OQ4X-ray2.40A/B/C/D/E120-250[»]
3QBZX-ray2.69A66-221[»]
ProteinModelPortaliP32325.
SMRiP32325. Positions 98-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32325.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 1910D box 1
Regioni62 – 709D box 2

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi83 – 886POLO box domain (PBD)-binding

Sequence similaritiesi

Contains 1 DBF4-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri654 – 70350DBF4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000112168.
InParanoidiP32325.
KOiK02309.
OMAiGSFGRCP.
OrthoDBiEOG79KPPX.

Family and domain databases

InterProiIPR013939. Regulatory_Dfp1/Him1.
IPR006572. Znf_DBF.
[Graphical view]
PfamiPF08630. Dfp1_Him1_M. 1 hit.
PF07535. zf-DBF. 1 hit.
[Graphical view]
SMARTiSM00586. ZnF_DBF. 1 hit.
[Graphical view]
PROSITEiPS51265. ZF_DBF4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSPTKMIIR SPLKETDTNL KHNNGIAAST TAAGHLNVFS NDNNCNNNNT
60 70 80 90 100
TESFPKKRSL ERLELQQQQH LHEKKRARIE RARSIEGAVQ VSKGTGLKNV
110 120 130 140 150
EPRVTPKELL EWQTNWKKIM KRDSRIYFDI TDDVEMNTYN KSKMDKRRDL
160 170 180 190 200
LKRGFLTLGA QITQFFDTTV TIVITRRSVE NIYLLKDTDI LSRAKKNYMK
210 220 230 240 250
VWSYEKAARF LKNLDVDLDH LSKTKSASLA APTLSNLLHN EKLYGPTDRD
260 270 280 290 300
PRTKRDDIHY FKYPHVYLYD LWQTWAPIIT LEWKPQELTN LDELPYPILK
310 320 330 340 350
IGSFGRCPFI GDRNYDESSY KRVVKRYSRD KANKKYALQL RALFQYHADT
360 370 380 390 400
LLNTSSVNDQ TKNLIFIPHT CNDSTKSFKK WMQEKAKNFE KTELKKTDDS
410 420 430 440 450
AVQDVRNEHA DQTDEKNSIL LNETETKEPP LKEEKENKQS IAEESNKYPQ
460 470 480 490 500
RKELAATPKL NHPVLATFAR QETEEVPDDL CTLKTKSRQA FEIKASGAHQ
510 520 530 540 550
SNDVATSFGN GLGPTRASVM SKNMKSLSRL MVDRKLGVKQ TNGNNKNYTA
560 570 580 590 600
TIATTAETSK ENRHRLDFNA LKKDEAPSKE TGKDSAVHLE TNRKPQNFPK
610 620 630 640 650
VATKSVSADS KVHNDIKITT TESPTASKKS TSTNVTLHFN AQTAQTAQPV
660 670 680 690 700
KKETVKNSGY CENCRVKYES LEQHIVSEKH LSFAENDLNF EAIDSLIENL

RFQI
Length:704
Mass (Da):80,690
Last modified:February 1, 1996 - v2
Checksum:iBDB93E72EF2ABC0B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1602GA → NT in CAA42819 (PubMed:1592236).Curated
Sequence conflicti177 – 1771R → RR in CAA42819 (PubMed:1592236).Curated
Sequence conflicti197 – 1971N → K in CAA42819 (PubMed:1592236).Curated
Sequence conflicti256 – 2561D → G in CAA42819 (PubMed:1592236).Curated
Sequence conflicti416 – 42510Missing in CAA42819 (PubMed:1592236).Curated
Sequence conflicti439 – 4391Q → R in CAA42819 (PubMed:1592236).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60279 Genomic DNA. Translation: CAA42819.1.
M83539 Genomic DNA. Translation: AAA34573.1.
X84162 Genomic DNA. Translation: CAA58969.1.
Z49209 Genomic DNA. Translation: CAA89082.1.
Z74348 Genomic DNA. Translation: CAA98869.1.
BK006938 Genomic DNA. Translation: DAA11899.1.
PIRiS25371.
RefSeqiNP_010337.3. NM_001180360.3.

Genome annotation databases

EnsemblFungiiYDR052C; YDR052C; YDR052C.
GeneIDi851623.
KEGGisce:YDR052C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60279 Genomic DNA. Translation: CAA42819.1.
M83539 Genomic DNA. Translation: AAA34573.1.
X84162 Genomic DNA. Translation: CAA58969.1.
Z49209 Genomic DNA. Translation: CAA89082.1.
Z74348 Genomic DNA. Translation: CAA98869.1.
BK006938 Genomic DNA. Translation: DAA11899.1.
PIRiS25371.
RefSeqiNP_010337.3. NM_001180360.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQ0X-ray2.70A/B/C/D/E/F/G/H/I/J120-250[»]
3OQ4X-ray2.40A/B/C/D/E120-250[»]
3QBZX-ray2.69A66-221[»]
ProteinModelPortaliP32325.
SMRiP32325. Positions 98-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32106. 130 interactions.
DIPiDIP-2290N.
IntActiP32325. 4 interactions.
MINTiMINT-364128.

PTM databases

iPTMnetiP32325.

Proteomic databases

MaxQBiP32325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR052C; YDR052C; YDR052C.
GeneIDi851623.
KEGGisce:YDR052C.

Organism-specific databases

EuPathDBiFungiDB:YDR052C.
SGDiS000002459. DBF4.

Phylogenomic databases

HOGENOMiHOG000112168.
InParanoidiP32325.
KOiK02309.
OMAiGSFGRCP.
OrthoDBiEOG79KPPX.

Enzyme and pathway databases

BioCyciYEAST:G3O-29662-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32325.
PROiP32325.

Family and domain databases

InterProiIPR013939. Regulatory_Dfp1/Him1.
IPR006572. Znf_DBF.
[Graphical view]
PfamiPF08630. Dfp1_Him1_M. 1 hit.
PF07535. zf-DBF. 1 hit.
[Graphical view]
SMARTiSM00586. ZnF_DBF. 1 hit.
[Graphical view]
PROSITEiPS51265. ZF_DBF4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Temperature-sensitive cdc7 mutations of Saccharomyces cerevisiae are suppressed by the DBF4 gene, which is required for the G1/S cell cycle transition."
    Kitada K., Johnston L.H., Sugino T., Sugino A.
    Genetics 131:21-29(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204626 / S288c / A364A.
  2. "Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle genes in Saccharomyces cerevisiae."
    Solomon N.A., Wright M.B., Chang S., Buckley A.M., Dumas L.B., Gaber R.F.
    Yeast 8:273-289(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV."
    Brandt P., Ramlow S., Otto B., Bloecker H.
    Yeast 12:85-90(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Cell cycle regulation of the yeast Cdc7 protein kinase by association with the Dbf4 protein."
    Jackson A.L., Pahl P.M., Harrison K., Rosamond J., Sclafani R.A.
    Mol. Cell. Biol. 13:2899-2908(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Interaction of Dbf4, the Cdc7 protein kinase regulatory subunit, with yeast replication origins in vivo."
    Dowell S.J., Romanowski P., Diffley J.F.
    Science 265:1243-1246(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  8. "A novel role for Cdc5p in DNA replication."
    Hardy C.F., Pautz A.
    Mol. Cell. Biol. 16:6775-6782(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC5, PHOSPHORYLATION.
  9. "Cell cycle regulation of DNA replication initiator factor Dbf4p."
    Cheng L., Collyer T., Hardy C.F.
    Mol. Cell. Biol. 19:4270-4278(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Cell cycle control of Cdc7p kinase activity through regulation of Dbf4p stability."
    Oshiro G., Owens J.C., Shellman Y., Sclafani R.A., Li J.J.
    Mol. Cell. Biol. 19:4888-4896(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "An N-terminal domain of Dbf4p mediates interaction with both origin recognition complex (ORC) and Rad53p and can deregulate late origin firing."
    Duncker B.P., Shimada K., Tsai-Pflugfelder M., Pasero P., Gasser S.M.
    Proc. Natl. Acad. Sci. U.S.A. 99:16087-16092(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ORC2; ORC3 AND RAD53.
  12. "Dual role of the Cdc7-regulatory protein Dbf4 during yeast meiosis."
    Valentin G., Schwob E., Della Seta F.
    J. Biol. Chem. 281:2828-2834(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEIOTIC REPLICATION.
  13. "Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression."
    Sheu Y.-J., Stillman B.
    Mol. Cell 24:101-113(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Dbf4-dependent CDC7 kinase links DNA replication to the segregation of homologous chromosomes in meiosis I."
    Matos J., Lipp J.J., Bogdanova A., Guillot S., Okaz E., Junqueira M., Shevchenko A., Zachariae W.
    Cell 135:662-678(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEIOTIC SPINDLE ORIENTATION.
  16. "Cdc28-Clb5 (CDK-S) and Cdc7-Dbf4 (DDK) collaborate to initiate meiotic recombination in yeast."
    Wan L., Niu H., Futcher B., Zhang C., Shokat K.M., Boulton S.J., Hollingsworth N.M.
    Genes Dev. 22:386-397(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEIOTIC RECOMBINATION.
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-623, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Dbf4-Cdc7 phosphorylation of Mcm2 is required for cell growth."
    Bruck I., Kaplan D.
    J. Biol. Chem. 284:28823-28831(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MCM2.
  19. "Cdc7p-Dbf4p regulates mitotic exit by inhibiting Polo kinase."
    Miller C.T., Gabrielse C., Chen Y.-C., Weinreich M.
    PLoS Genet. 5:E1000498-E1000498(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC5.
  20. "The Dbf4 motif C zinc finger promotes DNA replication and mediates resistance to genotoxic stress."
    Jones D.R., Prasad A.A., Chan P.K., Duncker B.P.
    Cell Cycle 9:2018-2026(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-661; CYS-664; HIS-674 AND HIS-680.
  21. "Dbf4 regulates the Cdc5 polo-like kinase through a distinct non-canonical binding interaction."
    Chen Y.-C., Weinreich M.
    J. Biol. Chem. 285:41244-41254(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC5, MUTAGENESIS OF ARG-83; SER-84; ILE-85; GLU-86; GLY-87 AND ALA-88.
  22. "Methods to study kinase regulation of the replication fork helicase."
    Kaplan D.L., Bruck I.
    Methods 51:358-362(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  23. "The Dbf4-Cdc7 kinase promotes S phase by alleviating an inhibitory activity in Mcm4."
    Sheu Y.-J., Stillman B.
    Nature 463:113-117(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REPLICATION INITIATION.

Entry informationi

Entry nameiDBF4_YEAST
AccessioniPrimary (citable) accession number: P32325
Secondary accession number(s): D6VS39, P32355
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.