DBF2_YEAST
ID DBF2_YEAST Reviewed; 572 AA.
AC P22204; D6VUM4;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Cell cycle protein kinase DBF2;
DE EC=2.7.11.1;
DE AltName: Full=Dumbbell forming protein 2;
GN Name=DBF2; OrderedLocusNames=YGR092W;
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 INDUCTION.
RX PubMed=2181271; DOI=10.1128/mcb.10.4.1358-1366.1990;
RA Johnston L.H., Eberly S.L., Chapman J.W., Araki H., Sugino A.;
RT "The product of the Saccharomyces cerevisiae cell cycle gene DBF2 has
RT homology with protein kinases and is periodically expressed in the cell
RT cycle.";
RL Mol. Cell. Biol. 10:1358-1366(1990).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=1916278; DOI=10.1016/0378-1119(91)90465-n;
RA Toyn J.H., Araki H., Sugino A., Johnston L.H.;
RT "The cell-cycle-regulated budding yeast gene DBF2, encoding a putative
RT protein kinase, has a homologue that is not under cell-cycle control.";
RL Gene 104:63-70(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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, PHOSPHORYLATION, AND INDUCTION.
RX PubMed=8131744; DOI=10.1002/j.1460-2075.1994.tb06359.x;
RA Toyn J.H., Johnston L.H.;
RT "The Dbf2 and Dbf20 protein kinases of budding yeast are activated after
RT the metaphase to anaphase cell cycle transition.";
RL EMBO J. 13:1103-1113(1994).
RN [6]
RP INTERACTION WITH MOB1, AND FUNCTION OF THE DBF2-MOB1 COMPLEX.
RX PubMed=9528782; DOI=10.1128/mcb.18.4.2100;
RA Komarnitsky S.I., Chiang Y.-C., Luca F.C., Chen J., Toyn J.H., Winey M.,
RA Johnston L.H., Denis C.L.;
RT "DBF2 protein kinase binds to and acts through the cell cycle-regulated
RT MOB1 protein.";
RL Mol. Cell. Biol. 18:2100-2107(1998).
RN [7]
RP FUNCTION.
RX PubMed=9613578; DOI=10.1007/s004380050712;
RA Grandin N., de Almeida A., Charbonneau M.;
RT "The Cdc14 phosphatase is functionally associated with the Dbf2 protein
RT kinase in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:104-116(1998).
RN [8]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10228157; DOI=10.1093/emboj/18.9.2424;
RA Fesquet D., Fitzpatrick P.J., Johnson A.L., Kramer K.M., Toyn J.H.,
RA Johnston L.H.;
RT "A Bub2p-dependent spindle checkpoint pathway regulates the Dbf2p kinase in
RT budding yeast.";
RL EMBO J. 18:2424-2434(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10984431; DOI=10.1242/jcs.113.19.3399;
RA Frenz L.M., Lee S.E., Fesquet D., Johnston L.H.;
RT "The budding yeast Dbf2 protein kinase localises to the centrosome and
RT moves to the bud neck in late mitosis.";
RL J. Cell Sci. 113:3399-3408(2000).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11378390; DOI=10.1016/s0960-9822(01)00228-7;
RA Lee S.E., Frenz L.M., Wells N.J., Johnson A.L., Johnston L.H.;
RT "Order of function of the budding-yeast mitotic exit-network proteins Tem1,
RT Cdc15, Mob1, Dbf2, and Cdc5.";
RL Curr. Biol. 11:784-788(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=11434459; DOI=10.1266/ggs.76.141;
RA Yoshida S., Toh-e A.;
RT "Regulation of the localization of Dbf2 and Mob1 during cell division of
RT Saccharomyces cerevisiae.";
RL Genes Genet. Syst. 76:141-147(2001).
RN [12]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11598184; DOI=10.1091/mbc.12.10.2961;
RA Visintin R., Amon A.;
RT "Regulation of the mitotic exit protein kinases Cdc15 and Dbf2.";
RL Mol. Biol. Cell 12:2961-2974(2001).
RN [13]
RP FUNCTION, ACTIVITY REGULATION, AND PHOSPHORYLATION AT SER-374 AND THR-544.
RX PubMed=11404483; DOI=10.1073/pnas.141098998;
RA Mah A.S., Jang J., Deshaies R.J.;
RT "Protein kinase Cdc15 activates the Dbf2-Mob1 kinase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7325-7330(2001).
RN [14]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=14551257; DOI=10.1091/mbc.e03-02-0095;
RA Visintin R., Stegmeier F., Amon A.;
RT "The role of the polo kinase Cdc5 in controlling Cdc14 localization.";
RL Mol. Biol. Cell 14:4486-4498(2003).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=12937277; DOI=10.1091/mbc.e03-04-0238;
RA Hwa Lim H., Yeong F.M., Surana U.;
RT "Inactivation of mitotic kinase triggers translocation of MEN components to
RT mother-daughter neck in yeast.";
RL Mol. Biol. Cell 14:4734-4743(2003).
RN [16]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=12832486; DOI=10.1128/mcb.23.14.5018-5030.2003;
RA Bardin A.J., Boselli M.G., Amon A.;
RT "Mitotic exit regulation through distinct domains within the protein kinase
RT Cdc15.";
RL Mol. Cell. Biol. 23:5018-5030(2003).
RN [17]
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 [18]
RP FUNCTION OF THE DBF2-MOB1 COMPLEX.
RX PubMed=16242037; DOI=10.1186/1471-2091-6-22;
RA Mah A.S., Elia A.E., Devgan G., Ptacek J., Schutkowski M., Snyder M.,
RA Yaffe M.B., Deshaies R.J.;
RT "Substrate specificity analysis of protein kinase complex Dbf2-Mob1 by
RT peptide library and proteome array screening.";
RL BMC Biochem. 6:22-22(2005).
RN [19]
RP SUBCELLULAR LOCATION, AND FUNCTION OF THE DBF2-MOB1 COMPLEX.
RX PubMed=16176976; DOI=10.1091/mbc.e05-04-0337;
RA Stoepel J., Ottey M.A., Kurischko C., Hieter P., Luca F.C.;
RT "The mitotic exit network Mob1p-Dbf2p kinase complex localizes to the
RT nucleus and regulates passenger protein localization.";
RL Mol. Biol. Cell 16:5465-5479(2005).
RN [20]
RP FUNCTION.
RX PubMed=18048916; DOI=10.1099/mic.0.2007/010298-0;
RA Makrantoni V., Dennison P., Stark M.J., Coote P.J.;
RT "A novel role for the yeast protein kinase Dbf2p in vacuolar H+-ATPase
RT function and sorbic acid stress tolerance.";
RL Microbiology 153:4016-4026(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY
RP 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).
RN [22]
RP FUNCTION IN PHOSPHORYLATION OF CDC14.
RX PubMed=19221193; DOI=10.1083/jcb.200812022;
RA Mohl D.A., Huddleston M.J., Collingwood T.S., Annan R.S., Deshaies R.J.;
RT "Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the
RT cytoplasm during exit from mitosis.";
RL J. Cell Biol. 184:527-539(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20 AND SER-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [24]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=20123997; DOI=10.1083/jcb.200911128;
RA Konig C., Maekawa H., Schiebel E.;
RT "Mutual regulation of cyclin-dependent kinase and the mitotic exit
RT network.";
RL J. Cell Biol. 188:351-368(2010).
RN [25]
RP FUNCTION.
RX PubMed=20442249; DOI=10.1242/jcs.063891;
RA Meitinger F., Petrova B., Lombardi I.M., Bertazzi D.T., Hub B.,
RA Zentgraf H., Pereira G.;
RT "Targeted localization of Inn1, Cyk3 and Chs2 by the mitotic-exit network
RT regulates cytokinesis in budding yeast.";
RL J. Cell Sci. 123:1851-1861(2010).
RN [26]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=22196726; DOI=10.1016/j.cell.2011.11.051;
RA Trcek T., Larson D.R., Moldon A., Query C.C., Singer R.H.;
RT "Single-molecule mRNA decay measurements reveal promoter- regulated mRNA
RT stability in yeast.";
RL Cell 147:1484-1497(2011).
RN [27]
RP FUNCTION.
RX PubMed=22573892; DOI=10.1091/mbc.e12-01-0033;
RA Oh Y., Chang K.J., Orlean P., Wloka C., Deshaies R., Bi E.;
RT "Mitotic exit kinase Dbf2 directly phosphorylates chitin synthase Chs2 to
RT regulate cytokinesis in budding yeast.";
RL Mol. Biol. Cell 23:2445-2456(2012).
RN [28]
RP FUNCTION.
RX PubMed=23447700; DOI=10.1091/mbc.e12-08-0608;
RA Meitinger F., Palani S., Hub B., Pereira G.;
RT "Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR
RT protein Hof1 during cytokinesis.";
RL Mol. Biol. Cell 24:1290-1304(2013).
CC -!- FUNCTION: Ser/Thr-protein kinase involved in the mitotic exit network
CC (MEN) and required after the metaphase to anaphase cell cycle
CC transition. Phosphorylates CHS2 to regulate its dynamics and chitin
CC synthesis at the division site during cytokinesis. Coordinates septin
CC and actomyosin ring (AMR) functions during cytokinesis through the
CC phosphorylation of HOF1. In complex with MOB1, phosphorylates CDC14 at
CC sites adjacent to its nuclear localization sequence, thereby retaining
CC CDC14 in the cytoplasm. Binds also to SWI5 and CLB2 mRNAs
CC cotranscriptionally to regulate their decay. In the nucleus, the DBF2-
CC MOB1 complex regulates passenger protein localization during anaphase.
CC Mediates sorbic acid stress tolerance through promoting vacuolar H(+)-
CC ATPase function, probably through phosphorylation of VMA1 and VMA2
CC subunits. {ECO:0000269|PubMed:10228157, ECO:0000269|PubMed:10984431,
CC ECO:0000269|PubMed:11378390, ECO:0000269|PubMed:11404483,
CC ECO:0000269|PubMed:11598184, ECO:0000269|PubMed:12832486,
CC ECO:0000269|PubMed:14551257, ECO:0000269|PubMed:16176976,
CC ECO:0000269|PubMed:16242037, ECO:0000269|PubMed:18048916,
CC ECO:0000269|PubMed:19221193, ECO:0000269|PubMed:20123997,
CC ECO:0000269|PubMed:20442249, ECO:0000269|PubMed:22196726,
CC ECO:0000269|PubMed:22573892, ECO:0000269|PubMed:23447700,
CC ECO:0000269|PubMed:8131744, ECO:0000269|PubMed:9528782,
CC ECO:0000269|PubMed:9613578}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Kinase activity is regulated by BUB2, CDC15 and
CC CDC5, and is maximal during nuclear division. CDK1 kinase inhibits
CC cellular DBF2-MOB1 kinase activity via phosphorylation of both CDC15
CC and MOB1. {ECO:0000269|PubMed:10228157, ECO:0000269|PubMed:11404483,
CC ECO:0000269|PubMed:12832486, ECO:0000269|PubMed:14551257,
CC ECO:0000269|PubMed:20123997}.
CC -!- SUBUNIT: Interacts with MOB1. MOB1-binding is required for a late
CC mitotic event. {ECO:0000269|PubMed:9528782}.
CC -!- INTERACTION:
CC P22204; P38074: HMT1; NbExp=4; IntAct=EBI-5569, EBI-8394;
CC P22204; P40484: MOB1; NbExp=15; IntAct=EBI-5569, EBI-11119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Bud neck. Nucleus. Note=Localizes on spindle
CC ole body (SPB) for much of the cell cycle and migrates from there to
CC the bud neck in late mitosis. SPB localization during anaphase
CC coincides with activation kinase activity and depends on TEM1 and
CC CDC15. In absence of BUB2, localizes to SPB in cell cycle stages other
CC than anaphase and telophase.
CC -!- INDUCTION: Periodically expressed in the cell cycle, with a peak before
CC the onset of budding. {ECO:0000269|PubMed:2181271,
CC ECO:0000269|PubMed:8131744}.
CC -!- PTM: Phosphorylation of Ser-374 and Thr-544 by CDC15 is essential for
CC activation of DBF2 kinase activity. {ECO:0000269|PubMed:11404483,
CC ECO:0000269|PubMed:8131744}.
CC -!- MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M34146; AAA34559.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z72877; CAA97095.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08185.1; -; Genomic_DNA.
DR PIR; S64387; S64387.
DR RefSeq; NP_011606.3; NM_001181221.3.
DR PDB; 5NCN; X-ray; 3.50 A; B=85-173.
DR PDBsum; 5NCN; -.
DR AlphaFoldDB; P22204; -.
DR SMR; P22204; -.
DR BioGRID; 33335; 928.
DR ComplexPortal; CPX-1683; DBF2-MOB1 kinase complex.
DR DIP; DIP-2319N; -.
DR IntAct; P22204; 70.
DR MINT; P22204; -.
DR STRING; 4932.YGR092W; -.
DR iPTMnet; P22204; -.
DR MaxQB; P22204; -.
DR PaxDb; P22204; -.
DR PRIDE; P22204; -.
DR EnsemblFungi; YGR092W_mRNA; YGR092W; YGR092W.
DR GeneID; 852984; -.
DR KEGG; sce:YGR092W; -.
DR SGD; S000003324; DBF2.
DR VEuPathDB; FungiDB:YGR092W; -.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000176430; -.
DR HOGENOM; CLU_000288_67_4_1; -.
DR InParanoid; P22204; -.
DR OMA; FPYEDTS; -.
DR BioCyc; YEAST:G3O-30802-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P22204; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P22204; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0034973; C:Sid2-Mob1 complex; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IC:ComplexPortal.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000280; P:nuclear division; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0032465; P:regulation of cytokinesis; IDA:ComplexPortal.
DR GO; GO:1901900; P:regulation of protein localization to cell division site; IMP:SGD.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..572
FT /note="Cell cycle protein kinase DBF2"
FT /id="PRO_0000085918"
FT DOMAIN 177..477
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 478..555
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 183..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 374
FT /note="Phosphoserine; by CDC15"
FT /evidence="ECO:0000269|PubMed:11404483,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 544
FT /note="Phosphothreonine; by CDC15"
FT /evidence="ECO:0000269|PubMed:11404483"
FT CONFLICT 11..12
FT /note="LL -> YM (in Ref. 1; AAA34559)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="H -> Y (in Ref. 1; AAA34559)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="D -> E (in Ref. 1; AAA34559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 66148 MW; 648C565D5CE7117D CRC64;
MLSKSEKNVD LLAGNMSNLS FDGHGTPGGT GLFPNQNITK RRTRPAGIND SPSPVKPSFF
PYEDTSNMDI DEVSQPDMDV SNSPKKLPPK FYERATSNKT QRVVSVCKMY FLEHYCDMFD
YVISRRQRTK QVLEYLQQQS QLPNSDQIKL NEEWSSYLQR EHQVLRKRRL KPKNRDFEMI
TQVGQGGYGQ VYLARKKDTK EVCALKILNK KLLFKLNETK HVLTERDILT TTRSEWLVKL
LYAFQDLQSL YLAMEFVPGG DFRTLLINTR CLKSGHARFY ISEMFCAVNA LHDLGYTHRD
LKPENFLIDA KGHIKLTDFG LAAGTISNER IESMKIRLEK IKDLEFPAFT EKSIEDRRKM
YNQLREKEIN YANSMVGSPD YMALEVLEGK KYDFTVDYWS LGCMLFESLV GYTPFSGSST
NETYDNLRRW KQTLRRPRQS DGRAAFSDRT WDLITRLIAD PINRLRSFEH VKRMSYFADI
NFSTLRSMIP PFTPQLDSET DAGYFDDFTS EADMAKYADV FKRQDKLTAM VDDSAVSSKL
VGFTFRHRNG KQGSSGILFN GLEHSDPFST FY
