CDC7_HUMAN
ID CDC7_HUMAN Reviewed; 574 AA.
AC O00311; D3DT31; O00558; Q5T5U5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Cell division cycle 7-related protein kinase;
DE Short=CDC7-related kinase;
DE Short=HsCdc7;
DE Short=huCdc7;
DE EC=2.7.11.1;
GN Name=CDC7; Synonyms=CDC7L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Testis;
RX PubMed=9250678; DOI=10.1093/emboj/16.14.4340;
RA Sato N., Arai K., Masai H.;
RT "Human and Xenopus cDNAs encoding budding yeast Cdc7-related kinases: in
RT vitro phosphorylation of MCM subunits by a putative human homologue of
RT Cdc7.";
RL EMBO J. 16:4340-4351(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9573348; DOI=10.1016/s0378-1119(98)00094-8;
RA Hess G.F., Drong R.F., Weiland K.L., Slightom J.L., Sclafani R.A.,
RA Hollingsworth R.E.;
RT "A human homolog of the yeast CDC7 gene is overexpressed in some tumors and
RT transformed cell lines.";
RL Gene 211:133-140(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=9405610; DOI=10.1073/pnas.94.26.14320;
RA Jiang W., Hunter T.;
RT "Identification and characterization of a human protein kinase related to
RT budding yeast Cdc7p.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14320-14325(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-23; VAL-99; TRP-112;
RP LEU-162 AND ARG-441.
RG NIEHS SNPs program;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH DBF4.
RX PubMed=10373557; DOI=10.1128/mcb.19.7.5083;
RA Kumagai H., Sato N., Yamada M., Mahony D., Seghezzi W., Lees E., Arai K.,
RA Masai H.;
RT "A novel growth- and cell cycle-regulated protein, ASK, activates human
RT Cdc7-related kinase and is essential for G1/S transition in mammalian
RT cells.";
RL Mol. Cell. Biol. 19:5083-5095(1999).
RN [9]
RP FUNCTION, AND INTERACTION WITH DBF4B.
RX PubMed=12065429; DOI=10.1093/emboj/cdf290;
RA Montagnoli A., Bosotti R., Villa F., Rialland M., Brotherton D.,
RA Mercurio C., Berthelsen J., Santocanale C.;
RT "Drf1, a novel regulatory subunit for human Cdc7 kinase.";
RL EMBO J. 21:3171-3181(2002).
RN [10]
RP INTERACTION WITH DBF4B.
RX PubMed=15668232; DOI=10.1074/jbc.m411653200;
RA Yoshizawa-Sugata N., Ishii A., Taniyama C., Matsui E., Arai K., Masai H.;
RT "A second human Dbf4/ASK-related protein, Drf1/ASKL1, is required for
RT efficient progression of S and M phases.";
RL J. Biol. Chem. 280:13062-13070(2005).
RN [11]
RP INTERACTION WITH DBF4 AND DBF4B.
RX PubMed=17062569; DOI=10.1074/jbc.m604457200;
RA Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C.,
RA Santocanale C.;
RT "Cdc7 is an active kinase in human cancer cells undergoing replication
RT stress.";
RL J. Biol. Chem. 282:208-215(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-162; MET-208; ASP-209; ARG-441; ILE-472
RP AND ALA-498.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Seems to phosphorylate critical substrates that regulate the
CC G1/S phase transition and/or DNA replication. Can phosphorylate MCM2
CC and MCM3. {ECO:0000269|PubMed:12065429}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Forms a complex with either DBF4/DBF4A or DBF4B, leading to
CC the activation of the kinase activity.
CC -!- INTERACTION:
CC O00311; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-374980, EBI-11524452;
CC O00311; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-374980, EBI-739580;
CC O00311; Q9UBU7: DBF4; NbExp=8; IntAct=EBI-374980, EBI-372690;
CC O00311; Q9UBU7-1: DBF4; NbExp=3; IntAct=EBI-374980, EBI-16017435;
CC O00311; P51114-2: FXR1; NbExp=3; IntAct=EBI-374980, EBI-11022345;
CC O00311; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-374980, EBI-948296;
CC O00311; Q08379: GOLGA2; NbExp=3; IntAct=EBI-374980, EBI-618309;
CC O00311; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-374980, EBI-11163335;
CC O00311; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-374980, EBI-2549423;
CC O00311; P42858: HTT; NbExp=3; IntAct=EBI-374980, EBI-466029;
CC O00311; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-374980, EBI-11522367;
CC O00311; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-374980, EBI-747204;
CC O00311; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-374980, EBI-1640423;
CC O00311; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-374980, EBI-1216080;
CC O00311; Q9BTE3: MCMBP; NbExp=2; IntAct=EBI-374980, EBI-749378;
CC O00311; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-374980, EBI-16439278;
CC O00311; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-374980, EBI-11522433;
CC O00311; Q14140: SERTAD2; NbExp=3; IntAct=EBI-374980, EBI-2822051;
CC O00311; O75886: STAM2; NbExp=3; IntAct=EBI-374980, EBI-373258;
CC O00311; P55061: TMBIM6; NbExp=3; IntAct=EBI-374980, EBI-1045825;
CC O00311; P14373: TRIM27; NbExp=3; IntAct=EBI-374980, EBI-719493;
CC O00311; O94972: TRIM37; NbExp=3; IntAct=EBI-374980, EBI-741602;
CC O00311; Q2TAA8: TSNAXIP1; NbExp=3; IntAct=EBI-374980, EBI-6872498;
CC O00311; P0CW01: TSPY10; NbExp=3; IntAct=EBI-374980, EBI-19697726;
CC O00311; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-374980, EBI-12369705;
CC O00311; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-374980, EBI-12017160;
CC O00311; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-374980, EBI-3918996;
CC O00311; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-374980, EBI-17494306;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms may be produced.;
CC Name=1;
CC IsoId=O00311-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc7/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB003698; BAA19962.1; -; mRNA.
DR EMBL; AF015592; AAC52080.1; -; mRNA.
DR EMBL; AF005209; AAB97512.1; -; mRNA.
DR EMBL; AY585721; AAS79323.1; -; Genomic_DNA.
DR EMBL; AL355871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73114.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73115.1; -; Genomic_DNA.
DR EMBL; BC110526; AAI10527.1; -; mRNA.
DR EMBL; BC110527; AAI10528.1; -; mRNA.
DR EMBL; BC111044; AAI11045.1; -; mRNA.
DR CCDS; CCDS734.1; -. [O00311-1]
DR RefSeq; NP_001127891.1; NM_001134419.1. [O00311-1]
DR RefSeq; NP_001127892.1; NM_001134420.1. [O00311-1]
DR RefSeq; NP_003494.1; NM_003503.3. [O00311-1]
DR RefSeq; XP_005271298.1; XM_005271241.2. [O00311-1]
DR PDB; 4F99; X-ray; 2.33 A; A=37-574.
DR PDB; 4F9A; X-ray; 2.17 A; A/C=37-574.
DR PDB; 4F9B; X-ray; 2.50 A; A/C=37-574.
DR PDB; 4F9C; X-ray; 2.08 A; A=37-574.
DR PDB; 5UWQ; X-ray; 2.28 A; D=456-473.
DR PDB; 5UWR; X-ray; 2.24 A; D=456-478.
DR PDB; 6YA6; X-ray; 1.44 A; A=37-467, A=534-574.
DR PDB; 6YA7; X-ray; 1.67 A; A=37-466, A=534-574.
DR PDB; 6YA8; X-ray; 1.79 A; A=37-467, A=534-574.
DR PDBsum; 4F99; -.
DR PDBsum; 4F9A; -.
DR PDBsum; 4F9B; -.
DR PDBsum; 4F9C; -.
DR PDBsum; 5UWQ; -.
DR PDBsum; 5UWR; -.
DR PDBsum; 6YA6; -.
DR PDBsum; 6YA7; -.
DR PDBsum; 6YA8; -.
DR AlphaFoldDB; O00311; -.
DR SMR; O00311; -.
DR BioGRID; 113914; 103.
DR CORUM; O00311; -.
DR DIP; DIP-31728N; -.
DR IntAct; O00311; 59.
DR MINT; O00311; -.
DR STRING; 9606.ENSP00000393139; -.
DR BindingDB; O00311; -.
DR ChEMBL; CHEMBL5443; -.
DR GuidetoPHARMACOLOGY; 1960; -.
DR iPTMnet; O00311; -.
DR PhosphoSitePlus; O00311; -.
DR BioMuta; CDC7; -.
DR EPD; O00311; -.
DR jPOST; O00311; -.
DR MassIVE; O00311; -.
DR MaxQB; O00311; -.
DR PaxDb; O00311; -.
DR PeptideAtlas; O00311; -.
DR PRIDE; O00311; -.
DR ProteomicsDB; 47836; -. [O00311-1]
DR Antibodypedia; 3628; 322 antibodies from 36 providers.
DR DNASU; 8317; -.
DR Ensembl; ENST00000234626.11; ENSP00000234626.6; ENSG00000097046.13. [O00311-1]
DR Ensembl; ENST00000428239.5; ENSP00000393139.1; ENSG00000097046.13. [O00311-1]
DR GeneID; 8317; -.
DR KEGG; hsa:8317; -.
DR MANE-Select; ENST00000234626.11; ENSP00000234626.6; NM_003503.4; NP_003494.1.
DR UCSC; uc001doe.4; human. [O00311-1]
DR CTD; 8317; -.
DR DisGeNET; 8317; -.
DR GeneCards; CDC7; -.
DR HGNC; HGNC:1745; CDC7.
DR HPA; ENSG00000097046; Tissue enhanced (testis).
DR MIM; 603311; gene.
DR neXtProt; NX_O00311; -.
DR OpenTargets; ENSG00000097046; -.
DR PharmGKB; PA26272; -.
DR VEuPathDB; HostDB:ENSG00000097046; -.
DR eggNOG; KOG1167; Eukaryota.
DR GeneTree; ENSGT00550000075011; -.
DR HOGENOM; CLU_000288_118_1_1; -.
DR InParanoid; O00311; -.
DR OMA; FYTKMDV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O00311; -.
DR TreeFam; TF101052; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; O00311; -.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; O00311; -.
DR SIGNOR; O00311; -.
DR BioGRID-ORCS; 8317; 813 hits in 1118 CRISPR screens.
DR ChiTaRS; CDC7; human.
DR GeneWiki; Cell_division_cycle_7-related_protein_kinase; -.
DR GenomeRNAi; 8317; -.
DR Pharos; O00311; Tchem.
DR PRO; PR:O00311; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00311; protein.
DR Bgee; ENSG00000097046; Expressed in secondary oocyte and 144 other tissues.
DR ExpressionAtlas; O00311; baseline and differential.
DR Genevisible; O00311; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:HGNC-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0044770; P:cell cycle phase transition; IMP:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:HGNC-UCL.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Isopeptide bond; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..574
FT /note="Cell division cycle 7-related protein kinase"
FT /id="PRO_0000085763"
FT DOMAIN 58..574
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 64..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 23
FT /note="Q -> P (in dbSNP:rs13447459)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019255"
FT VARIANT 99
FT /note="I -> V (in dbSNP:rs13447492)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019256"
FT VARIANT 112
FT /note="G -> W (in dbSNP:rs13447493)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019257"
FT VARIANT 162
FT /note="F -> L (in dbSNP:rs13447503)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
FT /id="VAR_019258"
FT VARIANT 208
FT /note="I -> M (in dbSNP:rs34979509)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040403"
FT VARIANT 209
FT /note="E -> D (in dbSNP:rs56327502)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040404"
FT VARIANT 441
FT /note="K -> R (in dbSNP:rs13447539)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
FT /id="VAR_019259"
FT VARIANT 472
FT /note="T -> I (in dbSNP:rs56381770)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040405"
FT VARIANT 498
FT /note="S -> A (in dbSNP:rs35055915)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040406"
FT CONFLICT 89
FT /note="L -> V (in Ref. 3; AAB97512)"
FT /evidence="ECO:0000305"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6YA6"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6YA7"
FT HELIX 151..170
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6YA6"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6YA7"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6YA8"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 394..409
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 420..431
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:6YA6"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 534..537
FT /evidence="ECO:0007829|PDB:6YA7"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:6YA6"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:6YA6"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:6YA6"
SQ SEQUENCE 574 AA; 63888 MW; 90D549BEE20AE583 CRC64;
MEASLGIQMD EPMAFSPQRD RFQAEGSLKK NEQNFKLAGV KKDIEKLYEA VPQLSNVFKI
EDKIGEGTFS SVYLATAQLQ VGPEEKIALK HLIPTSHPIR IAAELQCLTV AGGQDNVMGV
KYCFRKNDHV VIAMPYLEHE SFLDILNSLS FQEVREYMLN LFKALKRIHQ FGIVHRDVKP
SNFLYNRRLK KYALVDFGLA QGTHDTKIEL LKFVQSEAQQ ERCSQNKSHI ITGNKIPLSG
PVPKELDQQS TTKASVKRPY TNAQIQIKQG KDGKEGSVGL SVQRSVFGER NFNIHSSISH
ESPAVKLMKQ SKTVDVLSRK LATKKKAIST KVMNSAVMRK TASSCPASLT CDCYATDKVC
SICLSRRQQV APRAGTPGFR APEVLTKCPN QTTAIDMWSA GVIFLSLLSG RYPFYKASDD
LTALAQIMTI RGSRETIQAA KTFGKSILCS KEVPAQDLRK LCERLRGMDS STPKLTSDIQ
GHASHQPAIS EKTDHKASCL VQTPPGQYSG NSFKKGDSNS CEHCFDEYNT NLEGWNEVPD
EAYDLLDKLL DLNPASRITA EEALLHPFFK DMSL
