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Cell division cycle 7-related protein kinase (CDC7-related kinase) (HsCdc7) (huCdc7) (EC 2.7.11.1)

 CDC7_HUMAN              Reviewed;         574 AA.
O00311; D3DT31; O00558; Q5T5U5;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
12-AUG-2020, entry version 200.
RecName: Full=Cell division cycle 7-related protein kinase;
Short=CDC7-related kinase;
Short=HsCdc7;
Short=huCdc7;
EC=2.7.11.1;
Name=CDC7; Synonyms=CDC7L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver, and Testis;
PubMed=9250678; DOI=10.1093/emboj/16.14.4340;
Sato N., Arai K., Masai H.;
"Human and Xenopus cDNAs encoding budding yeast Cdc7-related kinases: in
vitro phosphorylation of MCM subunits by a putative human homologue of
Cdc7.";
EMBO J. 16:4340-4351(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9573348; DOI=10.1016/s0378-1119(98)00094-8;
Hess G.F., Drong R.F., Weiland K.L., Slightom J.L., Sclafani R.A.,
Hollingsworth R.E.;
"A human homolog of the yeast CDC7 gene is overexpressed in some tumors and
transformed cell lines.";
Gene 211:133-140(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
PubMed=9405610; DOI=10.1073/pnas.94.26.14320;
Jiang W., Hunter T.;
"Identification and characterization of a human protein kinase related to
budding yeast Cdc7p.";
Proc. Natl. Acad. Sci. U.S.A. 94:14320-14325(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-23; VAL-99; TRP-112;
LEU-162 AND ARG-441.
NIEHS SNPs program;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH DBF4.
PubMed=10373557; DOI=10.1128/mcb.19.7.5083;
Kumagai H., Sato N., Yamada M., Mahony D., Seghezzi W., Lees E., Arai K.,
Masai H.;
"A novel growth- and cell cycle-regulated protein, ASK, activates human
Cdc7-related kinase and is essential for G1/S transition in mammalian
cells.";
Mol. Cell. Biol. 19:5083-5095(1999).
[9]
FUNCTION, AND INTERACTION WITH DBF4B.
PubMed=12065429; DOI=10.1093/emboj/cdf290;
Montagnoli A., Bosotti R., Villa F., Rialland M., Brotherton D.,
Mercurio C., Berthelsen J., Santocanale C.;
"Drf1, a novel regulatory subunit for human Cdc7 kinase.";
EMBO J. 21:3171-3181(2002).
[10]
INTERACTION WITH DBF4B.
PubMed=15668232; DOI=10.1074/jbc.m411653200;
Yoshizawa-Sugata N., Ishii A., Taniyama C., Matsui E., Arai K., Masai H.;
"A second human Dbf4/ASK-related protein, Drf1/ASKL1, is required for
efficient progression of S and M phases.";
J. Biol. Chem. 280:13062-13070(2005).
[11]
INTERACTION WITH DBF4 AND DBF4B.
PubMed=17062569; DOI=10.1074/jbc.m604457200;
Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C.,
Santocanale C.;
"Cdc7 is an active kinase in human cancer cells undergoing replication
stress.";
J. Biol. Chem. 282:208-215(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-503, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-268, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[16]
VARIANTS [LARGE SCALE ANALYSIS] LEU-162; MET-208; ASP-209; ARG-441; ILE-472
AND ALA-498.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Seems to phosphorylate critical substrates that regulate the
G1/S phase transition and/or DNA replication. Can phosphorylate MCM2
and MCM3. {ECO:0000269|PubMed:12065429}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Forms a complex with either DBF4/DBF4A or DBF4B, leading to
the activation of the kinase activity.
-!- INTERACTION:
O00311; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-374980, EBI-11524452;
O00311; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-374980, EBI-739580;
O00311; Q9UBU7: DBF4; NbExp=7; IntAct=EBI-374980, EBI-372690;
O00311; Q9UBU7-1: DBF4; NbExp=3; IntAct=EBI-374980, EBI-16017435;
O00311; P51114-2: FXR1; NbExp=3; IntAct=EBI-374980, EBI-11022345;
O00311; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-374980, EBI-948296;
O00311; Q08379: GOLGA2; NbExp=3; IntAct=EBI-374980, EBI-618309;
O00311; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-374980, EBI-11163335;
O00311; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-374980, EBI-2549423;
O00311; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-374980, EBI-11522367;
O00311; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-374980, EBI-747204;
O00311; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-374980, EBI-1640423;
O00311; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-374980, EBI-1216080;
O00311; Q9BTE3: MCMBP; NbExp=2; IntAct=EBI-374980, EBI-749378;
O00311; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-374980, EBI-16439278;
O00311; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-374980, EBI-11522433;
O00311; Q14140: SERTAD2; NbExp=3; IntAct=EBI-374980, EBI-2822051;
O00311; O75886: STAM2; NbExp=3; IntAct=EBI-374980, EBI-373258;
O00311; P55061: TMBIM6; NbExp=3; IntAct=EBI-374980, EBI-1045825;
O00311; P14373: TRIM27; NbExp=3; IntAct=EBI-374980, EBI-719493;
O00311; O94972: TRIM37; NbExp=3; IntAct=EBI-374980, EBI-741602;
O00311; Q2TAA8: TSNAXIP1; NbExp=3; IntAct=EBI-374980, EBI-6872498;
O00311; P0CW01: TSPY10; NbExp=3; IntAct=EBI-374980, EBI-19697726;
O00311; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-374980, EBI-12369705;
O00311; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-374980, EBI-12017160;
O00311; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-374980, EBI-3918996;
O00311; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-374980, EBI-17494306;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms may be produced.;
Name=1;
IsoId=O00311-1; Sequence=Displayed;
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc7/";
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EMBL; AB003698; BAA19962.1; -; mRNA.
EMBL; AF015592; AAC52080.1; -; mRNA.
EMBL; AF005209; AAB97512.1; -; mRNA.
EMBL; AY585721; AAS79323.1; -; Genomic_DNA.
EMBL; AL355871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW73114.1; -; Genomic_DNA.
EMBL; CH471097; EAW73115.1; -; Genomic_DNA.
EMBL; BC110526; AAI10527.1; -; mRNA.
EMBL; BC110527; AAI10528.1; -; mRNA.
EMBL; BC111044; AAI11045.1; -; mRNA.
CCDS; CCDS734.1; -. [O00311-1]
RefSeq; NP_001127891.1; NM_001134419.1. [O00311-1]
RefSeq; NP_001127892.1; NM_001134420.1. [O00311-1]
RefSeq; NP_003494.1; NM_003503.3. [O00311-1]
RefSeq; XP_005271298.1; XM_005271241.2. [O00311-1]
PDB; 4F99; X-ray; 2.33 A; A=37-574.
PDB; 4F9A; X-ray; 2.17 A; A/C=37-574.
PDB; 4F9B; X-ray; 2.50 A; A/C=37-574.
PDB; 4F9C; X-ray; 2.08 A; A=37-574.
PDB; 5UWQ; X-ray; 2.28 A; D=456-473.
PDB; 5UWR; X-ray; 2.24 A; D=456-478.
PDBsum; 4F99; -.
PDBsum; 4F9A; -.
PDBsum; 4F9B; -.
PDBsum; 4F9C; -.
PDBsum; 5UWQ; -.
PDBsum; 5UWR; -.
SMR; O00311; -.
BioGRID; 113914; 46.
CORUM; O00311; -.
DIP; DIP-31728N; -.
IntAct; O00311; 45.
MINT; O00311; -.
STRING; 9606.ENSP00000393139; -.
BindingDB; O00311; -.
ChEMBL; CHEMBL5443; -.
GuidetoPHARMACOLOGY; 1960; -.
iPTMnet; O00311; -.
PhosphoSitePlus; O00311; -.
BioMuta; CDC7; -.
EPD; O00311; -.
jPOST; O00311; -.
MassIVE; O00311; -.
MaxQB; O00311; -.
PaxDb; O00311; -.
PeptideAtlas; O00311; -.
PRIDE; O00311; -.
ProteomicsDB; 47836; -. [O00311-1]
Antibodypedia; 3628; 297 antibodies.
DNASU; 8317; -.
Ensembl; ENST00000234626; ENSP00000234626; ENSG00000097046. [O00311-1]
Ensembl; ENST00000428239; ENSP00000393139; ENSG00000097046. [O00311-1]
GeneID; 8317; -.
KEGG; hsa:8317; -.
UCSC; uc001doe.4; human. [O00311-1]
CTD; 8317; -.
DisGeNET; 8317; -.
EuPathDB; HostDB:ENSG00000097046.12; -.
GeneCards; CDC7; -.
HGNC; HGNC:1745; CDC7.
HPA; ENSG00000097046; Low tissue specificity.
MIM; 603311; gene.
neXtProt; NX_O00311; -.
OpenTargets; ENSG00000097046; -.
PharmGKB; PA26272; -.
eggNOG; KOG1167; Eukaryota.
GeneTree; ENSGT00550000075011; -.
HOGENOM; CLU_000288_118_1_1; -.
InParanoid; O00311; -.
KO; K02214; -.
OMA; GLLHGCV; -.
OrthoDB; 1318335at2759; -.
PhylomeDB; O00311; -.
TreeFam; TF101052; -.
BRENDA; 2.7.11.1; 2681.
PathwayCommons; O00311; -.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-68962; Activation of the pre-replicative complex.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; O00311; -.
SIGNOR; O00311; -.
BioGRID-ORCS; 8317; 776 hits in 908 CRISPR screens.
ChiTaRS; CDC7; human.
GeneWiki; Cell_division_cycle_7-related_protein_kinase; -.
GenomeRNAi; 8317; -.
Pharos; O00311; Tchem.
PRO; PR:O00311; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; O00311; protein.
Bgee; ENSG00000097046; Expressed in secondary oocyte and 180 other tissues.
ExpressionAtlas; O00311; baseline and differential.
Genevisible; O00311; HS.
GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0072686; C:mitotic spindle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:HGNC-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IMP:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0044770; P:cell cycle phase transition; IMP:BHF-UCL.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:HGNC-UCL.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division;
Isopeptide bond; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1..574
/note="Cell division cycle 7-related protein kinase"
/id="PRO_0000085763"
DOMAIN 58..574
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 64..72
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 177
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 90
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 27
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163"
MOD_RES 503
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
CROSSLNK 268
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
VARIANT 23
/note="Q -> P (in dbSNP:rs13447459)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_019255"
VARIANT 99
/note="I -> V (in dbSNP:rs13447492)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_019256"
VARIANT 112
/note="G -> W (in dbSNP:rs13447493)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_019257"
VARIANT 162
/note="F -> L (in dbSNP:rs13447503)"
/evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
/id="VAR_019258"
VARIANT 208
/note="I -> M (in dbSNP:rs34979509)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040403"
VARIANT 209
/note="E -> D (in dbSNP:rs56327502)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040404"
VARIANT 441
/note="K -> R (in dbSNP:rs13447539)"
/evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
/id="VAR_019259"
VARIANT 472
/note="T -> I (in dbSNP:rs56381770)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040405"
VARIANT 498
/note="S -> A (in dbSNP:rs35055915)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040406"
CONFLICT 89
/note="L -> V (in Ref. 3; AAB97512)"
/evidence="ECO:0000305"
HELIX 42..50
/evidence="ECO:0000244|PDB:4F9C"
HELIX 52..56
/evidence="ECO:0000244|PDB:4F9C"
STRAND 59..66
/evidence="ECO:0000244|PDB:4F9C"
STRAND 68..79
/evidence="ECO:0000244|PDB:4F9C"
STRAND 84..92
/evidence="ECO:0000244|PDB:4F9C"
HELIX 98..110
/evidence="ECO:0000244|PDB:4F9C"
STRAND 121..126
/evidence="ECO:0000244|PDB:4F9C"
STRAND 129..135
/evidence="ECO:0000244|PDB:4F9C"
HELIX 142..146
/evidence="ECO:0000244|PDB:4F9C"
HELIX 151..170
/evidence="ECO:0000244|PDB:4F9C"
HELIX 180..182
/evidence="ECO:0000244|PDB:4F9C"
STRAND 183..186
/evidence="ECO:0000244|PDB:4F9C"
TURN 187..190
/evidence="ECO:0000244|PDB:4F9C"
STRAND 191..194
/evidence="ECO:0000244|PDB:4F9C"
HELIX 209..213
/evidence="ECO:0000244|PDB:4F9C"
TURN 217..219
/evidence="ECO:0000244|PDB:4F9A"
HELIX 377..379
/evidence="ECO:0000244|PDB:4F9C"
HELIX 382..385
/evidence="ECO:0000244|PDB:4F9C"
HELIX 394..409
/evidence="ECO:0000244|PDB:4F9C"
STRAND 412..415
/evidence="ECO:0000244|PDB:4F9C"
HELIX 420..431
/evidence="ECO:0000244|PDB:4F9C"
HELIX 433..442
/evidence="ECO:0000244|PDB:4F9C"
STRAND 445..451
/evidence="ECO:0000244|PDB:4F9C"
HELIX 458..465
/evidence="ECO:0000244|PDB:4F9C"
HELIX 540..549
/evidence="ECO:0000244|PDB:4F9C"
TURN 554..556
/evidence="ECO:0000244|PDB:4F9C"
HELIX 560..564
/evidence="ECO:0000244|PDB:4F9C"
HELIX 567..569
/evidence="ECO:0000244|PDB:4F9C"
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


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Related Genes :
[CDC7 CDC7L1] Cell division cycle 7-related protein kinase (CDC7-related kinase) (HsCdc7) (huCdc7) (EC 2.7.11.1)
[Cdc7 Cdc7l1] Cell division cycle 7-related protein kinase (CDC7-related kinase) (muCdc7) (EC 2.7.11.1)
[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[CDK11A CDC2L2 CDC2L3 PITSLREB] Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)
[Aurka Aik Airk Ark1 Aura Ayk1 Btak Iak1 Stk15 Stk6] Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora family kinase 1) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)
[AURKA AIK AIRK1 ARK1 AURA AYK1 BTAK IAK1 STK15 STK6] Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (hARK1) (Breast tumor-amplified kinase) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase aurora-A)
[air-2 stu-7 B0207.4] Aurora/IPL1-related protein kinase 2 (EC 2.7.11.1) (Serine/threonine-protein kinase aurora-B)
[NEK9 KIAA1995 NEK8 NERCC] Serine/threonine-protein kinase Nek9 (EC 2.7.11.1) (Nercc1 kinase) (Never in mitosis A-related kinase 9) (NimA-related protein kinase 9) (NimA-related kinase 8) (Nek8)
[AURKB AIK2 AIM1 AIRK2 ARK2 STK1 STK12 STK5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[NEK2 NEK2A NLK1] Serine/threonine-protein kinase Nek2 (EC 2.7.11.1) (HSPK 21) (Never in mitosis A-related kinase 2) (NimA-related protein kinase 2) (NimA-like protein kinase 1)
[AURKC AIE2 AIK3 AIRK3 ARK3 STK13] Aurora kinase C (EC 2.7.11.1) (Aurora 3) (Aurora/IPL1-related kinase 3) (ARK-3) (Aurora-related kinase 3) (Aurora/IPL1/Eg2 protein 2) (Serine/threonine-protein kinase 13) (Serine/threonine-protein kinase aurora-C)
[CDC28 CDK1 CAALFM_CR06050WA CaO19.11337 CaO19.3856] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 2)
[Cdk7 Cak Cdkn7 Crk4 Mo15 Mpk-7] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (P39 Mo15) (CDK-activating kinase) (CR4 protein kinase) (CRK4) (Cell division protein kinase 7) (Protein-tyrosine kinase MPK-7) (TFIIH basal transcription factor complex kinase subunit)
[Aurkc Aie1 Aik3 Airk3 Ark3 Stk13] Aurora kinase C (EC 2.7.11.1) (Aurora 3) (Aurora/IPL1-related kinase 3) (ARK-3) (Aurora-related kinase 3) (Aurora/IPL1/Eg2 protein 1) (Serine/threonine-protein kinase 13) (Serine/threonine-protein kinase aurora-C)
[CDKA-1 CDC2 CDC2A At3g48750 T21J18.20] Cyclin-dependent kinase A-1 (CDKA;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog A) (CDC2aAt)
[NEK6] Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6) (Protein kinase SID6-1512)
[NEK1 KIAA1901] Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) (Renal carcinoma antigen NY-REN-55)
[ASK7 BIN2 DWF12 SK21 UCU1 At4g18710 F28A21.120] Shaggy-related protein kinase eta (EC 2.7.11.1) (ASK-eta) (Protein BRASSINOSTEROID INSENSITIVE 2) (Protein ULTRACURVATA 1) (Shaggy-related protein kinase 21) (AtSK21)
[Aurkb Aik2 Aim1 Airk2 Ark2 Stk1 Stk12 Stk5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[CDKD-1 R2 Os05g0392300 LOC_Os05g32600 OJ1764_D01.12] Cyclin-dependent kinase D-1 (CDKD;1) (EC 2.7.11.22) (EC 2.7.11.23) (CDC2+/CDC28-related protein kinase R2) (CDK-activating kinase R2) (CAK-R2)
[Nek6] Serine/threonine-protein kinase Nek6 (EC 2.7.11.1) (Never in mitosis A-related kinase 6) (NimA-related protein kinase 6)

Bibliography :