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UniProtKB/Swiss-Prot entry O00311


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDC7_HUMAN
Primary accession number O00311
Secondary accession numbers O00558 Q5T5U5
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 86)
Name and origin of the protein
Protein name Cell division cycle 7-related protein kinase
Synonyms CDC7-related kinase
HsCdc7
huCdc7
EC 2.7.11.1
Gene name
Name: CDC7
Synonyms: CDC7L1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver, and Testis;
DOI=10.1093/emboj/16.14.4340; PubMed=9250678 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1016/S0378-1119(98)00094-8; PubMed=9573348 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1073/pnas.94.26.14320; PubMed=9405610 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
INTERACTION WITH DBF4.
PubMed=10373557 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH DBF4B.
DOI=10.1093/emboj/cdf290; PubMed=12065429 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH DBF4B.
DOI=10.1074/jbc.M411653200; PubMed=15668232 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
INTERACTION WITH DBF4 AND DBF4B.
DOI=10.1074/jbc.M604457200; PubMed=17062569 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-27, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
VARIANTS [LARGE SCALE ANALYSIS] LEU-162; MET-208; ASP-209; ARG-441; ILE-472 AND ALA-498.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB003698; BAA19962.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF015592; AAC52080.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005209; AAB97512.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY585721; AAS79323.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355871; CAI14446.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110526; AAI10527.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110527; AAI10528.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111044; AAI11045.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001127891.1; -.
NP_001127892.1; -.
NP_003494.1; -.
UniGene Hs.533573
3D structure databases
ModBase O00311.
Protein-protein interaction databases
IntAct O00311; 7.
PTM databases
PhosphoSite O00311; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
Organism-specific databases
GeneCards GC01P091678; -.
H-InvDB HIX0028491; -.
HGNC HGNC:1745; CDC7.
GenAtlas CDC7.
HPA CAB002669; -.
MIM 603311; gene. [NCBI / EBI]
PharmGKB PA134879457; -.
GeneCards O00311.
Gene expression databases
ArrayExpress O00311; -.
CleanEx HS_CDC7; -.
GermOnline ENSG00000097046; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HGNC).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0006260; Biological process: DNA replication (inferred from experiment from Reactome).
GO:0000082; Biological process: G1/S transition of mitotic cell cycle (traceable author statement from ProtInc).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from mutant phenotype from HGNC).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0033261; Biological process: regulation of S phase (inferred from mutant phenotype from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 3.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O00311; -.
Genome annotation databases
Ensembl ENSG00000097046; Homo sapiens. [Contig view]
GeneID 8317; -.
KEGG hsa:8317; -.
Phylogenomic databases
HOGENOM O00311; -.
HOVERGEN O00311; -.
Other
NextBio 31147; -.
SOURCE CDC7; Homo sapiens.
ProtoNet O00311.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Cell cycle; Cell division; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   574  574     Cell division cycle 7-related protein kinase. PRO_0000085763
DOMAIN   58   574  517     Protein kinase. 
NP_BIND   64    72  9     ATP (By similarity). 
ACT_SITE   177   177        Proton acceptor (By similarity). 
BINDING   90    90        ATP (By similarity). 
MOD_RES   16    16        Phosphoserine. 
MOD_RES   27    27        Phosphoserine. 
VARIANT   23    23  1     Q -> P (in dbSNP:rs13447459 [NCBI]). VAR_019255 
VARIANT   99    99  1     I -> V (in dbSNP:rs13447492 [NCBI]). VAR_019256 
VARIANT   112   112  1     G -> W (in dbSNP:rs13447493 [NCBI]). VAR_019257 
VARIANT   162   162  1     F -> L (in dbSNP:rs13447503 [NCBI]). VAR_019258 
VARIANT   208   208  1     I -> M. VAR_040403 
VARIANT   209   209  1     E -> D. VAR_040404 
VARIANT   441   441  1     K -> R (in dbSNP:rs13447539 [NCBI]). VAR_019259 
VARIANT   472   472  1     T -> I. VAR_040405 
VARIANT   498   498  1     S -> A. VAR_040406 
CONFLICT   89    89        L -> V (in Ref. 3; AAB97512). 
Sequence information
Length: 574 AA [This is the length of the unprocessed precursor] Molecular weight: 63888 Da [This is the MW of the unprocessed precursor] CRC64: 90D549BEE20AE583 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEASLGIQMD EPMAFSPQRD RFQAEGSLKK NEQNFKLAGV KKDIEKLYEA VPQLSNVFKI 

        70         80         90        100        110        120 
EDKIGEGTFS SVYLATAQLQ VGPEEKIALK HLIPTSHPIR IAAELQCLTV AGGQDNVMGV 

       130        140        150        160        170        180 
KYCFRKNDHV VIAMPYLEHE SFLDILNSLS FQEVREYMLN LFKALKRIHQ FGIVHRDVKP 

       190        200        210        220        230        240 
SNFLYNRRLK KYALVDFGLA QGTHDTKIEL LKFVQSEAQQ ERCSQNKSHI ITGNKIPLSG 

       250        260        270        280        290        300 
PVPKELDQQS TTKASVKRPY TNAQIQIKQG KDGKEGSVGL SVQRSVFGER NFNIHSSISH 

       310        320        330        340        350        360 
ESPAVKLMKQ SKTVDVLSRK LATKKKAIST KVMNSAVMRK TASSCPASLT CDCYATDKVC 

       370        380        390        400        410        420 
SICLSRRQQV APRAGTPGFR APEVLTKCPN QTTAIDMWSA GVIFLSLLSG RYPFYKASDD 

       430        440        450        460        470        480 
LTALAQIMTI RGSRETIQAA KTFGKSILCS KEVPAQDLRK LCERLRGMDS STPKLTSDIQ 

       490        500        510        520        530        540 
GHASHQPAIS EKTDHKASCL VQTPPGQYSG NSFKKGDSNS CEHCFDEYNT NLEGWNEVPD 

       550        560        570 
EAYDLLDKLL DLNPASRITA EEALLHPFFK DMSL 

O00311 in FASTA format

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