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O00311 (CDC7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division cycle 7-related protein kinase

Short name=CDC7-related kinase
Short name=HsCdc7
Short name=huCdc7
EC=2.7.11.1
Gene names
Name:CDC7
Synonyms:CDC7L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. Can phosphorylates MCM2 and MCM3. Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Subunit structure

Forms a complex with either DBF4/DBF4A or DBF4B, leading to the activation of the kinase activity.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell cycle phase transition

Inferred from mutant phenotype PubMed 17102137. Source: BHF-UCL

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 17102137. Source: HGNC

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: HGNC

intercellular bridge

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.1. Source: HGNC

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinase activity

Inferred from direct assay Ref.1. Source: HGNC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22540012PubMed 24299456. Source: IntAct

protein kinase activity

Inferred from mutant phenotype Ref.9Ref.10. Source: UniProt

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MCMBPQ9BTE32EBI-374980,EBI-749378

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms may be produced.
Isoform 1 (identifier: O00311-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Cell division cycle 7-related protein kinase
PRO_0000085763

Regions

Domain58 – 574517Protein kinase
Nucleotide binding64 – 729ATP By similarity

Sites

Active site1771Proton acceptor By similarity
Binding site901ATP By similarity

Amino acid modifications

Modified residue271Phosphoserine Ref.13

Natural variations

Natural variant231Q → P. Ref.4
Corresponds to variant rs13447459 [ dbSNP | Ensembl ].
VAR_019255
Natural variant991I → V. Ref.4
Corresponds to variant rs13447492 [ dbSNP | Ensembl ].
VAR_019256
Natural variant1121G → W. Ref.4
Corresponds to variant rs13447493 [ dbSNP | Ensembl ].
VAR_019257
Natural variant1621F → L. Ref.4 Ref.14
Corresponds to variant rs13447503 [ dbSNP | Ensembl ].
VAR_019258
Natural variant2081I → M. Ref.14
Corresponds to variant rs34979509 [ dbSNP | Ensembl ].
VAR_040403
Natural variant2091E → D. Ref.14
Corresponds to variant rs56327502 [ dbSNP | Ensembl ].
VAR_040404
Natural variant4411K → R. Ref.4 Ref.14
Corresponds to variant rs13447539 [ dbSNP | Ensembl ].
VAR_019259
Natural variant4721T → I. Ref.14
Corresponds to variant rs56381770 [ dbSNP | Ensembl ].
VAR_040405
Natural variant4981S → A. Ref.14
Corresponds to variant rs35055915 [ dbSNP | Ensembl ].
VAR_040406

Experimental info

Sequence conflict891L → V in AAB97512. Ref.3

Secondary structure

...................................................... 574
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 90D549BEE20AE583

FASTA57463,888
        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 

« Hide

References

« Hide 'large scale' references
[1]"Human and Xenopus cDNAs encoding budding yeast Cdc7-related kinases: in vitro phosphorylation of MCM subunits by a putative human homologue of Cdc7."
Sato N., Arai K., Masai H.
EMBO J. 16:4340-4351(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver and Testis.
[2]"A human homolog of the yeast CDC7 gene is overexpressed in some tumors and transformed cell lines."
Hess G.F., Drong R.F., Weiland K.L., Slightom J.L., Sclafani R.A., Hollingsworth R.E.
Gene 211:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Identification and characterization of a human protein kinase related to budding yeast Cdc7p."
Jiang W., Hunter T.
Proc. Natl. Acad. Sci. U.S.A. 94:14320-14325(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[4]NIEHS SNPs program
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-23; VAL-99; TRP-112; LEU-162 AND ARG-441.
[5]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"A novel growth- and cell cycle-regulated protein, ASK, activates human Cdc7-related kinase and is essential for G1/S transition in mammalian cells."
Kumagai H., Sato N., Yamada M., Mahony D., Seghezzi W., Lees E., Arai K., Masai H.
Mol. Cell. Biol. 19:5083-5095(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DBF4.
[9]"Drf1, a novel regulatory subunit for human Cdc7 kinase."
Montagnoli A., Bosotti R., Villa F., Rialland M., Brotherton D., Mercurio C., Berthelsen J., Santocanale C.
EMBO J. 21:3171-3181(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DBF4B.
[10]"A second human Dbf4/ASK-related protein, Drf1/ASKL1, is required for efficient progression of S and M phases."
Yoshizawa-Sugata N., Ishii A., Taniyama C., Matsui E., Arai K., Masai H.
J. Biol. Chem. 280:13062-13070(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DBF4B.
[11]"Cdc7 is an active kinase in human cancer cells undergoing replication stress."
Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C., Santocanale C.
J. Biol. Chem. 282:208-215(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DBF4 AND DBF4B.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-162; MET-208; ASP-209; ARG-441; ILE-472 AND ALA-498.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB003698 mRNA. Translation: BAA19962.1.
AF015592 mRNA. Translation: AAC52080.1.
AF005209 mRNA. Translation: AAB97512.1.
AY585721 Genomic DNA. Translation: AAS79323.1.
AL355871 Genomic DNA. Translation: CAI14446.1.
CH471097 Genomic DNA. Translation: EAW73114.1.
CH471097 Genomic DNA. Translation: EAW73115.1.
BC110526 mRNA. Translation: AAI10527.1.
BC110527 mRNA. Translation: AAI10528.1.
BC111044 mRNA. Translation: AAI11045.1.
CCDSCCDS734.1. [O00311-1]
RefSeqNP_001127891.1. NM_001134419.1. [O00311-1]
NP_001127892.1. NM_001134420.1. [O00311-1]
NP_003494.1. NM_003503.3. [O00311-1]
XP_005271298.1. XM_005271241.1. [O00311-1]
UniGeneHs.533573.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F99X-ray2.33A37-574[»]
4F9AX-ray2.17A/C37-574[»]
4F9BX-ray2.50A/C37-574[»]
4F9CX-ray2.08A37-574[»]
ProteinModelPortalO00311.
SMRO00311. Positions 37-572.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113914. 35 interactions.
DIPDIP-31728N.
IntActO00311. 14 interactions.
MINTMINT-1201209.
STRING9606.ENSP00000234626.

Chemistry

BindingDBO00311.
ChEMBLCHEMBL2111377.

PTM databases

PhosphoSiteO00311.

Proteomic databases

MaxQBO00311.
PaxDbO00311.
PRIDEO00311.

Protocols and materials databases

DNASU8317.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234626; ENSP00000234626; ENSG00000097046. [O00311-1]
ENST00000428239; ENSP00000393139; ENSG00000097046. [O00311-1]
GeneID8317.
KEGGhsa:8317.
UCSCuc001doe.3. human. [O00311-1]

Organism-specific databases

CTD8317.
GeneCardsGC01P091966.
HGNCHGNC:1745. CDC7.
HPACAB002669.
HPA035831.
MIM603311. gene.
neXtProtNX_O00311.
PharmGKBPA26272.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250270.
HOGENOMHOG000193450.
HOVERGENHBG003991.
InParanoidO00311.
KOK02214.
OMAATDKVCS.
OrthoDBEOG7VMP6J.
PhylomeDBO00311.
TreeFamTF101052.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
SignaLinkO00311.

Gene expression databases

ArrayExpressO00311.
BgeeO00311.
CleanExHS_CDC7.
GenevestigatorO00311.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMSSF56112. SSF56112. 3 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCell_division_cycle_7-related_protein_kinase.
GenomeRNAi8317.
NextBio31147.
PROO00311.
SOURCESearch...

Entry information

Entry nameCDC7_HUMAN
AccessionPrimary (citable) accession number: O00311
Secondary accession number(s): D3DT31, O00558, Q5T5U5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM