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UniProtKB/Swiss-Prot entry Q99741


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

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Entry information
Entry name CDC6_HUMAN
Primary accession number Q99741
Secondary accession number Q8TB30
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 72)
Name and origin of the protein
Protein name Cell division control protein 6 homolog
Synonyms CDC6-related protein
p62(cdc6)
HsCDC6
HsCDC18
Gene name
Name: CDC6
Synonyms: CDC18L
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].
DOI=10.1073/pnas.94.1.142; PubMed=8990175 [NCBI, ExPASy, EBI, Israel, Japan]
Williams R.S., Shohet R.V., Stillman B.;
"A human protein related to yeast Cdc6p.";
Proc. Natl. Acad. Sci. U.S.A. 94:142-147(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH PCNA; ORC1L AND CYCLIN-CDK.
PubMed=9566895 [NCBI, ExPASy, EBI, Israel, Japan]
Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., Parvin J.D., Dutta A.;
"Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase.";
Mol. Cell. Biol. 18:2758-2767(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-238; ASN-295; MET-299; HIS-378 AND ILE-441.
NIEHS SNPs program;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-441.
TISSUE=Brain;
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[6]
INTERACTION WITH HUWE1.
DOI=10.1091/mbc.E07-02-0173; PubMed=17567951 [NCBI, ExPASy, EBI, Israel, Japan]
Hall J.R., Kow E., Nevis K.R., Lu C.K., Luce K.S., Zhong Q., Cook J.G.;
"Cdc6 stability is regulated by the Huwe1 ubiquitin ligase after DNA damage.";
Mol. Biol. Cell 18:3340-3350(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-54, 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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
U77949; AAB38317.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF022109; AAC52071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY150310; AAN10296.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025232; AAH25232.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00014575; -.
RefSeq NP_001245.1; -.
UniGene Hs.405958
3D structure databases
PDB
2CCH; X-ray; 1.70 A; E/F=89-100.[ExPASy / RCSB / EBI]
2CCI; X-ray; 2.70 A; F/I=74-100.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2CCH; -.
2CCI; -.
ModBase Q99741.
Protein-protein interaction databases
DIP DIP:28154N; -.
IntAct Q99741; 12.
PTM databases
PhosphoSite Q99741; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
Organism-specific databases
GeneCards GC17P035697; -.
H-InvDB HIX0013795; -.
HGNC HGNC:1744; CDC6.
GenAtlas CDC6.
MIM 602627; gene. [NCBI / EBI]
PharmGKB PA134904022; -.
Gene expression databases
ArrayExpress Q99741; -.
Bgee Q99741; -.
CleanEx HS_CDC6; -.
GermOnline ENSG00000094804; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0017111; Molecular function: nucleoside-triphosphatase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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:0000076; Biological process: DNA replication checkpoint (traceable author statement from ProtInc).
GO:0007067; Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0008285; Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0000079; Biological process: regulation of cyclin-dependent protein kinase activity (traceable author statement from ProtInc).
GO:0007089; Biological process: traversing start control point of mitotic cell cycle (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003593; ATPase_AAA+_core.
IPR003959; ATPase_AAA_core.
IPR016314; Cdc6.
IPR015163; Cdc6_C.
Graphical view of domain structure.
Pfam PF00004; AAA; 1.
PF09079; Cdc6_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001767; Cdc6; 1.
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
Proteomic databases
PRIDE Q99741; -.
Genome annotation databases
Ensembl ENSG00000094804; Homo sapiens. [Contig view]
GeneID 990; -.
KEGG hsa:990; -.
Phylogenomic databases
HOGENOM Q99741; -.
HOVERGEN Q99741; -.
OMA Q99741; LYEAYSN.
Other
NextBio 4156; -.
PMAP-CutDB Q99741; -.
SOURCE CDC6; Homo sapiens.
ProtoNet Q99741.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell cycle; Cell division; Cytoplasm; DNA replication; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   560  560     Cell division control protein 6 homolog. PRO_0000150979
NP_BIND   202   209  8     ATP (Potential). 
MOD_RES   45    45        Phosphoserine. 
MOD_RES   54    54        Phosphoserine. 
MOD_RES   166   166        Phosphothreonine. 
VARIANT   238   238  1     T -> A (in dbSNP:rs4135010 [NCBI]). VAR_019349 
VARIANT   295   295  1     D -> N (in dbSNP:rs4135012 [NCBI]). VAR_019350 
VARIANT   299   299  1     T -> M (in dbSNP:rs4135013 [NCBI]). VAR_019351 
VARIANT   378   378  1     R -> H (in dbSNP:rs4135016 [NCBI]). VAR_019352 
VARIANT   441   441  1     V -> I (in dbSNP:rs13706 [NCBI]). VAR_019353 
Sequence information
Length: 560 AA [This is the length of the unprocessed precursor] Molecular weight: 62720 Da [This is the MW of the unprocessed precursor] CRC64: 3ED7DE4AF80CB017 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPQTRSQAQA TISFPKRKLS RALNKAKNSS DAKLEPTNVQ TVTCSPRVKA LPLSPRKRLG 

        70         80         90        100        110        120 
DDNLCNTPHL PPCSPPKQGK KENGPPHSHT LKGRRLVFDN QLTIKSPSKR ELAKVHQNKI 

       130        140        150        160        170        180 
LSSVRKSQEI TTNSEQRCPL KKESACVRLF KQEGTCYQQA KLVLNTAVPD RLPAREREMD 

       190        200        210        220        230        240 
VIRNFLREHI CGKKAGSLYL SGAPGTGKTA CLSRILQDLK KELKGFKTIM LNCMSLRTAQ 

       250        260        270        280        290        300 
AVFPAIAQEI CQEEVSRPAG KDMMRKLEKH MTAEKGPMIV LVLDEMDQLD SKGQDVLYTL 

       310        320        330        340        350        360 
FEWPWLSNSH LVLIGIANTL DLTDRILPRL QAREKCKPQL LNFPPYTRNQ IVTILQDRLN 

       370        380        390        400        410        420 
QVSRDQVLDN AAVQFCARKV SAVSGDVRKA LDVCRRAIEI VESDVKSQTI LKPLSECKSP 

       430        440        450        460        470        480 
SEPLIPKRVG LIHISQVISE VDGNRMTLSQ EGAQDSFPLQ QKILVCSLML LIRQLKIKEV 

       490        500        510        520        530        540 
TLGKLYEAYS KVCRKQQVAA VDQSECLSLS GLLEARGILG LKRNKETRLT KVFFKIEEKE 

       550        560 
IEHALKDKAL IGNILATGLP 

Q99741 in FASTA format

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