Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O00311

- CDC7_HUMAN

UniProt

O00311 - CDC7_HUMAN

Protein

Cell division cycle 7-related protein kinase

Gene

CDC7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. Can phosphorylates MCM2 and MCM3.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901ATPPROSITE-ProRule annotation
    Active sitei177 – 1771Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi64 – 729ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinase activity Source: HGNC
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein kinase activity Source: UniProt
    6. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell cycle phase transition Source: BHF-UCL
    2. cell division Source: UniProtKB-KW
    3. DNA replication Source: Reactome
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. positive regulation of cell proliferation Source: HGNC
    7. positive regulation of G2/M transition of mitotic cell cycle Source: UniProt
    8. positive regulation of nuclear cell cycle DNA replication Source: UniProt

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_6769. Activation of ATR in response to replication stress.
    SignaLinkiO00311.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division cycle 7-related protein kinase (EC:2.7.11.1)
    Short name:
    CDC7-related kinase
    Short name:
    HsCdc7
    Short name:
    huCdc7
    Gene namesi
    Name:CDC7
    Synonyms:CDC7L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1745. CDC7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. intercellular bridge Source: HPA
    3. microtubule cytoskeleton Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HGNC

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 574574Cell division cycle 7-related protein kinasePRO_0000085763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00311.
    PaxDbiO00311.
    PRIDEiO00311.

    PTM databases

    PhosphoSiteiO00311.

    Expressioni

    Gene expression databases

    ArrayExpressiO00311.
    BgeeiO00311.
    CleanExiHS_CDC7.
    GenevestigatoriO00311.

    Organism-specific databases

    HPAiCAB002669.
    HPA035831.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MCMBPQ9BTE32EBI-374980,EBI-749378

    Protein-protein interaction databases

    BioGridi113914. 35 interactions.
    DIPiDIP-31728N.
    IntActiO00311. 14 interactions.
    MINTiMINT-1201209.
    STRINGi9606.ENSP00000234626.

    Structurei

    Secondary structure

    1
    574
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 509
    Helixi52 – 565
    Beta strandi59 – 668
    Beta strandi68 – 7912
    Beta strandi84 – 929
    Helixi98 – 11013
    Beta strandi121 – 1266
    Beta strandi129 – 1357
    Helixi142 – 1465
    Helixi151 – 17020
    Helixi180 – 1823
    Beta strandi183 – 1864
    Turni187 – 1904
    Beta strandi191 – 1944
    Helixi209 – 2135
    Turni217 – 2193
    Helixi377 – 3793
    Helixi382 – 3854
    Helixi394 – 40916
    Beta strandi412 – 4154
    Helixi420 – 43112
    Helixi433 – 44210
    Beta strandi445 – 4517
    Helixi458 – 4658
    Helixi540 – 54910
    Turni554 – 5563
    Helixi560 – 5645
    Helixi567 – 5693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F99X-ray2.33A37-574[»]
    4F9AX-ray2.17A/C37-574[»]
    4F9BX-ray2.50A/C37-574[»]
    4F9CX-ray2.08A37-574[»]
    ProteinModelPortaliO00311.
    SMRiO00311. Positions 37-572.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 574517Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG250270.
    HOGENOMiHOG000193450.
    HOVERGENiHBG003991.
    InParanoidiO00311.
    KOiK02214.
    OMAiATDKVCS.
    OrthoDBiEOG7VMP6J.
    PhylomeDBiO00311.
    TreeFamiTF101052.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 3 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms may be produced.

    Isoform 1 (identifier: O00311-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEASLGIQMD EPMAFSPQRD RFQAEGSLKK NEQNFKLAGV KKDIEKLYEA    50
    VPQLSNVFKI EDKIGEGTFS SVYLATAQLQ VGPEEKIALK HLIPTSHPIR 100
    IAAELQCLTV AGGQDNVMGV KYCFRKNDHV VIAMPYLEHE SFLDILNSLS 150
    FQEVREYMLN LFKALKRIHQ FGIVHRDVKP SNFLYNRRLK KYALVDFGLA 200
    QGTHDTKIEL LKFVQSEAQQ ERCSQNKSHI ITGNKIPLSG PVPKELDQQS 250
    TTKASVKRPY TNAQIQIKQG KDGKEGSVGL SVQRSVFGER NFNIHSSISH 300
    ESPAVKLMKQ SKTVDVLSRK LATKKKAIST KVMNSAVMRK TASSCPASLT 350
    CDCYATDKVC SICLSRRQQV APRAGTPGFR APEVLTKCPN QTTAIDMWSA 400
    GVIFLSLLSG RYPFYKASDD LTALAQIMTI RGSRETIQAA KTFGKSILCS 450
    KEVPAQDLRK LCERLRGMDS STPKLTSDIQ GHASHQPAIS EKTDHKASCL 500
    VQTPPGQYSG NSFKKGDSNS CEHCFDEYNT NLEGWNEVPD EAYDLLDKLL 550
    DLNPASRITA EEALLHPFFK DMSL 574
    Length:574
    Mass (Da):63,888
    Last modified:July 1, 1997 - v1
    Checksum:i90D549BEE20AE583
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891L → V in AAB97512. (PubMed:9405610)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231Q → P.1 Publication
    Corresponds to variant rs13447459 [ dbSNP | Ensembl ].
    VAR_019255
    Natural varianti99 – 991I → V.1 Publication
    Corresponds to variant rs13447492 [ dbSNP | Ensembl ].
    VAR_019256
    Natural varianti112 – 1121G → W.1 Publication
    Corresponds to variant rs13447493 [ dbSNP | Ensembl ].
    VAR_019257
    Natural varianti162 – 1621F → L.2 Publications
    Corresponds to variant rs13447503 [ dbSNP | Ensembl ].
    VAR_019258
    Natural varianti208 – 2081I → M.1 Publication
    Corresponds to variant rs34979509 [ dbSNP | Ensembl ].
    VAR_040403
    Natural varianti209 – 2091E → D.1 Publication
    Corresponds to variant rs56327502 [ dbSNP | Ensembl ].
    VAR_040404
    Natural varianti441 – 4411K → R.2 Publications
    Corresponds to variant rs13447539 [ dbSNP | Ensembl ].
    VAR_019259
    Natural varianti472 – 4721T → I.1 Publication
    Corresponds to variant rs56381770 [ dbSNP | Ensembl ].
    VAR_040405
    Natural varianti498 – 4981S → A.1 Publication
    Corresponds to variant rs35055915 [ dbSNP | Ensembl ].
    VAR_040406

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS734.1. [O00311-1]
    RefSeqiNP_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]
    UniGeneiHs.533573.

    Genome annotation databases

    EnsembliENST00000234626; ENSP00000234626; ENSG00000097046. [O00311-1]
    ENST00000428239; ENSP00000393139; ENSG00000097046. [O00311-1]
    GeneIDi8317.
    KEGGihsa:8317.
    UCSCiuc001doe.3. human. [O00311-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS734.1. [O00311-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.533573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F99 X-ray 2.33 A 37-574 [» ]
    4F9A X-ray 2.17 A/C 37-574 [» ]
    4F9B X-ray 2.50 A/C 37-574 [» ]
    4F9C X-ray 2.08 A 37-574 [» ]
    ProteinModelPortali O00311.
    SMRi O00311. Positions 37-572.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113914. 35 interactions.
    DIPi DIP-31728N.
    IntActi O00311. 14 interactions.
    MINTi MINT-1201209.
    STRINGi 9606.ENSP00000234626.

    Chemistry

    BindingDBi O00311.
    ChEMBLi CHEMBL2111377.

    PTM databases

    PhosphoSitei O00311.

    Proteomic databases

    MaxQBi O00311.
    PaxDbi O00311.
    PRIDEi O00311.

    Protocols and materials databases

    DNASUi 8317.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234626 ; ENSP00000234626 ; ENSG00000097046 . [O00311-1 ]
    ENST00000428239 ; ENSP00000393139 ; ENSG00000097046 . [O00311-1 ]
    GeneIDi 8317.
    KEGGi hsa:8317.
    UCSCi uc001doe.3. human. [O00311-1 ]

    Organism-specific databases

    CTDi 8317.
    GeneCardsi GC01P091966.
    HGNCi HGNC:1745. CDC7.
    HPAi CAB002669.
    HPA035831.
    MIMi 603311. gene.
    neXtProti NX_O00311.
    PharmGKBi PA26272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250270.
    HOGENOMi HOG000193450.
    HOVERGENi HBG003991.
    InParanoidi O00311.
    KOi K02214.
    OMAi ATDKVCS.
    OrthoDBi EOG7VMP6J.
    PhylomeDBi O00311.
    TreeFami TF101052.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_6769. Activation of ATR in response to replication stress.
    SignaLinki O00311.

    Miscellaneous databases

    GeneWikii Cell_division_cycle_7-related_protein_kinase.
    GenomeRNAii 8317.
    NextBioi 31147.
    PROi O00311.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00311.
    Bgeei O00311.
    CleanExi HS_CDC7.
    Genevestigatori O00311.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 3 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiCDC7_HUMAN
    AccessioniPrimary (citable) accession number: O00311
    Secondary accession number(s): D3DT31, O00558, Q5T5U5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3