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O75909

- CCNK_HUMAN

UniProt

O75909 - CCNK_HUMAN

Protein

Cyclin-K

Gene

CCNK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).3 Publications

    GO - Molecular functioni

    1. cyclin-dependent protein serine/threonine kinase activity Source: MGI
    2. protein binding Source: IntAct
    3. protein kinase binding Source: MGI
    4. RNA polymerase II carboxy-terminal domain kinase activity Source: MGI

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. in utero embryonic development Source: Ensembl
    3. mitotic nuclear division Source: UniProtKB-KW
    4. negative regulation of cell cycle arrest Source: MGI
    5. protein phosphorylation Source: GOC
    6. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiO75909.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-K
    Gene namesi
    Name:CCNK
    Synonyms:CPR4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:1596. CCNK.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cyclin K-CDK12 complex Source: MGI
    2. cyclin K-CDK13 complex Source: MGI
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26161.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 580580Cyclin-KPRO_0000080478Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei324 – 3241Phosphoserine4 Publications
    Modified residuei329 – 3291Phosphoserine1 Publication
    Modified residuei340 – 3401Phosphoserine5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75909.
    PaxDbiO75909.
    PRIDEiO75909.

    PTM databases

    PhosphoSiteiO75909.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highest levels in testis.1 Publication

    Gene expression databases

    ArrayExpressiO75909.
    BgeeiO75909.
    CleanExiHS_CCNK.
    GenevestigatoriO75909.

    Organism-specific databases

    HPAiHPA000645.

    Interactioni

    Subunit structurei

    Regulatory subunit of cyclin-dependent kinases. Identified in a complex with a kinase and the RNA polymerase II holoenzyme. Interacts with POLR2A. Interacts with CDK12 and CDK13. Interacts with CDK9 according to PubMed:10574912; does not interact with CDK9 according to PubMed:22012619.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542532EBI-739806,EBI-930964

    Protein-protein interaction databases

    BioGridi114339. 28 interactions.
    IntActiO75909. 16 interactions.
    MINTiMINT-1437641.
    STRINGi9606.ENSP00000374529.

    Structurei

    Secondary structure

    1
    580
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 233
    Helixi28 – 336
    Helixi35 – 384
    Helixi43 – 6321
    Helixi68 – 8114
    Turni82 – 843
    Turni87 – 893
    Helixi92 – 10615
    Helixi113 – 12311
    Helixi126 – 1294
    Helixi130 – 1323
    Helixi136 – 15015
    Turni151 – 1533
    Helixi160 – 16910
    Helixi175 – 19218
    Turni193 – 1964
    Helixi197 – 1993
    Helixi203 – 21816
    Helixi222 – 2254
    Beta strandi226 – 2283
    Helixi234 – 2374
    Beta strandi239 – 2413
    Helixi244 – 25512
    Turni256 – 2583
    Beta strandi259 – 2613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I53X-ray1.50A11-267[»]
    4CXAX-ray3.15B/D11-267[»]
    4NSTX-ray2.20B/D1-267[»]
    4UN0X-ray3.15A/B11-267[»]
    ProteinModelPortaliO75909.
    SMRiO75909. Positions 14-267.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75909.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi312 – 3154Poly-Gln

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin C subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5333.
    HOGENOMiHOG000220828.
    HOVERGENiHBG050836.
    OMAiKIETSHP.
    OrthoDBiEOG7VQJCR.
    TreeFamiTF101010.

    Family and domain databases

    Gene3Di1.10.472.10. 1 hit.
    InterProiIPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10026. PTHR10026. 1 hit.
    PfamiPF00134. Cyclin_N. 1 hit.
    [Graphical view]
    SMARTiSM00385. CYCLIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75909-3) [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

    MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR    50
    REGARFIFDV GTRLGLHYDT LATGIIYFHR FYMFHSFKQF PRYVTGACCL 100
    FLAGKVEETP KKCKDIIKTA RSLLNDVQFG QFGDDPKEEV MVLERILLQT 150
    IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK LVQMAWTFVN DSLCTTLSLQ 200
    WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ DVPVDVLEDI 250
    CHQILDLYSQ GKQQMPHHTP HQLQQPPSLQ PTPQVPQVQQ SQPSQSSEPS 300
    QPQQKDPQQP AQQQQPAQQP KKPSPQPSSP RQVKRAVVVS PKEENKAAEP 350
    PPPKIPKIET THPPLPPAHP PPDRKPPLAA ALGEAEPPGP VDATDLPKVQ 400
    IPPPAHPAPV HQPPPLPHRP PPPPPSSYMT GMSTTSSYMS GEGYQSLQSM 450
    MKTEGPSYGA LPPAYGPPAH LPYHPHVYPP NPPPPPVPPP PASFPPPAIP 500
    PPTPGYPPPP PTYNPNFPPP PPRLPPTHAV PPHPPPGLGL PPASYPPPAV 550
    PPGGQPPVPP PIPPPGMPPV GGLGRAAWMR 580
    Length:580
    Mass (Da):64,240
    Last modified:December 16, 2008 - v2
    Checksum:i8A945E90359AD9F8
    GO
    Isoform 2 (identifier: O75909-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         308-354: QQPAQQQQPA...NKAAEPPPPK → LILLQGWACR...QLGGWGGQPG
         355-580: Missing.

    Show »
    Length:354
    Mass (Da):40,788
    Checksum:i39D8F18FC9429207
    GO
    Isoform 3 (identifier: O75909-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         351-357: PPPKIPK → APSQHLW
         358-580: Missing.

    Show »
    Length:357
    Mass (Da):41,293
    Checksum:iFA7DD89035A66105
    GO
    Isoform 4 (identifier: O75909-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         338-338: V → VSGLKQALGRAGFPGGGNTQV

    Show »
    Length:600
    Mass (Da):66,137
    Checksum:iA79E4E8B190E7199
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911D → T in BAD92610. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei308 – 35447QQPAQ…PPPPK → LILLQGWACRQPATHLLPSP LEDSLLCPRPFPHPACLQLG GWGGQPG in isoform 2. 2 PublicationsVSP_010830Add
    BLAST
    Alternative sequencei338 – 3381V → VSGLKQALGRAGFPGGGNTQ V in isoform 4. 2 PublicationsVSP_035970
    Alternative sequencei351 – 3577PPPKIPK → APSQHLW in isoform 3. 1 PublicationVSP_035971
    Alternative sequencei355 – 580226Missing in isoform 2. 2 PublicationsVSP_035972Add
    BLAST
    Alternative sequencei358 – 580223Missing in isoform 3. 1 PublicationVSP_035973Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060515 mRNA. Translation: AAD09978.1.
    BT006950 mRNA. Translation: AAP35596.1.
    AF542236 Genomic DNA. Translation: AAN06829.1.
    AL110504 Genomic DNA. No translation available.
    BC015935 mRNA. Translation: AAH15935.1.
    AH009612 Genomic DNA. Translation: AAF82290.1.
    BX247958 mRNA. Translation: CAD62298.1.
    AB209373 Transcribed RNA. Translation: BAD92610.1.
    CCDSiCCDS45160.1. [O75909-3]
    RefSeqiNP_001092872.1. NM_001099402.1. [O75909-3]
    XP_005268211.1. XM_005268154.2. [O75909-3]
    UniGeneiHs.510409.

    Genome annotation databases

    EnsembliENST00000389879; ENSP00000374529; ENSG00000090061. [O75909-3]
    GeneIDi8812.
    KEGGihsa:8812.
    UCSCiuc001ygi.4. human. [O75909-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060515 mRNA. Translation: AAD09978.1 .
    BT006950 mRNA. Translation: AAP35596.1 .
    AF542236 Genomic DNA. Translation: AAN06829.1 .
    AL110504 Genomic DNA. No translation available.
    BC015935 mRNA. Translation: AAH15935.1 .
    AH009612 Genomic DNA. Translation: AAF82290.1 .
    BX247958 mRNA. Translation: CAD62298.1 .
    AB209373 Transcribed RNA. Translation: BAD92610.1 .
    CCDSi CCDS45160.1. [O75909-3 ]
    RefSeqi NP_001092872.1. NM_001099402.1. [O75909-3 ]
    XP_005268211.1. XM_005268154.2. [O75909-3 ]
    UniGenei Hs.510409.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I53 X-ray 1.50 A 11-267 [» ]
    4CXA X-ray 3.15 B/D 11-267 [» ]
    4NST X-ray 2.20 B/D 1-267 [» ]
    4UN0 X-ray 3.15 A/B 11-267 [» ]
    ProteinModelPortali O75909.
    SMRi O75909. Positions 14-267.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114339. 28 interactions.
    IntActi O75909. 16 interactions.
    MINTi MINT-1437641.
    STRINGi 9606.ENSP00000374529.

    Chemistry

    ChEMBLi CHEMBL3038475.

    PTM databases

    PhosphoSitei O75909.

    Proteomic databases

    MaxQBi O75909.
    PaxDbi O75909.
    PRIDEi O75909.

    Protocols and materials databases

    DNASUi 8812.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389879 ; ENSP00000374529 ; ENSG00000090061 . [O75909-3 ]
    GeneIDi 8812.
    KEGGi hsa:8812.
    UCSCi uc001ygi.4. human. [O75909-3 ]

    Organism-specific databases

    CTDi 8812.
    GeneCardsi GC14P099947.
    HGNCi HGNC:1596. CCNK.
    HPAi HPA000645.
    MIMi 603544. gene.
    neXtProti NX_O75909.
    PharmGKBi PA26161.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5333.
    HOGENOMi HOG000220828.
    HOVERGENi HBG050836.
    OMAi KIETSHP.
    OrthoDBi EOG7VQJCR.
    TreeFami TF101010.

    Enzyme and pathway databases

    SignaLinki O75909.

    Miscellaneous databases

    ChiTaRSi CCNK. human.
    EvolutionaryTracei O75909.
    GeneWikii Cyclin_K.
    GenomeRNAii 8812.
    NextBioi 33052.
    PROi O75909.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75909.
    Bgeei O75909.
    CleanExi HS_CCNK.
    Genevestigatori O75909.

    Family and domain databases

    Gene3Di 1.10.472.10. 1 hit.
    InterProi IPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10026. PTHR10026. 1 hit.
    Pfami PF00134. Cyclin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00385. CYCLIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity."
      Edwards M.C., Wong C., Elledge S.J.
      Mol. Cell. Biol. 18:4291-4300(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. NIEHS SNPs program
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
      Tissue: Uterus.
    6. Elledge S., Gerber S., Rozet J., Perrault I., Ducroq D., Munnich A., Kaplan J.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-348 (ISOFORMS 1/3).
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-580 (ISOFORM 4).
      Tissue: Brain.
    8. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-580 (ISOFORM 4).
      Tissue: Neuroblastoma.
    9. "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription."
      Fu T.J., Peng J., Lee G., Price D.H., Flores O.
      J. Biol. Chem. 274:34527-34530(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDK9.
      Tissue: T-cell.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-329 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes."
      Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P., Luo Z., Cimermancic P., Ule J., Peterlin B.M.
      Genes Dev. 25:2158-2172(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9."
      Baek K., Brown R.S., Birrane G., Ladias J.A.
      J. Mol. Biol. 366:563-573(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-267.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-267 IN COMPLEX WITH CDK12, INTERACTION WITH CDK12.

    Entry informationi

    Entry nameiCCNK_HUMAN
    AccessioniPrimary (citable) accession number: O75909
    Secondary accession number(s): Q59FT6
    , Q86U16, Q96B63, Q9NNY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3