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O75909 (CCNK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Cyclin-K
Gene names
Name:CCNK
Synonyms:CPR4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.9 Ref.16

Subunit structure

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 Ref.9; does not interact with CDK9 according to Ref.16. Ref.1 Ref.9 Ref.16 Ref.19

Subcellular location

Nucleus Ref.16.

Tissue specificity

Ubiquitously expressed. Highest levels in testis. Ref.1

Sequence similarities

Belongs to the cyclin family. Cyclin C subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionCyclin
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.16. Source: MGI

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell cycle arrest

Inferred from genetic interaction Ref.1. Source: MGI

protein phosphorylation

Inferred from direct assay Ref.1. Source: GOC

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcyclin K-CDK12 complex

Inferred from physical interaction Ref.16. Source: MGI

cyclin K-CDK13 complex

Inferred from physical interaction Ref.16. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA polymerase II carboxy-terminal domain kinase activity

Inferred from direct assay Ref.1. Source: MGI

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: MGI

protein binding

Inferred from physical interaction PubMed 16713569. Source: IntAct

protein kinase binding

Inferred from physical interaction Ref.16. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN1P542532EBI-739806,EBI-930964

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75909-3)

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.
Isoform 2 (identifier: O75909-2)

The sequence of this isoform differs from the canonical sequence as follows:
     308-354: QQPAQQQQPA...NKAAEPPPPK → LILLQGWACR...QLGGWGGQPG
     355-580: Missing.
Isoform 3 (identifier: O75909-1)

The sequence of this isoform differs from the canonical sequence as follows:
     351-357: PPPKIPK → APSQHLW
     358-580: Missing.
Isoform 4 (identifier: O75909-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Cyclin-K
PRO_0000080478

Regions

Compositional bias312 – 3154Poly-Gln

Amino acid modifications

Modified residue3241Phosphoserine Ref.11 Ref.13 Ref.14 Ref.17
Modified residue3291Phosphoserine Ref.14
Modified residue3401Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14 Ref.17

Natural variations

Alternative sequence308 – 35447QQPAQ…PPPPK → LILLQGWACRQPATHLLPSP LEDSLLCPRPFPHPACLQLG GWGGQPG in isoform 2.
VSP_010830
Alternative sequence3381V → VSGLKQALGRAGFPGGGNTQ V in isoform 4.
VSP_035970
Alternative sequence351 – 3577PPPKIPK → APSQHLW in isoform 3.
VSP_035971
Alternative sequence355 – 580226Missing in isoform 2.
VSP_035972
Alternative sequence358 – 580223Missing in isoform 3.
VSP_035973

Experimental info

Sequence conflict1911D → T in BAD92610. Ref.7

Secondary structure

............................................ 580
Helix Strand Turn

Details...

Sequences

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

Last modified December 16, 2008. Version 2.
Checksum: 8A945E90359AD9F8

FASTA58064,240
        10         20         30         40         50         60 
MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR REGARFIFDV 

        70         80         90        100        110        120 
GTRLGLHYDT LATGIIYFHR FYMFHSFKQF PRYVTGACCL FLAGKVEETP KKCKDIIKTA 

       130        140        150        160        170        180 
RSLLNDVQFG QFGDDPKEEV MVLERILLQT IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK 

       190        200        210        220        230        240 
LVQMAWTFVN DSLCTTLSLQ WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ 

       250        260        270        280        290        300 
DVPVDVLEDI CHQILDLYSQ GKQQMPHHTP HQLQQPPSLQ PTPQVPQVQQ SQPSQSSEPS 

       310        320        330        340        350        360 
QPQQKDPQQP AQQQQPAQQP KKPSPQPSSP RQVKRAVVVS PKEENKAAEP PPPKIPKIET 

       370        380        390        400        410        420 
THPPLPPAHP PPDRKPPLAA ALGEAEPPGP VDATDLPKVQ IPPPAHPAPV HQPPPLPHRP 

       430        440        450        460        470        480 
PPPPPSSYMT GMSTTSSYMS GEGYQSLQSM MKTEGPSYGA LPPAYGPPAH LPYHPHVYPP 

       490        500        510        520        530        540 
NPPPPPVPPP PASFPPPAIP PPTPGYPPPP PTYNPNFPPP PPRLPPTHAV PPHPPPGLGL 

       550        560        570        580 
PPASYPPPAV PPGGQPPVPP PIPPPGMPPV GGLGRAAWMR 

« Hide

Isoform 2 [UniParc].

Checksum: 39D8F18FC9429207
Show »

FASTA35440,788
Isoform 3 [UniParc].

Checksum: FA7DD89035A66105
Show »

FASTA35741,293
Isoform 4 [UniParc].

Checksum: A79E4E8B190E7199
Show »

FASTA60066,137

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The structure and substrate specificity of human Cdk12/Cyclin K."
Boesken C.A., Farnung L., Hintermair C., Merzel Schachter M., Vogel-Bachmayr K., Blazek D., Anand K., Fisher R.P., Eick D., Geyer M.
Nat. Commun. 5:3505-3505(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-267 IN COMPLEX WITH CDK12, INTERACTION WITH CDK12.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45160.1. [O75909-3]
RefSeqNP_001092872.1. NM_001099402.1. [O75909-3]
XP_005268211.1. XM_005268154.2. [O75909-3]
UniGeneHs.510409.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I53X-ray1.50A11-267[»]
4CJYX-ray3.15A/B11-267[»]
4CXAX-ray3.15B/D11-267[»]
4NSTX-ray2.20B/D1-267[»]
ProteinModelPortalO75909.
SMRO75909. Positions 14-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114339. 30 interactions.
IntActO75909. 16 interactions.
MINTMINT-1437641.
STRING9606.ENSP00000374529.

Chemistry

ChEMBLCHEMBL3038475.

PTM databases

PhosphoSiteO75909.

Proteomic databases

MaxQBO75909.
PaxDbO75909.
PRIDEO75909.

Protocols and materials databases

DNASU8812.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389879; ENSP00000374529; ENSG00000090061. [O75909-3]
GeneID8812.
KEGGhsa:8812.
UCSCuc001ygi.4. human. [O75909-3]

Organism-specific databases

CTD8812.
GeneCardsGC14P099947.
HGNCHGNC:1596. CCNK.
HPAHPA000645.
MIM603544. gene.
neXtProtNX_O75909.
PharmGKBPA26161.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5333.
HOGENOMHOG000220828.
HOVERGENHBG050836.
OMAKIETSHP.
OrthoDBEOG7VQJCR.
TreeFamTF101010.

Enzyme and pathway databases

SignaLinkO75909.

Gene expression databases

ArrayExpressO75909.
BgeeO75909.
CleanExHS_CCNK.
GenevestigatorO75909.

Family and domain databases

Gene3D1.10.472.10. 1 hit.
InterProIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10026. PTHR10026. 1 hit.
PfamPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
ProtoNetSearch...

Other

ChiTaRSCCNK. human.
EvolutionaryTraceO75909.
GeneWikiCyclin_K.
GenomeRNAi8812.
NextBio33052.
PROO75909.
SOURCESearch...

Entry information

Entry nameCCNK_HUMAN
AccessionPrimary (citable) accession number: O75909
Secondary accession number(s): Q59FT6 expand/collapse secondary AC list , Q86U16, Q96B63, Q9NNY9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 138 of the entry and version 2 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

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 chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM