O75909 (CCNK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-K

Gene names

Name:	CCNK
Synonyms:	CPR4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in transcriptional regulation. In vitro, is associated with a kinase activity toward both RNA polymerase II C-terminal domain and CDK2 (CAK). Ref.9
Subunit structure	Part of a cyclin-kinase pair in the RNA polymerase II holoenzyme. Binds to CDK9.
Tissue specificity	Ubiquitously expressed. Highest levels in testis.
Sequence similarities	Belongs to the cyclin family. Cyclin C subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Transcription Transcription regulation
Coding sequence diversity	Alternative splicing
Molecular function	Cyclin
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle arrest Inferred from genetic interaction Ref.1. Source: MGI regulation of cyclin-dependent protein serine/threonine kinase activity Traceable author statement Ref.1. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from mutant phenotype PubMed 22012619. Source: MGI transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cyclin K-CDK12 complex Inferred from physical interaction PubMed 22012619. Source: MGI cyclin K-CDK13 complex Inferred from physical interaction PubMed 22012619. Source: MGI
Molecular_function	RNA 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 580

580

Cyclin-K

PRO_0000080478

Regions

Compositional bias

312 – 315

4

Poly-Gln

Amino acid modifications

Modified residue

324

1

Phosphoserine Ref.11 Ref.13 Ref.14 Ref.16

Modified residue

328

1

Phosphoserine By similarity

Modified residue

329

1

Phosphoserine Ref.14

Modified residue

340

1

Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14 Ref.16

Natural variations

Alternative sequence

308 – 354

47

QQPAQ…PPPPK → LILLQGWACRQPATHLLPSP LEDSLLCPRPFPHPACLQLG GWGGQPG in isoform 2.

VSP_010830

Alternative sequence

338

1

V → VSGLKQALGRAGFPGGGNTQ V in isoform 4.

VSP_035970

Alternative sequence

351 – 357

7

PPPKIPK → APSQHLW in isoform 3.

VSP_035971

Alternative sequence

355 – 580

226

Missing in isoform 2.

VSP_035972

Alternative sequence

358 – 580

223

Missing in isoform 3.

VSP_035973

Experimental info

Sequence conflict

191

1

D → T in BAD92610. Ref.7

Secondary structure

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580

Helix Strand Turn

Details...

Beta strand

21 – 23

3

Helix

28 – 33

6

Helix

35 – 38

4

Helix

43 – 63

21

Helix

68 – 81

14

Turn

82 – 84

3

Turn

87 – 89

3

Helix

92 – 106

15

Helix

113 – 123

11

Helix

126 – 129

4

Helix

130 – 132

3

Helix

136 – 150

15

Turn

151 – 153

3

Helix

160 – 169

10

Helix

175 – 192

18

Turn

193 – 196

4

Helix

197 – 199

3

Helix

203 – 218

16

Helix

222 – 225

4

Beta strand

226 – 228

3

Helix

234 – 237

4

Beta strand

239 – 241

3

Helix

244 – 255

12

Turn

256 – 258

3

Beta strand

259 – 261

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 8A945E90359AD9F8	FASTA	580	64,240
	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
	Isoform 2 [UniParc]. Checksum: 39D8F18FC9429207	FASTA	354	40,788
	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 QPQQKDPLIL LQGWACRQPA THLLPSPLED SLLCPRPFPH PACLQLGGWG GQPG
	Isoform 3 [UniParc]. Checksum: FA7DD89035A66105	FASTA	357	41,293
	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 QPQQKDPQQP AQQQQPAQQP KKPSPQPSSP RQVKRAVVVS PKEENKAAEP APSQHLW
	Isoform 4 [UniParc]. Checksum: A79E4E8B190E7199	FASTA	600	66,137
	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 RQVKRAVVSG LKQALGRAGF PGGGNTQVVS 370 380 390 400 410 420 PKEENKAAEP PPPKIPKIET THPPLPPAHP PPDRKPPLAA ALGEAEPPGP VDATDLPKVQ 430 440 450 460 470 480 IPPPAHPAPV HQPPPLPHRP PPPPPSSYMT GMSTTSSYMS GEGYQSLQSM MKTEGPSYGA 490 500 510 520 530 540 LPPAYGPPAH LPYHPHVYPP NPPPPPVPPP PASFPPPAIP PPTPGYPPPP PTYNPNFPPP 550 560 570 580 590 600 PPRLPPTHAV PPHPPPGLGL PPASYPPPAV PPGGQPPVPP PIPPPGMPPV GGLGRAAWMR

References

	« Hide 'large scale' referencesShow '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).
[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. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY.
[17]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS SNPs

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.

IPI

IPI00411579.
IPI00431127.
IPI00783214.
IPI00915260.

RefSeq

NP_001092872.1. NM_001099402.1.

UniGene

Hs.510409.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I53	X-ray	1.50	A	11-267	[»]

ProteinModelPortal

O75909.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75909. 16 interactions.

MINT

MINT-1437641.

STRING

9606.ENSP00000374529.

PTM databases

PhosphoSite

O75909.

Proteomic databases

PaxDb

O75909.

PRIDE

O75909.

Protocols and materials databases

DNASU

8812.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389879; ENSP00000374529; ENSG00000090061.

GeneID

8812.

KEGG

hsa:8812.

UCSC

uc001ygi.4. human.

Organism-specific databases

CTD

8812.

GeneCards

GC14P099947.

HGNC

HGNC:1596. CCNK.

HPA

HPA000645.

MIM

603544. gene.

neXtProt

NX_O75909.

PharmGKB

PA26161.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5333.

HOGENOM

HOG000220828.

HOVERGEN

HBG050836.

OrthoDB

EOG4KH2VJ.

Gene expression databases

ArrayExpress

O75909.

Bgee

O75909.

CleanEx

HS_CCNK.

Genevestigator

O75909.

GermOnline

ENSG00000090061. Homo sapiens.

Family and domain databases

Gene3D

1.10.472.10. 1 hit.

InterPro

IPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR006671. Cyclin_N.
[Graphical view]

PANTHER

PTHR10026. PTHR10026. 1 hit.

Pfam

PF00134. Cyclin_N. 1 hit.
[Graphical view]

SMART

SM00385. CYCLIN. 2 hits.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

PROSITE

PS00292. CYCLINS. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CCNK. human.

EvolutionaryTrace

O75909.

GenomeRNAi

8812.

NextBio

33052.

SOURCE

Search...

Entry information

Entry name

CCNK_HUMAN

Accession

Primary (citable) accession number: O75909
Secondary accession number(s): Q59FT6 , Q86U16, Q96B63, Q9NNY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.