Reviewed, UniProtKB/Swiss-Prot O75909 (CCNK_HUMAN)

Names and origin

Protein names

Recommended name:
    Cyclin-K

Gene names

Name:	CCNK
Synonyms:	CPR4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of cyclin-dependent protein kinase activity Ref.1 Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	1	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

9

1

Phosphoserine Ref.14

Modified residue

324

1

Phosphoserine Ref.14 Ref.10

Modified residue

329

1

Phosphoserine Ref.14 Ref.10 Ref.12

Modified residue

340

1

Phosphoserine Ref.14 Ref.11 Ref.13 Ref.15

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. Checksum: 39D8F18FC9429207		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. Checksum: FA7DD89035A66105		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. Checksum: A79E4E8B190E7199		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: 9632813] [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: 12508121] [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: 15489334] [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 (ISOFORM 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: 10574912] [Abstract] Cited for: FUNCTION. Tissue: T-cell.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-329, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, MASS SPECTROMETRY.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-324; SER-329 AND SER-340, MASS SPECTROMETRY.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, MASS SPECTROMETRY.
[16]	"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: 17169370] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-267.
+	Additional computationally mapped references.

Web resources

NIEHS SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AF270832 , AF270825, AF270826, AF270827, AF270828, AF270829, AF270830, AF270831 Genomic DNA. Translation: AAF82290.1.
BX247958 mRNA. Translation: CAD62298.1.
AB209373 pre-RNA. Translation: BAD92610.1.

RefSeq

NP_003849.2.

UniGene

Hs.705475

3D structure databases

PDBMSD

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

ModBase

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Protein-protein interaction databases