ID CCNK_HUMAN Reviewed; 580 AA. AC O75909; Q59FT6; Q86U16; Q96B63; Q9NNY9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 27-MAR-2024, entry version 211. DE RecName: Full=Cyclin-K; GN Name=CCNK; Synonyms=CPR4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, AND TISSUE RP SPECIFICITY. RX PubMed=9632813; DOI=10.1128/mcb.18.7.4291; RA Edwards M.C., Wong C., Elledge S.J.; RT "Human cyclin K, a novel RNA polymerase II-associated cyclin possessing RT both carboxy-terminal domain kinase and Cdk-activating kinase activity."; RL Mol. Cell. Biol. 18:4291-4300(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-348 (ISOFORMS 1/3). RA Elledge S., Gerber S., Rozet J., Perrault I., Ducroq D., Munnich A., RA Kaplan J.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-580 (ISOFORM 4). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-580 (ISOFORM 4). RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, AND INTERACTION WITH CDK9. RC TISSUE=T-cell; RX PubMed=10574912; DOI=10.1074/jbc.274.49.34527; RA Fu T.J., Peng J., Lee G., Price D.H., Flores O.; RT "Cyclin K functions as a CDK9 regulatory subunit and participates in RNA RT polymerase II transcription."; RL J. Biol. Chem. 274:34527-34530(1999). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-329 AND SER-340, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=22012619; DOI=10.1101/gad.16962311; RA Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P., RA Luo Z., Cimermancic P., Ule J., Peterlin B.M.; RT "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of RT expression of DNA damage response genes."; RL Genes Dev. 25:2158-2172(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-340, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP INVOLVEMENT IN IDDHDF, VARIANT IDDHDF GLU-111, AND CHARACTERIZATION OF RP VARIANT IDDHDF GLU-111. RX PubMed=30122539; DOI=10.1016/j.ajhg.2018.07.019; RA Fan Y., Yin W., Hu B., Kline A.D., Zhang V.W., Liang D., Sun Y., Wang L., RA Tang S., Powis Z., Li L., Yan H., Shi Z., Yang X., Chen Y., Wang J., RA Jiang Y., Tan H., Gu X., Wu L., Yu Y.; RT "De novo mutations of CCNK cause a syndromic neurodevelopmental disorder RT with distinctive facial dysmorphism."; RL Am. J. Hum. Genet. 103:448-455(2018). RN [21] RP INTERACTION WITH HHV-1 TRANSCRIPTIONAL REGULATOR ICP22 (MICROBIAL RP INFECTION). RX PubMed=34696162; DOI=10.3390/vaccines9101054; RA Isa N.F., Bensaude O., Aziz N.C., Murphy S.; RT "HSV-1 ICP22 Is a Selective Viral Repressor of Cellular RNA Polymerase II- RT Mediated Transcription Elongation."; RL Vaccines (Basel) 9:0-0(2021). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-267. RX PubMed=17169370; DOI=10.1016/j.jmb.2006.11.057; RA Baek K., Brown R.S., Birrane G., Ladias J.A.; RT "Crystal structure of human cyclin K, a positive regulator of cyclin- RT dependent kinase 9."; RL J. Mol. Biol. 366:563-573(2007). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-267 IN COMPLEX WITH CDK12, AND RP INTERACTION WITH CDK12. RX PubMed=24662513; DOI=10.1038/ncomms4505; RA Boesken C.A., Farnung L., Hintermair C., Merzel Schachter M., RA Vogel-Bachmayr K., Blazek D., Anand K., Fisher R.P., Eick D., Geyer M.; RT "The structure and substrate specificity of human Cdk12/Cyclin K."; RL Nat. Commun. 5:3505-3505(2014). CC -!- FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates CC activation of target kinases. Plays a role in transcriptional CC regulation via its role in regulating the phosphorylation of the C- CC terminal domain (CTD) of the large subunit of RNA polymerase II CC (POLR2A). {ECO:0000269|PubMed:10574912, ECO:0000269|PubMed:22012619, CC ECO:0000269|PubMed:9632813}. CC -!- SUBUNIT: Regulatory subunit of cyclin-dependent kinases. Identified in CC a complex with a kinase and the RNA polymerase II holoenzyme. Interacts CC with POLR2A. Interacts with CDK12 and CDK13. Interacts with CDK9 CC according to PubMed:10574912; does not interact with CDK9 according to CC PubMed:22012619. {ECO:0000269|PubMed:10574912, CC ECO:0000269|PubMed:22012619, ECO:0000269|PubMed:24662513, CC ECO:0000269|PubMed:9632813}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 1 CC (HHV-1) transcriptional regulator ICP22. {ECO:0000269|PubMed:34696162}. CC -!- INTERACTION: CC O75909; P54253: ATXN1; NbExp=2; IntAct=EBI-739806, EBI-930964; CC O75909; O14503: BHLHE40; NbExp=3; IntAct=EBI-739806, EBI-711810; CC O75909; Q14004: CDK13; NbExp=7; IntAct=EBI-739806, EBI-968626; CC O75909; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-739806, EBI-741037; CC O75909; O14777: NDC80; NbExp=3; IntAct=EBI-739806, EBI-715849; CC O75909; Q93062: RBPMS; NbExp=4; IntAct=EBI-739806, EBI-740322; CC O75909; Q08117: TLE5; NbExp=3; IntAct=EBI-739806, EBI-717810; CC O75909-2; P54253: ATXN1; NbExp=6; IntAct=EBI-12010594, EBI-930964; CC O75909-2; Q07002: CDK18; NbExp=3; IntAct=EBI-12010594, EBI-746238; CC O75909-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12010594, EBI-3867333; CC O75909-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12010594, EBI-742054; CC O75909-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-12010594, EBI-12193763; CC O75909-2; P31943: HNRNPH1; NbExp=3; IntAct=EBI-12010594, EBI-351590; CC O75909-2; P55795: HNRNPH2; NbExp=3; IntAct=EBI-12010594, EBI-352823; CC O75909-2; P49639: HOXA1; NbExp=5; IntAct=EBI-12010594, EBI-740785; CC O75909-2; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-12010594, EBI-3957665; CC O75909-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-12010594, EBI-11953846; CC O75909-2; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-12010594, EBI-12805508; CC O75909-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-12010594, EBI-10241353; CC O75909-2; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-12010594, EBI-11962084; CC O75909-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12010594, EBI-10261141; CC O75909-2; P12524-2: MYCL; NbExp=3; IntAct=EBI-12010594, EBI-18936665; CC O75909-2; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-12010594, EBI-12813389; CC O75909-2; O15160: POLR1C; NbExp=3; IntAct=EBI-12010594, EBI-1055079; CC O75909-2; P78424: POU6F2; NbExp=3; IntAct=EBI-12010594, EBI-12029004; CC O75909-2; P86480: PRR20D; NbExp=3; IntAct=EBI-12010594, EBI-12754095; CC O75909-2; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-12010594, EBI-12001422; CC O75909-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12010594, EBI-11741437; CC O75909-2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-12010594, EBI-11975223; CC O75909-2; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-12010594, EBI-740232; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22012619}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O75909-3; Sequence=Displayed; CC Name=2; CC IsoId=O75909-2; Sequence=VSP_010830, VSP_035972; CC Name=3; CC IsoId=O75909-1; Sequence=VSP_035971, VSP_035973; CC Name=4; CC IsoId=O75909-4; Sequence=VSP_035970; CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in testis. CC {ECO:0000269|PubMed:9632813}. CC -!- DISEASE: Intellectual developmental disorder with hypertelorism and CC distinctive facies (IDDHDF) [MIM:618147]: An autosomal dominant CC neurodevelopmental disorder characterized by developmental delay and CC intellectual disability, language defects, and distinctive facial CC dysmorphism including high hairline, hypertelorism, thin eyebrows, CC dysmorphic ears, broad nasal bridge and tip, and narrow jaw. CC {ECO:0000269|PubMed:30122539}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS SNPs; CC URL="http://egp.gs.washington.edu/data/ccnk/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF060515; AAD09978.1; -; mRNA. DR EMBL; BT006950; AAP35596.1; -; mRNA. DR EMBL; AF542236; AAN06829.1; -; Genomic_DNA. DR EMBL; AL110504; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015935; AAH15935.1; -; mRNA. DR EMBL; AH009612; AAF82290.1; -; Genomic_DNA. DR EMBL; BX247958; CAD62298.1; -; mRNA. DR EMBL; AB209373; BAD92610.1; -; Transcribed_RNA. DR CCDS; CCDS45160.1; -. [O75909-3] DR RefSeq; NP_001092872.1; NM_001099402.1. [O75909-3] DR RefSeq; XP_005268211.1; XM_005268154.4. [O75909-3] DR RefSeq; XP_011535577.1; XM_011537275.2. DR PDB; 2I53; X-ray; 1.50 A; A=11-267. DR PDB; 4CXA; X-ray; 3.15 A; B/D=11-267. DR PDB; 4NST; X-ray; 2.20 A; B/D=1-267. DR PDB; 4UN0; X-ray; 3.15 A; A/B=11-267. DR PDB; 5ACB; X-ray; 2.70 A; A/B=11-267. DR PDB; 5EFQ; X-ray; 2.00 A; B/D=1-267. DR PDB; 6B3E; X-ray; 3.06 A; B/D=1-267. DR PDB; 6CKX; X-ray; 2.80 A; B/D=1-267. DR PDB; 6TD3; X-ray; 3.46 A; C/F/I=1-267. DR PDB; 7NXJ; X-ray; 2.36 A; B/D=1-267. DR PDB; 7NXK; X-ray; 3.00 A; B/D=1-267. DR PDB; 8BU1; X-ray; 2.98 A; C/F/I=1-267. DR PDB; 8BU2; X-ray; 3.13 A; C/F/I=1-267. DR PDB; 8BU3; X-ray; 3.42 A; C/F/I=1-267. DR PDB; 8BU4; X-ray; 3.09 A; C/F/I=1-267. DR PDB; 8BU5; X-ray; 3.13 A; C/F/I=1-267. DR PDB; 8BU6; X-ray; 3.45 A; C/F/I=1-267. DR PDB; 8BU7; X-ray; 3.25 A; C/F/I=1-267. DR PDB; 8BU9; X-ray; 3.51 A; C/F/I=1-267. DR PDB; 8BUA; X-ray; 3.19 A; C/F/I=1-267. DR PDB; 8BUB; X-ray; 3.42 A; C/F/I=1-267. DR PDB; 8BUC; X-ray; 3.85 A; C/F/I=1-267. DR PDB; 8BUD; X-ray; 3.20 A; C/F/I=1-267. DR PDB; 8BUE; X-ray; 3.25 A; C/F/I=1-267. DR PDB; 8BUF; X-ray; 3.30 A; C/F/I=1-267. DR PDB; 8BUG; X-ray; 3.53 A; C/F/I=1-267. DR PDB; 8BUH; X-ray; 3.79 A; C/F/I=1-267. DR PDB; 8BUI; X-ray; 3.50 A; C/F/I=1-267. DR PDB; 8BUJ; X-ray; 3.62 A; C/F/I=1-267. DR PDB; 8BUK; X-ray; 3.41 A; C/F/I=1-267. DR PDB; 8BUL; X-ray; 3.40 A; C/F/I=1-267. DR PDB; 8BUM; X-ray; 3.36 A; C/F/I=1-267. DR PDB; 8BUN; X-ray; 3.08 A; C/F/I=1-267. DR PDB; 8BUO; X-ray; 3.58 A; C/F/I=1-267. DR PDB; 8BUP; X-ray; 3.41 A; C/F/I=1-267. DR PDB; 8BUQ; X-ray; 3.20 A; C/F/I=1-267. DR PDB; 8BUR; X-ray; 3.64 A; C/F/I=1-267. DR PDB; 8BUS; X-ray; 3.26 A; C/F/I=1-267. DR PDB; 8BUT; X-ray; 3.25 A; C/F/I=1-267. DR PDB; 8P81; X-ray; 2.68 A; B=1-267. DR PDBsum; 2I53; -. DR PDBsum; 4CXA; -. DR PDBsum; 4NST; -. DR PDBsum; 4UN0; -. DR PDBsum; 5ACB; -. DR PDBsum; 5EFQ; -. DR PDBsum; 6B3E; -. DR PDBsum; 6CKX; -. DR PDBsum; 6TD3; -. DR PDBsum; 7NXJ; -. DR PDBsum; 7NXK; -. DR PDBsum; 8BU1; -. DR PDBsum; 8BU2; -. DR PDBsum; 8BU3; -. DR PDBsum; 8BU4; -. DR PDBsum; 8BU5; -. DR PDBsum; 8BU6; -. DR PDBsum; 8BU7; -. DR PDBsum; 8BU9; -. DR PDBsum; 8BUA; -. DR PDBsum; 8BUB; -. DR PDBsum; 8BUC; -. DR PDBsum; 8BUD; -. DR PDBsum; 8BUE; -. DR PDBsum; 8BUF; -. DR PDBsum; 8BUG; -. DR PDBsum; 8BUH; -. DR PDBsum; 8BUI; -. DR PDBsum; 8BUJ; -. DR PDBsum; 8BUK; -. DR PDBsum; 8BUL; -. DR PDBsum; 8BUM; -. DR PDBsum; 8BUN; -. DR PDBsum; 8BUO; -. DR PDBsum; 8BUP; -. DR PDBsum; 8BUQ; -. DR PDBsum; 8BUR; -. DR PDBsum; 8BUS; -. DR PDBsum; 8BUT; -. DR PDBsum; 8P81; -. DR AlphaFoldDB; O75909; -. DR SMR; O75909; -. DR BioGRID; 114339; 119. DR ComplexPortal; CPX-241; Cyclin K-CDK12 complex. DR ComplexPortal; CPX-359; Cyclin K-CDK13 complex. DR CORUM; O75909; -. DR DIP; DIP-50081N; -. DR IntAct; O75909; 57. DR MINT; O75909; -. DR STRING; 9606.ENSP00000374529; -. DR BindingDB; O75909; -. DR ChEMBL; CHEMBL2346490; -. DR GlyCosmos; O75909; 1 site, 2 glycans. DR GlyGen; O75909; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; O75909; -. DR PhosphoSitePlus; O75909; -. DR SwissPalm; O75909; -. DR BioMuta; CCNK; -. DR EPD; O75909; -. DR jPOST; O75909; -. DR MassIVE; O75909; -. DR MaxQB; O75909; -. DR PaxDb; 9606-ENSP00000374529; -. DR PeptideAtlas; O75909; -. DR ProteomicsDB; 50259; -. [O75909-3] DR ProteomicsDB; 50260; -. [O75909-1] DR ProteomicsDB; 50261; -. [O75909-2] DR ProteomicsDB; 50262; -. [O75909-4] DR Pumba; O75909; -. DR Antibodypedia; 102; 204 antibodies from 23 providers. DR DNASU; 8812; -. DR Ensembl; ENST00000389879.9; ENSP00000374529.5; ENSG00000090061.17. [O75909-3] DR GeneID; 8812; -. DR KEGG; hsa:8812; -. DR MANE-Select; ENST00000389879.9; ENSP00000374529.5; NM_001099402.2; NP_001092872.1. DR UCSC; uc001ygi.5; human. [O75909-3] DR AGR; HGNC:1596; -. DR CTD; 8812; -. DR DisGeNET; 8812; -. DR GeneCards; CCNK; -. DR HGNC; HGNC:1596; CCNK. DR HPA; ENSG00000090061; Tissue enhanced (bone). DR MalaCards; CCNK; -. DR MIM; 603544; gene. DR MIM; 618147; phenotype. DR neXtProt; NX_O75909; -. DR OpenTargets; ENSG00000090061; -. DR Orphanet; 600668; CCNK-related neurodevelopmental disorder-severe intellectual disability-facial dysmorphism syndrome. DR PharmGKB; PA26161; -. DR VEuPathDB; HostDB:ENSG00000090061; -. DR eggNOG; KOG0834; Eukaryota. DR GeneTree; ENSGT00940000156384; -. DR HOGENOM; CLU_022000_0_2_1; -. DR InParanoid; O75909; -. DR OMA; FVIACCR; -. DR OrthoDB; 4848076at2759; -. DR PhylomeDB; O75909; -. DR TreeFam; TF101010; -. DR PathwayCommons; O75909; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat. DR Reactome; R-HSA-167287; HIV elongation arrest and recovery. DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation. DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR SignaLink; O75909; -. DR SIGNOR; O75909; -. DR BioGRID-ORCS; 8812; 775 hits in 1170 CRISPR screens. DR ChiTaRS; CCNK; human. DR EvolutionaryTrace; O75909; -. DR GeneWiki; Cyclin_K; -. DR GenomeRNAi; 8812; -. DR Pharos; O75909; Tbio. DR PRO; PR:O75909; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; O75909; Protein. DR Bgee; ENSG00000090061; Expressed in upper arm skin and 187 other cell types or tissues. DR ExpressionAtlas; O75909; baseline and differential. DR GO; GO:0002944; C:cyclin K-CDK12 complex; IPI:MGI. DR GO; GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI. DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:MGI. DR GO; GO:0019901; F:protein kinase binding; IPI:MGI. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:MGI. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006974; P:DNA damage response; IMP:MGI. DR GO; GO:0044828; P:negative regulation by host of viral genome replication; IDA:CACAO. DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0009966; P:regulation of signal transduction; IDA:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:GO_Central. DR CDD; cd20530; CYCLIN_CCNK_rpt1; 1. DR CDD; cd20531; CYCLIN_CCNK_rpt2; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR IDEAL; IID00695; -. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR043198; Cyclin/Ssn8. DR InterPro; IPR004367; Cyclin_C-dom. DR InterPro; IPR006671; Cyclin_N. DR PANTHER; PTHR10026; CYCLIN; 1. DR PANTHER; PTHR10026:SF51; CYCLIN-K; 1. DR Pfam; PF00134; Cyclin_N; 1. DR Pfam; PF21797; CycT2-like_C; 1. DR SMART; SM00385; CYCLIN; 2. DR SMART; SM01332; Cyclin_C; 1. DR SUPFAM; SSF47954; Cyclin-like; 2. DR Genevisible; O75909; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cyclin; KW Disease variant; Host-virus interaction; Intellectual disability; Mitosis; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..580 FT /note="Cyclin-K" FT /id="PRO_0000080478" FT REGION 262..580 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 284..319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 351..377 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 400..428 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 429..453 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..570 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 324 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88874" FT MOD_RES 329 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 340 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 308..354 FT /note="QQPAQQQQPAQQPKKPSPQPSSPRQVKRAVVVSPKEENKAAEPPPPK -> L FT ILLQGWACRQPATHLLPSPLEDSLLCPRPFPHPACLQLGGWGGQPG (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_010830" FT VAR_SEQ 338 FT /note="V -> VSGLKQALGRAGFPGGGNTQV (in isoform 4)" FT /evidence="ECO:0000303|Ref.7, ECO:0000303|Ref.8" FT /id="VSP_035970" FT VAR_SEQ 351..357 FT /note="PPPKIPK -> APSQHLW (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9632813" FT /id="VSP_035971" FT VAR_SEQ 355..580 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_035972" FT VAR_SEQ 358..580 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9632813" FT /id="VSP_035973" FT VARIANT 111 FT /note="K -> E (in IDDHDF; contrary to the wild-type FT protein, does not rescue morpholino knockdown phenotype in FT zebrafish; dbSNP:rs1566748800)" FT /evidence="ECO:0000269|PubMed:30122539" FT /id="VAR_081570" FT CONFLICT 191 FT /note="D -> T (in Ref. 7; BAD92610)" FT /evidence="ECO:0000305" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 28..33 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 35..38 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 43..63 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 68..81 FT /evidence="ECO:0007829|PDB:2I53" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:2I53" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 92..106 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 113..123 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 136..150 FT /evidence="ECO:0007829|PDB:2I53" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 160..169 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 175..192 FT /evidence="ECO:0007829|PDB:2I53" FT TURN 193..196 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 203..218 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:2I53" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 234..237 FT /evidence="ECO:0007829|PDB:2I53" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:2I53" FT HELIX 244..255 FT /evidence="ECO:0007829|PDB:2I53" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:2I53" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:2I53" SQ SEQUENCE 580 AA; 64240 MW; 8A945E90359AD9F8 CRC64; MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR REGARFIFDV GTRLGLHYDT LATGIIYFHR FYMFHSFKQF PRYVTGACCL FLAGKVEETP KKCKDIIKTA RSLLNDVQFG QFGDDPKEEV MVLERILLQT IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK LVQMAWTFVN DSLCTTLSLQ WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ DVPVDVLEDI CHQILDLYSQ GKQQMPHHTP HQLQQPPSLQ PTPQVPQVQQ SQPSQSSEPS QPQQKDPQQP AQQQQPAQQP KKPSPQPSSP RQVKRAVVVS PKEENKAAEP PPPKIPKIET THPPLPPAHP PPDRKPPLAA ALGEAEPPGP VDATDLPKVQ IPPPAHPAPV HQPPPLPHRP PPPPPSSYMT GMSTTSSYMS GEGYQSLQSM MKTEGPSYGA LPPAYGPPAH LPYHPHVYPP NPPPPPVPPP PASFPPPAIP PPTPGYPPPP PTYNPNFPPP PPRLPPTHAV PPHPPPGLGL PPASYPPPAV PPGGQPPVPP PIPPPGMPPV GGLGRAAWMR //