CCNK_HUMAN
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 03-AUG-2022, entry version 202.
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 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 [22]
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 -!- 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/";
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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. [O75909-3]
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 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 AlphaFoldDB; O75909; -.
DR SMR; O75909; -.
DR BioGRID; 114339; 108.
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; 56.
DR MINT; O75909; -.
DR STRING; 9606.ENSP00000374529; -.
DR BindingDB; O75909; -.
DR ChEMBL; CHEMBL2346490; -.
DR GlyGen; O75909; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O75909; -.
DR PhosphoSitePlus; O75909; -.
DR BioMuta; CCNK; -.
DR EPD; O75909; -.
DR jPOST; O75909; -.
DR MassIVE; O75909; -.
DR MaxQB; O75909; -.
DR PaxDb; O75909; -.
DR PeptideAtlas; O75909; -.
DR PRIDE; O75909; -.
DR ProteomicsDB; 50259; -. [O75909-3]
DR ProteomicsDB; 50260; -. [O75909-1]
DR ProteomicsDB; 50261; -. [O75909-2]
DR ProteomicsDB; 50262; -. [O75909-4]
DR Antibodypedia; 102; 188 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 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; AQPQQKD; -.
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; 746 hits in 1091 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 185 other tissues.
DR ExpressionAtlas; O75909; baseline and differential.
DR Genevisible; O75909; HS.
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:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
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:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; IDA:CACAO.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:ComplexPortal.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:2001165; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues; IMP:CACAO.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; 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; TAS:ProtInc.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR013763; Cyclin-like.
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; PTHR10026; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cyclin;
KW Disease variant; Intellectual disability; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; 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
