CCNK_MOUSE
ID CCNK_MOUSE Reviewed; 554 AA.
AC O88874; E9QKT7; Q8R068;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Cyclin-K;
GN Name=Ccnk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-222.
RC TISSUE=Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-329 AND SER-341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
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:22012619}.
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. Its interaction with CDK9
CC is controversial. {ECO:0000269|PubMed:22012619}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:22012619}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in testis.
CC Present throughout the seminiferous epithelium. Also highly expressed
CC in the developing oocyte.
CC -!- DEVELOPMENTAL STAGE: Found in 12.5 dpc embryo with abundant expression
CC in eye (retinal pigment epithelium) and ear (cochlea, crista ampullaris
CC of the semicircular canals).
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality. No homozygous
CC embryos are detected at any stage of embryonic development.
CC {ECO:0000269|PubMed:22012619}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; BC027297; AAH27297.1; -; mRNA.
DR EMBL; AC152059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF060517; AAD09979.1; -; mRNA.
DR AlphaFoldDB; O88874; -.
DR SMR; O88874; -.
DR ComplexPortal; CPX-251; Cyclin K-CDK12 complex.
DR ComplexPortal; CPX-366; Cyclin K-Cdk13 complex.
DR STRING; 10090.ENSMUSP00000098616; -.
DR iPTMnet; O88874; -.
DR PhosphoSitePlus; O88874; -.
DR EPD; O88874; -.
DR jPOST; O88874; -.
DR MaxQB; O88874; -.
DR PaxDb; O88874; -.
DR PeptideAtlas; O88874; -.
DR PRIDE; O88874; -.
DR ProteomicsDB; 281254; -.
DR MGI; MGI:1276106; Ccnk.
DR eggNOG; KOG0834; Eukaryota.
DR InParanoid; O88874; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR ChiTaRS; Ccnk; mouse.
DR PRO; PR:O88874; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88874; protein.
DR GO; GO:0002944; C:cyclin K-CDK12 complex; ISO:MGI.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; ISO:MGI.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO: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; ISO:MGI.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISO: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; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Cell cycle; Cell division; Cyclin; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..554
FT /note="Cyclin-K"
FT /id="PRO_0000080479"
FT REGION 262..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 73
FT /note="T -> N (in Ref. 1; AAH27297)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> K (in Ref. 3; AAD09979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61363 MW; DB2CE7B821834C46 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 PTPQVPQGPQ SQPSQGSEAA
QPPQKDSQQS AQQQQQQAQQ PKKPSPQPSP PRQAKRAVVV SPKEENKATE PPPPPKIPKL
EATHPPLPPA HPPPDRKPPL APALGEAEAT GPVETSDLPK VQIPPPAHPA PVHQPPPLPH
RPPPPPPSSY MTGMSTTSSY MSGEGYQSLQ SMMKTEGPSY GALPPASFPP PTIPPPTPGY
PPPPPTYNPN FPPPPPRLPP THAVPPHPPP GLGLPPASYP PPAVPPGGQP PVPPPIPPPG
MPPVGGLGRA AWMR
