CCNC_HUMAN
ID CCNC_HUMAN Reviewed; 283 AA.
AC P24863; B4DPZ1; Q9H543;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Cyclin-C;
DE AltName: Full=SRB11 homolog;
DE Short=hSRB11;
GN Name=CCNC;
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 1).
RX PubMed=1833066; DOI=10.1016/0092-8674(91)90042-w;
RA Lew D.J., Dulic V., Reed S.I.;
RT "Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
RT function in yeast.";
RL Cell 66:1197-1206(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8833152; DOI=10.1006/geno.1996.0112;
RA Li H., Lahti J.M., Valentine M., Saito M., Reed S.I., Look A.T., Kidd V.J.;
RT "Molecular cloning and chromosomal localization of the human cyclin C
RT (CCNC) and cyclin E (CCNE) genes: deletion of the CCNC gene in human
RT tumors.";
RL Genomics 32:253-259(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP FUNCTION.
RX PubMed=8700522;
RA Rickert P., Seghezzi W., Shanahan F., Cho H., Lees E.;
RT "Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase II.";
RL Oncogene 12:2631-2640(1996).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A FORM OF THE
RP MEDIATOR COMPLEX.
RX PubMed=9734358; DOI=10.1016/s1097-2765(00)80131-8;
RA Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.;
RT "NAT, a human complex containing Srb polypeptides that functions as a
RT negative regulator of activated transcription.";
RL Mol. Cell 2:213-222(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
RP COMPLEX.
RX PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1;
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RT "A novel human SRB/MED-containing cofactor complex, SMCC, involved in
RT transcription regulation.";
RL Mol. Cell 3:97-108(1999).
RN [8]
RP ERRATUM OF PUBMED:10024883.
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RL Mol. Cell 3:541-541(1999).
RN [9]
RP INTERACTION WITH MED6.
RX PubMed=10993082; DOI=10.1038/35024111;
RA Akoulitchev S., Chuikov S., Reinberg D.;
RT "TFIIH is negatively regulated by cdk8-containing mediator complexes.";
RL Nature 407:102-106(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH MED1 AND MED10.
RX PubMed=16595664; DOI=10.1074/jbc.m601983200;
RA Baek H.J., Kang Y.K., Roeder R.G.;
RT "Human Mediator enhances basal transcription by facilitating recruitment of
RT transcription factor IIB during preinitiation complex assembly.";
RL J. Biol. Chem. 281:15172-15181(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
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 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CDK8 AND INHIBITOR.
RX PubMed=21806996; DOI=10.1016/j.jmb.2011.07.020;
RA Schneider E.V., Bottcher J., Blaesse M., Neumann L., Huber R., Maskos K.;
RT "The structure of CDK8/CycC implicates specificity in the CDK/cyclin family
RT and reveals interaction with a deep pocket binder.";
RL J. Mol. Biol. 412:251-266(2011).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC regulated gene transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. Binds to and activates cyclin-
CC dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain)
CC of the large subunit of RNA polymerase II (RNAp II), which may inhibit
CC the formation of a transcription initiation complex.
CC {ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:8700522}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. The cylin/CDK pair formed
CC by CCNC/CDK8 also associates with the large subunit of RNA polymerase
CC II. {ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:21806996, ECO:0000269|PubMed:9734358}.
CC -!- INTERACTION:
CC P24863; Q92870-2: APBB2; NbExp=3; IntAct=EBI-395261, EBI-21535880;
CC P24863; Q9UBL3: ASH2L; NbExp=3; IntAct=EBI-395261, EBI-540797;
CC P24863; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-395261, EBI-465872;
CC P24863; Q9BX70: BTBD2; NbExp=3; IntAct=EBI-395261, EBI-710091;
CC P24863; P55212: CASP6; NbExp=3; IntAct=EBI-395261, EBI-718729;
CC P24863; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-395261, EBI-10175300;
CC P24863; P24863: CCNC; NbExp=3; IntAct=EBI-395261, EBI-395261;
CC P24863; Q00526: CDK3; NbExp=7; IntAct=EBI-395261, EBI-1245761;
CC P24863; Q00535: CDK5; NbExp=2; IntAct=EBI-395261, EBI-1041567;
CC P24863; P49336: CDK8; NbExp=37; IntAct=EBI-395261, EBI-394377;
CC P24863; P42772: CDKN2B; NbExp=3; IntAct=EBI-395261, EBI-711280;
CC P24863; Q96M91: CFAP53; NbExp=3; IntAct=EBI-395261, EBI-742422;
CC P24863; P61024: CKS1B; NbExp=3; IntAct=EBI-395261, EBI-456371;
CC P24863; O43186: CRX; NbExp=4; IntAct=EBI-395261, EBI-748171;
CC P24863; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-395261, EBI-740680;
CC P24863; Q3B820: FAM161A; NbExp=3; IntAct=EBI-395261, EBI-719941;
CC P24863; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-395261, EBI-742802;
CC P24863; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-395261, EBI-6658203;
CC P24863; O15409: FOXP2; NbExp=3; IntAct=EBI-395261, EBI-983612;
CC P24863; Q6PJQ5: FOXR2; NbExp=3; IntAct=EBI-395261, EBI-8468543;
CC P24863; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-395261, EBI-372506;
CC P24863; P14136: GFAP; NbExp=3; IntAct=EBI-395261, EBI-744302;
CC P24863; Q53GS7: GLE1; NbExp=3; IntAct=EBI-395261, EBI-1955541;
CC P24863; Q49A26: GLYR1; NbExp=3; IntAct=EBI-395261, EBI-2804292;
CC P24863; Q08379: GOLGA2; NbExp=3; IntAct=EBI-395261, EBI-618309;
CC P24863; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-395261, EBI-14103818;
CC P24863; P42858: HTT; NbExp=9; IntAct=EBI-395261, EBI-466029;
CC P24863; Q9ULR0: ISY1; NbExp=3; IntAct=EBI-395261, EBI-2557660;
CC P24863; A1A4E9: KRT13; NbExp=3; IntAct=EBI-395261, EBI-10171552;
CC P24863; P19012: KRT15; NbExp=3; IntAct=EBI-395261, EBI-739566;
CC P24863; P08779: KRT16; NbExp=3; IntAct=EBI-395261, EBI-356410;
CC P24863; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-395261, EBI-3044087;
CC P24863; Q15323: KRT31; NbExp=6; IntAct=EBI-395261, EBI-948001;
CC P24863; O76011: KRT34; NbExp=3; IntAct=EBI-395261, EBI-1047093;
CC P24863; P13473-2: LAMP2; NbExp=3; IntAct=EBI-395261, EBI-21591415;
CC P24863; P80188: LCN2; NbExp=3; IntAct=EBI-395261, EBI-11911016;
CC P24863; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-395261, EBI-741037;
CC P24863; O95983-2: MBD3; NbExp=3; IntAct=EBI-395261, EBI-11978579;
CC P24863; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-395261, EBI-10182361;
CC P24863; P50222: MEOX2; NbExp=3; IntAct=EBI-395261, EBI-748397;
CC P24863; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-395261, EBI-16439278;
CC P24863; O14880: MGST3; NbExp=3; IntAct=EBI-395261, EBI-724754;
CC P24863; P17568: NDUFB7; NbExp=3; IntAct=EBI-395261, EBI-1246238;
CC P24863; P19404: NDUFV2; NbExp=6; IntAct=EBI-395261, EBI-713665;
CC P24863; I6L9F6: NEFL; NbExp=3; IntAct=EBI-395261, EBI-10178578;
CC P24863; Q9HAN9: NMNAT1; NbExp=4; IntAct=EBI-395261, EBI-3917542;
CC P24863; Q96F24: NRBF2; NbExp=3; IntAct=EBI-395261, EBI-2362014;
CC P24863; Q02548: PAX5; NbExp=3; IntAct=EBI-395261, EBI-296331;
CC P24863; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-395261, EBI-740845;
CC P24863; Q8TD55-2: PLEKHO2; NbExp=3; IntAct=EBI-395261, EBI-12905986;
CC P24863; O60664: PLIN3; NbExp=3; IntAct=EBI-395261, EBI-725795;
CC P24863; D3DTS7: PMP22; NbExp=3; IntAct=EBI-395261, EBI-25882629;
CC P24863; Q96PV4: PNMA5; NbExp=4; IntAct=EBI-395261, EBI-10171633;
CC P24863; P78424: POU6F2; NbExp=3; IntAct=EBI-395261, EBI-12029004;
CC P24863; Q99633: PRPF18; NbExp=3; IntAct=EBI-395261, EBI-2798416;
CC P24863; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-395261, EBI-5280197;
CC P24863; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-395261, EBI-1053259;
CC P24863; P06400: RB1; NbExp=4; IntAct=EBI-395261, EBI-491274;
CC P24863; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-395261, EBI-740773;
CC P24863; Q04864-2: REL; NbExp=3; IntAct=EBI-395261, EBI-10829018;
CC P24863; P40937: RFC5; NbExp=5; IntAct=EBI-395261, EBI-712376;
CC P24863; Q8N443: RIBC1; NbExp=5; IntAct=EBI-395261, EBI-10265323;
CC P24863; P15927: RPA2; NbExp=3; IntAct=EBI-395261, EBI-621404;
CC P24863; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-395261, EBI-6257312;
CC P24863; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-395261, EBI-748621;
CC P24863; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-395261, EBI-2623095;
CC P24863; Q92529: SHC3; NbExp=3; IntAct=EBI-395261, EBI-79084;
CC P24863; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-395261, EBI-11959123;
CC P24863; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-395261, EBI-5235340;
CC P24863; Q6ZRS2-3: SRCAP; NbExp=3; IntAct=EBI-395261, EBI-12029182;
CC P24863; O75528: TADA3; NbExp=3; IntAct=EBI-395261, EBI-473249;
CC P24863; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-395261, EBI-11955057;
CC P24863; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-395261, EBI-11139477;
CC P24863; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-395261, EBI-12090309;
CC P24863; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-395261, EBI-765817;
CC P24863; Q9HCM9: TRIM39; NbExp=4; IntAct=EBI-395261, EBI-739510;
CC P24863; P61086: UBE2K; NbExp=3; IntAct=EBI-395261, EBI-473850;
CC P24863; P40337-2: VHL; NbExp=3; IntAct=EBI-395261, EBI-12157263;
CC P24863; Q9NP79: VTA1; NbExp=3; IntAct=EBI-395261, EBI-740160;
CC P24863; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-395261, EBI-11419867;
CC P24863; P17022: ZNF18; NbExp=4; IntAct=EBI-395261, EBI-8648067;
CC P24863; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-395261, EBI-743265;
CC P24863; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-395261, EBI-4395669;
CC P24863; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-395261, EBI-4395732;
CC P24863; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-395261, EBI-10240849;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P24863-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24863-2; Sequence=VSP_043075;
CC -!- TISSUE SPECIFICITY: Highest levels in pancreas. High levels in heart,
CC liver, skeletal muscle and kidney. Low levels in brain.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50825.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; M74091; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U40739; AAC50825.1; ALT_INIT; Genomic_DNA.
DR EMBL; U40728; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40729; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40730; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40731; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40732; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40733; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40734; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40735; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40736; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40737; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; U40738; AAC50825.1; JOINED; Genomic_DNA.
DR EMBL; AK298558; BAG60753.1; -; mRNA.
DR EMBL; AL137784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS34502.1; -. [P24863-1]
DR CCDS; CCDS47461.1; -. [P24863-2]
DR PIR; A40268; A40268.
DR RefSeq; NP_001013417.1; NM_001013399.1. [P24863-2]
DR RefSeq; NP_005181.2; NM_005190.3. [P24863-1]
DR PDB; 3RGF; X-ray; 2.20 A; B=1-283.
DR PDB; 4CRL; X-ray; 2.40 A; B=1-283.
DR PDB; 4F6S; X-ray; 2.60 A; B=1-283.
DR PDB; 4F6U; X-ray; 2.10 A; B=1-283.
DR PDB; 4F6W; X-ray; 2.39 A; B=1-283.
DR PDB; 4F70; X-ray; 3.00 A; B=1-283.
DR PDB; 4F7J; X-ray; 2.60 A; B=1-283.
DR PDB; 4F7L; X-ray; 2.90 A; B=1-283.
DR PDB; 4F7N; X-ray; 2.65 A; B=1-283.
DR PDB; 4F7S; X-ray; 2.20 A; B=1-283.
DR PDB; 4G6L; X-ray; 2.70 A; B=1-283.
DR PDB; 5BNJ; X-ray; 2.64 A; B=1-283.
DR PDB; 5CEI; X-ray; 2.24 A; B=1-283.
DR PDB; 5FGK; X-ray; 2.36 A; B=1-264.
DR PDB; 5HBE; X-ray; 2.38 A; B=1-264.
DR PDB; 5HBH; X-ray; 2.50 A; B=1-264.
DR PDB; 5HBJ; X-ray; 3.00 A; B=1-264.
DR PDB; 5HNB; X-ray; 2.35 A; B=1-264.
DR PDB; 5HVY; X-ray; 2.39 A; B=1-283.
DR PDB; 5I5Z; X-ray; 2.60 A; B=1-264.
DR PDB; 5ICP; X-ray; 2.18 A; B=1-264.
DR PDB; 5IDN; X-ray; 2.26 A; B=1-264.
DR PDB; 5IDP; X-ray; 2.65 A; B=1-264.
DR PDB; 5XQX; X-ray; 2.30 A; B=2-264.
DR PDB; 5XS2; X-ray; 2.04 A; B=2-264.
DR PDB; 6QTG; X-ray; 2.70 A; B=1-283.
DR PDB; 6QTJ; X-ray; 2.48 A; B=1-283.
DR PDB; 6R3S; X-ray; 2.19 A; B=1-283.
DR PDB; 6T41; X-ray; 2.45 A; B=1-283.
DR PDB; 6TPA; X-ray; 2.80 A; B=1-283.
DR PDB; 6Y0A; X-ray; 2.19 A; B=1-280.
DR PDBsum; 3RGF; -.
DR PDBsum; 4CRL; -.
DR PDBsum; 4F6S; -.
DR PDBsum; 4F6U; -.
DR PDBsum; 4F6W; -.
DR PDBsum; 4F70; -.
DR PDBsum; 4F7J; -.
DR PDBsum; 4F7L; -.
DR PDBsum; 4F7N; -.
DR PDBsum; 4F7S; -.
DR PDBsum; 4G6L; -.
DR PDBsum; 5BNJ; -.
DR PDBsum; 5CEI; -.
DR PDBsum; 5FGK; -.
DR PDBsum; 5HBE; -.
DR PDBsum; 5HBH; -.
DR PDBsum; 5HBJ; -.
DR PDBsum; 5HNB; -.
DR PDBsum; 5HVY; -.
DR PDBsum; 5I5Z; -.
DR PDBsum; 5ICP; -.
DR PDBsum; 5IDN; -.
DR PDBsum; 5IDP; -.
DR PDBsum; 5XQX; -.
DR PDBsum; 5XS2; -.
DR PDBsum; 6QTG; -.
DR PDBsum; 6QTJ; -.
DR PDBsum; 6R3S; -.
DR PDBsum; 6T41; -.
DR PDBsum; 6TPA; -.
DR PDBsum; 6Y0A; -.
DR AlphaFoldDB; P24863; -.
DR SMR; P24863; -.
DR BioGRID; 107333; 192.
DR ComplexPortal; CPX-1969; Cyclin C-CDK8 complex.
DR ComplexPortal; CPX-3232; CKM complex variant 1.
DR ComplexPortal; CPX-3263; CKM complex variant 2.
DR ComplexPortal; CPX-330; Cyclin C-CDK3 complex.
DR CORUM; P24863; -.
DR DIP; DIP-32920N; -.
DR IntAct; P24863; 124.
DR MINT; P24863; -.
DR STRING; 9606.ENSP00000428982; -.
DR BindingDB; P24863; -.
DR ChEMBL; CHEMBL3038474; -.
DR ChEMBL; CHEMBL3883323; -.
DR iPTMnet; P24863; -.
DR PhosphoSitePlus; P24863; -.
DR SwissPalm; P24863; -.
DR BioMuta; CCNC; -.
DR DMDM; 166214910; -.
DR EPD; P24863; -.
DR jPOST; P24863; -.
DR MassIVE; P24863; -.
DR MaxQB; P24863; -.
DR PaxDb; P24863; -.
DR PeptideAtlas; P24863; -.
DR PRIDE; P24863; -.
DR ProteomicsDB; 54234; -. [P24863-1]
DR ProteomicsDB; 54235; -. [P24863-2]
DR Antibodypedia; 4188; 360 antibodies from 32 providers.
DR DNASU; 892; -.
DR Ensembl; ENST00000520429.6; ENSP00000428982.1; ENSG00000112237.13. [P24863-1]
DR Ensembl; ENST00000523799.5; ENSP00000430014.1; ENSG00000112237.13. [P24863-2]
DR Ensembl; ENST00000523985.5; ENSP00000430119.1; ENSG00000112237.13. [P24863-2]
DR GeneID; 892; -.
DR KEGG; hsa:892; -.
DR MANE-Select; ENST00000520429.6; ENSP00000428982.1; NM_005190.4; NP_005181.2.
DR UCSC; uc003pqd.4; human. [P24863-1]
DR CTD; 892; -.
DR DisGeNET; 892; -.
DR GeneCards; CCNC; -.
DR HGNC; HGNC:1581; CCNC.
DR HPA; ENSG00000112237; Low tissue specificity.
DR MIM; 123838; gene.
DR neXtProt; NX_P24863; -.
DR OpenTargets; ENSG00000112237; -.
DR PharmGKB; PA26149; -.
DR VEuPathDB; HostDB:ENSG00000112237; -.
DR eggNOG; KOG0794; Eukaryota.
DR GeneTree; ENSGT00940000155625; -.
DR InParanoid; P24863; -.
DR OMA; SHHQQWL; -.
DR PhylomeDB; P24863; -.
DR PathwayCommons; P24863; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; P24863; -.
DR SIGNOR; P24863; -.
DR BioGRID-ORCS; 892; 281 hits in 1107 CRISPR screens.
DR ChiTaRS; CCNC; human.
DR GeneWiki; CCNC_(gene); -.
DR GenomeRNAi; 892; -.
DR Pharos; P24863; Tbio.
DR PRO; PR:P24863; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P24863; protein.
DR Bgee; ENSG00000112237; Expressed in parotid gland and 207 other tissues.
DR ExpressionAtlas; P24863; baseline and differential.
DR Genevisible; P24863; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0045023; P:G0 to G1 transition; IDA:ComplexPortal.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR006671; Cyclin_N.
DR InterPro; IPR028367; CyclinC/Ssn8.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF7; PTHR10026:SF7; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cyclin; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..283
FT /note="Cyclin-C"
FT /id="PRO_0000080420"
FT DOMAIN 46..144
FT /note="Cyclin N-terminal"
FT REGION 252..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043075"
FT TURN 1..3
FT /evidence="ECO:0007829|PDB:4F6U"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:5XS2"
FT TURN 26..31
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 34..54
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:5XS2"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:5XS2"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5HBE"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:5XS2"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:5XS2"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:5XS2"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:4F7S"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:5XS2"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5XS2"
SQ SEQUENCE 283 AA; 33243 MW; CF8AC5E94E621F4C CRC64;
MAGNFWQSSH YLQWILDKQD LLKERQKDLK FLSEEEYWKL QIFFTNVIQA LGEHLKLRQQ
VIATATVYFK RFYARYSLKS IDPVLMAPTC VFLASKVEEF GVVSNTRLIA AATSVLKTRF
SYAFPKEFPY RMNHILECEF YLLELMDCCL IVYHPYRPLL QYVQDMGQED MLLPLAWRIV
NDTYRTDLCL LYPPFMIALA CLHVACVVQQ KDARQWFAEL SVDMEKILEI IRVILKLYEQ
WKNFDERKEM ATILSKMPKP KPPPNSEGEQ GPNGSQNSSY SQS
