CCNH_HUMAN
ID CCNH_HUMAN Reviewed; 323 AA.
AC P51946; Q53X72; Q8TBL9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Cyclin-H;
DE AltName: Full=MO15-associated protein;
DE AltName: Full=p34;
DE AltName: Full=p37;
GN Name=CCNH;
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], AND PROTEIN SEQUENCE OF 2-20; 106-133 AND
RP 256-279.
RC TISSUE=Liver;
RX PubMed=8078587; DOI=10.1038/371254a0;
RA Maekelae T.P., Tassan J.-P., Nigg E.A., Frutiger S., Hughes G.J.,
RA Weinberg R.A.;
RT "A cyclin associated with the CDK-activating kinase MO15.";
RL Nature 371:254-257(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 10-21; 90-102 AND
RP 190-197.
RX PubMed=8069918; DOI=10.1016/0092-8674(94)90535-5;
RA Fisher R.P., Morgan D.O.;
RT "A novel cyclin associates with MO15/CDK7 to form the CDK-activating
RT kinase.";
RL Cell 78:713-724(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-270.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-28; VAL-54; ARG-138 AND
RP ALA-270.
RG NIEHS SNPs program;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-270.
RC TISSUE=Bone marrow, Brain, Embryonic brain, and Urinary bladder;
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 FUNCTION.
RX PubMed=7533895; DOI=10.1038/374283a0;
RA Shiekhattar R., Mermelstein F., Fisher R.P., Drapkin R., Dynlacht B.,
RA Wessling H.C., Morgan D.O., Reinberg D.;
RT "Cdk-activating kinase complex is a component of human transcription factor
RT TFIIH.";
RL Nature 374:283-287(1995).
RN [7]
RP IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines that
RT conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [8]
RP FUNCTION.
RX PubMed=10024882; DOI=10.1016/s1097-2765(00)80177-x;
RA Tirode F., Busso D., Coin F., Egly J.-M.;
RT "Reconstitution of the transcription factor TFIIH: assignment of functions
RT for the three enzymatic subunits, XPB, XPD, and cdk7.";
RL Mol. Cell 3:87-95(1999).
RN [9]
RP PHOSPHORYLATION AT SER-5 AND SER-304, AND MUTAGENESIS OF SER-5 AND SER-304.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, 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-132; THR-315 AND SER-322, 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 THR-315, AND IDENTIFICATION BY
RP 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 THR-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315 AND SER-322, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND IDENTIFICATION BY
RP 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-132 AND THR-315, AND
RP IDENTIFICATION BY 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 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8836101; DOI=10.1038/nsb1096-849;
RA Kim K.K., Chamberlin H.M., Morgan D.O., Kim S.-H.;
RT "Three-dimensional structure of human cyclin H, a positive regulator of the
RT CDK-activating kinase.";
RL Nat. Struct. Biol. 3:849-855(1996).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-287.
RX PubMed=9118957; DOI=10.1093/emboj/16.5.958;
RA Andersen G., Busso D., Poterszman A., Hwang J.R., Wurtz J.-M., Ripp R.,
RA Thierry J.-C., Egly J.-M., Moras D.;
RT "The structure of cyclin H: common mode of kinase activation and specific
RT features.";
RL EMBO J. 16:958-967(1997).
CC -!- FUNCTION: Regulates CDK7, the catalytic subunit of the CDK-activating
CC kinase (CAK) enzymatic complex. CAK activates the cyclin-associated
CC kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK
CC complexed to the core-TFIIH basal transcription factor activates RNA
CC polymerase II by serine phosphorylation of the repetitive C-terminal
CC domain (CTD) of its large subunit (POLR2A), allowing its escape from
CC the promoter and elongation of the transcripts. Involved in cell cycle
CC control and in RNA transcription by RNA polymerase II. Its expression
CC and activity are constant throughout the cell cycle.
CC {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:7533895}.
CC -!- SUBUNIT: Associates primarily with CDK7 and MAT1 to form the CAK
CC complex. CAK can further associate with the core-TFIIH to form the
CC TFIIH basal transcription factor. {ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC P51946; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-741406, EBI-2548012;
CC P51946; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-741406, EBI-739580;
CC P51946; Q8IYT3: CCDC170; NbExp=3; IntAct=EBI-741406, EBI-2808089;
CC P51946; P50991: CCT4; NbExp=3; IntAct=EBI-741406, EBI-356876;
CC P51946; P24941: CDK2; NbExp=4; IntAct=EBI-741406, EBI-375096;
CC P51946; Q00526: CDK3; NbExp=3; IntAct=EBI-741406, EBI-1245761;
CC P51946; Q00534: CDK6; NbExp=5; IntAct=EBI-741406, EBI-295663;
CC P51946; P56545: CTBP2; NbExp=5; IntAct=EBI-741406, EBI-741533;
CC P51946; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-741406, EBI-742054;
CC P51946; Q9UNI6: DUSP12; NbExp=7; IntAct=EBI-741406, EBI-715161;
CC P51946; Q08379: GOLGA2; NbExp=9; IntAct=EBI-741406, EBI-618309;
CC P51946; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-741406, EBI-717919;
CC P51946; Q6P597: KLC3; NbExp=4; IntAct=EBI-741406, EBI-1643885;
CC P51946; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-741406, EBI-348259;
CC P51946; Q9Y216: MTMR7; NbExp=6; IntAct=EBI-741406, EBI-10293003;
CC P51946; O14777: NDC80; NbExp=3; IntAct=EBI-741406, EBI-715849;
CC P51946; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-741406, EBI-79165;
CC P51946; Q13136: PPFIA1; NbExp=6; IntAct=EBI-741406, EBI-745426;
CC P51946; P25786: PSMA1; NbExp=9; IntAct=EBI-741406, EBI-359352;
CC P51946; P10276: RARA; NbExp=2; IntAct=EBI-741406, EBI-413374;
CC P51946; Q15669: RHOH; NbExp=3; IntAct=EBI-741406, EBI-1244971;
CC P51946; P31947: SFN; NbExp=4; IntAct=EBI-741406, EBI-476295;
CC P51946; O95295: SNAPIN; NbExp=3; IntAct=EBI-741406, EBI-296723;
CC P51946; O60504: SORBS3; NbExp=3; IntAct=EBI-741406, EBI-741237;
CC P51946; Q9Y2D8: SSX2IP; NbExp=4; IntAct=EBI-741406, EBI-2212028;
CC P51946; Q99081-3: TCF12; NbExp=3; IntAct=EBI-741406, EBI-11952764;
CC P51946; P15884-3: TCF4; NbExp=3; IntAct=EBI-741406, EBI-13636688;
CC P51946; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-741406, EBI-11059915;
CC P51946; Q8N720: ZNF655; NbExp=3; IntAct=EBI-741406, EBI-625509;
CC P51946; O60232: ZNRD2; NbExp=4; IntAct=EBI-741406, EBI-741415;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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/ccnh/";
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DR EMBL; U11791; AAA21361.1; -; mRNA.
DR EMBL; U12685; AAA57006.1; -; mRNA.
DR EMBL; CR407658; CAG28586.1; -; mRNA.
DR EMBL; AF477979; AAL74271.1; -; Genomic_DNA.
DR EMBL; BC005280; AAH05280.1; -; mRNA.
DR EMBL; BC016705; AAH16705.1; -; mRNA.
DR EMBL; BC016823; AAH16823.1; -; mRNA.
DR EMBL; BC022351; AAH22351.1; -; mRNA.
DR CCDS; CCDS4064.1; -.
DR PIR; I38731; I38731.
DR RefSeq; NP_001230.1; NM_001239.3.
DR PDB; 1JKW; X-ray; 2.60 A; A=1-323.
DR PDB; 1KXU; X-ray; 2.60 A; A=1-323.
DR PDB; 6O9L; EM; 7.20 A; 9=1-323.
DR PDB; 6XBZ; EM; 2.80 A; I=1-323.
DR PDB; 6XD3; EM; 3.30 A; I=1-323.
DR PDB; 7B5O; EM; 2.50 A; I=1-323.
DR PDB; 7B5Q; EM; 2.50 A; I=1-323.
DR PDB; 7EGB; EM; 3.30 A; 9=1-323.
DR PDB; 7EGC; EM; 3.90 A; 9=1-323.
DR PDB; 7ENA; EM; 4.07 A; 9=1-323.
DR PDB; 7ENC; EM; 4.13 A; 9=1-323.
DR PDB; 7LBM; EM; 4.80 A; f=1-323.
DR PDB; 7NVR; EM; 4.50 A; 9=1-323.
DR PDBsum; 1JKW; -.
DR PDBsum; 1KXU; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6XBZ; -.
DR PDBsum; 6XD3; -.
DR PDBsum; 7B5O; -.
DR PDBsum; 7B5Q; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; P51946; -.
DR SMR; P51946; -.
DR BioGRID; 107342; 83.
DR ComplexPortal; CPX-578; Cyclin-dependent protein kinase-activating kinase complex.
DR CORUM; P51946; -.
DR DIP; DIP-5996N; -.
DR IntAct; P51946; 95.
DR MINT; P51946; -.
DR STRING; 9606.ENSP00000256897; -.
DR BindingDB; P51946; -.
DR ChEMBL; CHEMBL2111288; -.
DR ChEMBL; CHEMBL3038473; -.
DR ChEMBL; CHEMBL4523632; -.
DR GlyGen; P51946; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51946; -.
DR PhosphoSitePlus; P51946; -.
DR BioMuta; CCNH; -.
DR DMDM; 1706232; -.
DR EPD; P51946; -.
DR jPOST; P51946; -.
DR MassIVE; P51946; -.
DR MaxQB; P51946; -.
DR PaxDb; P51946; -.
DR PeptideAtlas; P51946; -.
DR PRIDE; P51946; -.
DR ProteomicsDB; 56451; -.
DR Antibodypedia; 12934; 540 antibodies from 37 providers.
DR DNASU; 902; -.
DR Ensembl; ENST00000256897.9; ENSP00000256897.4; ENSG00000134480.16.
DR GeneID; 902; -.
DR KEGG; hsa:902; -.
DR MANE-Select; ENST00000256897.9; ENSP00000256897.4; NM_001239.4; NP_001230.1.
DR UCSC; uc003kjb.4; human.
DR CTD; 902; -.
DR DisGeNET; 902; -.
DR GeneCards; CCNH; -.
DR HGNC; HGNC:1594; CCNH.
DR HPA; ENSG00000134480; Low tissue specificity.
DR MalaCards; CCNH; -.
DR MIM; 601953; gene.
DR neXtProt; NX_P51946; -.
DR OpenTargets; ENSG00000134480; -.
DR PharmGKB; PA26159; -.
DR VEuPathDB; HostDB:ENSG00000134480; -.
DR eggNOG; KOG2496; Eukaryota.
DR GeneTree; ENSGT00390000008634; -.
DR InParanoid; P51946; -.
DR PhylomeDB; P51946; -.
DR TreeFam; TF101008; -.
DR PathwayCommons; P51946; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR SignaLink; P51946; -.
DR SIGNOR; P51946; -.
DR BioGRID-ORCS; 902; 739 hits in 1087 CRISPR screens.
DR ChiTaRS; CCNH; human.
DR EvolutionaryTrace; P51946; -.
DR GeneWiki; Cyclin_H; -.
DR GenomeRNAi; 902; -.
DR Pharos; P51946; Tbio.
DR PRO; PR:P51946; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P51946; protein.
DR Bgee; ENSG00000134480; Expressed in calcaneal tendon and 199 other tissues.
DR ExpressionAtlas; P51946; baseline and differential.
DR Genevisible; P51946; HS.
DR GO; GO:0070516; C:CAK-ERCC2 complex; IDA:UniProtKB.
DR GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:UniProtKB.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; 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:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ARUK-UCL.
DR CDD; cd00043; CYCLIN; 1.
DR DisProt; DP00307; -.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR031658; Cyclin_C_2.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR027081; CyclinH/Ccl1.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF16899; Cyclin_C_2; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR TIGRFAMs; TIGR00569; ccl1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cyclin; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..323
FT /note="Cyclin-H"
FT /id="PRO_0000080471"
FT REGION 297..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine; by CDK8"
FT /evidence="ECO:0000269|PubMed:10993082"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine; by CDK8"
FT /evidence="ECO:0000269|PubMed:10993082"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 28
FT /note="R -> L (in dbSNP:rs2234942)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_013067"
FT VARIANT 54
FT /note="M -> V (in dbSNP:rs3093785)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_013068"
FT VARIANT 138
FT /note="K -> R (in dbSNP:rs2266691)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_013069"
FT VARIANT 270
FT /note="V -> A (in dbSNP:rs2230641)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_013070"
FT MUTAGEN 5
FT /note="S->A: No effect on the transcriptional activity of
FT the reconstituted TFIIH complex."
FT /evidence="ECO:0000269|PubMed:10993082"
FT MUTAGEN 304
FT /note="S->A: No effect on the transcriptional activity of
FT the reconstituted TFIIH complex."
FT /evidence="ECO:0000269|PubMed:10993082"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 16..37
FT /evidence="ECO:0007829|PDB:7B5O"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1JKW"
FT HELIX 50..69
FT /evidence="ECO:0007829|PDB:7B5O"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:7B5Q"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:7B5O"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:7B5O"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 133..153
FT /evidence="ECO:0007829|PDB:7B5O"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1KXU"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:7B5O"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1KXU"
FT HELIX 242..260
FT /evidence="ECO:0007829|PDB:7B5O"
FT HELIX 267..282
FT /evidence="ECO:0007829|PDB:7B5O"
SQ SEQUENCE 323 AA; 37643 MW; BB48D55DA397A0E4 CRC64;
MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP HEEMTLCKYY
EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI
LENPEILRKT ADDFLNRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE
NRTCLSQLLD IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD
DYVSKKSKHE EEEWTDDDLV ESL
