GenomeNet

Database: UniProt
Entry: CCNH_MOUSE
LinkDB: CCNH_MOUSE
Original site: CCNH_MOUSE 
ID   CCNH_MOUSE              Reviewed;         323 AA.
AC   Q61458; Q9CVJ0; Q9JHV7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Cyclin-H;
GN   Name=Ccnh;
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 [MRNA].
RC   TISSUE=Spermatocyte;
RX   PubMed=11319144; DOI=10.1095/biolreprod64.5.1400;
RA   Kim J.M., McGaughy J.T., Bogle R.K., Ravnik S.E.;
RT   "Meiotic expression of the cyclin H/Cdk7 complex in male germ cells of the
RT   mouse.";
RL   Biol. Reprod. 64:1400-1408(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-109.
RC   STRAIN=CD-1; TISSUE=Testis;
RA   Hall F.L., Wu L.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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).
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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in both the germinal and somatic cells of
CC       the testis.
CC   -!- DEVELOPMENTAL STAGE: Higher expression during spermatogenesis from the
CC       mitotic stages to the meiotic stages.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC       {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; AF287135; AAF90198.1; -; mRNA.
DR   EMBL; AK007910; BAB25343.1; -; mRNA.
DR   EMBL; AK078059; BAC37112.1; -; mRNA.
DR   EMBL; BC038861; AAH38861.1; -; mRNA.
DR   EMBL; X82441; CAA57822.1; -; mRNA.
DR   CCDS; CCDS26666.1; -.
DR   PIR; S48862; S48862.
DR   RefSeq; NP_001334516.1; NM_001347587.1.
DR   RefSeq; NP_001334517.1; NM_001347588.1.
DR   RefSeq; NP_075732.1; NM_023243.6.
DR   AlphaFoldDB; Q61458; -.
DR   SMR; Q61458; -.
DR   BioGRID; 211635; 4.
DR   ComplexPortal; CPX-3268; Cyclin-dependent protein kinase-activating kinase complex.
DR   STRING; 10090.ENSMUSP00000022030; -.
DR   iPTMnet; Q61458; -.
DR   PhosphoSitePlus; Q61458; -.
DR   EPD; Q61458; -.
DR   MaxQB; Q61458; -.
DR   PaxDb; 10090-ENSMUSP00000022030; -.
DR   ProteomicsDB; 281253; -.
DR   Pumba; Q61458; -.
DR   Antibodypedia; 12934; 621 antibodies from 37 providers.
DR   DNASU; 66671; -.
DR   Ensembl; ENSMUST00000022030.11; ENSMUSP00000022030.5; ENSMUSG00000021548.11.
DR   GeneID; 66671; -.
DR   KEGG; mmu:66671; -.
DR   UCSC; uc007riu.1; mouse.
DR   AGR; MGI:1913921; -.
DR   CTD; 902; -.
DR   MGI; MGI:1913921; Ccnh.
DR   VEuPathDB; HostDB:ENSMUSG00000021548; -.
DR   eggNOG; KOG2496; Eukaryota.
DR   GeneTree; ENSGT00390000008634; -.
DR   HOGENOM; CLU_022620_0_0_1; -.
DR   InParanoid; Q61458; -.
DR   OMA; KTTNHPI; -.
DR   OrthoDB; 5481790at2759; -.
DR   PhylomeDB; Q61458; -.
DR   TreeFam; TF101008; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR   Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   BioGRID-ORCS; 66671; 26 hits in 81 CRISPR screens.
DR   ChiTaRS; Ccnh; mouse.
DR   PRO; PR:Q61458; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q61458; Protein.
DR   Bgee; ENSMUSG00000021548; Expressed in interventricular septum and 254 other cell types or tissues.
DR   ExpressionAtlas; Q61458; baseline and differential.
DR   Genevisible; Q61458; MM.
DR   GO; GO:0070516; C:CAK-ERCC2 complex; ISO:MGI.
DR   GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; ISO:MGI.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:MGI.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR   GO; GO:0070985; C:transcription factor TFIIK complex; ISO:MGI.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:MGI.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
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; ISS:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; ISO:MGI.
DR   CDD; cd20524; CYCLIN_CCNH_rpt1; 1.
DR   CDD; cd20525; CYCLIN_CCNH_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR013763; Cyclin-like_dom.
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   NCBIfam; TIGR00569; ccl1; 1.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF8; CYCLIN-H; 1.
DR   Pfam; PF16899; Cyclin_C_2; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cyclin; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..323
FT                   /note="Cyclin-H"
FT                   /id="PRO_0000080472"
FT   REGION          295..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..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:0000250|UniProtKB:P51946"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51946"
FT   MOD_RES         304
FT                   /note="Phosphoserine; by CDK8"
FT                   /evidence="ECO:0000250|UniProtKB:P51946"
FT   MOD_RES         315
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P51946"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51946"
SQ   SEQUENCE   323 AA;  37506 MW;  C0905C879DA299A8 CRC64;
     MYHSSSQKRH WTFASEEQLA RLRADANRKF KCKAVANGKV LPNDPVFLEP HEELTLCKYY
     EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
     SSPQFVGNLR ESPLGQERAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDIKTRYPM
     LENPEILRKT ADDFLSRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE
     NRTCLSQLLD IMKSMRNLVK KYEPPRSDEV AVLKQKLERC HSSDLALNAV TKKRKGYEDD
     DYVSKKPKQE EEEWTDDDLV DSL
//
DBGET integrated database retrieval system