CCNH_RAT
ID CCNH_RAT Reviewed; 323 AA.
AC Q9R1A0; Q99JE5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cyclin-H;
GN Name=Ccnh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RX PubMed=10501206; DOI=10.1046/j.1471-4159.1999.0731598.x;
RA Jin K., Nagayama T., Chen J., Stetler A.R., Kawaguchi K., Simon R.P.,
RA Graham S.H.;
RT "Molecular cloning of a cell cycle regulation gene cyclin H from ischemic
RT rat brain: expression in neurons after global cerebral ischemia.";
RL J. Neurochem. 73:1598-1608(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11252168; DOI=10.1007/s003350010268;
RA Laes J.-F., Quan X., Ravoet M., van Vooren P., van Reeth T., Szpirer J.,
RA Szpirer C.;
RT "Analysis of candidate genes included in the mammary cancer susceptibility
RT 1 (Mcs1) region.";
RL Mamm. Genome 12:199-206(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; AF154914; AAD46521.1; -; mRNA.
DR EMBL; AJ276495; CAC37406.1; -; mRNA.
DR EMBL; BC059109; AAH59109.1; -; mRNA.
DR RefSeq; NP_443213.2; NM_052981.2.
DR AlphaFoldDB; Q9R1A0; -.
DR SMR; Q9R1A0; -.
DR STRING; 10116.ENSRNOP00000039039; -.
DR iPTMnet; Q9R1A0; -.
DR PhosphoSitePlus; Q9R1A0; -.
DR PaxDb; Q9R1A0; -.
DR PRIDE; Q9R1A0; -.
DR Ensembl; ENSRNOT00000049423; ENSRNOP00000039039; ENSRNOG00000031656.
DR GeneID; 84389; -.
DR KEGG; rno:84389; -.
DR UCSC; RGD:69419; rat.
DR CTD; 902; -.
DR RGD; 69419; Ccnh.
DR eggNOG; KOG2496; Eukaryota.
DR GeneTree; ENSGT00390000008634; -.
DR HOGENOM; CLU_022620_0_0_1; -.
DR InParanoid; Q9R1A0; -.
DR OMA; FRVEQNT; -.
DR OrthoDB; 1469819at2759; -.
DR PhylomeDB; Q9R1A0; -.
DR TreeFam; TF101008; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-RNO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-RNO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-RNO-72086; mRNA Capping.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR PRO; PR:Q9R1A0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000031656; Expressed in heart and 20 other tissues.
DR Genevisible; Q9R1A0; RN.
DR GO; GO:0070516; C:CAK-ERCC2 complex; ISO:RGD.
DR GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:RGD.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR GO; GO:0070985; C:transcription factor TFIIK complex; ISO:RGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
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 from RNA polymerase II promoter; ISO:RGD.
DR CDD; cd00043; CYCLIN; 1.
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 Cell cycle; Cyclin; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..323
FT /note="Cyclin-H"
FT /id="PRO_0000080473"
FT REGION 296..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..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:0007744|PubMed:22673903"
FT CONFLICT 125..126
FT /note="FV -> KE (in Ref. 2; CAC37406)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> R (in Ref. 2; CAC37406)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="ML -> SR (in Ref. 1; AAD46521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 37610 MW; 7993FEDE265C2A96 CRC64;
MYHNSSQKRH WTFASEEQLA RLRADANRKF KCKAVANGKV LPNDPLFLEP HEEMTLCKYY
EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDIKTRYPM
LENPEILRKT ADDFLSRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE
NRTCLSQLLD IMKSMRNLVK KYEPPRSEEV AILKQKLERC HSSDLALNMV TKKRKGYEDD
DYVSKKPKQE EEEWTDDDLV DAL
