ID   CCNH_MACFA              Reviewed;         323 AA.
AC   Q4R7U4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cyclin-H;
GN   Name=CCNH; ORFNames=QtsA-14371;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB168718; BAE00828.1; -; mRNA.
DR   RefSeq; NP_001271512.1; NM_001284583.1.
DR   AlphaFoldDB; Q4R7U4; -.
DR   SMR; Q4R7U4; -.
DR   STRING; 9541.XP_005557386.1; -.
DR   GeneID; 101865367; -.
DR   CTD; 902; -.
DR   eggNOG; KOG2496; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:UniProt.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR   GO; GO:0070985; C:transcription factor TFIIK complex; IEA:InterPro.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell cycle; Cyclin; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..323
FT                   /note="Cyclin-H"
FT                   /id="PRO_0000273975"
FT   REGION          299..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..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         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;  37681 MW;  52505C5FDCA2E706 CRC64;
     MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP HEEMTLCKYY
     EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
     SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI
     LENPEILRKT ADDFLNRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLRE
     NRTCLSQLLD IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD
     DYVPKKSKHE EEEWTDDDLV ESL