ID H0VB42_CAVPO Unreviewed; 251 AA.
AC H0VB42;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Cyclin-H {ECO:0000256|ARBA:ARBA00019496};
GN Name=CCNH {ECO:0000313|Ensembl:ENSCPOP00000007107.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000007107.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000007107.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000007107.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00025343}.
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:0000256|ARBA:ARBA00026042}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000256|ARBA:ARBA00008638}.
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DR EMBL; AAKN02002506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0VB42; -.
DR Ensembl; ENSCPOT00000007969.3; ENSCPOP00000007107.3; ENSCPOG00000007894.4.
DR VEuPathDB; HostDB:ENSCPOG00000007894; -.
DR GeneTree; ENSGT00390000008634; -.
DR HOGENOM; CLU_022620_0_0_1; -.
DR OMA; KTTNHPI; -.
DR TreeFam; TF101008; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000007894; Expressed in adrenal gland and 13 other cell types or tissues.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
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 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 1..78
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 223..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 29069 MW; F6AA040B200EC955 CRC64;
MPRSVVGTAC MYFKRFYLNN SVMEYHPRII MLTCAFLACK VDEFNVSSPQ FVGNLRESPL
GQEKALEQIL EYELLLIQQL NFHLIVHNPY RPFEGFLIDI KTRYPMLENP EVLRKTADDF
LNRIALTDAY LLYTPSQIAL TAILSSASRA GITMESYLSE SLMLRENRTC LSQLLDIMKS
MRNLVKKYEP PRPEEVAALK QKLERCHSAE LALNVVTKKR KGYEDDDYVS KKSKHEEEEW
TDDDLVDSLN V
//
