ID A0A1S3F6E7_DIPOR Unreviewed; 323 AA.
AC A0A1S3F6E7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cyclin-H {ECO:0000256|ARBA:ARBA00019496};
GN Name=Ccnh {ECO:0000313|RefSeq:XP_012871397.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012871397.1};
RN [1] {ECO:0000313|RefSeq:XP_012871397.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012871397.1};
RG RefSeq;
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 RefSeq; XP_012871397.1; XM_013015943.1.
DR AlphaFoldDB; A0A1S3F6E7; -.
DR STRING; 10020.ENSDORP00000001341; -.
DR GeneID; 105985402; -.
DR KEGG; dord:105985402; -.
DR CTD; 902; -.
DR InParanoid; A0A1S3F6E7; -.
DR OMA; KTTNHPI; -.
DR OrthoDB; 5481790at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0070516; C:CAK-ERCC2 complex; IEA:Ensembl.
DR GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IEA:Ensembl.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:Ensembl.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IEA:Ensembl.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:Ensembl.
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:UP000081671}.
FT DOMAIN 62..152
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 298..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 37607 MW; 51692A28E2067040 CRC64;
MYHNSSQKRH WTFASEEQLA RLRADANRKF KCKAVANGKV LPNDPVFLEP HEEMTLCKYY
EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV
SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDIKTRYPM
LENPEILRKT ADDFLNRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLRE
NRICLSQLLD TMKNMRNLVK KYEPPRSEEV AVLKQKLERC HSSELGLNVI TKKRKGYEED
GYVSKKSKQE EEEWTDDDLV DSL
//
