CCNT1_BOVIN
ID CCNT1_BOVIN Reviewed; 727 AA.
AC Q6T8E9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cyclin-T1;
DE Short=CycT1;
GN Name=CCNT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BIV TAT (MICROBIAL
RP INFECTION).
RX PubMed=14972556; DOI=10.1016/j.virol.2003.10.003;
RA Das C., Edgcomb S.P., Peteranderl R., Chen L., Frankel A.D.;
RT "Evidence for conformational flexibility in the Tat-TAR recognition motif
RT of cyclin T1.";
RL Virology 318:306-317(2004).
CC -!- FUNCTION: Regulatory subunit of the cyclin-dependent kinase pair
CC (CDK9/cyclin-T1) complex, also called positive transcription elongation
CC factor B (P-TEFb), which is proposed to facilitate the transition from
CC abortive to productive elongation by phosphorylating the CTD (C-
CC terminal domain) of the large subunit of RNA polymerase II (RNA Pol
CC II). {ECO:0000250}.
CC -!- SUBUNIT: Cyclin-T1 is the predominant cyclin that associates with CDK9
CC to form a heterodimer called P-TEFb. P-TEFb forms a complex with
CC AFF4/AF5Q31. Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin.
CC Component of the 7SK snRNP complex at least composed of P-TEFb
CC (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3
CC proteins and 7SK and U6 snRNAs. Interacts with BRD4, targets chromatin
CC binding. Interacts with JMJD6. Interacts with MDFIC. Interacts with
CC HSF1. Interacts with HTATSF1. Interacts with AFF4. Interacts with
CC TBX21. {ECO:0000250|UniProtKB:O60563}.
CC -!- SUBUNIT: (Microbial infection) Binds to BIV Tat, however Tat binds TAR
CC RNA in a Cyc-T1-independent mode. {ECO:0000269|PubMed:14972556}.
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; AY428555; AAQ93805.1; -; mRNA.
DR RefSeq; NP_001001147.1; NM_001001147.1.
DR AlphaFoldDB; Q6T8E9; -.
DR SMR; Q6T8E9; -.
DR STRING; 9913.ENSBTAP00000007703; -.
DR PaxDb; Q6T8E9; -.
DR PRIDE; Q6T8E9; -.
DR Ensembl; ENSBTAT00000007703; ENSBTAP00000007703; ENSBTAG00000005861.
DR GeneID; 407194; -.
DR KEGG; bta:407194; -.
DR CTD; 904; -.
DR VEuPathDB; HostDB:ENSBTAG00000005861; -.
DR VGNC; VGNC:26978; CCNT1.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000159544; -.
DR HOGENOM; CLU_012994_1_0_1; -.
DR InParanoid; Q6T8E9; -.
DR OMA; PSMFEYR; -.
DR OrthoDB; 1437076at2759; -.
DR TreeFam; TF101014; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000005861; Expressed in neutrophil and 110 other tissues.
DR ExpressionAtlas; Q6T8E9; baseline and differential.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070691; C:P-TEFb complex; IEA:Ensembl.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1903655; P:phosphorylation of RNA polymerase II C-terminal domain serine 2 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:1903654; P:phosphorylation of RNA polymerase II C-terminal domain serine 5 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR028863; CCNT1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF42; PTHR10026:SF42; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cyclin;
KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..727
FT /note="Cyclin-T1"
FT /id="PRO_0000236233"
FT REGION 487..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..420
FT /evidence="ECO:0000255"
FT MOTIF 253..270
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 487..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..531
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 391
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
SQ SEQUENCE 727 AA; 81307 MW; 6F3CD78B1CD52D59 CRC64;
MEGERKNNNK RWYFTREQLE NSPSRRFGLD PDKELSNRQQ AANLLQDMGQ RLNVSQLTIN
TAIVYMHRFY MIQSFTQFHR NSVAPAALFL AAKVEEQPKK LEHVIKVAHT CLHPQESLPD
TRSEAYLQQV QDLVILESII LQTLGFELTI DHPHTHVVKC TQLVRASKDL AQTSYFMATN
SLHLTTFSLQ YTPPVVACVC IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE
FLQILEKTPN RLKRIWNWRA WQADRKTKAD DRGADENSSE QTILNMISQS SSDTTIAGLM
SMSASSTTSA VPSLPATEDS KSNLSNVEML SSERWLSSHP PFKVEPAQGY RKSENLALVG
ADHSLQQDGS NAFVSQKQNS KSVPSAKVSL KEYRAKHAEE LAAQKRQLEN MEANVKSQYA
YAAQNLLSHH DSHSSVILKM PIEGSENPER PFLEKTDKTA LKMRIPMTGG DKAASIKPEE
IKMRIKVHTA ADKHNSVDDS VTKNREHKEK HKTHPSNHHH HHNHHSHKHS HSQLPAGTGN
KRLGDPKHSS QTSTLAHKPY SLSSSFSSSS SSRKRPLPEE TGGVAYDHST KTAKSAKSSS
INFSFPPLPT MAQLPGHSSD TSGLHFSQPS CKTRVPHMKL DKSSTGANSH NTPQTTDYQD
TVNMLNSLLN AQGVQPTQPP AFEYVHSYGE YMNPRAGGMS SRSGNTDKPR PPPLPSEPPP
PLPPLPK
