CCNT1_PANTR
ID CCNT1_PANTR Reviewed; 725 AA.
AC Q8HXN7;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cyclin-T1;
DE Short=CycT1;
DE Short=Cyclin-T;
GN Name=CCNT1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12441807; DOI=10.1097/00002030-200211220-00015;
RA Rollman E.N., Lund L.H., Sjostrand D.E., Leitner T., Wahren B.E.;
RT "A unique amino acid deletion in the chimpanzee cyclin T1 does not affect
RT Tat trans-activation of HIV.";
RL AIDS 16:2335-2337(2002).
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). In case of SIV infection, binds to the nuclear transcriptional
CC activator Tat, increasing Tat's affinity for the transactivating
CC response RNA element (TAR RNA). Serves as an essential cofactor for
CC Tat, by promoting RNA Pol II activation, allowing transcription of
CC viral genes.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF520776; AAN73282.1; -; mRNA.
DR RefSeq; NP_001009054.1; NM_001009054.1.
DR AlphaFoldDB; Q8HXN7; -.
DR SMR; Q8HXN7; -.
DR STRING; 9598.ENSPTRP00000008350; -.
DR PaxDb; Q8HXN7; -.
DR Ensembl; ENSPTRT00000009038; ENSPTRP00000008350; ENSPTRG00000004883.
DR GeneID; 450146; -.
DR KEGG; ptr:450146; -.
DR CTD; 904; -.
DR VGNC; VGNC:5328; CCNT1.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000159544; -.
DR HOGENOM; CLU_012994_1_0_1; -.
DR InParanoid; Q8HXN7; -.
DR OrthoDB; 1437076at2759; -.
DR TreeFam; TF101014; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000004883; Expressed in spleen and 21 other tissues.
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 2: Evidence at transcript 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..725
FT /note="Cyclin-T1"
FT /id="PRO_0000080494"
FT REGION 359..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..424
FT /evidence="ECO:0000255"
FT MOTIF 252..269
FT /note="Nuclear localization signal, and interaction with
FT Tat-TAR RNA"
FT /evidence="ECO:0000255"
FT COMPBIAS 486..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 260
FT /note="Essential for interacting with SIV Tat"
FT /evidence="ECO:0000250"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 389
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 341
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
SQ SEQUENCE 725 AA; 80569 MW; A21C398F6A4378A1 CRC64;
MEGERKNNKR WYFTREQLEN SPSRRFGVDP DKELSYRQQA ANLLQDMGQR LNVSQLTINT
AIVYMHRFYM IQSFTQFPGN SVAPAALFLA AKVEEQPKKL EHVIKVAHTC LHPQESLPDT
RSEAYLQQVQ DLVILESIIL QTLGFELTID HPHTHVVKCT QLVRASKDLA QTSYFMATNS
LHLTTFSLQY TPPVVACVCI HLACKWSNWE IPVSTDGKHW WEYVDATVTL ELLDELTHEF
LQILEKTPNR LKRIWNWRAC EAAKKTKADD RGTDEKTSEQ TILNMISQSS SDTTIAGLMS
MSTSTTSAVP SLPVSEESSS NLTSVEMLPG KRWLSSQPSF KLEPTQGHRT SENLALTGVD
HSLPQDGSNA FISQKQNSKS VPSAKVSLKE YRAKHAEELA AQKRQLENME ANVKSQYAYA
AQNLLSHHDS HSSVILKMPI EGSENPERPF LEKADKTALK MRIPVAGGDK AASSKPEEIK
MRIKVHAAAD KHNSVEDSVT KSREHKEKHK THPSNHHHHH NHHSHKHSHS QLPVGTGNKR
PGDPKHSSQT SNLAHKTYSL SSSFSSSSST RKRGPSEETG GAVFDHPAKI AKSTKSSSLN
FSFPSLPTMA QMPGHSSDTS GLSFSQPSCK TRVPHSKLDK GPTGANGHNT TQTIDYQDTV
NMLHSLLSAQ GVQPTQPTAF EFVRPYSDYL NPRAGGISSR SGNTDKPRPP PLPSEPPPPL
PPLPK
