CCNT1_HORSE
ID CCNT1_HORSE Reviewed; 727 AA.
AC Q9XT26; Q9TTX6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cyclin-T1;
DE Short=CycT1;
DE Short=Cyclin-T;
GN Name=CCNT1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH EIAV TAT.
RC TISSUE=Fibroblast;
RX PubMed=10373508; DOI=10.1128/mcb.19.7.4592;
RA Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.;
RT "Highly divergent lentiviral Tat proteins activate viral gene expression by
RT a common mechanism.";
RL Mol. Cell. Biol. 19:4592-4599(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10623752; DOI=10.1128/jvi.74.2.892-898.2000;
RA Taube R., Fujinaga K., Irwin D., Wimmer J., Geyer M., Peterlin B.M.;
RT "Interactions between equine cyclin T1, Tat, and TAR are disrupted by a
RT leucine-to-valine substitution found in human cyclin T1.";
RL J. Virol. 74:892-898(2000).
RN [3]
RP IDENTIFICATION IN A COMPLEX WITH HTATSF1; P-TEFB AND RNA POL II.
RX PubMed=10964778; DOI=10.1006/viro.2000.0480;
RA Sune C., Goldstrohm A.C., Peng J., Price D.H., Garcia-Blanco M.A.;
RT "An in vitro transcription system that recapitulates equine infectious
RT anemia virus tat-mediated inhibition of human immunodeficiency virus type 1
RT Tat activity demonstrates a role for positive transcription elongation
RT factor b and associated proteins in the mechanism of Tat activation.";
RL Virology 274:356-366(2000).
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 production elongation by phosphorylating the CTD (C-
CC terminal domain) of the large subunit of RNA polymerase II (RNAP II)
CC (By similarity). In case of equine infectious anemia virus (EIAV)
CC infection, binds to the nuclear transcriptional activator Tat,
CC increasing Tat's affinity for the transactivating response RNA element
CC (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA
CC Pol II activation, allowing transcription of viral genes.
CC {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; AF137509; AAD38518.1; -; mRNA.
DR EMBL; AF190905; AAF04138.1; -; mRNA.
DR RefSeq; NP_001075315.1; NM_001081846.1.
DR PDB; 2W2H; X-ray; 3.25 A; A/B=5-267.
DR PDBsum; 2W2H; -.
DR AlphaFoldDB; Q9XT26; -.
DR SMR; Q9XT26; -.
DR STRING; 9796.ENSECAP00000013646; -.
DR PaxDb; Q9XT26; -.
DR GeneID; 100033893; -.
DR KEGG; ecb:100033893; -.
DR CTD; 904; -.
DR HOGENOM; CLU_012994_1_0_1; -.
DR InParanoid; Q9XT26; -.
DR OMA; PSMFEYR; -.
DR OrthoDB; 1437076at2759; -.
DR TreeFam; TF101014; -.
DR EvolutionaryTrace; Q9XT26; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 3D-structure; 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_0000080492"
FT REGION 302..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..427
FT /evidence="ECO:0000255"
FT MOTIF 253..270
FT /note="Nuclear localization signal, and interaction with
FT Tat-TAR RNA"
FT /evidence="ECO:0000255"
FT COMPBIAS 486..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..532
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..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 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT MOD_RES 566
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 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60563"
FT CONFLICT 96
FT /note="E -> G (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="R -> W (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="Q -> E (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="N -> K (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="I -> T (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="A -> V (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="A -> T (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="S -> P (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="M -> I (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="L -> P (in Ref. 2; AAF04138)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2W2H"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2W2H"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 179..184
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2W2H"
FT TURN 221..225
FT /evidence="ECO:0007829|PDB:2W2H"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:2W2H"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2W2H"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:2W2H"
SQ SEQUENCE 727 AA; 81013 MW; BFC2A398D6B35BCE CRC64;
MEGERKNNNK RWYFTREQLE NSPSRRFGLD PDKELSYRQQ AANLLQDMGQ RLNVSQLTIN
TAIVYMHRFY MIQSFTQFHR NSVAPAALFL AAKVEEQPKK LEHVIKVAHA CLHPQESLPD
TRSEAYLQQV QDLVILESII LQTLGFELTI DHPHTHVVKC TQLVRASKDL AQTSYFMATN
SLHLTTFSLQ YTPPVVACVC IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE
FLQILEKTPN RLKRIRNWRA CQAAKKTKAD DRGTDENTSE QTILNMISQS SSDTTIAGLM
SMSTSSTTST VPSLPTTEES SSNLSGVEML QGERWLSSQP PFKLEPAQGH RTSENLALIG
VDHSLQQDGS NAFISQKQNS SKSVPSAKVS LKEYRAKHAE ELAAQKRQLE NMEANVKSQY
AYAAQNLLSH HDSHSSVILK MPIEGSENPE RPFLEKPDKT ALKMRIPVAS GDKAASSKPE
EIKMRIKVHA APDKHNSIDD SVTKSREHKE KHKTHPSNHH HHHNHHSHKH SHSQLPAGTG
NKRPGDPKHS SQTSTLAHKT YSLSSSFSSS SSSRKRGPPE ETGGALFDHP AKIAKSTKSS
SINFFPPLPT MAQLPGHSSD TSGLPFSQPS CKTRVPHMKL DKGPTGANGH NTTQTIDYQD
TVNMLHSLLH AQGVQPTQPP ALEFVHSYGE YLNPRAGGMP SRSGNTDKPR LPPLPSEPPP
PLPPLPK
