HEXI1_BOVIN
ID HEXI1_BOVIN Reviewed; 320 AA.
AC Q0X0C4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein HEXIM1;
GN Name=HEXIM1;
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].
RC TISSUE=Ovary;
RA Kaneyama K., Ushizawa K., Takahashi T., Hashizume K.;
RT "Cloning and expression of L3 in bovine ovarian follicles.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional regulator which functions as a general RNA
CC polymerase II transcription inhibitor. Core component of the 7SK RNP
CC complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large
CC inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation
CC and subsequent transcriptional elongation. May also regulate NF-kappa-
CC B, ESR1, NR3C1 and CIITA-dependent transcriptional activity. Plays a
CC role in the regulation of DNA virus-mediated innate immune response by
CC assembling into the HDP-RNP complex, a complex that serves as a
CC platform for IRF3 phosphorylation and subsequent innate immune response
CC activation through the cGAS-STING pathway.
CC {ECO:0000250|UniProtKB:O94992}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with HEXIM2; probably dimeric.
CC Core component of the 7SK RNP complex, at least composed of 7SK RNA,
CC LARP7, MEPCE, HEXIM1 (or HEXIM2) and P-TEFb (composed of CDK9 and
CC CCNT1/cyclin-T1). Interacts with the N-CoR complex through NCOR1.
CC Interacts with ESR1 and NR3C1. May interact with NF-kappa-B through
CC RELA. Interacts with CCNT2; mediates formation of a tripartite complex
CC with KPNA2. Part of the HDP-RNP complex composed of at least HEXIM1,
CC PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14,
CC and MATR3) and NEAT1 non-coding RNA. {ECO:0000250|UniProtKB:O94992}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94992}. Cytoplasm
CC {ECO:0000250|UniProtKB:O94992}. Note=Binds alpha-importin and is mostly
CC nuclear. {ECO:0000250|UniProtKB:O94992}.
CC -!- DOMAIN: The coiled-coil domain mediates oligomerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HEXIM family. {ECO:0000305}.
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DR EMBL; AB205339; BAF02382.1; -; mRNA.
DR EMBL; BC120426; AAI20427.1; -; mRNA.
DR RefSeq; NP_001069649.1; NM_001076181.2.
DR AlphaFoldDB; Q0X0C4; -.
DR SMR; Q0X0C4; -.
DR STRING; 9913.ENSBTAP00000007955; -.
DR PaxDb; Q0X0C4; -.
DR PRIDE; Q0X0C4; -.
DR Ensembl; ENSBTAT00000007955; ENSBTAP00000007955; ENSBTAG00000006056.
DR GeneID; 539696; -.
DR KEGG; bta:539696; -.
DR CTD; 10614; -.
DR VEuPathDB; HostDB:ENSBTAG00000006056; -.
DR VGNC; VGNC:29826; HEXIM1.
DR eggNOG; ENOG502QQP8; Eukaryota.
DR GeneTree; ENSGT00390000002808; -.
DR HOGENOM; CLU_066028_0_0_1; -.
DR InParanoid; Q0X0C4; -.
DR OMA; CHDSEAN; -.
DR OrthoDB; 1055089at2759; -.
DR TreeFam; TF336851; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000006056; Expressed in myometrium and 103 other tissues.
DR GO; GO:0120259; C:7SK snRNP; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0106140; F:P-TEFb complex binding; IEA:Ensembl.
DR GO; GO:0002218; P:activation of innate immune response; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR InterPro; IPR024872; HEXIM.
DR PANTHER; PTHR13469; PTHR13469; 2.
DR Pfam; PF15313; HEXIM; 1.
DR PRINTS; PR02094; HEXIMFAMILY.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..320
FT /note="Protein HEXIM1"
FT /id="PRO_0000305262"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..138
FT /note="Basic region; mediates nuclear localization and
FT interaction with 7SK snRNA and NR3C1"
FT /evidence="ECO:0000250"
FT REGION 163..166
FT /note="Interaction with P-TEFb"
FT /evidence="ECO:0000250"
FT REGION 171..211
FT /note="Autoinhibitory acidic region; in absence of 7SK
FT snRNA interacts with the basic region preventing
FT interaction with P-TEFb and modulating subcellular
FT localization"
FT /evidence="ECO:0000250"
FT REGION 174..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..275
FT /note="Mediates interaction with CCNT1"
FT /evidence="ECO:0000250"
FT REGION 271..316
FT /note="Required for inhibition of ESR1-dependent
FT transcription"
FT /evidence="ECO:0000250"
FT COILED 244..310
FT /evidence="ECO:0000255"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94992"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94992"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94992"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94992"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94992"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R409"
SQ SEQUENCE 320 AA; 36317 MW; 1BB5CFD0189A4F39 CRC64;
MAEPLLSEFQ HQPQTSNCTG AVAVHEERNP DRPPGAEERV PEEDSRWQSR ASPKSGGSPG
HGGEGSLEPQ PSPLKTQVCP ESSCPEAGEK GQNGDDLSAG GAPPQQRQVG KKKHRRRPSK
KKRLWKPYYT LTWEEKKKFD EKQSLRASRI RAEMFAKGQP VAPYNTTQFL MDDHDQEEPD
LKTGLYPKRA AAKSDDTSDE DFMEEAGEED GGSDGMGGDG SEFLQRDFSE TYERYHAESL
QNMSKQELIK EYLELEKCLS RMEDENNRLR LESQRLDGDD ARVRELELEL DRLRAENLQL
LTENELHRQQ ERAPLSNFGD
