ID   HEXI2_BOVIN             Reviewed;         287 AA.
AC   Q0X0E2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Protein HEXIM2;
GN   Name=HEXIM2;
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 (DEC-2004) 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.
CC       {ECO:0000250|UniProtKB:Q96MH2}.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with HEXIM1; 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 CCNT2. {ECO:0000250|UniProtKB:Q96MH2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96MH2}.
CC   -!- DOMAIN: The coiled-coil domain mediates oligomerization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HEXIM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF02367.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB196139; BAF02367.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; Q0X0E2; -.
DR   SMR; Q0X0E2; -.
DR   STRING; 9913.ENSBTAP00000034708; -.
DR   PaxDb; Q0X0E2; -.
DR   eggNOG; ENOG502QQP8; Eukaryota.
DR   HOGENOM; CLU_066028_1_0_1; -.
DR   InParanoid; Q0X0E2; -.
DR   Proteomes; UP000009136; Unplaced.
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: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   InterPro; IPR024872; HEXIM.
DR   InterPro; IPR024876; HEXIM2.
DR   PANTHER; PTHR13469; PTHR13469; 1.
DR   PANTHER; PTHR13469:SF3; PTHR13469:SF3; 1.
DR   Pfam; PF15313; HEXIM; 1.
DR   PRINTS; PR02094; HEXIMFAMILY.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..287
FT                   /note="Protein HEXIM2"
FT                   /id="PRO_0000305266"
FT   REGION          1..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..145
FT                   /note="Interaction with P-TEFb"
FT                   /evidence="ECO:0000250"
FT   REGION          227..287
FT                   /note="Interaction with CCNT1, HEXIM1 and HEXIM2"
FT                   /evidence="ECO:0000250"
FT   REGION          266..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          208..278
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        89..103
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
SQ   SEQUENCE   287 AA;  32804 MW;  8932AD5FCD2E41C3 CRC64;
     MKDWEQKKVA SPNQPPPAAL EEAKISGTCG SPRTSPEPHD PGGSQPLTPR MESHSEEEDR
     PGAGGGLGWN GRSPRTQSLG ACSAEAMLAR KKHRRRPSKR KRHWRPYLEL SWAEKQQRDE
     RQSQRASRVR EEMFAKGQPV APYNTTQFLM NDRDPEEPNL VPQGASHPGS SGESEAGDSD
     GQGRARGEFQ QKDFSEAYER YHTESLQGRS KEELVRDYLD LERRLSQAEE EMRRLRQLRG
     CTNWRPCYQV EELAAEVERL RTENQRLRQE NEMWNREGGR RGGQPGS