ID   HEXI2_MOUSE             Reviewed;         313 AA.
AC   Q3TVI4; Q9D4C7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 122.
DE   RecName: Full=Protein HEXIM2;
GN   Name=Hexim2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-80, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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=BAB30344.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK016624; BAB30344.1; ALT_FRAME; mRNA.
DR   EMBL; AK140145; BAE24255.1; -; mRNA.
DR   EMBL; AK160110; BAE35634.1; -; mRNA.
DR   EMBL; AL662804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL731805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026458; AAH26458.1; -; mRNA.
DR   EMBL; BC115597; AAI15598.1; -; mRNA.
DR   EMBL; BC115598; AAI15599.1; -; mRNA.
DR   CCDS; CCDS25514.1; -.
DR   RefSeq; NP_001123987.1; NM_001130515.1.
DR   RefSeq; NP_001123988.1; NM_001130516.1.
DR   RefSeq; NP_081934.1; NM_027658.2.
DR   RefSeq; XP_006534291.1; XM_006534228.2.
DR   RefSeq; XP_006534292.1; XM_006534229.2.
DR   RefSeq; XP_006534293.1; XM_006534230.2.
DR   RefSeq; XP_006534294.1; XM_006534231.3.
DR   AlphaFoldDB; Q3TVI4; -.
DR   SMR; Q3TVI4; -.
DR   IntAct; Q3TVI4; 1.
DR   STRING; 10090.ENSMUSP00000053678; -.
DR   iPTMnet; Q3TVI4; -.
DR   PhosphoSitePlus; Q3TVI4; -.
DR   EPD; Q3TVI4; -.
DR   jPOST; Q3TVI4; -.
DR   MaxQB; Q3TVI4; -.
DR   PaxDb; 10090-ENSMUSP00000053678; -.
DR   PeptideAtlas; Q3TVI4; -.
DR   ProteomicsDB; 273336; -.
DR   Antibodypedia; 17593; 194 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000062530.5; ENSMUSP00000053678.5; ENSMUSG00000043372.13.
DR   Ensembl; ENSMUST00000107037.8; ENSMUSP00000102652.2; ENSMUSG00000043372.13.
DR   GeneID; 71059; -.
DR   KEGG; mmu:71059; -.
DR   UCSC; uc007ltp.2; mouse.
DR   AGR; MGI:1918309; -.
DR   CTD; 124790; -.
DR   MGI; MGI:1918309; Hexim2.
DR   VEuPathDB; HostDB:ENSMUSG00000043372; -.
DR   eggNOG; ENOG502QQP8; Eukaryota.
DR   GeneTree; ENSGT00390000002808; -.
DR   HOGENOM; CLU_066028_1_0_1; -.
DR   InParanoid; Q3TVI4; -.
DR   OMA; MWNREGS; -.
DR   OrthoDB; 2905032at2759; -.
DR   PhylomeDB; Q3TVI4; -.
DR   TreeFam; TF336851; -.
DR   BioGRID-ORCS; 71059; 0 hits in 80 CRISPR screens.
DR   PRO; PR:Q3TVI4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q3TVI4; Protein.
DR   Bgee; ENSMUSG00000043372; Expressed in primary oocyte and 150 other cell types or tissues.
DR   ExpressionAtlas; Q3TVI4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0017069; F:snRNA binding; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   Gene3D; 6.10.250.2910; -; 1.
DR   InterPro; IPR024872; HEXIM.
DR   PANTHER; PTHR13469; HEXAMETHYLENE BISACETAMIDE INDUCIBLE 1; 1.
DR   PANTHER; PTHR13469:SF3; PROTEIN HEXIM2; 1.
DR   Pfam; PF15313; HEXIM; 1.
DR   PRINTS; PR02094; HEXIMFAMILY.
DR   Genevisible; Q3TVI4; MM.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..313
FT                   /note="Protein HEXIM2"
FT                   /id="PRO_0000305268"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..142
FT                   /note="Interaction with P-TEFb"
FT                   /evidence="ECO:0000250"
FT   REGION          155..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..286
FT                   /note="Interaction with CCNT1, HEXIM1 and HEXIM2"
FT                   /evidence="ECO:0000250"
FT   REGION          267..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          207..276
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MH2"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   313 AA;  35397 MW;  37DC31F063D7C60A CRC64;
     MATVNHTNCN TASPAALEEA KTSGGLRSPQ IAHEPHDFGG SQLLPSGQEI QSEDEGTVPA
     GDGSSCNIRG SRTQSPGGCS VEAVLARKKH RRRPSKRKRH WRPYLELSWA EKQQRDERQS
     QRASRVREEM FAKGQPLAPY NTTQFLMNDR DLEEPNLDVL HGPSHSGSGG ENEAGDSDGQ
     GRAHGEFQQR DFSEAYERYH TESLQGRSKQ ELVRDYLDLE RRLSQAEQET RRLRQLQGCS
     SRQPCQQVEE LAAEVERLRT ENQRLRQENE MWNREGGYCD QEKPASEGTP WPKVEAPFQT
     HTGQLGHREA GDR
//