HEXI2_MOUSE
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 03-AUG-2022, entry version 115.
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; Q3TVI4; -.
DR PeptideAtlas; Q3TVI4; -.
DR PRIDE; Q3TVI4; -.
DR ProteomicsDB; 273336; -.
DR Antibodypedia; 17593; 173 antibodies from 29 providers.
DR Ensembl; ENSMUST00000062530; ENSMUSP00000053678; ENSMUSG00000043372.
DR Ensembl; ENSMUST00000107037; ENSMUSP00000102652; ENSMUSG00000043372.
DR GeneID; 71059; -.
DR KEGG; mmu:71059; -.
DR UCSC; uc007ltp.2; mouse.
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; 1055089at2759; -.
DR PhylomeDB; Q3TVI4; -.
DR TreeFam; TF336851; -.
DR BioGRID-ORCS; 71059; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q3TVI4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3TVI4; protein.
DR Bgee; ENSMUSG00000043372; Expressed in primary oocyte and 147 other tissues.
DR ExpressionAtlas; Q3TVI4; baseline and differential.
DR Genevisible; Q3TVI4; MM.
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:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
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 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
