ID HEXI2_HUMAN Reviewed; 286 AA. AC Q96MH2; D3DX66; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 167. DE RecName: Full=Protein HEXIM2; DE AltName: Full=Hexamethylene bis-acetamide-inducible protein 2; GN Name=HEXIM2; ORFNames=L3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15334068; DOI=10.1038/sj.onc.1207921; RA Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., RA Cerveny C., Law C.-L., Wahl A., Carter P.; RT "Suppression subtractive hybridization and expression profiling identifies RT a unique set of genes overexpressed in non-small-cell lung cancer."; RL Oncogene 23:7734-7745(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, Prostate, and Uterus; 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 [5] RP FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, AND MUTAGENESIS OF RP THR-143. RX PubMed=15713662; DOI=10.1074/jbc.m500424200; RA Byers S.A., Price J.P., Cooper J.J., Li Q., Price D.H.; RT "HEXIM2, a HEXIM1-related protein, regulates positive transcription RT elongation factor b through association with 7SK."; RL J. Biol. Chem. 280:16360-16367(2005). RN [6] RP FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, INTERACTION WITH HEXIM1, RP OLIGOMERIZATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=15713661; DOI=10.1074/jbc.m500912200; RA Yik J.H.N., Chen R., Pezda A.C., Zhou Q.; RT "Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance RT of active and inactive positive transcription elongation factor b complexes RT for control of transcription."; RL J. Biol. Chem. 280:16368-16376(2005). RN [7] RP OLIGOMERIZATION, INTERACTION WITH CCNT1, AND SUBCELLULAR LOCATION. RX PubMed=15994294; DOI=10.1074/jbc.m502471200; RA Dulac C., Michels A.A., Fraldi A., Bonnet F., Nguyen V.T., Napolitano G., RA Lania L., Bensaude O.; RT "Transcription-dependent association of multiple positive transcription RT elongation factor units to a HEXIM multimer."; RL J. Biol. Chem. 280:30619-30629(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-32; THR-46; SER-51; RP SER-53; SER-71; SER-76 AND SER-81, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [12] RP INTERACTION WITH CCNT2. RX PubMed=19883659; DOI=10.1016/j.jmb.2009.10.055; RA Czudnochowski N., Vollmuth F., Baumann S., Vogel-Bachmayr K., Geyer M.; RT "Specificity of Hexim1 and Hexim2 complex formation with cyclin T1/T2, RT importin alpha and 7SK snRNA."; RL J. Mol. Biol. 395:28-41(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-53, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-53, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-76, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-32; SER-39; SER-51; RP SER-53 AND SER-76, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Transcriptional regulator which functions as a general RNA CC polymerase II transcription inhibitor (PubMed:15713661, CC PubMed:15713662). Core component of the 7SK RNP complex: in cooperation CC with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex CC preventing RNA polymerase II phosphorylation and subsequent CC transcriptional elongation (PubMed:15713661, PubMed:15713662). CC {ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15713662}. CC -!- SUBUNIT: Homooligomer and heterooligomer with HEXIM1; probably dimeric CC (PubMed:15713661, PubMed:15994294). Core component of the 7SK RNP CC complex, at least composed of 7SK RNA, LARP7, MEPCE, HEXIM1 (or HEXIM2) CC and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) (PubMed:15713661, CC PubMed:15713662, PubMed:15994294). Interacts with CCNT2 CC (PubMed:19883659). {ECO:0000269|PubMed:15713661, CC ECO:0000269|PubMed:15713662, ECO:0000269|PubMed:15994294, CC ECO:0000269|PubMed:19883659}. CC -!- INTERACTION: CC Q96MH2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-5460660, EBI-10173507; CC Q96MH2; O43865: AHCYL1; NbExp=4; IntAct=EBI-5460660, EBI-2371423; CC Q96MH2; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-5460660, EBI-297683; CC Q96MH2; Q08289: CACNB2; NbExp=3; IntAct=EBI-5460660, EBI-2874501; CC Q96MH2; P27918: CFP; NbExp=3; IntAct=EBI-5460660, EBI-9038570; CC Q96MH2; O43310-2: CTIF; NbExp=3; IntAct=EBI-5460660, EBI-12180013; CC Q96MH2; Q8NFT6-2: DBF4B; NbExp=3; IntAct=EBI-5460660, EBI-12205861; CC Q96MH2; Q9UHF1: EGFL7; NbExp=3; IntAct=EBI-5460660, EBI-949532; CC Q96MH2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-5460660, EBI-719941; CC Q96MH2; O95995: GAS8; NbExp=3; IntAct=EBI-5460660, EBI-1052570; CC Q96MH2; P15976: GATA1; NbExp=3; IntAct=EBI-5460660, EBI-3909284; CC Q96MH2; O94992: HEXIM1; NbExp=4; IntAct=EBI-5460660, EBI-2832510; CC Q96MH2; Q96MH2: HEXIM2; NbExp=5; IntAct=EBI-5460660, EBI-5460660; CC Q96MH2; P49639: HOXA1; NbExp=3; IntAct=EBI-5460660, EBI-740785; CC Q96MH2; O75031: HSF2BP; NbExp=3; IntAct=EBI-5460660, EBI-7116203; CC Q96MH2; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-5460660, EBI-8638439; CC Q96MH2; O00505: KPNA3; NbExp=3; IntAct=EBI-5460660, EBI-358297; CC Q96MH2; Q5T749: KPRP; NbExp=3; IntAct=EBI-5460660, EBI-10981970; CC Q96MH2; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-5460660, EBI-10241252; CC Q96MH2; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-5460660, EBI-739832; CC Q96MH2; P50222: MEOX2; NbExp=3; IntAct=EBI-5460660, EBI-748397; CC Q96MH2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-5460660, EBI-16439278; CC Q96MH2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5460660, EBI-79165; CC Q96MH2; P11309: PIM1; NbExp=3; IntAct=EBI-5460660, EBI-696621; CC Q96MH2; Q13526: PIN1; NbExp=6; IntAct=EBI-5460660, EBI-714158; CC Q96MH2; Q9GZV8: PRDM14; NbExp=4; IntAct=EBI-5460660, EBI-3957793; CC Q96MH2; P25786: PSMA1; NbExp=3; IntAct=EBI-5460660, EBI-359352; CC Q96MH2; D3DU92: RNPS1; NbExp=3; IntAct=EBI-5460660, EBI-10176640; CC Q96MH2; Q15287: RNPS1; NbExp=3; IntAct=EBI-5460660, EBI-395959; CC Q96MH2; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-5460660, EBI-3957636; CC Q96MH2; O00560: SDCBP; NbExp=3; IntAct=EBI-5460660, EBI-727004; CC Q96MH2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-5460660, EBI-5235340; CC Q96MH2; O43609: SPRY1; NbExp=3; IntAct=EBI-5460660, EBI-3866665; CC Q96MH2; O43597: SPRY2; NbExp=3; IntAct=EBI-5460660, EBI-742487; CC Q96MH2; O75528: TADA3; NbExp=3; IntAct=EBI-5460660, EBI-473249; CC Q96MH2; Q99081: TCF12; NbExp=4; IntAct=EBI-5460660, EBI-722877; CC Q96MH2; Q99081-3: TCF12; NbExp=4; IntAct=EBI-5460660, EBI-11952764; CC Q96MH2; P54274: TERF1; NbExp=2; IntAct=EBI-5460660, EBI-710997; CC Q96MH2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-5460660, EBI-11741437; CC Q96MH2; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-5460660, EBI-2505861; CC Q96MH2; Q14142: TRIM14; NbExp=3; IntAct=EBI-5460660, EBI-2820256; CC Q96MH2; Q9BUY5: ZNF426; NbExp=5; IntAct=EBI-5460660, EBI-743265; CC Q96MH2; O60304: ZNF500; NbExp=3; IntAct=EBI-5460660, EBI-18234077; CC Q96MH2; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-5460660, EBI-373363; CC Q96MH2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-5460660, EBI-625509; CC Q96MH2; Q32M78: ZNF699; NbExp=3; IntAct=EBI-5460660, EBI-10217363; CC Q96MH2; Q5FWF6: ZNF789; NbExp=3; IntAct=EBI-5460660, EBI-13076752; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15994294}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in CC testis. HEXIM1 and HEXIM2 are differentially expressed. CC {ECO:0000269|PubMed:15713661}. CC -!- INDUCTION: Up-regulated by HMBA (hexamethylene bisacetamide) (at CC protein level). {ECO:0000269|PubMed:15713661}. CC -!- DOMAIN: The coiled-coil domain mediates oligomerization. CC -!- SIMILARITY: Belongs to the HEXIM family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY598322; AAT06733.1; -; mRNA. DR EMBL; AK056946; BAB71319.1; -; mRNA. DR EMBL; CH471178; EAW51541.1; -; Genomic_DNA. DR EMBL; CH471178; EAW51542.1; -; Genomic_DNA. DR EMBL; BC003531; AAH03531.1; -; mRNA. DR EMBL; BC012474; AAH12474.1; -; mRNA. DR EMBL; BC025970; AAH25970.1; -; mRNA. DR CCDS; CCDS11496.1; -. DR RefSeq; NP_001290365.1; NM_001303436.1. DR RefSeq; NP_001290366.1; NM_001303437.1. DR RefSeq; NP_001290367.1; NM_001303438.1. DR RefSeq; NP_001290368.1; NM_001303439.1. DR RefSeq; NP_001290369.1; NM_001303440.1. DR RefSeq; NP_001290370.1; NM_001303441.1. DR RefSeq; NP_001290371.1; NM_001303442.1. DR RefSeq; NP_001290372.1; NM_001303443.1. DR RefSeq; NP_001290373.1; NM_001303444.1. DR RefSeq; NP_653209.1; NM_144608.2. DR RefSeq; XP_011522608.1; XM_011524306.2. DR RefSeq; XP_016879656.1; XM_017024167.1. DR RefSeq; XP_016879657.1; XM_017024168.1. DR RefSeq; XP_016879658.1; XM_017024169.1. DR RefSeq; XP_016879659.1; XM_017024170.1. DR AlphaFoldDB; Q96MH2; -. DR SMR; Q96MH2; -. DR BioGRID; 125888; 84. DR IntAct; Q96MH2; 66. DR MINT; Q96MH2; -. DR STRING; 9606.ENSP00000302276; -. DR iPTMnet; Q96MH2; -. DR PhosphoSitePlus; Q96MH2; -. DR BioMuta; HEXIM2; -. DR DMDM; 74732374; -. DR EPD; Q96MH2; -. DR jPOST; Q96MH2; -. DR MassIVE; Q96MH2; -. DR MaxQB; Q96MH2; -. DR PaxDb; 9606-ENSP00000302276; -. DR PeptideAtlas; Q96MH2; -. DR ProteomicsDB; 77356; -. DR Pumba; Q96MH2; -. DR Antibodypedia; 17593; 194 antibodies from 29 providers. DR DNASU; 124790; -. DR Ensembl; ENST00000307275.7; ENSP00000302276.2; ENSG00000168517.11. DR Ensembl; ENST00000585340.2; ENSP00000468251.2; ENSG00000168517.11. DR Ensembl; ENST00000586681.6; ENSP00000465086.2; ENSG00000168517.11. DR Ensembl; ENST00000589230.6; ENSP00000466200.2; ENSG00000168517.11. DR Ensembl; ENST00000591070.6; ENSP00000464807.2; ENSG00000168517.11. DR Ensembl; ENST00000591576.5; ENSP00000465727.1; ENSG00000168517.11. DR Ensembl; ENST00000592695.1; ENSP00000467517.1; ENSG00000168517.11. DR Ensembl; ENST00000593138.6; ENSP00000468773.2; ENSG00000168517.11. DR GeneID; 124790; -. DR KEGG; hsa:124790; -. DR MANE-Select; ENST00000589230.6; ENSP00000466200.2; NM_001303441.2; NP_001290370.1. DR UCSC; uc002iih.2; human. DR AGR; HGNC:28591; -. DR CTD; 124790; -. DR GeneCards; HEXIM2; -. DR HGNC; HGNC:28591; HEXIM2. DR HPA; ENSG00000168517; Tissue enhanced (skeletal muscle, testis). DR MIM; 615695; gene. DR neXtProt; NX_Q96MH2; -. DR OpenTargets; ENSG00000168517; -. DR PharmGKB; PA142671695; -. DR VEuPathDB; HostDB:ENSG00000168517; -. DR eggNOG; ENOG502QQP8; Eukaryota. DR GeneTree; ENSGT00390000002808; -. DR HOGENOM; CLU_066028_1_0_1; -. DR InParanoid; Q96MH2; -. DR OMA; MWNREGS; -. DR OrthoDB; 2905032at2759; -. DR PhylomeDB; Q96MH2; -. DR TreeFam; TF336851; -. DR PathwayCommons; Q96MH2; -. DR SignaLink; Q96MH2; -. DR BioGRID-ORCS; 124790; 10 hits in 1158 CRISPR screens. DR GeneWiki; HEXIM2; -. DR GenomeRNAi; 124790; -. DR Pharos; Q96MH2; Tbio. DR PRO; PR:Q96MH2; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96MH2; Protein. DR Bgee; ENSG00000168517; Expressed in gastrocnemius and 122 other cell types or tissues. DR ExpressionAtlas; Q96MH2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL. DR GO; GO:0097322; F:7SK snRNA binding; IDA:UniProtKB. DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:HGNC-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0017069; F:snRNA binding; IDA:HGNC-UCL. DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:HGNC-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:HGNC-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:HGNC-UCL. 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; Q96MH2; HS. PE 1: Evidence at protein level; KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..286 FT /note="Protein HEXIM2" FT /id="PRO_0000305267" FT REGION 1..195 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 140..143 FT /note="Interaction with P-TEFb" FT REGION 226..286 FT /note="Interaction with CCNT1, HEXIM1 and HEXIM2" FT /evidence="ECO:0000269|PubMed:15713661, FT ECO:0000269|PubMed:15994294" FT COILED 207..277 FT /evidence="ECO:0000255" FT COMPBIAS 87..101 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 102..130 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..195 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 32 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 46 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648" FT MOD_RES 51 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 53 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MUTAGEN 143 FT /note="T->A: Loss of interaction with P-TEFb." FT /evidence="ECO:0000269|PubMed:15713662" FT MUTAGEN 143 FT /note="T->D: Loss of interaction with P-TEFb." FT /evidence="ECO:0000269|PubMed:15713662" SQ SEQUENCE 286 AA; 32419 MW; 58576D72096A8A6F CRC64; MMATPNQTAC NAESPVALEE AKTSGAPGSP QTPPERHDSG GSLPLTPRME SHSEDEDLAG AVGGLGWNSR SPRTQSPGGC SAEAVLARKK HRRRPSKRKR HWRPYLELSW AEKQQRDERQ SQRASRVREE MFAKGQPVAP YNTTQFLMND RDPEEPNLDV PHGISHPGSS GESEAGDSDG RGRAHGEFQR KDFSETYERF HTESLQGRSK QELVRDYLEL EKRLSQAEEE TRRLQQLQAC TGQQSCRQVE ELAAEVQRLR TENQRLRQEN QMWNREGCRC DEEPGT //