HEXI2_HUMAN
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 03-AUG-2022, entry version 159.
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}.
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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_011522609.2; XM_011524307.2.
DR RefSeq; XP_011522610.2; XM_011524308.2.
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; 80.
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; Q96MH2; -.
DR PeptideAtlas; Q96MH2; -.
DR PRIDE; Q96MH2; -.
DR ProteomicsDB; 77356; -.
DR Antibodypedia; 17593; 173 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 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 PhylomeDB; Q96MH2; -.
DR TreeFam; TF336851; -.
DR PathwayCommons; Q96MH2; -.
DR SignaLink; Q96MH2; -.
DR BioGRID-ORCS; 124790; 10 hits in 1080 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 120 other tissues.
DR ExpressionAtlas; Q96MH2; baseline and differential.
DR Genevisible; Q96MH2; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:HGNC-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC-UCL.
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..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
