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Protein HEXIM1 (Cardiac lineage protein 1) (Estrogen down-regulated gene 1 protein) (Hexamethylene bis-acetamide-inducible protein 1) (Menage a quatre protein 1)

 HEXI1_HUMAN             Reviewed;         359 AA.
O94992; B2R8Y5;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 130.
RecName: Full=Protein HEXIM1;
AltName: Full=Cardiac lineage protein 1;
AltName: Full=Estrogen down-regulated gene 1 protein;
AltName: Full=Hexamethylene bis-acetamide-inducible protein 1;
AltName: Full=Menage a quatre protein 1;
Name=HEXIM1; Synonyms=CLP1, EDG1, HIS1, MAQ1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Vascular smooth muscle;
Kusuhara M., Nagasaki K., Kimura K., Maass N., Manabe T., Ishikawa S.,
Aikawa M., Miyazaki K., Yamaguchi K.;
"Cloning of hexamethylene-bis-acetamide-inducible transcript, HEXIM1,
in human vascular smooth muscle cells.";
Biomed. Res. 20:273-279(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pericardium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY ESTROGEN.
PubMed=12941847;
Wittmann B.M., Wang N., Montano M.M.;
"Identification of a novel inhibitor of breast cell growth that is
down-regulated by estrogens and decreased in breast tumors.";
Cancer Res. 63:5151-5158(2003).
[5]
FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION, AND INDUCTION
BY HMBA.
PubMed=12581153; DOI=10.1046/j.1365-2443.2003.00618.x;
Ouchida R., Kusuhara M., Shimizu N., Hisada T., Makino Y.,
Morimoto C., Handa H., Ohsuzu F., Tanaka H.;
"Suppression of NF-kappaB-dependent gene expression by a hexamethylene
bisacetamide-inducible protein HEXIM1 in human vascular smooth muscle
cells.";
Genes Cells 8:95-107(2003).
[6]
FUNCTION.
PubMed=14580347; DOI=10.1016/S1097-2765(03)00388-5;
Yik J.H.N., Chen R., Nishimura R., Jennings J.L., Link A.J., Zhou Q.;
"Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II
transcription by the coordinated actions of HEXIM1 and 7SK snRNA.";
Mol. Cell 12:971-982(2003).
[7]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
7SK SNRNP COMPLEX, INTERACTION WITH CCNT1, AND SUBCELLULAR LOCATION.
PubMed=12832472; DOI=10.1128/MCB.23.14.4859-4869.2003;
Michels A.A., Nguyen V.T., Fraldi A., Labas V., Edwards M., Bonnet F.,
Lania L., Bensaude O.;
"MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
transcription-dependent manner.";
Mol. Cell. Biol. 23:4859-4869(2003).
[8]
FUNCTION, MUTAGENESIS OF 152-LYS--ARG-155; TYR-203 AND THR-205, AND
INTERACTION WITH P-TEFB.
PubMed=15201869; DOI=10.1038/sj.emboj.7600275;
Michels A.A., Fraldi A., Li Q., Adamson T.E., Bonnet F., Nguyen V.T.,
Sedore S.C., Price J.P., Price D.H., Lania L., Bensaude O.;
"Binding of the 7SK snRNA turns the HEXIM1 protein into a P-TEFb
(CDK9/cyclin T) inhibitor.";
EMBO J. 23:2608-2619(2004).
[9]
INTERACTION WITH P-TEFB.
PubMed=15169877; DOI=10.1128/MCB.24.12.5094-5105.2004;
Yik J.H.N., Chen R., Pezda A.C., Samford C.S., Zhou Q.;
"A human immunodeficiency virus type 1 Tat-like arginine-rich RNA-
binding domain is essential for HEXIM1 to inhibit RNA polymerase II
transcription through 7SK snRNA-mediated inactivation of P-TEFb.";
Mol. Cell. Biol. 24:5094-5105(2004).
[10]
SUBCELLULAR LOCATION, INTERACTION WITH THE 7SK SNRNA AND P-TEFB, AND
MUTAGENESIS OF 154-ARG--ARG-156.
PubMed=16362050; DOI=10.1038/sj.emboj.7600883;
Barboric M., Kohoutek J., Price J.P., Blazek D., Price D.H.,
Peterlin B.M.;
"Interplay between 7SK snRNA and oppositely charged regions in HEXIM1
direct the inhibition of P-TEFb.";
EMBO J. 24:4291-4303(2005).
[11]
FUNCTION, INTERACTION WITH HEXIM2, OLIGOMERIZATION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=15713661; DOI=10.1074/jbc.M500912200;
Yik J.H.N., Chen R., Pezda A.C., Zhou Q.;
"Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
balance of active and inactive positive transcription elongation
factor b complexes for control of transcription.";
J. Biol. Chem. 280:16368-16376(2005).
[12]
INTERACTION WITH CCNT1.
PubMed=15855166; DOI=10.1074/jbc.M501431200;
Schulte A., Czudnochowski N., Barboric M., Schoenichen A., Blazek D.,
Peterlin B.M., Geyer M.;
"Identification of a cyclin T-binding domain in Hexim1 and biochemical
analysis of its binding competition with HIV-1 Tat.";
J. Biol. Chem. 280:24968-24977(2005).
[13]
OLIGOMERIZATION, AND MUTAGENESIS OF PHE-208 AND TYR-271.
PubMed=15965233; DOI=10.1074/jbc.M502712200;
Li Q., Price J.P., Byers S.A., Cheng D., Peng J., Price D.H.;
"Analysis of the large inactive P-TEFb complex indicates that it
contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb
molecules containing Cdk9 phosphorylated at threonine 186.";
J. Biol. Chem. 280:28819-28826(2005).
[14]
INTERACTION WITH P-TEFB, OLIGOMERIZATION, AND MUTAGENESIS OF LEU-287;
LEU-294; LEU-332 AND LEU-339.
PubMed=16377779; DOI=10.1093/nar/gki997;
Blazek D., Barboric M., Kohoutek J., Oven I., Peterlin B.M.;
"Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region
directs the inhibition of P-TEFb.";
Nucleic Acids Res. 33:7000-7010(2005).
[15]
FUNCTION IN ESR1-DEPENDENT TRANSCRIPTION, AND INTERACTION WITH ESR1.
PubMed=15940264; DOI=10.1038/sj.onc.1208728;
Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.;
"The breast cell growth inhibitor, estrogen down regulated gene 1,
modulates a novel functional interaction between estrogen receptor
alpha and transcriptional elongation factor cyclin T1.";
Oncogene 24:5576-5588(2005).
[16]
FUNCTION IN NR3C1-DEPENDENT TRANSCRIPTION, AND INTERACTION WITH NR3C1.
PubMed=15941832; DOI=10.1073/pnas.0409863102;
Shimizu N., Ouchida R., Yoshikawa N., Hisada T., Watanabe H.,
Okamoto K., Kusuhara M., Handa H., Morimoto C., Tanaka H.;
"HEXIM1 forms a transcriptionally abortive complex with glucocorticoid
receptor without involving 7SK RNA and positive transcription
elongation factor b.";
Proc. Natl. Acad. Sci. U.S.A. 102:8555-8560(2005).
[17]
FUNCTION IN CIITA-DEPENDENT TRANSCRIPTION.
PubMed=17088550; DOI=10.1073/pnas.0603079103;
Kohoutek J., Blazek D., Peterlin B.M.;
"Hexim1 sequesters positive transcription elongation factor b from the
class II transactivator on MHC class II promoters.";
Proc. Natl. Acad. Sci. U.S.A. 103:17349-17354(2006).
[18]
IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
"Systematic analysis of the protein interaction network for the human
transcription machinery reveals the identity of the 7SK capping
enzyme.";
Mol. Cell 27:262-274(2007).
[19]
INTERACTION WITH NCOR1.
PubMed=17452463; DOI=10.1128/MCB.00857-06;
Fu J., Yoon H.-G., Qin J., Wong J.;
"Regulation of P-TEFb elongation complex activity by CDK9
acetylation.";
Mol. Cell. Biol. 27:4641-4651(2007).
[20]
SUBCELLULAR LOCATION.
PubMed=17395637; DOI=10.1093/nar/gkm150;
Li Q., Cooper J.J., Altwerger G.H., Feldkamp M.D., Shea M.A.,
Price D.H.;
"HEXIM1 is a promiscuous double-stranded RNA-binding protein and
interacts with RNAs in addition to 7SK in cultured cells.";
Nucleic Acids Res. 35:2503-2512(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-98; SER-233;
THR-236; SER-237 AND SER-252, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-236; SER-237
AND SER-252, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
INTERACTION WITH CCNT2.
PubMed=19883659; DOI=10.1016/j.jmb.2009.10.055;
Czudnochowski N., Vollmuth F., Baumann S., Vogel-Bachmayr K.,
Geyer M.;
"Specificity of Hexim1 and Hexim2 complex formation with cyclin T1/T2,
importin alpha and 7SK snRNA.";
J. Mol. Biol. 395:28-41(2010).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-236; SER-237
AND SER-252, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5;
XRCC6; SFPQ; NONO; PSPC1; RBM14 AND MATR3.
PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
"HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex
that regulates DNA-mediated innate immune response.";
Mol. Cell 67:387-399(2017).
[29]
STRUCTURE BY NMR OF 255-359, SUBUNIT, AND INTERACTION WITH CCNT1.
PubMed=17724342; DOI=10.1073/pnas.0701848104;
Dames S.A., Schoenichen A., Schulte A., Barboric M., Peterlin B.M.,
Grzesiek S., Geyer M.;
"Structure of the Cyclin T binding domain of Hexim1 and molecular
basis for its recognition of P-TEFb.";
Proc. Natl. Acad. Sci. U.S.A. 104:14312-14317(2007).
-!- FUNCTION: Transcriptional regulator which functions as a general
RNA polymerase II transcription inhibitor (PubMed:14580347,
PubMed:15713661, PubMed:15201869). In cooperation with 7SK snRNA
sequesters P-TEFb in a large inactive 7SK snRNP complex preventing
RNA polymerase II phosphorylation and subsequent transcriptional
elongation (PubMed:12832472, PubMed:14580347, PubMed:15713661,
PubMed:15201869). May also regulate NF-kappa-B, ESR1, NR3C1 and
CIITA-dependent transcriptional activity (PubMed:15940264,
PubMed:15941832, PubMed:17088550). Plays a role in the regulation
of DNA virus-mediated innate immune response by assembling into
the HDP-RNP complex, a complex that serves as a platform for IRF3
phosphorylation and subsequent innate immune response activation
through the cGAS-STING pathway (PubMed:28712728).
{ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12832472,
ECO:0000269|PubMed:14580347, ECO:0000269|PubMed:15201869,
ECO:0000269|PubMed:15713661, ECO:0000269|PubMed:15940264,
ECO:0000269|PubMed:15941832, ECO:0000269|PubMed:17088550,
ECO:0000269|PubMed:28712728}.
-!- SUBUNIT: Homooligomer and heterooligomer with HEXIM2; probably
dimeric (PubMed:15713661, PubMed:15965233, PubMed:16377779).
Component of the 7SK snRNP complex at least composed of P-TEFb
(composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3,
SART3 proteins and 7SK and U6 snRNAs (PubMed:12832472,
PubMed:15201869, PubMed:15169877, PubMed:16362050,
PubMed:15713661, PubMed:15855166, PubMed:16377779,
PubMed:17643375, PubMed:17724342). Interacts with the N-CoR
complex through NCOR1 (PubMed:17452463). Interacts with ESR1 and
NR3C1 (PubMed:15940264, PubMed:15941832). May interact with NF-
kappa-B through RELA (PubMed:12581153). Interacts with CCNT2;
mediates formation of a tripartite complex with KPNA2
(PubMed:19883659). Part of the HDP-RNP complex composed of at
least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ,
NONO, PSPC1, RBM14, and MATR3) and NEAT1 non-coding RNA
(PubMed:28712728). {ECO:0000269|PubMed:12581153,
ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:15169877,
ECO:0000269|PubMed:15201869, ECO:0000269|PubMed:15713661,
ECO:0000269|PubMed:15855166, ECO:0000269|PubMed:15940264,
ECO:0000269|PubMed:15941832, ECO:0000269|PubMed:15965233,
ECO:0000269|PubMed:16362050, ECO:0000269|PubMed:16377779,
ECO:0000269|PubMed:17452463, ECO:0000269|PubMed:17643375,
ECO:0000269|PubMed:17724342, ECO:0000269|PubMed:19883659,
ECO:0000269|PubMed:28712728}.
-!- INTERACTION:
O60563:CCNT1; NbExp=8; IntAct=EBI-2832510, EBI-2479671;
P50750:CDK9; NbExp=9; IntAct=EBI-2832510, EBI-1383449;
Q4G0J3:LARP7; NbExp=6; IntAct=EBI-2832510, EBI-2371923;
Q15554:TERF2; NbExp=2; IntAct=EBI-2832510, EBI-706637;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12581153,
ECO:0000269|PubMed:12832472, ECO:0000269|PubMed:12941847,
ECO:0000269|PubMed:16362050, ECO:0000269|PubMed:17395637}.
Cytoplasm {ECO:0000269|PubMed:12581153,
ECO:0000269|PubMed:17395637}. Note=Binds alpha-importin and is
mostly nuclear (PubMed:16362050).
-!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
in placenta. HEXIM1 and HEXIM2 are differentially expressed.
Expressed in endocrine tissues. {ECO:0000269|PubMed:12941847,
ECO:0000269|PubMed:15713661}.
-!- INDUCTION: Up-regulated by HMBA (hexamethylene bisacetamide) (at
protein level). Down-regulated by estrogen.
{ECO:0000269|PubMed:12581153, ECO:0000269|PubMed:12941847,
ECO:0000269|PubMed:15713661}.
-!- DOMAIN: The coiled-coil domain mediates oligomerization.
-!- MISCELLANEOUS: Inhibits Tat activity which is required for HIV-1
transcription.
-!- SIMILARITY: Belongs to the HEXIM family. {ECO:0000305}.
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EMBL; AB021179; BAA36166.1; -; mRNA.
EMBL; AK313557; BAG36332.1; -; mRNA.
EMBL; BC006460; AAH06460.1; -; mRNA.
CCDS; CCDS11495.1; -.
RefSeq; NP_006451.1; NM_006460.2.
UniGene; Hs.586945; -.
UniGene; Hs.741758; -.
UniGene; Hs.745252; -.
PDB; 2GD7; NMR; -; A/B=255-359.
PDB; 3S9G; X-ray; 2.10 A; A/B=255-359.
PDBsum; 2GD7; -.
PDBsum; 3S9G; -.
ProteinModelPortal; O94992; -.
SMR; O94992; -.
BioGrid; 115860; 56.
CORUM; O94992; -.
DIP; DIP-46463N; -.
IntAct; O94992; 17.
STRING; 9606.ENSP00000328773; -.
ChEMBL; CHEMBL3120044; -.
iPTMnet; O94992; -.
PhosphoSitePlus; O94992; -.
BioMuta; HEXIM1; -.
EPD; O94992; -.
MaxQB; O94992; -.
PaxDb; O94992; -.
PeptideAtlas; O94992; -.
PRIDE; O94992; -.
DNASU; 10614; -.
Ensembl; ENST00000332499; ENSP00000328773; ENSG00000186834.
GeneID; 10614; -.
KEGG; hsa:10614; -.
UCSC; uc002iig.4; human.
CTD; 10614; -.
DisGeNET; 10614; -.
EuPathDB; HostDB:ENSG00000186834.3; -.
GeneCards; HEXIM1; -.
HGNC; HGNC:24953; HEXIM1.
HPA; CAB011625; -.
HPA; HPA008926; -.
MIM; 607328; gene.
neXtProt; NX_O94992; -.
OpenTargets; ENSG00000186834; -.
PharmGKB; PA142671694; -.
eggNOG; ENOG410IH8I; Eukaryota.
eggNOG; ENOG4111K9Z; LUCA.
GeneTree; ENSGT00390000002808; -.
HOGENOM; HOG000060338; -.
HOVERGEN; HBG053249; -.
InParanoid; O94992; -.
KO; K15189; -.
OMA; EAWGQQQ; -.
OrthoDB; EOG091G0Y9A; -.
PhylomeDB; O94992; -.
TreeFam; TF336851; -.
ChiTaRS; HEXIM1; human.
EvolutionaryTrace; O94992; -.
GeneWiki; HEXIM1; -.
GenomeRNAi; 10614; -.
PRO; PR:O94992; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000186834; -.
CleanEx; HS_CLP1; -.
CleanEx; HS_HEXIM1; -.
Genevisible; O94992; HS.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0097322; F:7SK snRNA binding; IDA:UniProtKB.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:HGNC.
GO; GO:0017069; F:snRNA binding; IDA:HGNC.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:HGNC.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:HGNC.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC.
GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IMP:CACAO.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR024872; HEXIM.
PANTHER; PTHR13469; PTHR13469; 1.
Pfam; PF15313; HEXIM; 1.
PRINTS; PR02094; HEXIMFAMILY.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Cytoplasm; Immunity;
Innate immunity; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation.
CHAIN 1 359 Protein HEXIM1.
/FTId=PRO_0000305263.
REGION 150 177 Basic region; mediates nuclear
localization and interaction with 7SK
snRNA and NR3C1.
{ECO:0000269|PubMed:15941832}.
REGION 202 205 Interaction with P-TEFb.
REGION 210 250 Autoinhibitory acidic region; in absence
of 7SK snRNA interacts with the basic
region preventing interaction with P-TEFb
and modulating subcellular localization.
REGION 286 314 Mediates interaction with CCNT1.
REGION 310 355 Required for inhibition of ESR1-dependent
transcription.
COILED 283 349 {ECO:0000255}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 236 236 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R409}.
MUTAGEN 152 155 KHRR->ILAA: Abolishes interaction with
7SK snRNA. {ECO:0000269|PubMed:15201869}.
MUTAGEN 154 156 RRR->AAA: Abolishes interaction with 7SK
snRNA. {ECO:0000269|PubMed:16362050}.
MUTAGEN 203 203 Y->D: Abolishes interaction with P-TEFb;
when associated with D-205.
{ECO:0000269|PubMed:15201869}.
MUTAGEN 205 205 T->D: Abolishes interaction with P-TEFb.
Same effect; when associated with D-203.
{ECO:0000269|PubMed:15201869}.
MUTAGEN 208 208 F->A,D,K: Partial loss of function.
{ECO:0000269|PubMed:15965233}.
MUTAGEN 271 271 Y->A,E: Loss of function.
{ECO:0000269|PubMed:15965233}.
MUTAGEN 287 287 L->A: Loss of oligomerization; when
associated with A-294; A-332 and A-339.
Loss of function and interaction with P-
TEFb; when associated with A-294.
{ECO:0000269|PubMed:16377779}.
MUTAGEN 294 294 L->A: Loss of oligomerization; when
associated with A-287; A-332 and A-339.
Loss of function and interaction with P-
TEFb; when associated with A-287.
{ECO:0000269|PubMed:16377779}.
MUTAGEN 332 332 L->A: Loss of oligomerization; when
associated with A-287; A-294 and A-339.
{ECO:0000269|PubMed:16377779}.
MUTAGEN 339 339 L->A: Loss of oligomerization; when
associated with A-287; A-294 and A-332.
{ECO:0000269|PubMed:16377779}.
HELIX 268 280 {ECO:0000244|PDB:3S9G}.
HELIX 284 315 {ECO:0000244|PDB:3S9G}.
HELIX 319 348 {ECO:0000244|PDB:3S9G}.
SEQUENCE 359 AA; 40623 MW; B12845C4E2595FF0 CRC64;
MAEPFLSEYQ HQPQTSNCTG AAAVQEELNP ERPPGAEERV PEEDSRWQSR AFPQLGGRPG
PEGEGSLESQ PPPLQTQACP ESSCLREGEK GQNGDDSSAG GDFPPPAEVE PTPEAELLAQ
PCHDSEASKL GAPAAGGEEE WGQQQRQLGK KKHRRRPSKK KRHWKPYYKL TWEEKKKFDE
KQSLRASRIR AEMFAKGQPV APYNTTQFLM DDHDQEEPDL KTGLYSKRAA AKSDDTSDDD
FMEEGGEEDG GSDGMGGDGS EFLQRDFSET YERYHTESLQ NMSKQELIKE YLELEKCLSR
MEDENNRLRL ESKRLGGDDA RVRELELELD RLRAENLQLL TENELHRQQE RAPLSKFGD


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