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O94992

- HEXI1_HUMAN

UniProt

O94992 - HEXI1_HUMAN

Protein

Protein HEXIM1

Gene

HEXIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity.9 Publications

    GO - Molecular functioni

    1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: HGNC
    2. protein binding Source: IntAct
    3. snRNA binding Source: HGNC

    GO - Biological processi

    1. heart development Source: Ensembl
    2. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: HGNC
    3. negative regulation of transcription, DNA-templated Source: HGNC
    4. negative regulation of transcription from RNA polymerase II promoter Source: HGNC
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein HEXIM1
    Alternative name(s):
    Cardiac lineage protein 1
    Estrogen down-regulated gene 1 protein
    Hexamethylene bis-acetamide-inducible protein 1
    Menage a quatre protein 1
    Gene namesi
    Name:HEXIM1
    Synonyms:CLP1, EDG1, HIS1, MAQ1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:24953. HEXIM1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Binds alpha-importin and is mostly nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. nucleus Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi152 – 1554KHRR → ILAA: Abolishes interaction with 7SK snRNA. 1 Publication
    Mutagenesisi154 – 1563RRR → AAA: Abolishes interaction with 7SK snRNA. 1 Publication
    Mutagenesisi203 – 2031Y → D: Abolishes interaction with P-TEFb; when associated with D-205. 2 Publications
    Mutagenesisi205 – 2051T → D: Abolishes interaction with P-TEFb. Same effect; when associated with D-203. 2 Publications
    Mutagenesisi208 – 2081F → A, D or K: Partial loss of function. 2 Publications
    Mutagenesisi271 – 2711Y → A or E: Loss of function. 2 Publications
    Mutagenesisi287 – 2871L → 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. 2 Publications
    Mutagenesisi294 – 2941L → 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. 2 Publications
    Mutagenesisi332 – 3321L → A: Loss of oligomerization; when associated with A-287; A-294 and A-339. 2 Publications
    Mutagenesisi339 – 3391L → A: Loss of oligomerization; when associated with A-287; A-294 and A-332. 2 Publications

    Organism-specific databases

    PharmGKBiPA142671694.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Protein HEXIM1PRO_0000305263Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei97 – 971Phosphoserine1 Publication
    Modified residuei98 – 981Phosphoserine1 Publication
    Modified residuei233 – 2331Phosphoserine3 Publications
    Modified residuei236 – 2361Phosphothreonine3 Publications
    Modified residuei237 – 2371Phosphoserine3 Publications
    Modified residuei252 – 2521Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO94992.
    PaxDbiO94992.
    PeptideAtlasiO94992.
    PRIDEiO94992.

    PTM databases

    PhosphoSiteiO94992.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with higher expression in placenta. HEXIM1 and HEXIM2 are differentially expressed. Expressed in endocrine tissues.2 Publications

    Inductioni

    Up-regulated by HMBA (hexamethylene bisacetamide) (at protein level). Down-regulated by estrogen.3 Publications

    Gene expression databases

    BgeeiO94992.
    CleanExiHS_CLP1.
    HS_HEXIM1.
    GenevestigatoriO94992.

    Organism-specific databases

    HPAiCAB011625.
    HPA008926.

    Interactioni

    Subunit structurei

    Homooligomer and heterooligomer with HEXIM2; probably dimeric. 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. Interacts with the N-CoR complex through NCOR1. Interacts with ESR1 and NR3C1. May interact with NF-kappa-B through RELA.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDK9P507507EBI-2832510,EBI-1383449
    LARP7Q4G0J35EBI-2832510,EBI-2371923

    Protein-protein interaction databases

    BioGridi115860. 29 interactions.
    DIPiDIP-46463N.
    IntActiO94992. 5 interactions.
    STRINGi9606.ENSP00000328773.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi268 – 28013
    Helixi284 – 31532
    Helixi319 – 34830

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GD7NMR-A/B255-359[»]
    3S9GX-ray2.10A/B255-359[»]
    ProteinModelPortaliO94992.
    SMRiO94992. Positions 254-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94992.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 17728Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1Add
    BLAST
    Regioni202 – 2054Interaction with P-TEFb
    Regioni210 – 25041Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localizationAdd
    BLAST
    Regioni286 – 31429Mediates interaction with CCNT1Add
    BLAST
    Regioni310 – 35546Required for inhibition of ESR1-dependent transcriptionAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili283 – 34967Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled-coil domain mediates oligomerization.

    Sequence similaritiesi

    Belongs to the HEXIM family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG72325.
    HOGENOMiHOG000060338.
    HOVERGENiHBG053249.
    InParanoidiO94992.
    KOiK15189.
    OMAiKGQNGDD.
    OrthoDBiEOG771281.
    PhylomeDBiO94992.
    TreeFamiTF336851.

    Family and domain databases

    InterProiIPR024872. HEXIM.
    [Graphical view]
    PANTHERiPTHR13469. PTHR13469. 1 hit.
    PfamiPF15313. HEXIM. 1 hit.
    [Graphical view]
    PRINTSiPR02094. HEXIMFAMILY.

    Sequencei

    Sequence statusi: Complete.

    O94992-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEPFLSEYQ HQPQTSNCTG AAAVQEELNP ERPPGAEERV PEEDSRWQSR    50
    AFPQLGGRPG PEGEGSLESQ PPPLQTQACP ESSCLREGEK GQNGDDSSAG 100
    GDFPPPAEVE PTPEAELLAQ PCHDSEASKL GAPAAGGEEE WGQQQRQLGK 150
    KKHRRRPSKK KRHWKPYYKL TWEEKKKFDE KQSLRASRIR AEMFAKGQPV 200
    APYNTTQFLM DDHDQEEPDL KTGLYSKRAA AKSDDTSDDD FMEEGGEEDG 250
    GSDGMGGDGS EFLQRDFSET YERYHTESLQ NMSKQELIKE YLELEKCLSR 300
    MEDENNRLRL ESKRLGGDDA RVRELELELD RLRAENLQLL TENELHRQQE 350
    RAPLSKFGD 359
    Length:359
    Mass (Da):40,623
    Last modified:May 1, 1999 - v1
    Checksum:iB12845C4E2595FF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021179 mRNA. Translation: BAA36166.1.
    AK313557 mRNA. Translation: BAG36332.1.
    BC006460 mRNA. Translation: AAH06460.1.
    CCDSiCCDS11495.1.
    RefSeqiNP_006451.1. NM_006460.2.
    UniGeneiHs.586945.
    Hs.741758.
    Hs.745252.

    Genome annotation databases

    EnsembliENST00000332499; ENSP00000328773; ENSG00000186834.
    GeneIDi10614.
    KEGGihsa:10614.
    UCSCiuc002iig.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021179 mRNA. Translation: BAA36166.1 .
    AK313557 mRNA. Translation: BAG36332.1 .
    BC006460 mRNA. Translation: AAH06460.1 .
    CCDSi CCDS11495.1.
    RefSeqi NP_006451.1. NM_006460.2.
    UniGenei Hs.586945.
    Hs.741758.
    Hs.745252.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GD7 NMR - A/B 255-359 [» ]
    3S9G X-ray 2.10 A/B 255-359 [» ]
    ProteinModelPortali O94992.
    SMRi O94992. Positions 254-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115860. 29 interactions.
    DIPi DIP-46463N.
    IntActi O94992. 5 interactions.
    STRINGi 9606.ENSP00000328773.

    PTM databases

    PhosphoSitei O94992.

    Proteomic databases

    MaxQBi O94992.
    PaxDbi O94992.
    PeptideAtlasi O94992.
    PRIDEi O94992.

    Protocols and materials databases

    DNASUi 10614.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332499 ; ENSP00000328773 ; ENSG00000186834 .
    GeneIDi 10614.
    KEGGi hsa:10614.
    UCSCi uc002iig.3. human.

    Organism-specific databases

    CTDi 10614.
    GeneCardsi GC17P043224.
    HGNCi HGNC:24953. HEXIM1.
    HPAi CAB011625.
    HPA008926.
    MIMi 607328. gene.
    neXtProti NX_O94992.
    PharmGKBi PA142671694.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72325.
    HOGENOMi HOG000060338.
    HOVERGENi HBG053249.
    InParanoidi O94992.
    KOi K15189.
    OMAi KGQNGDD.
    OrthoDBi EOG771281.
    PhylomeDBi O94992.
    TreeFami TF336851.

    Miscellaneous databases

    ChiTaRSi HEXIM1. human.
    EvolutionaryTracei O94992.
    GeneWikii HEXIM1.
    GenomeRNAii 10614.
    NextBioi 40326.
    PROi O94992.
    SOURCEi Search...

    Gene expression databases

    Bgeei O94992.
    CleanExi HS_CLP1.
    HS_HEXIM1.
    Genevestigatori O94992.

    Family and domain databases

    InterProi IPR024872. HEXIM.
    [Graphical view ]
    PANTHERi PTHR13469. PTHR13469. 1 hit.
    Pfami PF15313. HEXIM. 1 hit.
    [Graphical view ]
    PRINTSi PR02094. HEXIMFAMILY.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of hexamethylene-bis-acetamide-inducible transcript, HEXIM1, in human vascular smooth muscle cells."
      Kusuhara M., Nagasaki K., Kimura K., Maass N., Manabe T., Ishikawa S., Aikawa M., Miyazaki K., Yamaguchi K.
      Biomed. Res. 20:273-279(1999)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Vascular smooth muscle.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pericardium.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    4. "Identification of a novel inhibitor of breast cell growth that is down-regulated by estrogens and decreased in breast tumors."
      Wittmann B.M., Wang N., Montano M.M.
      Cancer Res. 63:5151-5158(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY ESTROGEN.
    5. "Suppression of NF-kappaB-dependent gene expression by a hexamethylene bisacetamide-inducible protein HEXIM1 in human vascular smooth muscle cells."
      Ouchida R., Kusuhara M., Shimizu N., Hisada T., Makino Y., Morimoto C., Handa H., Ohsuzu F., Tanaka H.
      Genes Cells 8:95-107(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION, INDUCTION BY HMBA.
    6. "Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA."
      Yik J.H.N., Chen R., Nishimura R., Jennings J.L., Link A.J., Zhou Q.
      Mol. Cell 12:971-982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner."
      Michels A.A., Nguyen V.T., Fraldi A., Labas V., Edwards M., Bonnet F., Lania L., Bensaude O.
      Mol. Cell. Biol. 23:4859-4869(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, INTERACTION WITH CCNT1, SUBCELLULAR LOCATION.
    8. "Binding of the 7SK snRNA turns the HEXIM1 protein into a P-TEFb (CDK9/cyclin T) inhibitor."
      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.
      EMBO J. 23:2608-2619(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 152-LYS--ARG-155; TYR-203 AND THR-205, INTERACTION WITH P-TEFB.
    9. "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."
      Yik J.H.N., Chen R., Pezda A.C., Samford C.S., Zhou Q.
      Mol. Cell. Biol. 24:5094-5105(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH P-TEFB.
    10. "Interplay between 7SK snRNA and oppositely charged regions in HEXIM1 direct the inhibition of P-TEFb."
      Barboric M., Kohoutek J., Price J.P., Blazek D., Price D.H., Peterlin B.M.
      EMBO J. 24:4291-4303(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THE 7SK SNRNA AND P-TEFB, MUTAGENESIS OF 154-ARG--ARG-156.
    11. "Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance of active and inactive positive transcription elongation factor b complexes for control of transcription."
      Yik J.H.N., Chen R., Pezda A.C., Zhou Q.
      J. Biol. Chem. 280:16368-16376(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HEXIM2, OLIGOMERIZATION, TISSUE SPECIFICITY, INDUCTION.
    12. "Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat."
      Schulte A., Czudnochowski N., Barboric M., Schoenichen A., Blazek D., Peterlin B.M., Geyer M.
      J. Biol. Chem. 280:24968-24977(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNT1.
    13. "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."
      Li Q., Price J.P., Byers S.A., Cheng D., Peng J., Price D.H.
      J. Biol. Chem. 280:28819-28826(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, MUTAGENESIS OF PHE-208 AND TYR-271.
    14. "Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb."
      Blazek D., Barboric M., Kohoutek J., Oven I., Peterlin B.M.
      Nucleic Acids Res. 33:7000-7010(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH P-TEFB, OLIGOMERIZATION, MUTAGENESIS OF LEU-287; LEU-294; LEU-332 AND LEU-339.
    15. "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."
      Wittmann B.M., Fujinaga K., Deng H., Ogba N., Montano M.M.
      Oncogene 24:5576-5588(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ESR1-DEPENDENT TRANSCRIPTION, INTERACTION WITH ESR1.
    16. "HEXIM1 forms a transcriptionally abortive complex with glucocorticoid receptor without involving 7SK RNA and positive transcription elongation factor b."
      Shimizu N., Ouchida R., Yoshikawa N., Hisada T., Watanabe H., Okamoto K., Kusuhara M., Handa H., Morimoto C., Tanaka H.
      Proc. Natl. Acad. Sci. U.S.A. 102:8555-8560(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NR3C1-DEPENDENT TRANSCRIPTION, INTERACTION WITH NR3C1.
    17. "Hexim1 sequesters positive transcription elongation factor b from the class II transactivator on MHC class II promoters."
      Kohoutek J., Blazek D., Peterlin B.M.
      Proc. Natl. Acad. Sci. U.S.A. 103:17349-17354(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIITA-DEPENDENT TRANSCRIPTION.
    18. "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
      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.
      Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
    19. "Regulation of P-TEFb elongation complex activity by CDK9 acetylation."
      Fu J., Yoon H.-G., Qin J., Wong J.
      Mol. Cell. Biol. 27:4641-4651(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOR1.
    20. "HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells."
      Li Q., Cooper J.J., Altwerger G.H., Feldkamp M.D., Shea M.A., Price D.H.
      Nucleic Acids Res. 35:2503-2512(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-98; SER-233; THR-236; SER-237 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-236; SER-237 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-236; SER-237 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb."
      Dames S.A., Schoenichen A., Schulte A., Barboric M., Peterlin B.M., Grzesiek S., Geyer M.
      Proc. Natl. Acad. Sci. U.S.A. 104:14312-14317(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 255-359, SUBUNIT, INTERACTION WITH CCNT1.

    Entry informationi

    Entry nameiHEXI1_HUMAN
    AccessioniPrimary (citable) accession number: O94992
    Secondary accession number(s): B2R8Y5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Inhibits Tat activity which is required for HIV-1 transcription.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3