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Q96MH2

- HEXI2_HUMAN

UniProt

Q96MH2 - HEXI2_HUMAN

Protein

Protein HEXIM2

Gene

HEXIM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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.2 Publications

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein HEXIM2
    Alternative name(s):
    Hexamethylene bis-acetamide-inducible protein 2
    Gene namesi
    Name:HEXIM2
    ORF Names:L3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:28591. HEXIM2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi143 – 1431T → A: Loss of interaction with P-TEFb. 1 Publication
    Mutagenesisi143 – 1431T → D: Loss of interaction with P-TEFb. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671695.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 286286Protein HEXIM2PRO_0000305267Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei32 – 321Phosphothreonine1 Publication
    Modified residuei46 – 461Phosphothreonine2 Publications
    Modified residuei51 – 511Phosphoserine3 Publications
    Modified residuei53 – 531Phosphoserine3 Publications
    Modified residuei71 – 711Phosphoserine1 Publication
    Modified residuei76 – 761Phosphoserine1 Publication
    Modified residuei81 – 811Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96MH2.
    PaxDbiQ96MH2.
    PRIDEiQ96MH2.

    PTM databases

    PhosphoSiteiQ96MH2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with higher expression in testis. HEXIM1 and HEXIM2 are differentially expressed.1 Publication

    Inductioni

    Up-regulated by HMBA (hexamethylene bisacetamide) (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ96MH2.
    BgeeiQ96MH2.
    CleanExiHS_HEXIM2.
    GenevestigatoriQ96MH2.

    Organism-specific databases

    HPAiHPA023323.
    HPA028455.

    Interactioni

    Subunit structurei

    Homooligomer and heterooligomer with HEXIM1; 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.2 Publications

    Protein-protein interaction databases

    BioGridi125888. 7 interactions.
    IntActiQ96MH2. 3 interactions.
    STRINGi9606.ENSP00000302276.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96MH2.
    SMRiQ96MH2. Positions 187-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni140 – 1434Interaction with P-TEFb
    Regioni226 – 28661Interaction with CCNT1, HEXIM1 and HEXIM2Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili207 – 27771Sequence 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.
    HOVERGENiHBG107976.
    InParanoidiQ96MH2.
    KOiK15189.
    OMAiPCRQVEE.
    OrthoDBiEOG771281.
    PhylomeDBiQ96MH2.
    TreeFamiTF336851.

    Family and domain databases

    InterProiIPR024872. HEXIM.
    IPR024876. HEXIM2.
    [Graphical view]
    PANTHERiPTHR13469. PTHR13469. 1 hit.
    PTHR13469:SF3. PTHR13469:SF3. 1 hit.
    PfamiPF15313. HEXIM. 1 hit.
    [Graphical view]
    PRINTSiPR02094. HEXIMFAMILY.

    Sequencei

    Sequence statusi: Complete.

    Q96MH2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMATPNQTAC NAESPVALEE AKTSGAPGSP QTPPERHDSG GSLPLTPRME    50
    SHSEDEDLAG AVGGLGWNSR SPRTQSPGGC SAEAVLARKK HRRRPSKRKR 100
    HWRPYLELSW AEKQQRDERQ SQRASRVREE MFAKGQPVAP YNTTQFLMND 150
    RDPEEPNLDV PHGISHPGSS GESEAGDSDG RGRAHGEFQR KDFSETYERF 200
    HTESLQGRSK QELVRDYLEL EKRLSQAEEE TRRLQQLQAC TGQQSCRQVE 250
    ELAAEVQRLR TENQRLRQEN QMWNREGCRC DEEPGT 286
    Length:286
    Mass (Da):32,419
    Last modified:December 1, 2001 - v1
    Checksum:i58576D72096A8A6F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY598322 mRNA. Translation: AAT06733.1.
    AK056946 mRNA. Translation: BAB71319.1.
    CH471178 Genomic DNA. Translation: EAW51541.1.
    CH471178 Genomic DNA. Translation: EAW51542.1.
    BC003531 mRNA. Translation: AAH03531.1.
    BC012474 mRNA. Translation: AAH12474.1.
    BC025970 mRNA. Translation: AAH25970.1.
    CCDSiCCDS11496.1.
    RefSeqiNP_653209.1. NM_144608.1.
    XP_005257095.1. XM_005257038.2.
    XP_005257096.1. XM_005257039.2.
    XP_005257097.1. XM_005257040.2.
    XP_005257098.1. XM_005257041.2.
    XP_006721751.1. XM_006721688.1.
    XP_006721752.1. XM_006721689.1.
    UniGeneiHs.56382.

    Genome annotation databases

    EnsembliENST00000307275; ENSP00000302276; ENSG00000168517.
    ENST00000591576; ENSP00000465727; ENSG00000168517.
    ENST00000592695; ENSP00000467517; ENSG00000168517.
    GeneIDi124790.
    KEGGihsa:124790.
    UCSCiuc002iih.1. human.

    Polymorphism databases

    DMDMi74732374.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY598322 mRNA. Translation: AAT06733.1 .
    AK056946 mRNA. Translation: BAB71319.1 .
    CH471178 Genomic DNA. Translation: EAW51541.1 .
    CH471178 Genomic DNA. Translation: EAW51542.1 .
    BC003531 mRNA. Translation: AAH03531.1 .
    BC012474 mRNA. Translation: AAH12474.1 .
    BC025970 mRNA. Translation: AAH25970.1 .
    CCDSi CCDS11496.1.
    RefSeqi NP_653209.1. NM_144608.1.
    XP_005257095.1. XM_005257038.2.
    XP_005257096.1. XM_005257039.2.
    XP_005257097.1. XM_005257040.2.
    XP_005257098.1. XM_005257041.2.
    XP_006721751.1. XM_006721688.1.
    XP_006721752.1. XM_006721689.1.
    UniGenei Hs.56382.

    3D structure databases

    ProteinModelPortali Q96MH2.
    SMRi Q96MH2. Positions 187-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125888. 7 interactions.
    IntActi Q96MH2. 3 interactions.
    STRINGi 9606.ENSP00000302276.

    PTM databases

    PhosphoSitei Q96MH2.

    Polymorphism databases

    DMDMi 74732374.

    Proteomic databases

    MaxQBi Q96MH2.
    PaxDbi Q96MH2.
    PRIDEi Q96MH2.

    Protocols and materials databases

    DNASUi 124790.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307275 ; ENSP00000302276 ; ENSG00000168517 .
    ENST00000591576 ; ENSP00000465727 ; ENSG00000168517 .
    ENST00000592695 ; ENSP00000467517 ; ENSG00000168517 .
    GeneIDi 124790.
    KEGGi hsa:124790.
    UCSCi uc002iih.1. human.

    Organism-specific databases

    CTDi 124790.
    GeneCardsi GC17P043238.
    HGNCi HGNC:28591. HEXIM2.
    HPAi HPA023323.
    HPA028455.
    MIMi 615695. gene.
    neXtProti NX_Q96MH2.
    PharmGKBi PA142671695.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72325.
    HOGENOMi HOG000060338.
    HOVERGENi HBG107976.
    InParanoidi Q96MH2.
    KOi K15189.
    OMAi PCRQVEE.
    OrthoDBi EOG771281.
    PhylomeDBi Q96MH2.
    TreeFami TF336851.

    Miscellaneous databases

    GeneWikii HEXIM2.
    GenomeRNAii 124790.
    NextBioi 81380.
    PROi Q96MH2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96MH2.
    Bgeei Q96MH2.
    CleanExi HS_HEXIM2.
    Genevestigatori Q96MH2.

    Family and domain databases

    InterProi IPR024872. HEXIM.
    IPR024876. HEXIM2.
    [Graphical view ]
    PANTHERi PTHR13469. PTHR13469. 1 hit.
    PTHR13469:SF3. PTHR13469:SF3. 1 hit.
    Pfami PF15313. HEXIM. 1 hit.
    [Graphical view ]
    PRINTSi PR02094. HEXIMFAMILY.
    ProtoNeti Search...

    Publicationsi

    1. "Suppression subtractive hybridization and expression profiling identifies a unique set of genes overexpressed in non-small-cell lung cancer."
      Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., Cerveny C., Law C.-L., Wahl A., Carter P.
      Oncogene 23:7734-7745(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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: Skeletal muscle.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Eye, Prostate and Uterus.
    5. "HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK."
      Byers S.A., Price J.P., Cooper J.J., Li Q., Price D.H.
      J. Biol. Chem. 280:16360-16367(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, MUTAGENESIS OF THR-143.
    6. "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, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, INTERACTION WITH HEXIM1, OLIGOMERIZATION, TISSUE SPECIFICITY, INDUCTION.
    7. "Transcription-dependent association of multiple positive transcription elongation factor units to a HEXIM multimer."
      Dulac C., Michels A.A., Fraldi A., Bonnet F., Nguyen V.T., Napolitano G., Lania L., Bensaude O.
      J. Biol. Chem. 280:30619-30629(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: OLIGOMERIZATION, INTERACTION WITH CCNT1, SUBCELLULAR LOCATION.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-32; THR-46; SER-51; SER-53; SER-71; SER-76 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHEXI2_HUMAN
    AccessioniPrimary (citable) accession number: Q96MH2
    Secondary accession number(s): D3DX66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 103 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

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3