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Q9HBM6

- TAF9B_HUMAN

UniProt

Q9HBM6 - TAF9B_HUMAN

Protein

Transcription initiation factor TFIID subunit 9B

Gene

TAF9B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transcription corepressor activity Source: BHF-UCL

    GO - Biological processi

    1. DNA-templated transcription, initiation Source: InterPro
    2. negative regulation of apoptotic process Source: BHF-UCL
    3. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    4. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    5. positive regulation of cell growth Source: UniProtKB
    6. programmed cell death Source: Ensembl
    7. protein stabilization Source: BHF-UCL
    8. response to organic cyclic compound Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription initiation factor TFIID subunit 9B
    Alternative name(s):
    Neuronal cell death-related protein 7
    Short name:
    DN-7
    Transcription initiation factor TFIID subunit 9-like
    Transcription-associated factor TAFII31L
    Gene namesi
    Name:TAF9B
    Synonyms:TAF9L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17306. TAF9B.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. transcription factor TFIID complex Source: UniProtKB
    2. transcription factor TFTC complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38225.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Transcription initiation factor TFIID subunit 9BPRO_0000118891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei159 – 1591Phosphothreonine1 Publication
    Modified residuei174 – 1741Phosphothreonine1 Publication
    Modified residuei177 – 1771Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HBM6.
    PaxDbiQ9HBM6.
    PRIDEiQ9HBM6.

    PTM databases

    PhosphoSiteiQ9HBM6.

    Expressioni

    Gene expression databases

    BgeeiQ9HBM6.
    CleanExiHS_TAF9B.
    GenevestigatoriQ9HBM6.

    Organism-specific databases

    HPAiHPA045275.

    Interactioni

    Subunit structurei

    Binds TAF5 and TAF6. Component of TFIID and the TATA-binding protein-free TAF complex (TFTC). TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Binds N-terminal domain of p53/TP53 which is essential for transcription.1 Publication

    Protein-protein interaction databases

    BioGridi119639. 21 interactions.
    IntActiQ9HBM6. 2 interactions.
    MINTiMINT-1441128.
    STRINGi9606.ENSP00000339917.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HBM6.
    SMRiQ9HBM6. Positions 13-76.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi244 – 2496Poly-AspSequence Analysis

    Sequence similaritiesi

    Belongs to the TAF9 family.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG5094.
    HOGENOMiHOG000231730.
    HOVERGENiHBG002304.
    InParanoidiQ9HBM6.
    KOiK03133.
    OMAiNMANESN.
    OrthoDBiEOG7HF1KM.
    PhylomeDBiQ9HBM6.
    TreeFamiTF351417.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR003162. TFIID-31.
    [Graphical view]
    PANTHERiPTHR12075. PTHR12075. 1 hit.
    PfamiPF02291. TFIID-31kDa. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9HBM6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESGKMAPPK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI    50
    LDDAKIYSSH AKKPNVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN 100
    QTPLPLIKPY AGPRLPPDRY CLTAPNYRLK SLIKKGPNQG RLVPRLSVGA 150
    VSSKPTTPTI ATPQTVSVPN KVATPMSVTS QRFTVQIPPS QSTPVKPVPA 200
    TTAVQNVLIN PSMIGPKNIL ITTNMVSSQN TANEANPLKR KHEDDDDNDI 250
    M 251
    Length:251
    Mass (Da):27,622
    Last modified:March 1, 2001 - v1
    Checksum:iEB3A1116F7E8BCA0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31S → L in AAD27786. 1 PublicationCurated
    Sequence conflicti209 – 2091I → D in AAD27786. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077053 mRNA. Translation: AAD27786.1.
    AF220509 mRNA. Translation: AAG09711.1.
    AL049589 Genomic DNA. Translation: CAI42952.1.
    CH471104 Genomic DNA. Translation: EAW98601.1.
    BC009566 mRNA. Translation: AAH09566.1.
    BC010350 mRNA. Translation: AAH10350.1.
    BC071649 mRNA. Translation: AAH71649.1.
    BC146952 mRNA. Translation: AAI46953.1.
    BC146960 mRNA. Translation: AAI46961.1.
    CCDSiCCDS35340.1.
    RefSeqiNP_057059.2. NM_015975.4.
    UniGeneiHs.592248.

    Genome annotation databases

    EnsembliENST00000341864; ENSP00000339917; ENSG00000187325.
    GeneIDi51616.
    KEGGihsa:51616.
    UCSCiuc004eda.3. human.

    Polymorphism databases

    DMDMi74752778.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077053 mRNA. Translation: AAD27786.1 .
    AF220509 mRNA. Translation: AAG09711.1 .
    AL049589 Genomic DNA. Translation: CAI42952.1 .
    CH471104 Genomic DNA. Translation: EAW98601.1 .
    BC009566 mRNA. Translation: AAH09566.1 .
    BC010350 mRNA. Translation: AAH10350.1 .
    BC071649 mRNA. Translation: AAH71649.1 .
    BC146952 mRNA. Translation: AAI46953.1 .
    BC146960 mRNA. Translation: AAI46961.1 .
    CCDSi CCDS35340.1.
    RefSeqi NP_057059.2. NM_015975.4.
    UniGenei Hs.592248.

    3D structure databases

    ProteinModelPortali Q9HBM6.
    SMRi Q9HBM6. Positions 13-76.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119639. 21 interactions.
    IntActi Q9HBM6. 2 interactions.
    MINTi MINT-1441128.
    STRINGi 9606.ENSP00000339917.

    PTM databases

    PhosphoSitei Q9HBM6.

    Polymorphism databases

    DMDMi 74752778.

    Proteomic databases

    MaxQBi Q9HBM6.
    PaxDbi Q9HBM6.
    PRIDEi Q9HBM6.

    Protocols and materials databases

    DNASUi 51616.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341864 ; ENSP00000339917 ; ENSG00000187325 .
    GeneIDi 51616.
    KEGGi hsa:51616.
    UCSCi uc004eda.3. human.

    Organism-specific databases

    CTDi 51616.
    GeneCardsi GC0XM077385.
    H-InvDB HIX0176727.
    HGNCi HGNC:17306. TAF9B.
    HPAi HPA045275.
    MIMi 300754. gene.
    neXtProti NX_Q9HBM6.
    PharmGKBi PA38225.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5094.
    HOGENOMi HOG000231730.
    HOVERGENi HBG002304.
    InParanoidi Q9HBM6.
    KOi K03133.
    OMAi NMANESN.
    OrthoDBi EOG7HF1KM.
    PhylomeDBi Q9HBM6.
    TreeFami TF351417.

    Miscellaneous databases

    GeneWikii TAF9B.
    GenomeRNAii 51616.
    NextBioi 55524.
    PROi Q9HBM6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9HBM6.
    CleanExi HS_TAF9B.
    Genevestigatori Q9HBM6.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR003162. TFIID-31.
    [Graphical view ]
    PANTHERi PTHR12075. PTHR12075. 1 hit.
    Pfami PF02291. TFIID-31kDa. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human neuronal cell death related gene in neuron-7 (DN-7)."
      Peng Y., Song H., Zhou J., Huang Q., Dai M., Mao Y., Yu Y., Xu X., Luo B., Chen J., Hu R.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: PituitaryImported.
    2. "Characterization of a new TAFII31 gene located in Xq13.3."
      Villard L.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: BrainImported and Urinary bladderImported.
    6. "TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9."
      Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B., Scheer E., Tora L.
      Mol. Cell. Biol. 25:4638-4649(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TFTC-HAT COMPLEX, INTERACTION WITH TAF5 AND TAF6.
    7. "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 THR-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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 THR-174 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTAF9B_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBM6
    Secondary accession number(s): B2RUZ9, Q9Y2S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 125 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 X
      Human chromosome X: 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