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Q12962

- TAF10_HUMAN

UniProt

Q12962 - TAF10_HUMAN

Protein

Transcription initiation factor TFIID subunit 10

Gene

TAF10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. estrogen receptor binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA polymerase binding Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. DNA-templated transcription, initiation Source: UniProtKB
    3. gene expression Source: Reactome
    4. histone deubiquitination Source: UniProtKB
    5. histone H3 acetylation Source: UniProtKB
    6. protein homooligomerization Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. transcription elongation from RNA polymerase II promoter Source: Reactome
    9. transcription from RNA polymerase II promoter Source: UniProtKB
    10. transcription initiation from RNA polymerase II promoter Source: UniProtKB
    11. viral process Source: Reactome

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_172610. HATs acetylate histones.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_6233. Transcription of the HIV genome.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6332. HIV Transcription Initiation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription initiation factor TFIID subunit 10
    Alternative name(s):
    STAF28
    Transcription initiation factor TFIID 30 kDa subunit
    Short name:
    TAF(II)30
    Short name:
    TAFII-30
    Short name:
    TAFII30
    Gene namesi
    Name:TAF10
    Synonyms:TAF2A, TAF2H, TAFII30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11543. TAF10.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. PCAF complex Source: UniProtKB
    5. perinuclear region of cytoplasm Source: HGNC
    6. STAGA complex Source: UniProtKB
    7. transcription factor TFIID complex Source: UniProtKB
    8. transcription factor TFTC complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi189 – 1891K → Q: Abolishes methylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA36318.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 218217Transcription initiation factor TFIID subunit 10PRO_0000118897Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei189 – 1891N6-methyllysine2 Publications

    Post-translational modificationi

    Monomethylated at Lys-189 by SETD7, leading to increase its affinity for RNA polymerase II.

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    MaxQBiQ12962.
    PaxDbiQ12962.
    PeptideAtlasiQ12962.
    PRIDEiQ12962.

    PTM databases

    PhosphoSiteiQ12962.

    Expressioni

    Gene expression databases

    BgeeiQ12962.
    CleanExiHS_TAF10.
    GenevestigatoriQ12962.

    Organism-specific databases

    HPAiCAB022405.
    HPA004148.

    Interactioni

    Subunit structurei

    TFIID and PCAF are composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TBP is not part of TFTC. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, SUPT3H, TAF5L TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22. Interacts with TAF3.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN7O152656EBI-708376,EBI-708350
    SETD7Q8WTS62EBI-708376,EBI-1268586

    Protein-protein interaction databases

    BioGridi112744. 66 interactions.
    DIPiDIP-297N.
    IntActiQ12962. 14 interactions.
    MINTiMINT-1425043.
    STRINGi9606.ENSP00000299424.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F69X-ray1.30B186-195[»]
    3M53X-ray1.85B186-195[»]
    3M54X-ray1.60B186-195[»]
    3M55X-ray1.55B186-195[»]
    3M56X-ray1.65B186-195[»]
    3M57X-ray1.70B186-195[»]
    3M58X-ray1.40B186-195[»]
    3M59X-ray1.70B186-195[»]
    3M5AX-ray1.75B186-195[»]
    4J7FX-ray1.59B186-195[»]
    4J7IX-ray2.56B186-195[»]
    4J83X-ray1.70B186-195[»]
    4J8OX-ray1.63B186-195[»]
    ProteinModelPortaliQ12962.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi187 – 1893[KR]-[STA]-K motif

    Domaini

    The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase.

    Sequence similaritiesi

    Belongs to the TAF10 family.Curated

    Phylogenomic databases

    eggNOGiCOG5162.
    HOGENOMiHOG000285966.
    HOVERGENiHBG079227.
    InParanoidiQ12962.
    KOiK03134.
    OMAiQNDIRES.
    OrthoDBiEOG7P02KJ.
    PhylomeDBiQ12962.
    TreeFamiTF313156.

    Family and domain databases

    InterProiIPR003923. TFIID_30kDa.
    [Graphical view]
    PANTHERiPTHR21242. PTHR21242. 1 hit.
    PfamiPF03540. TFIID_30kDa. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017246. TFIID_TAF10. 1 hit.
    PRINTSiPR01443. TFIID30KDSUB.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q12962-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSCSGSGADP EAAPASAASA PGPAPPVSAP AALPSSTAAE NKASPAGTAG    50
    GPGAGAAAGG TGPLAARAGE PAERRGAAPV SAGGAAPPEG AISNGVYVLP 100
    SAANGDVKPV VSSTPLVDFL MQLEDYTPTI PDAVTGYYLN RAGFEASDPR 150
    IIRLISLAAQ KFISDIANDA LQHCKMKGTA SGSSRSKSKD RKYTLTMEDL 200
    TPALSEYGIN VKKPHYFT 218
    Length:218
    Mass (Da):21,711
    Last modified:November 1, 1996 - v1
    Checksum:i032ED5CA97EBE411
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921I → T.1 Publication
    Corresponds to variant rs3176311 [ dbSNP | Ensembl ].
    VAR_013706

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13991 mRNA. Translation: AAA62230.1.
    U25816 Genomic DNA. Translation: AAB61242.1.
    AF498312 Genomic DNA. Translation: AAM14627.1.
    CR541943 mRNA. Translation: CAG46741.1.
    CH471064 Genomic DNA. Translation: EAW68687.1.
    BC012088 mRNA. Translation: AAH12088.1.
    CCDSiCCDS7769.1.
    PIRiA57694.
    RefSeqiNP_006275.1. NM_006284.3.
    UniGeneiHs.5158.

    Genome annotation databases

    EnsembliENST00000299424; ENSP00000299424; ENSG00000166337.
    GeneIDi6881.
    KEGGihsa:6881.
    UCSCiuc001mej.2. human.

    Polymorphism databases

    DMDMi3024688.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13991 mRNA. Translation: AAA62230.1 .
    U25816 Genomic DNA. Translation: AAB61242.1 .
    AF498312 Genomic DNA. Translation: AAM14627.1 .
    CR541943 mRNA. Translation: CAG46741.1 .
    CH471064 Genomic DNA. Translation: EAW68687.1 .
    BC012088 mRNA. Translation: AAH12088.1 .
    CCDSi CCDS7769.1.
    PIRi A57694.
    RefSeqi NP_006275.1. NM_006284.3.
    UniGenei Hs.5158.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F69 X-ray 1.30 B 186-195 [» ]
    3M53 X-ray 1.85 B 186-195 [» ]
    3M54 X-ray 1.60 B 186-195 [» ]
    3M55 X-ray 1.55 B 186-195 [» ]
    3M56 X-ray 1.65 B 186-195 [» ]
    3M57 X-ray 1.70 B 186-195 [» ]
    3M58 X-ray 1.40 B 186-195 [» ]
    3M59 X-ray 1.70 B 186-195 [» ]
    3M5A X-ray 1.75 B 186-195 [» ]
    4J7F X-ray 1.59 B 186-195 [» ]
    4J7I X-ray 2.56 B 186-195 [» ]
    4J83 X-ray 1.70 B 186-195 [» ]
    4J8O X-ray 1.63 B 186-195 [» ]
    ProteinModelPortali Q12962.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112744. 66 interactions.
    DIPi DIP-297N.
    IntActi Q12962. 14 interactions.
    MINTi MINT-1425043.
    STRINGi 9606.ENSP00000299424.

    PTM databases

    PhosphoSitei Q12962.

    Polymorphism databases

    DMDMi 3024688.

    Proteomic databases

    MaxQBi Q12962.
    PaxDbi Q12962.
    PeptideAtlasi Q12962.
    PRIDEi Q12962.

    Protocols and materials databases

    DNASUi 6881.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299424 ; ENSP00000299424 ; ENSG00000166337 .
    GeneIDi 6881.
    KEGGi hsa:6881.
    UCSCi uc001mej.2. human.

    Organism-specific databases

    CTDi 6881.
    GeneCardsi GC11M006627.
    HGNCi HGNC:11543. TAF10.
    HPAi CAB022405.
    HPA004148.
    MIMi 600475. gene.
    neXtProti NX_Q12962.
    PharmGKBi PA36318.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5162.
    HOGENOMi HOG000285966.
    HOVERGENi HBG079227.
    InParanoidi Q12962.
    KOi K03134.
    OMAi QNDIRES.
    OrthoDBi EOG7P02KJ.
    PhylomeDBi Q12962.
    TreeFami TF313156.

    Enzyme and pathway databases

    Reactomei REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_172610. HATs acetylate histones.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_6233. Transcription of the HIV genome.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6332. HIV Transcription Initiation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

    Miscellaneous databases

    ChiTaRSi TAF10. human.
    GeneWikii TAF10.
    GenomeRNAii 6881.
    NextBioi 26883.
    PROi Q12962.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q12962.
    CleanExi HS_TAF10.
    Genevestigatori Q12962.

    Family and domain databases

    InterProi IPR003923. TFIID_30kDa.
    [Graphical view ]
    PANTHERi PTHR21242. PTHR21242. 1 hit.
    Pfami PF03540. TFIID_30kDa. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017246. TFIID_TAF10. 1 hit.
    PRINTSi PR01443. TFIID30KDSUB.
    ProtoNeti Search...

    Publicationsi

    1. "Human TAFII30 is present in a distinct TFIID complex and is required for transcriptional activation by the estrogen receptor."
      Jacq X., Brou C., Lutz Y., Davidson I., Chambon P., Tora L.
      Cell 79:107-117(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Organization and chromosomal localization of the gene (TAF2H) encoding the human TBP-associated factor II 30 (TAFII30)."
      Scheer E., Mattei M.-G., Jacq X., Chambon P., Tora L.
      Genomics 29:269-272(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    3. NIEHS SNPs program
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-92.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Kidney.
    7. Cited for: PROTEIN SEQUENCE OF 43-67, SUBUNIT, SUBCELLULAR LOCATION.
    8. "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
      Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
      Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF12 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily."
      Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J., Nakatani Y.
      Mol. Cell 2:869-875(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H; TAF6L; TAF12; TRRAP AND TAF9.
    10. "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."
      Brand M., Yamamoto K., Staub A., Tora L.
      J. Biol. Chem. 274:18285-18289(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; TRRAP; GCN5L2 AND TAF10.
    11. "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger."
      Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.
      Mol. Cell. Biol. 21:5109-5121(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAF3.
    12. "Gene-specific modulation of TAF10 function by SET9-mediated methylation."
      Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.
      Mol. Cell 14:175-182(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-189, MUTAGENESIS OF LYS-189.
    13. "Structural basis for the methylation site specificity of SET7/9."
      Couture J.-F., Collazo E., Hauk G., Trievel R.C.
      Nat. Struct. Mol. Biol. 13:140-146(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MOTIF, METHYLATION AT LYS-189.
    14. "Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis."
      Cavusoglu N., Brand M., Tora L., van Dorsselaer A.
      Proteomics 3:217-223(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
      Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
      Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN STAGA COMPLEX.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTAF10_HUMAN
    AccessioniPrimary (citable) accession number: Q12962
    Secondary accession number(s): O00703, Q13175, Q6FH13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 155 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3