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Q15545

- TAF7_HUMAN

UniProt

Q15545 - TAF7_HUMAN

Protein

Transcription initiation factor TFIID subunit 7

Gene

TAF7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).

    GO - Molecular functioni

    1. histone acetyltransferase binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. thyroid hormone receptor binding Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. transcription factor binding Source: UniProtKB
    6. transcription regulatory region DNA binding Source: UniProtKB
    7. vitamin D receptor binding Source: UniProtKB

    GO - Biological processi

    1. DNA-templated transcription, initiation Source: UniProtKB
    2. intracellular estrogen receptor signaling pathway Source: Ensembl
    3. negative regulation of histone acetylation Source: UniProtKB
    4. negative regulation of protein kinase activity Source: UniProtKB
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. spermine transport Source: UniProtKB
    9. transcription from RNA polymerase II promoter Source: UniProtKB
    10. transcription initiation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiQ15545.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription initiation factor TFIID subunit 7
    Alternative name(s):
    RNA polymerase II TBP-associated factor subunit F
    Transcription initiation factor TFIID 55 kDa subunit
    Short name:
    TAF(II)55
    Short name:
    TAFII-55
    Short name:
    TAFII55
    Gene namesi
    Name:TAF7
    Synonyms:TAF2F, TAFII55
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:11541. TAF7.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: HPA
    2. MLL1 complex Source: UniProtKB
    3. nucleus Source: HPA
    4. transcription factor TFIID complex Source: UniProtKB
    5. transcription factor TFTC complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51K → R: Abolishes methylation in vitro. 1 Publication
    Mutagenesisi264 – 2641S → A: Reduced H3 acetylation and transcription at target promoters. 1 Publication
    Mutagenesisi264 – 2641S → D: 50% reduction in TAF1-binding, reduced incorporation of TAF7 into TFIID complexes. 1 Publication

    Organism-specific databases

    PharmGKBiPA36316.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Transcription initiation factor TFIID subunit 7PRO_0000118881Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei171 – 1711Phosphoserine2 Publications
    Modified residuei213 – 2131Phosphoserine2 Publications
    Modified residuei264 – 2641Phosphoserine6 Publications

    Post-translational modificationi

    Phosphorylated by CIITA. Phosphorylation at Ser-264 by TAF1 in early G1 phase disrupts binding to TAF1.7 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15545.
    PaxDbiQ15545.
    PRIDEiQ15545.

    PTM databases

    PhosphoSiteiQ15545.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    BgeeiQ15545.
    CleanExiHS_TAF7.
    GenevestigatoriQ15545.

    Organism-specific databases

    HPAiHPA006429.

    Interactioni

    Subunit structurei

    TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TAFII250, TAFII100, TAFII28, TAFII20, and TAFII18, but not with TAFII30 or TBP. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Binds to CIITA and TAF1 and inhibits their acetyltransferase activity, thereby repressing activated transcription and behaving as a repressor at these promoters.2 Publications

    Protein-protein interaction databases

    BioGridi112742. 33 interactions.
    DIPiDIP-29047N.
    IntActiQ15545. 8 interactions.
    MINTiMINT-3031780.
    STRINGi9606.ENSP00000312709.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15545.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili244 – 349106Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 53[KR]-[STA]-K motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi227 – 2304Poly-Ser

    Domaini

    The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase, which methylates Lys-5 in vitro.By similarity

    Sequence similaritiesi

    Belongs to the TAF7 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5414.
    HOGENOMiHOG000035121.
    HOVERGENiHBG013606.
    InParanoidiQ15545.
    KOiK03132.
    OMAiKQGHGSS.
    OrthoDBiEOG7GJ6FT.
    PhylomeDBiQ15545.
    TreeFamiTF313044.

    Family and domain databases

    InterProiIPR006751. TAFII55_prot_cons_reg.
    [Graphical view]
    PfamiPF04658. TAFII55_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15545-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD    50
    GRHGIVRVDR VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD 100
    GDLYPPVEEP VASTDPKASK KKDKDKEKKF IWNHGITLPL KNVRKRRFRK 150
    TAKKKYIESP DVEKEVKRLL STDAEAVSTR WEIIAEDETK EAENQGLDIS 200
    SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD EEDINIIDTE 250
    EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK 300
    RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK 349
    Length:349
    Mass (Da):40,259
    Last modified:November 1, 1996 - v1
    Checksum:i0AAFD3E33E3CCD6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti283 – 2831K → N in AAB60347. (PubMed:7824954)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti178 – 1781S → R.
    VAR_005629

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97999 mRNA. Translation: CAA66636.1.
    U18062 mRNA. Translation: AAB60347.1.
    AF349038 Genomic DNA. Translation: AAK30585.1.
    AK314837 mRNA. Translation: BAG37356.1.
    CH471062 Genomic DNA. Translation: EAW61966.1.
    BC032737 mRNA. Translation: AAH32737.1.
    CCDSiCCDS4259.1.
    PIRiI38904.
    RefSeqiNP_005633.2. NM_005642.2.
    UniGeneiHs.438838.

    Genome annotation databases

    EnsembliENST00000313368; ENSP00000312709; ENSG00000178913.
    GeneIDi6879.
    KEGGihsa:6879.
    UCSCiuc003ljg.3. human.

    Polymorphism databases

    DMDMi3024690.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97999 mRNA. Translation: CAA66636.1 .
    U18062 mRNA. Translation: AAB60347.1 .
    AF349038 Genomic DNA. Translation: AAK30585.1 .
    AK314837 mRNA. Translation: BAG37356.1 .
    CH471062 Genomic DNA. Translation: EAW61966.1 .
    BC032737 mRNA. Translation: AAH32737.1 .
    CCDSi CCDS4259.1.
    PIRi I38904.
    RefSeqi NP_005633.2. NM_005642.2.
    UniGenei Hs.438838.

    3D structure databases

    ProteinModelPortali Q15545.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112742. 33 interactions.
    DIPi DIP-29047N.
    IntActi Q15545. 8 interactions.
    MINTi MINT-3031780.
    STRINGi 9606.ENSP00000312709.

    PTM databases

    PhosphoSitei Q15545.

    Polymorphism databases

    DMDMi 3024690.

    Proteomic databases

    MaxQBi Q15545.
    PaxDbi Q15545.
    PRIDEi Q15545.

    Protocols and materials databases

    DNASUi 6879.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313368 ; ENSP00000312709 ; ENSG00000178913 .
    GeneIDi 6879.
    KEGGi hsa:6879.
    UCSCi uc003ljg.3. human.

    Organism-specific databases

    CTDi 6879.
    GeneCardsi GC05M140678.
    HGNCi HGNC:11541. TAF7.
    HPAi HPA006429.
    MIMi 600573. gene.
    neXtProti NX_Q15545.
    PharmGKBi PA36316.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5414.
    HOGENOMi HOG000035121.
    HOVERGENi HBG013606.
    InParanoidi Q15545.
    KOi K03132.
    OMAi KQGHGSS.
    OrthoDBi EOG7GJ6FT.
    PhylomeDBi Q15545.
    TreeFami TF313044.

    Enzyme and pathway databases

    SignaLinki Q15545.

    Miscellaneous databases

    ChiTaRSi TAF7. human.
    GeneWikii TAF7.
    GenomeRNAii 6879.
    NextBioi 26869.
    PROi Q15545.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15545.
    CleanExi HS_TAF7.
    Genevestigatori Q15545.

    Family and domain databases

    InterProi IPR006751. TAFII55_prot_cons_reg.
    [Graphical view ]
    Pfami PF04658. TAFII55_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multiple interactions between hTAFII55 and other TFIID subunits. Requirements for the formation of stable ternary complexes between hTAFII55 and the TATA-binding protein."
      Lavigne A.C., Mengus G., May M., Dubrowskaya V., Tora L., Davidson I.
      J. Biol. Chem. 271:19774-19780(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators."
      Chiang C.-M., Roeder R.G.
      Science 267:531-536(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The intronless and TATA-less human TAFII55 gene contains a functional initiator and a downstream promoter element."
      Zhou T., Chiang C.-M.
      J. Biol. Chem. 276:25503-25511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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: Brain.
    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: Skin.
    7. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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, MUTAGENESIS OF LYS-5.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene transcription by TFIID subunits TAF1 and TAF7."
      Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.
      Mol. Cell. Biol. 32:3358-3369(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAF1, MISCELLANEOUS, PHOSPHORYLATION AT SER-264, MUTAGENESIS OF SER-264.
    16. "Transcriptional coactivator CIITA, a functional homolog of TAF1, has kinase activity."
      Soe K.C., Devaiah B.N., Singer D.S.
      Biochim. Biophys. Acta 1829:1184-1190(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CIITA.

    Entry informationi

    Entry nameiTAF7_HUMAN
    AccessioniPrimary (citable) accession number: Q15545
    Secondary accession number(s): B2RBV9, Q13036
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 127 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

    Overexpression of TAF7 in HeLa cells inhibits cyclin D1 and cyclin A gene transcription and causes the cells to accumulate in early S phase. In contrast, depletion of TAF7 from TFIID complexes by siRNAs increases histone H3 acetylation at both cyclin promoters and stimulates cyclins CCND1 and CCNA gene transcription.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3