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Q15545 (TAF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TAF7
Synonyms:TAF2F, TAFII55
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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).

Subunit structure

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. Ref.7 Ref.15

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous.

Domain

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

Post-translational modification

Phosphorylated by CIITA. Phosphorylation at Ser-264 by TAF1 in early G1 phase disrupts binding to TAF1. Ref.15 Ref.16

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.

Sequence similarities

Belongs to the TAF7 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, initiation

Inferred from direct assay PubMed 9603525. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone acetylation

Inferred from direct assay PubMed 11592977. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay PubMed 18391197. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11592977PubMed 16407123PubMed 18391197. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11592977PubMed 16407123PubMed 18391197. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12676957. Source: UniProtKB

spermine transport

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 16407123PubMed 9603525. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

MLL1 complex

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFIID complex

Inferred from direct assay Ref.2. Source: UniProtKB

transcription factor TFTC complex

Inferred from direct assay PubMed 9603525. Source: UniProtKB

   Molecular_functionhistone acetyltransferase binding

Inferred from physical interaction PubMed 11592977. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2. Source: UniProtKB

thyroid hormone receptor binding

Inferred from physical interaction PubMed 10409738. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.2. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 11005381PubMed 12676957Ref.2. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18391197. Source: UniProtKB

vitamin D receptor binding

Inferred from physical interaction PubMed 10409738. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Transcription initiation factor TFIID subunit 7
PRO_0000118881

Regions

Coiled coil244 – 349106 Potential
Motif3 – 53[KR]-[STA]-K motif
Compositional bias227 – 2304Poly-Ser

Amino acid modifications

Modified residue1711Phosphoserine Ref.11
Modified residue2131Phosphoserine Ref.8
Modified residue2641Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Natural variations

Natural variant1781S → R.
VAR_005629

Experimental info

Mutagenesis51K → R: Abolishes methylation in vitro. Ref.9
Mutagenesis2641S → A: Reduced H3 acetylation and transcription at target promoters. Ref.15
Mutagenesis2641S → D: 50% reduction in TAF1-binding, reduced incorporation of TAF7 into TFIID complexes. Ref.15
Sequence conflict2831K → N in AAB60347. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q15545 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0AAFD3E33E3CCD6E

FASTA34940,259
        10         20         30         40         50         60 
MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD GRHGIVRVDR 

        70         80         90        100        110        120 
VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD GDLYPPVEEP VASTDPKASK 

       130        140        150        160        170        180 
KKDKDKEKKF IWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR 

       190        200        210        220        230        240 
WEIIAEDETK EAENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD 

       250        260        270        280        290        300 
EEDINIIDTE EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK 

       310        320        330        340 
RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4259.1.
PIRI38904.
RefSeqNP_005633.2. NM_005642.2.
UniGeneHs.438838.

3D structure databases

ProteinModelPortalQ15545.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112742. 33 interactions.
DIPDIP-29047N.
IntActQ15545. 8 interactions.
MINTMINT-3031780.
STRING9606.ENSP00000312709.

PTM databases

PhosphoSiteQ15545.

Polymorphism databases

DMDM3024690.

Proteomic databases

MaxQBQ15545.
PaxDbQ15545.
PRIDEQ15545.

Protocols and materials databases

DNASU6879.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313368; ENSP00000312709; ENSG00000178913.
GeneID6879.
KEGGhsa:6879.
UCSCuc003ljg.3. human.

Organism-specific databases

CTD6879.
GeneCardsGC05M140678.
HGNCHGNC:11541. TAF7.
HPAHPA006429.
MIM600573. gene.
neXtProtNX_Q15545.
PharmGKBPA36316.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5414.
HOGENOMHOG000035121.
HOVERGENHBG013606.
InParanoidQ15545.
KOK03132.
OMAKQGHGSS.
OrthoDBEOG7GJ6FT.
PhylomeDBQ15545.
TreeFamTF313044.

Enzyme and pathway databases

SignaLinkQ15545.

Gene expression databases

BgeeQ15545.
CleanExHS_TAF7.
GenevestigatorQ15545.

Family and domain databases

InterProIPR006751. TAFII55_prot_cons_reg.
[Graphical view]
PfamPF04658. TAFII55_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTAF7. human.
GeneWikiTAF7.
GenomeRNAi6879.
NextBio26869.
PROQ15545.
SOURCESearch...

Entry information

Entry nameTAF7_HUMAN
AccessionPrimary (citable) accession number: Q15545
Secondary accession number(s): B2RBV9, Q13036
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM