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Q12962 (TAF10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TAF10
Synonyms:TAF2A, TAF2H, TAFII30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15

Subcellular location

Nucleus Ref.7 Ref.8.

Domain

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

Post-translational modification

Monomethylated at Lys-189 by SETD7, leading to increase its affinity for RNA polymerase II. Ref.12 Ref.13

Sequence similarities

Belongs to the TAF10 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   PTMAcetylation
Methylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, initiation

Inferred from direct assay PubMed 9212049PubMed 9603525. Source: UniProtKB

chromatin organization

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay Ref.8Ref.7. Source: UniProtKB

histone deubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred by curator PubMed 7729427. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 9603525. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentPCAF complex

Inferred from direct assay Ref.7. Source: UniProtKB

STAGA complex

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 15870280. Source: HGNC

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15870280. Source: HGNC

transcription factor TFIID complex

Inferred from direct assay Ref.12PubMed 7729427Ref.1. Source: UniProtKB

transcription factor TFTC complex

Inferred from direct assay Ref.10PubMed 9603525. Source: UniProtKB

   Molecular_functionRNA polymerase binding

Inferred from direct assay Ref.12. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.13. Source: UniProtKB

estrogen receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 7729427. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN7O152656EBI-708376,EBI-708350
SETD7Q8WTS62EBI-708376,EBI-1268586

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 218217Transcription initiation factor TFIID subunit 10
PRO_0000118897

Regions

Motif187 – 1893[KR]-[STA]-K motif

Amino acid modifications

Modified residue21N-acetylserine Ref.16
Modified residue1891N6-methyllysine Ref.12 Ref.13

Natural variations

Natural variant921I → T. Ref.3
Corresponds to variant rs3176311 [ dbSNP | Ensembl ].
VAR_013706

Experimental info

Mutagenesis1891K → Q: Abolishes methylation. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q12962 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 032ED5CA97EBE411

FASTA21821,711
        10         20         30         40         50         60 
MSCSGSGADP EAAPASAASA PGPAPPVSAP AALPSSTAAE NKASPAGTAG GPGAGAAAGG 

        70         80         90        100        110        120 
TGPLAARAGE PAERRGAAPV SAGGAAPPEG AISNGVYVLP SAANGDVKPV VSSTPLVDFL 

       130        140        150        160        170        180 
MQLEDYTPTI PDAVTGYYLN RAGFEASDPR IIRLISLAAQ KFISDIANDA LQHCKMKGTA 

       190        200        210 
SGSSRSKSKD RKYTLTMEDL TPALSEYGIN VKKPHYFT 

« Hide

References

« Hide 'large scale' references
[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]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: Kidney.
[7]"Histone-like TAFs within the PCAF histone acetylase complex."
Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J., Howard B.H., Qin J., Nakatani Y.
Cell 94:35-44(1998) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7769.1.
PIRA57694.
RefSeqNP_006275.1. NM_006284.3.
UniGeneHs.5158.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ12962.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112744. 66 interactions.
DIPDIP-297N.
IntActQ12962. 14 interactions.
MINTMINT-1425043.
STRING9606.ENSP00000299424.

PTM databases

PhosphoSiteQ12962.

Polymorphism databases

DMDM3024688.

Proteomic databases

MaxQBQ12962.
PaxDbQ12962.
PeptideAtlasQ12962.
PRIDEQ12962.

Protocols and materials databases

DNASU6881.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299424; ENSP00000299424; ENSG00000166337.
GeneID6881.
KEGGhsa:6881.
UCSCuc001mej.2. human.

Organism-specific databases

CTD6881.
GeneCardsGC11M006627.
HGNCHGNC:11543. TAF10.
HPACAB022405.
HPA004148.
MIM600475. gene.
neXtProtNX_Q12962.
PharmGKBPA36318.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5162.
HOGENOMHOG000285966.
HOVERGENHBG079227.
InParanoidQ12962.
KOK03134.
OMAQNDIRES.
OrthoDBEOG7P02KJ.
PhylomeDBQ12962.
TreeFamTF313156.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_172623. Chromatin organization.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ12962.
CleanExHS_TAF10.
GenevestigatorQ12962.

Family and domain databases

InterProIPR003923. TFIID_30kDa.
[Graphical view]
PANTHERPTHR21242. PTHR21242. 1 hit.
PfamPF03540. TFIID_30kDa. 1 hit.
[Graphical view]
PIRSFPIRSF017246. TFIID_TAF10. 1 hit.
PRINTSPR01443. TFIID30KDSUB.
ProtoNetSearch...

Other

ChiTaRSTAF10. human.
GeneWikiTAF10.
GenomeRNAi6881.
NextBio26883.
PROQ12962.
SOURCESearch...

Entry information

Entry nameTAF10_HUMAN
AccessionPrimary (citable) accession number: Q12962
Secondary accession number(s): O00703, Q13175, Q6FH13
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 153 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 11

Human chromosome 11: entries, gene names and cross-references to MIM