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Reviewed, UniProtKB/Swiss-Prot Q12962 (TAF10_HUMAN)

Last modified November 25, 2008. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transcription initiation factor TFIID subunit 10
Alternative name(s):
    Transcription initiation factor TFIID 30 kDa subunit
      Short name=TAF(II)30
      Short name=TAFII-30
      Short name=TAFII30
    STAF28
Gene names
Name: TAF10
Synonyms: TAF2A, TAF2H, TAFII30
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Interacts with TAF3.

Subcellular location

Nucleus.

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.

Sequence similarities

Belongs to the TAF10 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SETD7Q8WTS62EBI-708376,EBI-1268586

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 218218Transcription initiation factor TFIID subunit 10
PRO_0000118897

Regions

Motif187 – 1893[KR]-[STA]-K motif

Amino acid modifications

Modified residue1891N6-methyllysine

Natural variations

Natural variant921I → T: dbSNP rs3176311.
VAR_013706

Experimental info

Mutagenesis1891K → Q: Abolishes methylation

Sequences

Sequence LengthMass (Da)Tools
Q12962-1 [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: 7923369] [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: 8530084] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[3]"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
Rieder M.J., Braun A.C., Montoya M.A., Chung M.-W., Nguyen C.P., Nguyen D.A., Livingston R.J., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-92.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]"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: 9674425] [Abstract]
Cited for: PROTEIN SEQUENCE OF 43-67, SUBUNIT, SUBCELLULAR LOCATION.
[6]"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: 11564863] [Abstract]
Cited for: MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF12 AND TAF9.
[7]"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: 9885574] [Abstract]
Cited for: IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H; TAF6L; TAF12; TRRAP AND TAF9.
[8]"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: 10373431] [Abstract]
Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; TRRAP; GCN5L2 AND TAF10.
[9]"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: 11438666] [Abstract]
Cited for: INTERACTION WITH TAF3.
[10]"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: 15099517] [Abstract]
Cited for: METHYLATION AT LYS-189, MUTAGENESIS OF LYS-189.
[11]"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: 16415881] [Abstract]
Cited for: MOTIF, METHYLATION AT LYS-189.
[12]"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: 12601814] [Abstract]
Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U13991 mRNA. Translation: AAA62230.1.
U25816 Genomic DNA. Translation: AAB61242.1.
AF498312 Genomic DNA. Translation: AAM14627.1.
BC012088 mRNA. Translation: AAH12088.1.
PIRA57694.
RefSeqNP_006275.1.
UniGeneHs.705378

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29046N.
DIP:297N.
IntActQ12962.

PTM databases

PhosphoSiteQ12962.

Polymorphism databases

NIEHS-SNPsSearch...

Proteomic databases

PeptideAtlasQ12962.

Genome annotation databases

EnsemblENSG00000166337. Homo sapiens. [Contig view]
GeneID6881.
KEGGhsa:6881.

Organism-specific databases

H-InvDBHIX0009409.
HGNCHGNC:11543. TAF10.
HPAHPA004148.
MIM600475. gene.
PharmGKBPA36318.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ12962.
HOVERGENQ12962.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

CleanExHS_TAF10.
GermOnlineENSG00000166337. Homo sapiens.

Family and domain databases

InterProIPR003923. TFIID_30kD.
[Graphical view]
PANTHERPTHR21242. TFIID_30kD. 1 hit.
PfamPF03540. TFIID_30kDa. 1 hit.
[Graphical view]
PIRSFPIRSF017246. TFIID_TAF10. 1 hit.
PRINTSPR01443. TFIID30KDSUB.
ProtoNetSearch...

Other Resources

LinkHubQ12962.
NextBio26883.
SOURCESearch...

Entry information

Entry nameTAF10_HUMAN
AccessionPrimary (citable) accession number: Q12962
Secondary accession number(s): O00703, Q13175
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents