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Q16514 (TAF12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 12
Alternative name(s):
Transcription initiation factor TFIID 20/15 kDa subunits
Short name=TAFII-20/TAFII-15
Short name=TAFII20/TAFII15
Gene names
Name:TAF12
Synonyms:TAF15, TAF2J, TAFII20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
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). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription.

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. Interacts directly with TBP; additional interactions between TAFII20 and TAFII28 or TAFII30 were detected. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, STAF65-gamma/KIAA0764, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Interacts (isoform TAFII15 and isoform TAFII20)with ATF7 (via the transactivation domain); the interaction is prevented by sumoylation of ATF7 and promotes (isoform TAFII20 only) the transactivation of ATF7. Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Nucleus Ref.10 Ref.11.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the TAF12 family.

Contains 1 histone-fold domain.

Ontologies

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

Inferred from direct assay PubMed 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.11. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of RNA biosynthetic process

Inferred from direct assay Ref.11. Source: GOC

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

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.10. Source: UniProtKB

STAGA complex

Inferred from direct assay Ref.11. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor TFIID complex

Inferred from direct assay PubMed 14580349. Source: MGI

transcription factor TFTC complex

Inferred from direct assay PubMed 9603525. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15601843. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11438666PubMed 17264123PubMed 7667268Ref.4. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.11. Source: UniProtKB

transcription factor binding

Inferred from direct assay PubMed 17264123. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform TAFII20 (identifier: Q16514-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform TAFII15 (identifier: Q16514-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Transcription initiation factor TFIID subunit 12
PRO_0000033580

Amino acid modifications

Modified residue431Phosphothreonine Ref.15
Modified residue511Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue591Phosphothreonine Ref.14

Natural variations

Alternative sequence1 – 3030Missing in isoform TAFII15.
VSP_018888

Secondary structure

....... 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform TAFII20 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 054B017CD7BF99CE

FASTA16117,924
        10         20         30         40         50         60 
MNQFGPSALI NLSNFSSIKP EPASTPPQGS MANSTAVVKI PGTPGAGGRL SPENNQVLTK 

        70         80         90        100        110        120 
KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC QLARHRKSST LEVKDVQLHL 

       130        140        150        160 
ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ RMALIRKTTK K 

« Hide

Isoform TAFII15 [UniParc].

Checksum: 655B769918311CE1
Show »

FASTA13114,825

References

« Hide 'large scale' references
[1]"A histone octamer-like structure within TFIID."
Hoffmann A., Chiang C.M., Oelgeschlager T., Xie X., Burley S.K., Nakatani Y., Roeder R.G.
Nature 380:356-359(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20).
[2]"Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation."
Hoffmann A., Roeder R.G.
J. Biol. Chem. 271:18194-18202(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAFII15 AND TAFII20).
[3]"Isolation and characterization of a cDNA encoding a novel human transcription factor TFIID subunit containing similarities with histones H2B and H3."
Choi B., Bando M., Hasegawa S., Horikoshi M.
Gene 169:263-267(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20).
[4]"Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID."
Mengus G., May M., Jacq X., Staub A., Tora L., Chambon P., Davidson I.
EMBO J. 14:1520-1531(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20), PARTIAL PROTEIN SEQUENCE.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAFII20).
[6]NIEHS SNPs program
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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].
[9]"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] (ISOFORM TAFII20).
Tissue: Lung.
[10]"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 50-60 AND 115-122, SUBUNIT, SUBCELLULAR LOCATION.
[11]"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 SF3B3; GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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; TAF10; TRRAP AND TAF9.
[13]"A functional interaction between ATF7 and TAF12 that is modulated by TAF4."
Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C., Chatton B.
Oncogene 24:3472-3483(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7.
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND THR-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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 THR-43 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs."
Gangloff Y.-G., Werten S., Romier C., Carre L., Poch O., Moras D., Davidson I.
Mol. Cell. Biol. 20:340-351(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 57-128 IN COMPLEX WITH TAF4.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57693 mRNA. Translation: AAC50600.1.
U57693 mRNA. Translation: AAC50601.1.
D50544 mRNA. Translation: BAA09112.1.
X84002 mRNA. Translation: CAA58826.1.
BT007031 mRNA. Translation: AAP35678.1.
AY206865 Genomic DNA. Translation: AAO13491.1.
AL513497 Genomic DNA. Translation: CAI22291.1.
CH471059 Genomic DNA. Translation: EAX07682.1.
CH471059 Genomic DNA. Translation: EAX07683.1.
BC011986 mRNA. Translation: AAH11986.1.
CCDSCCDS326.1. [Q16514-1]
PIRJC4676.
RefSeqNP_001128690.1. NM_001135218.1. [Q16514-1]
NP_005635.1. NM_005644.3. [Q16514-1]
XP_006710924.1. XM_006710861.1. [Q16514-1]
UniGeneHs.530251.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3OX-ray2.30B/D57-128[»]
ProteinModelPortalQ16514.
SMRQ16514. Positions 55-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112746. 25 interactions.
DIPDIP-496N.
IntActQ16514. 6 interactions.
MINTMINT-3032603.
STRING9606.ENSP00000263974.

PTM databases

PhosphoSiteQ16514.

Polymorphism databases

DMDM3024708.

Proteomic databases

MaxQBQ16514.
PaxDbQ16514.
PRIDEQ16514.

Protocols and materials databases

DNASU6883.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263974; ENSP00000263974; ENSG00000120656. [Q16514-1]
ENST00000373824; ENSP00000362930; ENSG00000120656. [Q16514-1]
GeneID6883.
KEGGhsa:6883.
UCSCuc001bqx.3. human. [Q16514-1]

Organism-specific databases

CTD6883.
GeneCardsGC01M028915.
HGNCHGNC:11545. TAF12.
HPAHPA008519.
MIM600773. gene.
neXtProtNX_Q16514.
PharmGKBPA36320.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5624.
HOGENOMHOG000035092.
HOVERGENHBG055174.
InParanoidQ16514.
KOK03126.
OMAMHSLHEN.
OrthoDBEOG769ZMW.
PhylomeDBQ16514.
TreeFamTF323652.

Enzyme and pathway databases

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

Gene expression databases

BgeeQ16514.
CleanExHS_TAF12.
HS_TAF15.
GenevestigatorQ16514.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR003228. TFIID_sub.
[Graphical view]
PfamPF03847. TFIID_20kDa. 1 hit.
[Graphical view]
ProDomPD012998. PD012998. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ16514.
GeneWikiTAF12.
GenomeRNAi6883.
NextBio26891.
PROQ16514.
SOURCESearch...

Entry information

Entry nameTAF12_HUMAN
AccessionPrimary (citable) accession number: Q16514
Secondary accession number(s): D3DPM5, Q15775, Q5T077
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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM