Q16514 (TAF12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Protein existence	Evidence 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.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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative initiation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	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 transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB viral reproduction Traceable author statement. Source: Reactome
Cellular component	PCAF complex Inferred from direct assay Ref.10. Source: UniProtKB STAGA complex Inferred from direct assay Ref.11. Source: UniProtKB transcription factor TFIID complex Inferred from direct assay. Source: MGI transcription factor TFTC complex Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from direct assay. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.11. Source: UniProtKB transcription factor binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 161

161

Transcription initiation factor TFIID subunit 12

PRO_0000033580

Amino acid modifications

Modified residue

43

1

Phosphothreonine Ref.16

Modified residue

51

1

Phosphoserine Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Modified residue

59

1

Phosphothreonine Ref.15

Natural variations

Alternative sequence

1 – 30

30

Missing in isoform TAFII15.

VSP_018888

Secondary structure

1

.

.

.

.

.

.

.

161

Helix Strand Turn

Details...

Helix

60 – 70

11

Helix

78 – 105

28

Helix

113 – 123

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform TAFII20 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 054B017CD7BF99CE	FASTA	161	17,924
	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
	Isoform TAFII15 [UniParc]. Checksum: 655B769918311CE1	FASTA	131	14,825
	10 20 30 40 50 60 MANSTAVVKI PGTPGAGGRL SPENNQVLTK KKLQDLVREV DPNEQLDEDV EEMLLQIADD 70 80 90 100 110 120 FIESVVTAAC QLARHRKSST LEVKDVQLHL ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ 130 RMALIRKTTK K

References

	« Hide 'large scale' referencesShow '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: 8598932] [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: 8663456] [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: 8647459] [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: 7729427] [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. , 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: 16710414] [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. , 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: 15489334] [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: 9674425] [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: 11564863] [Abstract] Cited for: MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SF3B3; GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 AND TAF9.
[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: 9885574] [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: 15735663] [Abstract] Cited for: INTERACTION WITH ATF7.
[14]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND THR-59, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY.
[18]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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: 10594036] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 57-128 IN COMPLEX WITH TAF4.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00002806.
IPI00759817.

PIR

JC4676.

RefSeq

NP_001128690.1. NM_001135218.1.
NP_005635.1. NM_005644.3.

UniGene

Hs.530251.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H3O	X-ray	2.30	B/D	57-128	[»]

ProteinModelPortal

Q16514.

SMR

Q16514. Positions 55-128.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-496N.

IntAct

Q16514. 7 interactions.

MINT

MINT-3032603.

STRING

Q16514.

PTM databases

PhosphoSite

Q16514.

Polymorphism databases

DMDM

3024708.

Proteomic databases

PRIDE

Q16514.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263974; ENSP00000263974; ENSG00000120656.
ENST00000373824; ENSP00000362930; ENSG00000120656.

GeneID

6883.

KEGG

hsa:6883.

UCSC

uc001bqw.1. human.

Organism-specific databases

CTD

6883.

GeneCards

GC01M028915.

H-InvDB

HIX0000335.

HGNC

HGNC:11545. TAF12.

HPA

HPA008519.

MIM

600773. gene.

neXtProt

NX_Q16514.

PharmGKB

PA36320.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11764.

GeneTree

ENSGT00390000002144.

HOGENOM

HBG283035.

HOVERGEN

HBG055174.

InParanoid

Q16514.

OMA

VAKMPGT.

OrthoDB

EOG4ZCT5X.

PhylomeDB

Q16514.

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q16514.

Bgee

Q16514.

CleanEx

HS_TAF12.
HS_TAF15.

Genevestigator

Q16514.

GermOnline

ENSG00000120656. Homo sapiens.

Family and domain databases

InterPro

IPR009072. Histone-fold.
IPR003228. TFIID_sub.
[Graphical view]

Gene3D

G3DSA:1.10.20.10. Histone-fold. 1 hit.

KO

K03126.

Pfam

PF03847. TFIID_20kDa. 1 hit.
[Graphical view]

ProDom

PD012998. PD012998. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF47113. Histone-fold. 1 hit.

ProtoNet

Search...

Other

NextBio

26891.

SOURCE

Search...

Entry information

Entry name

TAF12_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.