P49848 (TAF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 6

Alternative name(s):
RNA polymerase II TBP-associated factor subunit E
Transcription initiation factor TFIID 70 kDa subunit
Short name=TAF(II)70
Short name=TAFII-70
Short name=TAFII70
Transcription initiation factor TFIID 80 kDa subunit
Short name=TAF(II)80
Short name=TAFII-80
Short name=TAFII80

Gene names

Name:	TAF6
Synonyms:	TAF2E, TAFII70

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	677 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). TIIFD is 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. Interacts directly with TBP, TAF1/TAFII250, TAF9/TAFII31 AND TAF12/TAFII20. The TAF6/TAFII70-TAF9/TAFII31 heterodimer forms an octamer complex with the TAF4B/TFII105-TAF12/TFIID20 heterodimer. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Also interacts with the GTFs, TFIIEalpha/GTF2E1 and TFIIFalpha/GTF2F1. Component of the TFTC-HAT complex. Ref.1 Ref.2 Ref.11
Subcellular location	Nucleus.
Sequence similarities	Belongs to the TAF6 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of cell cycle Inferred from direct assay. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro 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	MLL1 complex Inferred from direct assay Ref.10. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA 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 Ref.11. Source: UniProtKB protein binding Inferred from physical interaction Ref.11Ref.2. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49848-1)

Also known as: Alpha;

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 2 (identifier: P49848-2)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     477-486: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 677	677	Transcription initiation factor TFIID subunit 6		PRO_0000118873
Amino acid modifications
	Modified residue	626	1	Phosphoserine Ref.13
	Modified residue	634	1	Phosphoserine Ref.13
	Modified residue	636	1	Phosphoserine Ref.13
	Modified residue	653	1	Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14 Ref.15
	Modified residue	660	1	Phosphothreonine Ref.12 Ref.13 Ref.14 Ref.15
	Modified residue	670	1	Phosphoserine Ref.14
	Modified residue	672	1	Phosphoserine Ref.14
Natural variations
	Alternative sequence	477 – 486	10	Missing in isoform 2.		VSP_037476
	Natural variant	36	1	C → S. Ref.4 Corresponds to variant rs4134897 [ dbSNP | Ensembl ].		VAR_014349
Experimental info
	Sequence conflict	196	1	K → E in CAH10485. Ref.3
	Sequence conflict	417	1	R → W in CAH10485. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 06C6BFA563580823	FASTA	677	72,668
	10 20 30 40 50 60 MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM 70 80 90 100 110 120 GKRQKLTTSD IDYALKLKNV EPLYGFHAQE FIPFRFASGG GRELYFYEEK EVDLSDIINT 130 140 150 160 170 180 PLPRVPLDVC LKAHWLSIEG CQPAIPENPP PAPKEQQKAE ATEPLKSAKP GQEEDGPLKG 190 200 210 220 230 240 KGQGATTADG KGKEKKAPPL LEGAPLRLKP RSIHELSVEQ QLYYKEITEA CVGSCEAKRA 250 260 270 280 290 300 EALQSIATDP GLYQMLPRFS TFISEGVRVN VVQNNLALLI YLMRMVKALM DNPTLYLEKY 310 320 330 340 350 360 VHELIPAVMT CIVSRQLCLR PDVDNHWALR DFAARLVAQI CKHFSTTTNN IQSRITKTFT 370 380 390 400 410 420 KSWVDEKTPW TTRYGSIAGL AELGHDVIKT LILPRLQQEG ERIRSVLDGP VLSNIDRIGA 430 440 450 460 470 480 DHVQSLLLKH CAPVLAKLRP PPDNQDAYRA EFGSLGPLLC SQVVKARAQA ALQAQQVNRT 490 500 510 520 530 540 TLTITQPRPT LTLSQAPQPG PRTPGLLKVP GSIALPVQTL VSARAAAPPQ PSPPPTKFIV 550 560 570 580 590 600 MSSSSSAPST QQVLSLSTSA PGSGSTTTSP VTTTVPSVQP IVKLVSTATT APPSTAPSGP 610 620 630 640 650 660 GSVQKYIVVS LPPTGEGKGG PTSHPSPVPP PASSPSPLSG SALCGGKQEA GDSPPPAPGT 670 PKANGSQPNS GSPQPAP
	Isoform 2 (Gamma) [UniParc]. Checksum: 85488E83976800FC	FASTA	667	71,540
	10 20 30 40 50 60 MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM 70 80 90 100 110 120 GKRQKLTTSD IDYALKLKNV EPLYGFHAQE FIPFRFASGG GRELYFYEEK EVDLSDIINT 130 140 150 160 170 180 PLPRVPLDVC LKAHWLSIEG CQPAIPENPP PAPKEQQKAE ATEPLKSAKP GQEEDGPLKG 190 200 210 220 230 240 KGQGATTADG KGKEKKAPPL LEGAPLRLKP RSIHELSVEQ QLYYKEITEA CVGSCEAKRA 250 260 270 280 290 300 EALQSIATDP GLYQMLPRFS TFISEGVRVN VVQNNLALLI YLMRMVKALM DNPTLYLEKY 310 320 330 340 350 360 VHELIPAVMT CIVSRQLCLR PDVDNHWALR DFAARLVAQI CKHFSTTTNN IQSRITKTFT 370 380 390 400 410 420 KSWVDEKTPW TTRYGSIAGL AELGHDVIKT LILPRLQQEG ERIRSVLDGP VLSNIDRIGA 430 440 450 460 470 480 DHVQSLLLKH CAPVLAKLRP PPDNQDAYRA EFGSLGPLLC SQVVKARAQA ALQAQQPRPT 490 500 510 520 530 540 LTLSQAPQPG PRTPGLLKVP GSIALPVQTL VSARAAAPPQ PSPPPTKFIV MSSSSSAPST 550 560 570 580 590 600 QQVLSLSTSA PGSGSTTTSP VTTTVPSVQP IVKLVSTATT APPSTAPSGP GSVQKYIVVS 610 620 630 640 650 660 LPPTGEGKGG PTSHPSPVPP PASSPSPLSG SALCGGKQEA GDSPPPAPGT PKANGSQPNS GSPQPAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal conserved interactions with other subunits of TFIID." Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R. EMBO J. 12:5303-5309(1993) [PubMed: 8262073] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 78-95 AND 501-521, INTERACTION WITH TBP AND TAF1. Tissue: Cervix carcinoma.
[2]	"Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors." Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., Roeder R.G. Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995) [PubMed: 7667268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 78-103; 113-127; 368-383 AND 441-455, INTERACTION WITH TBP; TAF1; TAF9; TAF12; GTF2F1 AND GTF2E1. Tissue: Placenta.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain cortex.
[4]	NIEHS SNPs program Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-36.
[5]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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 1). Tissue: Pancreas.
[8]	"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.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 15960975] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[11]	"Core promoter binding by histone-like TAF complexes." Shao H., Revach M., Moshonov S., Tzuman Y., Gazit K., Albeck S., Unger T., Dikstein R. Mol. Cell. Biol. 25:206-219(2005) [PubMed: 15601843] [Abstract] Cited for: INTERACTION WITH TAF9 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B, DNA-BINDING.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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 SER-626; SER-634; SER-636; SER-653 AND THR-660, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653; THR-660; SER-670 AND SER-672, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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-653 AND THR-660, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	L25444 mRNA. Translation: AAA63643.1. U31659 mRNA. Translation: AAA84390.1. CR627390 mRNA. Translation: CAH10485.1. AY149894 Genomic DNA. Translation: AAN10295.1. CH236956 Genomic DNA. Translation: EAL23851.1. CH236956 Genomic DNA. Translation: EAL23852.1. CH471091 Genomic DNA. Translation: EAW76589.1. CH471091 Genomic DNA. Translation: EAW76591.1. CH471091 Genomic DNA. Translation: EAW76592.1. BC018115 mRNA. Translation: AAH18115.1.
IPI	IPI00028579. IPI00376952.
RefSeq	NP_005632.1. NM_005641.3. NP_647476.1. NM_139315.2.
UniGene	Hs.489309.
3D structure databases
ProteinModelPortal	P49848.
SMR	P49848. Positions 9-76.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29288N. DIP-773N.
IntAct	P49848. 7 interactions.
MINT	MINT-1211769.
STRING	P49848.
PTM databases
PhosphoSite	P49848.
Polymorphism databases
DMDM	1729810.
Proteomic databases
PRIDE	P49848.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000344095; ENSP00000344537; ENSG00000106290. ENST00000437822; ENSP00000399982; ENSG00000106290. ENST00000452041; ENSP00000416396; ENSG00000106290. ENST00000453269; ENSP00000389575; ENSG00000106290. ENST00000472509; ENSP00000419760; ENSG00000106290.
GeneID	6878.
KEGG	hsa:6878.
UCSC	uc003uti.1. human.
Organism-specific databases
CTD	6878.
GeneCards	GC07M099704.
H-InvDB	HIX0006909.
HGNC	HGNC:11540. TAF6.
HPA	HPA006566.
MIM	602955. gene.
neXtProt	NX_P49848.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000063704.
HOVERGEN	HBG012489.
InParanoid	P49848.
OrthoDB	EOG4MKNG0.
PhylomeDB	P49848.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription. REACT_6185. HIV Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P49848.
Bgee	P49848.
CleanEx	HS_TAF6.
Genevestigator	P49848.
GermOnline	ENSG00000106290. Homo sapiens.
Family and domain databases
InterPro	IPR011442. DUF1546. IPR009072. Histone-fold. IPR004823. TAF_TATA-bd. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K03131.
Pfam	PF07571. DUF1546. 1 hit. PF02969. TAF. 1 hit. [Graphical view]
SMART	SM00803. TAF. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
ProtoNet	Search...
Other
NextBio	26859.
SOURCE	Search...

Entry information

Entry name

TAF6_HUMAN

Accession

Primary (citable) accession number: P49848
Secondary accession number(s): A4D2B2 , A4D2B3, D6W5U2, Q6AI29

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 119 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.