Q16594 (TAF9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 9

Alternative name(s):
RNA polymerase II TBP-associated factor subunit G
STAF31/32
Transcription initiation factor TFIID 31 kDa subunit
Short name=TAFII-31
Short name=TAFII31
Transcription initiation factor TFIID 32 kDa subunit
Short name=TAFII-32
Short name=TAFII32

Gene names

Name:	TAF9
Synonyms:	TAF2G, TAFII31

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	264 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. Ref.14
Subunit structure	Component of TFIID, the TATA-binding protein-free TAF complex (TFTC), the PCAF complex and the STAGA transcription coactivator-HAT complex. The PCAF complex consists at least of TADA2L/ADA2, SUPT3H/SPT3, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. The STAGA transcription coactivator-HAT complex consists at least of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Binds N-terminal domain of p53/TP53 which is essential for transcription. 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. Binds TFIIB and the Herpes simplex virus activator VP16. Forms a heterodimer with TAF6/TAFII80 in a complex with the TAF4B/TAFII105-TAF12/TAFII20 heterodimer. Also interacts with TAF5. Binds directly DNA. Increased DNA binding when complexed with TAF6/TAFII80. Ref.1 Ref.2 Ref.8 Ref.13 Ref.14
Subcellular location	Nucleus Ref.8 Ref.9.
Induction	6 to 8-fold by apoptotic signals. Ref.14
Sequence similarities	Belongs to the TAF9 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	histone H3 acetylation Inferred from direct assay Ref.9Ref.8. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.14. Source: BHF-UCL negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: BHF-UCL positive regulation of cell growth Inferred from mutant phenotype Ref.14. Source: UniProtKB positive regulation of response to cytokine stimulus Inferred from mutant phenotype. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL response to DNA damage stimulus Inferred by curator. Source: BHF-UCL response to interleukin-1 Inferred from mutant phenotype. Source: BHF-UCL transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular component	MLL1 complex Inferred from direct assay Ref.11. Source: UniProtKB PCAF complex Inferred from direct assay Ref.8. Source: UniProtKB STAGA complex Inferred from direct assay Ref.9. Source: UniProtKB pre-snoRNP complex Inferred from direct assay. Source: BHF-UCL transcription factor TFIID complex Inferred from direct assay Ref.14. Source: UniProtKB transcription factor TFTC complex Inferred from direct assay Ref.14. Source: UniProtKB
Molecular function	C2H2 zinc finger domain binding Inferred from physical interaction. Source: BHF-UCL activating transcription factor binding Inferred from physical interaction. Source: BHF-UCL p53 binding Inferred from physical interaction. Source: BHF-UCL transcription coactivator activity Inferred from direct assay Ref.9. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KAT2B	Q92831	3	EBI-712521,EBI-477430
TAF6L	Q9Y6J9	3	EBI-712521,EBI-743984

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoform 1 and isoform 2 are produced by the same gene but are translated from different initiation codons and use different reading frames so they display no identity in their protein sequences. This arrangement is conserved in mammals but these proteins are produced by separate genes in non-mammalian species.

Isoform 2 (identifier: Q16594-1)

Also known as: TAF9;

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 1 (identifier: Q9Y3D8-1)

Also known as: AK6;

The sequence of this isoform can be found in the external entry Q9Y3D8.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform 3 (identifier: Q9Y3D8-2)

The sequence of this isoform can be found in the external entry Q9Y3D8.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 264	264	Transcription initiation factor TFIID subunit 9		PRO_0000118888
Regions
	DNA binding	120 – 137	18	Ref.13
	Compositional bias	250 – 262	13	Poly-Asp
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.19
	Modified residue	5	1	N6-acetyllysine Ref.19
	Modified residue	85	1	Phosphoserine Ref.15
	Modified residue	108	1	N6-acetyllysine Ref.19
	Modified residue	149	1	Phosphoserine Ref.18
	Modified residue	155	1	Phosphoserine Ref.17
	Modified residue	158	1	Phosphoserine Ref.17 Ref.18
	Modified residue	159	1	Phosphothreonine Ref.16 Ref.18
	Modified residue	161	1	Phosphothreonine Ref.16
	Modified residue	178	1	Phosphothreonine Ref.16
	Modified residue	181	1	Phosphoserine Ref.16
Natural variations
	Natural variant	6	1	T → M. Ref.5 Corresponds to variant rs4252233 [ dbSNP | Ensembl ].		VAR_016279
	Natural variant	210	1	Q → H. Corresponds to variant rs11542580 [ dbSNP | Ensembl ].		VAR_052260
Experimental info
	Sequence conflict	46	1	Y → V AA sequence Ref.8
	Sequence conflict	225	1	L → F in AAH03400. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (TAF9) [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 1925AEC65D6C84C7	FASTA	264	28,974
	10 20 30 40 50 60 MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH 70 80 90 100 110 120 AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN QTPLPLIKPY SGPRLPPDRY 130 140 150 160 170 180 CLTAPNYRLK SLQKKASTSA GRITVPRLSV GSVTSRPSTP TLGTPTPQTM SVSTKVGTPM 190 200 210 220 230 240 SLTGQRFTVQ MPTSQSPAVK ASIPATSAVQ NVLINPSLIG SKNILITTNM MSSQNTANES 250 260 SNALKRKRED DDDDDDDDDD YDNL
	Isoform 1 (AK6) [UniParc]. See Q9Y3D8.		–	–
	Isoform 3 [UniParc]. See Q9Y3D8.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human TAFII31 protein is a transcriptional coactivator of the p53 protein." Lu H., Levine A.J. Proc. Natl. Acad. Sci. U.S.A. 92:5154-5158(1995) [PubMed: 7761466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VP16 AND TFIIB.
[2]	"Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation." Klemm R.D., Goodrich J.A., Zhou S., Tjian R. Proc. Natl. Acad. Sci. U.S.A. 92:5788-5792(1995) [PubMed: 7597030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAF6.
[3]	"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]. Tissue: Brain.
[4]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NIEHS SNPs program Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-6.
[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]. Tissue: Placenta and Testis.
[8]	"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 25-55; 79-89; 176-200 AND 223-246, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"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; TAF10 AND TAF12.
[10]	"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; TAF12 AND TRRAP.
[11]	"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.
[12]	"Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locus." Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I. J. Biol. Chem. 280:36429-36441(2005) [PubMed: 16079131] [Abstract] Cited for: ALTERNATIVE SPLICING.
[13]	"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 TAF6 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B, DNA-BINDING.
[14]	"TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9." Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B., Scheer E., Tora L. Mol. Cell. Biol. 25:4638-4649(2005) [PubMed: 15899866] [Abstract] Cited for: FUNCTION, SUBUNIT, INDUCTION, INTERACTION WITH TAF5 AND TAF6.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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-159; THR-161; THR-178 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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-155 AND SER-158, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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-149; SER-158 AND THR-159, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5 AND LYS-108, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	U25112 mRNA. Translation: AAA91318.1. U21858 mRNA. Translation: AAC50153.1. U30504 mRNA. Translation: AAA84389.1. BT019652 mRNA. Translation: AAV38458.1. AY189986 Genomic DNA. Translation: AAN84793.1. CH471137 Genomic DNA. Translation: EAW51295.1. CH471137 Genomic DNA. Translation: EAW51296.1. BC003400 mRNA. Translation: AAH03400.1. BC033320 mRNA. Translation: AAH33320.1.
IPI	IPI00002993.
PIR	I39141.
RefSeq	NP_001015892.1. NM_001015892.1. NP_003178.1. NM_003187.4.
UniGene	Hs.653163.
3D structure databases
ProteinModelPortal	Q16594.
SMR	Q16594. Positions 13-76.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-435N.
IntAct	Q16594. 42 interactions.
MINT	MINT-2860193.
STRING	Q16594.
PTM databases
PhosphoSite	Q16594.
Polymorphism databases
DMDM	2498981.
Proteomic databases
PRIDE	Q16594.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217893; ENSP00000217893; ENSG00000085231. ENST00000328663; ENSP00000370193; ENSG00000085231.
GeneID	6880.
KEGG	hsa:6880.
UCSC	uc003jwc.1. human.
Organism-specific databases
CTD	6880.
GeneCards	GC05M068683.
HGNC	HGNC:11542. TAF9.
HPA	CAB005361.
MIM	600822. gene.
neXtProt	NX_Q16594.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06099.
GeneTree	ENSGT00390000001626.
HOGENOM	HBG320253.
HOVERGEN	HBG002304.
InParanoid	Q16594.
OMA	IEDAKIY.
PhylomeDB	Q16594.
Enzyme and pathway databases
Reactome	REACT_1788. Transcription. REACT_6185. HIV Infection. REACT_71. Gene Expression.
Gene expression databases
Bgee	Q16594.
CleanEx	HS_TAF9.
Genevestigator	Q16594.
GermOnline	ENSG00000185057. Homo sapiens.
Family and domain databases
InterPro	IPR009072. Histone-fold. IPR003162. TFIID-31. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K14535.
PANTHER	PTHR12075. TFIID-31. 1 hit.
Pfam	PF02291. TFIID-31kDa. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
ProtoNet	Search...
Other
NextBio	26873.
SOURCE	Search...

Entry information

Entry name

TAF9_HUMAN

Accession

Primary (citable) accession number: Q16594
Secondary accession number(s): D3DWA3, Q5U0D1, Q9BTS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 121 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.