HUMAN:TAF7

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TAF7 (synonyms: TAF2F, TAFII55)
Protein Name(s)	Transcription initiation factor TFIID subunit 7 RNA polymerase II TBP-associated factor subunit F Transcription initiation factor TFIID 55 kDa subunit TAF(II)55 TAFII-55 TAFII55
External Links
UniProt	Q15545
EMBL	X97999 U18062 AF349038 AK314837 CH471062 BC032737
CCDS	CCDS4259.1
PIR	I38904
RefSeq	NP_005633.2
UniGene	Hs.438838
PDB	4RGW 5FUR
PDBsum	4RGW 5FUR
ProteinModelPortal	Q15545
SMR	Q15545
BioGrid	112742
DIP	DIP-29047N
IntAct	Q15545
MINT	MINT-3031780
STRING	9606.ENSP00000312709
iPTMnet	Q15545
PhosphoSite	Q15545
BioMuta	TAF7
DMDM	3024690
EPD	Q15545
MaxQB	Q15545
PaxDb	Q15545
PRIDE	Q15545
DNASU	6879
Ensembl	ENST00000313368
GeneID	6879
KEGG	hsa:6879
UCSC	uc003ljg.4
CTD	6879
GeneCards	TAF7
HGNC	HGNC:11541
HPA	HPA006429
MIM	600573
neXtProt	NX_Q15545
PharmGKB	PA36316
eggNOG	KOG4011 COG5414
GeneTree	ENSGT00390000010815
HOGENOM	HOG000035121
HOVERGEN	HBG013606
InParanoid	Q15545
KO	K03132
OMA	QMLVCTL
OrthoDB	EOG7GJ6FT
PhylomeDB	Q15545
TreeFam	TF313044
SignaLink	Q15545
ChiTaRS	TAF7
GeneWiki	TAF7
GenomeRNAi	6879
PRO	PR:Q15545
Proteomes	UP000005640
Bgee	Q15545
CleanEx	HS_TAF7
ExpressionAtlas	Q15545
Genevisible	Q15545
GO	GO:0005794 GO:0071339 GO:0005654 GO:0005669 GO:0033276 GO:0035035 GO:0046966 GO:0003713 GO:0008134 GO:0044212 GO:0042809 GO:0006352 GO:0030520 GO:0035067 GO:0006469 GO:0000122 GO:0045892 GO:0045944 GO:0051123 GO:0000296 GO:0006366 GO:0006367
InterPro	IPR006751
Pfam	PF04658
SMART	SM01370

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0090241	negative regulation of histone H4 acetylation	PMID:20937824^[1]	ECO:0000314			P		Figure 2 shows that TAF7 purified from HeLa cells decreased CIITA-mediated acetylation of histone 4. Increasing concentrations of TAF7 resulted in lower acetylation of H4.	complete CACAO 12219
	GO:0045344	negative regulation of MHC class I biosynthetic process	PMID:20937824^[1]	ECO:0000314			P		Figure 3A shows that TAF7 prevents the transcription of MHC class I promoters in HeLa cells. This process prevents the biosynthesis of MHC class I molecules. No TAF7 mutants were used to obtain this conclusion.	complete CACAO 12220
	GO:0045347	negative regulation of MHC class II biosynthetic process	PMID:20937824^[1]	ECO:0000315			P		Figure 4 shows that HeLa cells with siRNA knowckdown of TAF7 expressed elevated levels of MHC class II genes (DRA and DRB). Therefore, TAF7 negatively regulates the biosynthesis of MHC class II molecules.	complete CACAO 12221
enables	GO:0001097	TFIIH-class transcription factor complex binding	PMID:18391197^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	PMID:25412659^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21675	C		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	PMID:24927529^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	PMID:27007846^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
contributes_to	GO:0061628	H3K27me3 modified histone binding	PMID:24927529^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21675	F		Seeded From UniProt	complete
involved_in	GO:0060260	regulation of transcription initiation from RNA polymerase II promoter	PMID:24927529^[4]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:25412659^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21675	F	positively_regulates:(GO:0008283)	Seeded From UniProt	complete
part_of	GO:0071339	MLL1 complex	PMID:15960975^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046966	thyroid hormone receptor binding	PMID:10409738^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04625	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:12676957^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:18391197^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:11592977^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:16407123^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044212	transcription regulatory region DNA binding	PMID:18391197^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042809	vitamin D receptor binding	PMID:10409738^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P11473	F		Seeded From UniProt	complete
involved_in	GO:0035067	negative regulation of histone acetylation	PMID:11592977^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035035	histone acetyltransferase binding	PMID:11592977^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q80UV9	F		Seeded From UniProt	complete
part_of	GO:0033276	transcription factor TFTC complex	PMID:9603525^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:7824954^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08047	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:11005381^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00613	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:12676957^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05412	F		Seeded From UniProt	complete
enables	GO:0106140	P-TEFb complex binding	PMID:18391197^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006469	negative regulation of protein kinase activity	PMID:18391197^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	PMID:9603525^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	PMID:16407123^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	PMID:7824954^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006352	DNA-templated transcription, initiation	PMID:9603525^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	PMID:7824954^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:7824954^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0003700	DNA-binding transcription factor activity	PMID:9603525^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000296	spermine transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6R1L1	P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:11592977^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:16407123^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:18391197^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051123	RNA polymerase II preinitiation complex assembly	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000260034 SGD:S000004840	P		Seeded From UniProt	complete
enables	GO:0044212	transcription regulatory region DNA binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000260034 UniProtKB:Q15545	F		Seeded From UniProt	complete
enables	GO:0035035	histone acetyltransferase binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346348 PANTHER:PTN000260034 UniProtKB:Q15545	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000260034 UniProtKB:Q15545	F		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346348 PANTHER:PTN000260034	P		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346348 PANTHER:PTN000260034 PomBase:SPAC13F5.02c SGD:S000004840 UniProtKB:Q15545	C		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000260034 UniProtKB:Q15545	F		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	PMID:14580349^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0035035	histone acetyltransferase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	F		Seeded From UniProt	complete
involved_in	GO:0030520	intracellular estrogen receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	P		Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	P		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	C		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9R1C0 ensembl:ENSMUSP00000065645	C		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006751 InterPro:IPR037817	C		Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006751	P		Seeded From UniProt	complete
part_of	GO:0005669	transcription factor TFIID complex	PMID:25412659^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	Reactome:R-HSA-75953 Reactome:R-HSA-73779	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	Reactome:R-HSA-73857	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-9613497 Reactome:R-HSA-9613494 Reactome:R-HSA-75949 Reactome:R-HSA-75873 Reactome:R-HSA-75869 Reactome:R-HSA-75866 Reactome:R-HSA-75864 Reactome:R-HSA-75862 Reactome:R-HSA-75861 Reactome:R-HSA-75856 Reactome:R-HSA-75850 Reactome:R-HSA-75095 Reactome:R-HSA-73946 Reactome:R-HSA-6805399 Reactome:R-HSA-109639 Reactome:R-HSA-109638 Reactome:R-HSA-109637 Reactome:R-HSA-109636	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Devaiah, BN et al. (2010) Novel functions for TAF7, a regulator of TAF1-independent transcription. J. Biol. Chem. 285 38772-80 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Gegonne, A et al. (2008) TFIID component TAF7 functionally interacts with both TFIIH and P-TEFb. Proc. Natl. Acad. Sci. U.S.A. 105 5367-72 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Wang, H et al. (2014) Crystal structure of a TAF1-TAF7 complex in human transcription factor IID reveals a promoter binding module. Cell Res. 24 1433-44 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Bhattacharya, S et al. (2014) Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D. Proc. Natl. Acad. Sci. U.S.A. 111 9103-8 PubMed GONUTS page
↑ Louder, RK et al. (2016) Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. Nature 531 604-9 PubMed GONUTS page
↑ Dou, Y et al. (2005) Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121 873-85 PubMed GONUTS page
↑ ^7.0 ^7.1 Lavigne, AC et al. (1999) Human TAF(II)55 interacts with the vitamin D(3) and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties. Mol. Cell. Biol. 19 5486-94 PubMed GONUTS page
↑ ^8.0 ^8.1 Munz, C et al. (2003) TAF7 (TAFII55) plays a role in the transcription activation by c-Jun. J. Biol. Chem. 278 21510-6 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Gegonne, A et al. (2001) TAFII55 binding to TAFII250 inhibits its acetyltransferase activity. Proc. Natl. Acad. Sci. U.S.A. 98 12432-7 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Gegonne, A et al. (2006) TAF7: a possible transcription initiation check-point regulator. Proc. Natl. Acad. Sci. U.S.A. 103 602-7 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Wieczorek, E et al. (1998) Function of TAF(II)-containing complex without TBP in transcription by RNA polymerase II. Nature 393 187-91 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Chiang, CM & Roeder, RG (1995) Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators. Science 267 531-6 PubMed GONUTS page
↑ Yuan, CX & Gurley, WB (2000) Potential targets for HSF1 within the preinitiation complex. Cell Stress Chaperones 5 229-42 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Guermah, M et al. (2003) The TBN protein, which is essential for early embryonic mouse development, is an inducible TAFII implicated in adipogenesis. Mol. Cell 12 991-1001 PubMed GONUTS page

[PMID:20937824-1] 1.0 ^1.1 ^1.2 Devaiah, BN et al. (2010) Novel functions for TAF7, a regulator of TAF1-independent transcription. J. Biol. Chem. 285 38772-80 PubMed GONUTS page

[PMID:18391197-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Gegonne, A et al. (2008) TFIID component TAF7 functionally interacts with both TFIIH and P-TEFb. Proc. Natl. Acad. Sci. U.S.A. 105 5367-72 PubMed GONUTS page

[PMID:25412659-3] 3.0 ^3.1 ^3.2 Wang, H et al. (2014) Crystal structure of a TAF1-TAF7 complex in human transcription factor IID reveals a promoter binding module. Cell Res. 24 1433-44 PubMed GONUTS page

[PMID:24927529-4] 4.0 ^4.1 ^4.2 Bhattacharya, S et al. (2014) Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D. Proc. Natl. Acad. Sci. U.S.A. 111 9103-8 PubMed GONUTS page

[PMID:27007846-5] Louder, RK et al. (2016) Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. Nature 531 604-9 PubMed GONUTS page

[PMID:15960975-6] Dou, Y et al. (2005) Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121 873-85 PubMed GONUTS page

[PMID:10409738-7] 7.0 ^7.1 Lavigne, AC et al. (1999) Human TAF(II)55 interacts with the vitamin D(3) and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties. Mol. Cell. Biol. 19 5486-94 PubMed GONUTS page

[PMID:12676957-8] 8.0 ^8.1 Munz, C et al. (2003) TAF7 (TAFII55) plays a role in the transcription activation by c-Jun. J. Biol. Chem. 278 21510-6 PubMed GONUTS page

[PMID:11592977-9] 9.0 ^9.1 ^9.2 ^9.3 Gegonne, A et al. (2001) TAFII55 binding to TAFII250 inhibits its acetyltransferase activity. Proc. Natl. Acad. Sci. U.S.A. 98 12432-7 PubMed GONUTS page

[PMID:16407123-10] 10.0 ^10.1 ^10.2 Gegonne, A et al. (2006) TAF7: a possible transcription initiation check-point regulator. Proc. Natl. Acad. Sci. U.S.A. 103 602-7 PubMed GONUTS page

[PMID:9603525-11] 11.0 ^11.1 ^11.2 ^11.3 Wieczorek, E et al. (1998) Function of TAF(II)-containing complex without TBP in transcription by RNA polymerase II. Nature 393 187-91 PubMed GONUTS page

[PMID:7824954-12] 12.0 ^12.1 ^12.2 ^12.3 Chiang, CM & Roeder, RG (1995) Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators. Science 267 531-6 PubMed GONUTS page

[PMID:11005381-13] Yuan, CX & Gurley, WB (2000) Potential targets for HSF1 within the preinitiation complex. Cell Stress Chaperones 5 229-42 PubMed GONUTS page

[PMID:21873635-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:14580349-15] Guermah, M et al. (2003) The TBN protein, which is essential for early embryonic mouse development, is an inducible TAFII implicated in adipogenesis. Mol. Cell 12 991-1001 PubMed GONUTS page

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HUMAN:TAF7

Contents

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References

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