Q15545 (TAF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 7

Alternative name(s):
RNA polymerase II TBP-associated factor subunit F
Transcription initiation factor TFIID 55 kDa subunit
Short name=TAF(II)55
Short name=TAFII-55
Short name=TAFII55

Gene names

Name:	TAF7
Synonyms:	TAF2F, TAFII55

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

General annotation (Comments)

Function	Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).
Subunit structure	TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TAFII250, TAFII100, TAFII28, TAFII20, and TAFII18, but not with TAFII30 or TBP. 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.
Subcellular location	Nucleus.
Tissue specificity	Ubiquitous.
Domain	The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase, which methylates Lys-5 in vitro By similarity.
Sequence similarities	Belongs to the TAF7 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of histone acetylation Inferred from direct assay. Source: UniProtKB negative regulation of protein kinase activity Inferred from direct assay. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB spermine transport Inferred from sequence or structural similarity. Source: UniProtKB transcription initiation from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA MLL1 complex Inferred from direct assay Ref.7. Source: UniProtKB transcription factor TFIID complex Inferred from direct assay Ref.2. Source: UniProtKB transcription factor TFTC complex Inferred from direct assay. Source: UniProtKB
Molecular function	histone acetyltransferase binding Inferred from physical interaction. Source: UniProtKB thyroid hormone receptor binding Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.2. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: UniProtKB vitamin D receptor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 349	349	Transcription initiation factor TFIID subunit 7		PRO_0000118881
Regions
	Coiled coil	244 – 349	106	Potential
	Motif	3 – 5	3	[KR]-[STA]-K motif
	Compositional bias	227 – 230	4	Poly-Ser
Amino acid modifications
	Modified residue	171	1	Phosphoserine Ref.11 Ref.12
	Modified residue	201	1	Phosphoserine Ref.10
	Modified residue	213	1	Phosphoserine Ref.8
	Modified residue	227	1	Phosphoserine Ref.8
	Modified residue	228	1	Phosphoserine Ref.8
	Modified residue	229	1	Phosphoserine Ref.8
	Modified residue	230	1	Phosphoserine Ref.8
	Modified residue	264	1	Phosphoserine Ref.10 Ref.11 Ref.12
Natural variations
	Natural variant	178	1	S → R.		VAR_005629
Experimental info
	Mutagenesis	5	1	K → R: Abolishes methylation in vitro. Ref.9
	Sequence conflict	283	1	K → N in AAB60347. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q15545 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0AAFD3E33E3CCD6E	FASTA	349	40,259
	10 20 30 40 50 60 MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD GRHGIVRVDR 70 80 90 100 110 120 VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD GDLYPPVEEP VASTDPKASK 130 140 150 160 170 180 KKDKDKEKKF IWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR 190 200 210 220 230 240 WEIIAEDETK EAENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD 250 260 270 280 290 300 EEDINIIDTE EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK 310 320 330 340 RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple interactions between hTAFII55 and other TFIID subunits. Requirements for the formation of stable ternary complexes between hTAFII55 and the TATA-binding protein." Lavigne A.C., Mengus G., May M., Dubrowskaya V., Tora L., Davidson I. J. Biol. Chem. 271:19774-19780(1996) [PubMed: 8702684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators." Chiang C.-M., Roeder R.G. Science 267:531-536(1995) [PubMed: 7824954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The intronless and TATA-less human TAFII55 gene contains a functional initiator and a downstream promoter element." Zhou T., Chiang C.-M. J. Biol. Chem. 276:25503-25511(2001) [PubMed: 11340078] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	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].
[6]	"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: Skin.
[7]	"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.
[8]	"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-213; SER-227; SER-228; SER-229 AND SER-230, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Structural basis for the methylation site specificity of SET7/9." Couture J.-F., Collazo E., Hauk G., Trievel R.C. Nat. Struct. Mol. Biol. 13:140-146(2006) [PubMed: 16415881] [Abstract] Cited for: MOTIF, MUTAGENESIS OF LYS-5.
[10]	"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-201 AND SER-264, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-171 AND SER-264, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-171 AND SER-264, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97999 mRNA. Translation: CAA66636.1. U18062 mRNA. Translation: AAB60347.1. AF349038 Genomic DNA. Translation: AAK30585.1. AK314837 mRNA. Translation: BAG37356.1. CH471062 Genomic DNA. Translation: EAW61966.1. BC032737 mRNA. Translation: AAH32737.1.
IPI	IPI00018111.
PIR	I38904.
RefSeq	NP_005633.2. NM_005642.2.
UniGene	Hs.438838.
3D structure databases
ProteinModelPortal	Q15545.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29047N. DIP-429N.
IntAct	Q15545. 7 interactions.
STRING	Q15545.
PTM databases
PhosphoSite	Q15545.
Polymorphism databases
DMDM	3024690.
Proteomic databases
PRIDE	Q15545.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313368; ENSP00000312709; ENSG00000178913.
GeneID	6879.
KEGG	hsa:6879.
UCSC	uc003ljg.1. human.
Organism-specific databases
CTD	6879.
GeneCards	GC05M140678.
H-InvDB	HIX0024831.
HGNC	HGNC:11541. TAF7.
HPA	HPA006429.
MIM	600573. gene.
neXtProt	NX_Q15545.
PharmGKB	PA36316.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04289.
GeneTree	ENSGT00390000010815.
HOGENOM	HBG714544.
HOVERGEN	HBG013606.
InParanoid	Q15545.
OMA	CQMLVCT.
OrthoDB	EOG4V4389.
PhylomeDB	Q15545.
Gene expression databases
ArrayExpress	Q15545.
Bgee	Q15545.
CleanEx	HS_TAF7.
Genevestigator	Q15545.
GermOnline	ENSG00000178913. Homo sapiens.
Family and domain databases
InterPro	IPR006751. TAFII55_prot_cons_reg. [Graphical view]
KO	K03132.
Pfam	PF04658. TAFII55_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	26869.
SOURCE	Search...

Entry information

Entry name

TAF7_HUMAN

Accession

Primary (citable) accession number: Q15545
Secondary accession number(s): B2RBV9, Q13036

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 105 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.