Q5VWG9 (TAF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription initiation factor TFIID subunit 3

Alternative name(s):
140 kDa TATA box-binding protein-associated factor
TBP-associated factor 3
Transcription initiation factor TFIID 140 kDa subunit
Short name=TAF(II)140
Short name=TAF140
Short name=TAFII-140
Short name=TAFII140

Gene names

Name:

TAF3

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

General annotation (Comments)

Function	Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.
Subunit structure	Belongs to the TFIID complex which is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TAF10 via the histone fold. Interacts with TAF13, TBP, SAP130 and GCN5L2. Interacts with TBPL2. Ref.1
Subcellular location	Nucleus Ref.1.
Sequence similarities	Belongs to the TAF3 family. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAH45106.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH62352.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH73884.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	maintenance of protein location in nucleus Inferred from direct assay. Source: HGNC negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	transcription factor TFIID complex Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 929	929	Transcription initiation factor TFIID subunit 3		PRO_0000245528
Regions
	Zinc finger	865 – 915	51	PHD-type
	Compositional bias	136 – 141	6	Poly-Glu
	Compositional bias	163 – 168	6	Poly-Glu
	Compositional bias	507 – 746	240	Lys-rich
	Compositional bias	779 – 833	55	Pro-rich
Amino acid modifications
	Modified residue	183	1	Phosphoserine Ref.6
	Modified residue	199	1	Phosphoserine Ref.9
	Modified residue	229	1	Phosphoserine Ref.5 Ref.8 Ref.9
	Modified residue	236	1	Phosphoserine Ref.5
	Modified residue	243	1	Phosphoserine Ref.5 Ref.8 Ref.9
	Modified residue	266	1	N6-acetyllysine Ref.10
	Modified residue	267	1	Phosphoserine Ref.7
	Modified residue	291	1	Phosphoserine Ref.8
	Modified residue	297	1	Phosphoserine Ref.5 Ref.8 Ref.9
	Modified residue	301	1	Phosphoserine Ref.9
	Modified residue	364	1	Phosphothreonine Ref.8
	Modified residue	410	1	Phosphoserine Ref.5 Ref.6
	Modified residue	411	1	Phosphoserine Ref.6
	Modified residue	413	1	Phosphoserine Ref.6
	Modified residue	415	1	Phosphoserine Ref.6
	Modified residue	501	1	Phosphothreonine Ref.9
	Modified residue	776	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	349	1	S → T. Corresponds to variant rs17366712 [ dbSNP | Ensembl ].		VAR_052254
	Natural variant	442	1	N → S. Ref.3 Corresponds to variant rs4747647 [ dbSNP | Ensembl ].		VAR_052255
	Natural variant	696	1	V → A. Ref.4 Corresponds to variant rs1244229 [ dbSNP | Ensembl ].		VAR_052256
	Natural variant	696	1	V → L. Corresponds to variant rs10795583 [ dbSNP | Ensembl ].		VAR_052257
Experimental info
	Mutagenesis	23	1	W → R: Loss of interaction with TAF10. Ref.1
	Sequence conflict	23 – 25	3	WDS → TRP in CAB56032. Ref.4
	Sequence conflict	533	1	M → K in AAH73884. Ref.3
	Sequence conflict	696	1	V → P in AAH62352. Ref.3
	Sequence conflict	700	1	E → K in CAB56032. Ref.4
	Sequence conflict	707	1	E → K in AAH62352. Ref.3
	Sequence conflict	713	1	E → K in AAH62352. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q5VWG9 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: C951754B5B532E72	FASTA	929	103,582
	10 20 30 40 50 60 MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH RYSELYGRTD 70 80 90 100 110 120 PILDDVGEAF QLMGVSLHEL EDYIHNIEPV TFPHQIPSFP VSKNNVLQFP QPGSKDAEER 130 140 150 160 170 180 KEYIPDYLPP IVSSQEEEEE EQVPTDGGTS AEAMQVPLEE DDELEEEEII NDENFLGKRP 190 200 210 220 230 240 LDSPEAEELP AMKRPRLLST KGDTLDVVLL EAREPLSSIN TQKIPPMLSP VHVQDSTDLA 250 260 270 280 290 300 PPSPEPPMLA PVAKSQMPTA KPLETKSFTP KTKTKTSSPG QKTKSPKTAQ SPAMVGSPIR 310 320 330 340 350 360 SPKTVSKEKK SPGRSKSPKS PKSPKVTTHI PQTPVRPETP NRTPSATLSE KISKETIQVK 370 380 390 400 410 420 QIQTPPDAGK LNSENQPKKA VVADKTIEAS IDAVIARACA EREPDPFEFS SGSESEGDIF 430 440 450 460 470 480 TSPKRISGPE CTTPKASTSA NNFTKSGSTP LPLSGGTSSS DNSWTMDASI DEVVRKAKLG 490 500 510 520 530 540 TPSNMPPNFP YISSPSVSPP TPEPLHKVYE EKTKLPSSVE VKKKLKKELK TKMKKKEKQR 550 560 570 580 590 600 DREREKDKNK DKSKEKDKVK EKEKDKETGR ETKYPWKEFL KEEEADPYKF KIKEFEDVDP 610 620 630 640 650 660 KVKLKDGLVR KEKEKHKDKK KDREKGKKDK DKREKEKVKD KGREDKMKAP APPLVLPPKE 670 680 690 700 710 720 LALPLFSPAT ASRVPAMLPS LLPVLPEKLF EEKEKVKEKE KKKDKKEKKK KKEKEKEKKE 730 740 750 760 770 780 KEREKEKRER EKREKEKEKH KHEKIKVEPV ALAPSPVIPR LTLRVGAGQD KIVISKVVPA 790 800 810 820 830 840 PEAKPAPSQN RPKTPPPAPA PAPGPMLVSP APVPLPLLAQ AAAGPALLPS PGPAASGASA 850 860 870 880 890 900 KAPVRSVVTE TVSTYVIRDE WGNQIWICPG CNKPDDGSPM IGCDDCDDWY HWPCVGIMTA 910 920 PPEEMQWFCP KCANKKKDKK HKKRKHRAH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger." Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I. Mol. Cell. Biol. 21:5109-5121(2001) [PubMed: 11438666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH TAF10; TAF13; TBP; SAP130 AND GCN5L2, MUTAGENESIS OF TRP-23. Tissue: Cervix carcinoma.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] OF 1-714, VARIANT SER-442. Tissue: Bone, Skin and Uterus.
[4]	"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] OF 23-703, VARIANT ALA-696. Tissue: Uterus.
[5]	"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-229; SER-236; SER-243; SER-297 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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-183; SER-410; SER-411; SER-413 AND SER-415, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-229; SER-243; SER-291; SER-297 AND THR-364, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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-199; SER-229; SER-243; SER-297; SER-301 AND THR-501, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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 LYS-266 AND LYS-776, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ292190 mRNA. Translation: CAC34475.1. AL390294, AL159172, AL353754 Genomic DNA. Translation: CAH73142.1. AL353754, AL159172, AL390294 Genomic DNA. Translation: CAH73451.1. AL159172, AL353754, AL390294 Genomic DNA. Translation: CAI15661.1. BC045106 mRNA. Translation: AAH45106.1. Sequence problems. BC073884 mRNA. Translation: AAH73884.1. Different initiation. BC062352 mRNA. Translation: AAH62352.1. Different initiation. AL117661 mRNA. Translation: CAB56032.1.
IPI	IPI00853240.
PIR	T17342.
RefSeq	NP_114129.1. NM_031923.2.
UniGene	Hs.527688. Hs.709995.
3D structure databases
ProteinModelPortal	Q5VWG9.
SMR	Q5VWG9. Positions 855-921.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5VWG9. 2 interactions.
STRING	Q5VWG9.
PTM databases
PhosphoSite	Q5VWG9.
Polymorphism databases
DMDM	74747393.
Proteomic databases
PRIDE	Q5VWG9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000344293; ENSP00000340271; ENSG00000165632.
GeneID	83860.
KEGG	hsa:83860.
UCSC	uc009xis.1. human.
Organism-specific databases
CTD	83860.
GeneCards	GC10P007860.
H-InvDB	HIX0025228. HIX0026560. HIX0201494.
HGNC	HGNC:17303. TAF3.
MIM	606576. gene.
neXtProt	NX_Q5VWG9.
PharmGKB	PA38222.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00580000081562.
HOGENOM	HBG713530.
HOVERGEN	HBG083188.
InParanoid	Q5VWG9.
OMA	NFPYISS.
OrthoDB	EOG4V9TQC.
Gene expression databases
ArrayExpress	Q5VWG9.
Bgee	Q5VWG9.
CleanEx	HS_TAF3.
Genevestigator	Q5VWG9.
GermOnline	ENSG00000165632. Homo sapiens.
Family and domain databases
InterPro	IPR006565. BTP. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KO	K14650.
Pfam	PF07524. Bromo_TP. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00576. BTP. 1 hit. SM00249. PHD. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	72861.
SOURCE	Search...

Entry information

Entry name

TAF3_HUMAN

Accession

Primary (citable) accession number: Q5VWG9
Secondary accession number(s): Q6GMS5 , Q6P6B5, Q86VY6, Q9BQS9, Q9UFI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	December 7, 2004
Last modified:	December 14, 2011
This is version 79 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.