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UniProtKB/Swiss-Prot entry Q5VWG9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TAF3_HUMAN
Primary accession number Q5VWG9
Secondary accession numbers Q6GMS5 Q6P6B5 Q86VY6 Q9BQS9 Q9UFI8
Integrated into Swiss-Prot on July 11, 2006
Sequence was last modified on December 7, 2004 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 54)
Name and origin of the protein
Protein name Transcription initiation factor TFIID subunit 3
Synonyms TBP-associated factor 3
Transcription initiation factor TFIID 140 kDa subunit
140 kDa TATA box-binding protein-associated factor
TAF140
TAFII140
Gene name
Name: TAF3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION WITH TAF10, TAF13, TBP, SAP130 AND GCN5L2, AND MUTAGENESIS OF TRP-23.
TISSUE=Cervix carcinoma;
DOI=10.1128/MCB.21.15.5109-5121.2001; PubMed=11438666 [NCBI, ExPASy, EBI, Israel, Japan]
Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger.";
Mol. Cell. Biol. 21:5109-5121(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-714, AND VARIANT SER-442.
TISSUE=Bone, Skin, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-703, AND VARIANT ALA-696.
TISSUE=Uterus;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-236; SER-243; SER-297 AND SER-410, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-410; SER-411; SER-413 AND SER-415, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
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: 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.
  • SUBCELLULAR LOCATION: Nucleus.
  • SIMILARITY: Belongs to the TAF3 family.
  • SIMILARITY: Contains 1 PHD-type zinc finger.
  • SEQUENCE CAUTION:
    • Sequence=AAH45106.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ292190; CAC34475.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390294; CAH73142.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL159172; CAH73142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353754; CAH73142.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353754; CAH73451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL159172; CAH73451.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390294; CAH73451.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL159172; CAI15661.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353754; CAI15661.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390294; CAI15661.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC045106; AAH45106.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073884; AAH73884.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062352; AAH62352.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL117661; CAB56032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00853240; -.
PIR T17342; T17342.
RefSeq NP_114129.1; -.
UniGene Hs.708133
3D structure databases
ModBase Q5VWG9.
Organism-specific databases
GeneCards GC10P007898; -.
HGNC HGNC:17303; TAF3.
GenAtlas TAF3.
MIM 606576; gene. [NCBI / EBI]
PharmGKB PA38222; -.
Gene expression databases
ArrayExpress Q5VWG9; -.
Bgee Q5VWG9; -.
CleanEx HS_TAF3; -.
GermOnline ENSG00000165632; Homo sapiens.
Ontologies
GO
GO:0005669; Cellular component: transcription factor TFIID complex (inferred from direct assay from UniProtKB).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051457; Biological process: maintenance of protein location in nucleus (inferred from direct assay from HGNC).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006565; BTP.
IPR019786; Zinc_finger_PHD-type_CS.
IPR001965; Znf_PHD.
IPR019787; Znf_PHD-finger.
Graphical view of domain structure.
Pfam PF07524; Bromo_TP; 1.
PF00628; PHD; 1.
Pfam graphical view of domain structure.
SMART SM00576; BTP; 1.
SM00249; PHD; 1.
SMART graphical view of domain structure.
PROSITE PS01359; ZF_PHD_1; 1.
PS50016; ZF_PHD_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q5VWG9; -.
Genome annotation databases
Ensembl ENSG00000165632; Homo sapiens. [Contig view]
GeneID 83860; -.
KEGG hsa:83860; -.
Phylogenomic databases
HOGENOM Q5VWG9; -.
HOVERGEN Q5VWG9; -.
OMA Q5VWG9; KQIQTPP.
Other
NextBio 72861; -.
SOURCE TAF3; Homo sapiens.
ProtoNet Q5VWG9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   929  929     Transcription initiation factor TFIID subunit 3. PRO_0000245528
ZN_FING   865   915  51     PHD-type. 
COMPBIAS   136   141  6     Poly-Glu. 
COMPBIAS   163   168  6     Poly-Glu. 
COMPBIAS   507   746  240     Lys-rich. 
COMPBIAS   779   833  55     Pro-rich. 
MOD_RES   183   183        Phosphoserine. 
MOD_RES   229   229        Phosphoserine. 
MOD_RES   236   236        Phosphoserine. 
MOD_RES   243   243        Phosphoserine. 
MOD_RES   267   267        Phosphoserine. 
MOD_RES   297   297        Phosphoserine. 
MOD_RES   410   410        Phosphoserine. 
MOD_RES   411   411        Phosphoserine. 
MOD_RES   413   413        Phosphoserine. 
MOD_RES   415   415        Phosphoserine. 
VARIANT   349   349  1     S -> T (in dbSNP:rs17366712 [NCBI]). VAR_052254 
VARIANT   442   442  1     N -> S (in dbSNP:rs4747647 [NCBI]). VAR_052255 
VARIANT   598   598  1     V -> L (in dbSNP:rs17366712 [NCBI]). VAR_026980 
VARIANT   696   696  1     V -> A (in dbSNP:rs1244229 [NCBI]). VAR_052256 
VARIANT   696   696  1     V -> L (in dbSNP:rs10795583 [NCBI]). VAR_052257 
VARIANT   927   927  1     R -> S (in dbSNP:rs10795583 [NCBI]). VAR_026981 
MUTAGEN   23    23        W->R: Loss of interaction with TAF10. 
CONFLICT   23    25        WDS -> TRP (in Ref. 4; CAB56032). 
CONFLICT   533   533        M -> K (in Ref. 3; AAH73884). 
CONFLICT   696   696        V -> P (in Ref. 3; AAH62352). 
CONFLICT   700   700        E -> K (in Ref. 4; CAB56032). 
CONFLICT   707   707        E -> K (in Ref. 3; AAH62352). 
CONFLICT   713   713        E -> K (in Ref. 3; AAH62352). 
Sequence information
Length: 929 AA [This is the length of the unprocessed precursor] Molecular weight: 103582 Da [This is the MW of the unprocessed precursor] CRC64: C951754B5B532E72 [This is a checksum on the sequence]
        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 

Q5VWG9 in FASTA format

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