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Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)

 TAF1_HUMAN              Reviewed;        1872 AA.
P21675; A5CVC8; A5CVC9; A5CVD0; A5CVD1; B1Q2X3; Q59FZ3; Q6IUZ1;
Q70Q86; Q70Q87; Q70T00; Q70T01; Q70T02; Q70T03;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
30-AUG-2017, entry version 198.
RecName: Full=Transcription initiation factor TFIID subunit 1;
EC=2.3.1.48;
EC=2.7.11.1;
AltName: Full=Cell cycle gene 1 protein;
AltName: Full=TBP-associated factor 250 kDa;
Short=p250;
AltName: Full=Transcription initiation factor TFIID 250 kDa subunit;
Short=TAF(II)250;
Short=TAFII-250;
Short=TAFII250;
Name=TAF1; Synonyms=BA2R, CCG1, CCGS, TAF2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Laryngeal carcinoma;
PubMed=2038334; DOI=10.1128/MCB.11.6.3317;
Sekiguchi T., Nohiro Y., Nakamura Y., Hisamoto N., Nishimoto T.;
"The human CCG1 gene, essential for progression of the G1 phase,
encodes a 210-kilodalton nuclear DNA-binding protein.";
Mol. Cell. Biol. 11:3317-3325(1991).
[2]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3169001;
Sekiguchi T., Miyata T., Nishimoto T.;
"Molecular cloning of the cDNA of human X chromosomal gene (CCG1)
which complements the temperature-sensitive G1 mutants, tsBN462 and
ts13, of the BHK cell line.";
EMBO J. 7:1683-1687(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TBP AND
TAFS.
PubMed=7680771; DOI=10.1038/362175a0;
Ruppert S., Wang E.H., Tjian R.;
"Cloning and expression of human TAFII250: a TBP-associated factor
implicated in cell-cycle regulation.";
Nature 362:175-179(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N-TAF1), AND INVOLVEMENT IN DYT3.
TISSUE=Brain;
PubMed=17273961; DOI=10.1086/512129;
Makino S., Kaji R., Ando S., Tomizawa M., Yasuno K., Goto S.,
Matsumoto S., Tabuena M.D., Maranon E., Dantes M., Lee L.V.,
Ogasawara K., Tooyama I., Akatsu H., Nishimura M., Tamiya G.;
"Reduced neuron-specific expression of the TAF1 gene is associated
with X-linked dystonia-parkinsonism.";
Am. J. Hum. Genet. 80:393-406(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-269.
NIEHS SNPs program;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 837-1872 (ISOFORM 4).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1801 (ISOFORMS 2A; 2C AND 2D),
NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1592 (ISOFORM 2E), NUCLEOTIDE
SEQUENCE [MRNA] OF 1498-1801 (ISOFORM 3), AND INVOLVEMENT IN DYT3.
TISSUE=Fetal brain;
PubMed=12928496; DOI=10.1073/pnas.1831949100;
Nolte D., Niemann S., Muller U.;
"Specific sequence changes in multiple transcript system DYT3 are
associated with X-linked dystonia parkinsonism.";
Proc. Natl. Acad. Sci. U.S.A. 100:10347-10352(2003).
[9]
SEQUENCE REVISION.
Nolte D.;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1347-1801 (ISOFORMS 2E; 2G; 2H AND 2I),
AND ALTERNATIVE SPLICING.
PubMed=17952504; DOI=10.1007/s00335-007-9063-z;
Herzfeld T., Nolte D., Muller U.;
"Structural and functional analysis of the human TAF1/DYT3 multiple
transcript system.";
Mamm. Genome 18:787-795(2007).
[11]
FUNCTION.
PubMed=8450888; DOI=10.1038/362179a0;
Hisatake K., Hasegawa S., Takada R., Nakatani Y., Horikoshi M.,
Roeder R.G.;
"The p250 subunit of native TATA box-binding factor TFIID is the cell-
cycle regulatory protein CCG1.";
Nature 362:179-181(1993).
[12]
FUNCTION, PHOSPHORYLATION AT SER-137 AND SER-307, AND ATP-BINDING.
PubMed=8625415; DOI=10.1016/S0092-8674(00)81055-7;
Dikstein R., Ruppert S., Tjian R.;
"TAFII250 is a bipartite protein kinase that phosphorylates the base
transcription factor RAP74.";
Cell 84:781-790(1996).
[13]
INTERACTION WITH SV40 LARGE T ANTIGEN.
PubMed=8647434; DOI=10.1101/gad.10.11.1369;
Damania B., Alwine J.C.;
"TAF-like function of SV40 large T antigen.";
Genes Dev. 10:1369-1381(1996).
[14]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 ICP4.
PubMed=8649420; DOI=10.1128/MCB.16.6.3085;
Carrozza M.J., DeLuca N.A.;
"Interaction of the viral activator protein ICP4 with TFIID through
TAF250.";
Mol. Cell. Biol. 16:3085-3093(1996).
[15]
FUNCTION, AND MUTAGENESIS.
PubMed=9660973; DOI=10.1016/S1097-2765(00)80089-1;
O'Brien T., Tjian R.;
"Functional analysis of the human TAFII250 N-terminal kinase domain.";
Mol. Cell 1:905-911(1998).
[16]
FUNCTION, INTERACTION WITH RB1, AND ATP-BINDING.
PubMed=9858607; DOI=10.1128/MCB.19.1.846;
Siegert J.L., Robbins P.D.;
"Rb inhibits the intrinsic kinase activity of TATA-binding protein-
associated factor TAFII250.";
Mol. Cell. Biol. 19:846-854(1999).
[17]
INTERACTION WITH ASF1A.
PubMed=10759893; DOI=10.1046/j.1365-2443.2000.00319.x;
Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.;
"A human homologue of yeast anti-silencing factor has histone
chaperone activity.";
Genes Cells 5:221-233(2000).
[18]
FUNCTION.
PubMed=11278496; DOI=10.1074/jbc.M009385200;
Solow S., Salunek M., Ryan R., Lieberman P.M.;
"Taf(II) 250 phosphorylates human transcription factor IIA on serine
residues important for TBP binding and transcription activity.";
J. Biol. Chem. 276:15886-15892(2001).
[19]
INTERACTION WITH ASF1A.
PubMed=12093919; DOI=10.1073/pnas.142627899;
Chimura T., Kuzuhara T., Horikoshi M.;
"Identification and characterization of CIA/ASF1 as an interactor of
bromodomains associated with TFIID.";
Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002).
[20]
INTERACTION WITH ASF1A AND ASF1B.
PubMed=12842904; DOI=10.1074/jbc.M303549200;
Umehara T., Horikoshi M.;
"Transcription initiation factor IID-interactive histone chaperone
CIA-II implicated in mammalian spermatogenesis.";
J. Biol. Chem. 278:35660-35667(2003).
[21]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=15053879; DOI=10.1016/S1097-2765(04)00123-6;
Li H.-H., Li A.G., Sheppard H.M., Liu X.;
"Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role
for TAF1 in cell G1 progression.";
Mol. Cell 13:867-878(2004).
[22]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
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.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[23]
HISTONE ACETYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF GLU-721 AND
827-MET--ASP-829.
PubMed=15870300; DOI=10.1128/MCB.25.10.4321-4332.2005;
Hilton T.L., Li Y., Dunphy E.L., Wang E.H.;
"TAF1 histone acetyltransferase activity in Sp1 activation of the
cyclin D1 promoter.";
Mol. Cell. Biol. 25:4321-4332(2005).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1826, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1700 (ISOFORMS 2A AND
4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1702 (ISOFORM 2G),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1697 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
ENZYME REGULATION.
PubMed=22711989; DOI=10.1128/MCB.00416-12;
Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.;
"Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene
transcription by TFIID subunits TAF1 and TAF7.";
Mol. Cell. Biol. 32:3358-3369(2012).
[28]
MISCELLANEOUS.
PubMed=23184149; DOI=10.1093/hmg/dds499;
Herzfeld T., Nolte D., Grznarova M., Hofmann A., Schultze J.L.,
Muller U.;
"X-linked dystonia parkinsonism syndrome (XDP, lubag): disease-
specific sequence change DSC3 in TAF1/DYT3 affects genes in vesicular
transport and dopamine metabolism.";
Hum. Mol. Genet. 22:941-951(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-549 AND LYS-562, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[31]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1359-1638.
PubMed=10827952; DOI=10.1126/science.288.5470.1422;
Jacobson R.H., Ladurner A.G., King D.S., Tjian R.;
"Structure and function of a human TAFII250 double bromodomain
module.";
Science 288:1422-1425(2000).
[32]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1501-1635, AND SUBUNIT.
PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
Gingras A.C., Arrowsmith C.H., Knapp S.;
"Histone recognition and large-scale structural analysis of the human
bromodomain family.";
Cell 149:214-231(2012).
[33]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 579-1215 IN COMPLEX WITH
TAF7, FUNCTION, AND INTERACTION WITH TAF7.
PubMed=25412659; DOI=10.1038/cr.2014.148;
Wang H., Curran E.C., Hinds T.R., Wang E.H., Zheng N.;
"Crystal structure of a TAF1-TAF7 complex in human transcription
factor IID reveals a promoter binding module.";
Cell Res. 24:1433-1444(2014).
[34]
STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), AND SUBCELLULAR
LOCATION.
PubMed=27007846; DOI=10.1038/nature17394;
Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.;
"Structure of promoter-bound TFIID and model of human pre-initiation
complex assembly.";
Nature 531:604-609(2016).
[35]
VARIANTS [LARGE SCALE ANALYSIS] VAL-269; GLY-297; ASP-453; LYS-651 AND
ILE-691.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[36]
INVOLVEMENT IN MRXS33, AND VARIANTS MRXS33 SER-575; ARG-786; HIS-955;
TRP-1225; THR-1316; HIS-1431 AND HIS-1496.
PubMed=26637982; DOI=10.1016/j.ajhg.2015.11.005;
O'Rawe J.A., Wu Y., Doerfel M.J., Rope A.F., Au P.Y.,
Parboosingh J.S., Moon S., Kousi M., Kosma K., Smith C.S., Tzetis M.,
Schuette J.L., Hufnagel R.B., Prada C.E., Martinez F., Orellana C.,
Crain J., Caro-Llopis A., Oltra S., Monfort S., Jimenez-Barron L.T.,
Swensen J., Ellingwood S., Smith R., Fang H., Ospina S., Stegmann S.,
Den Hollander N., Mittelman D., Highnam G., Robison R., Yang E.,
Faivre L., Roubertie A., Riviere J.B., Monaghan K.G., Wang K.,
Davis E.E., Katsanis N., Kalscheuer V.M., Wang E.H., Metcalfe K.,
Kleefstra T., Innes A.M., Kitsiou-Tzeli S., Rosello M., Keegan C.E.,
Lyon G.J.;
"TAF1 Variants Are Associated with Dysmorphic Features, Intellectual
Disability, and Neurological Manifestations.";
Am. J. Hum. Genet. 97:922-932(2015).
[37]
VARIANTS ASP-472 AND CYS-1169.
PubMed=25644381; DOI=10.1038/mp.2014.193;
Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T.,
Love M.I., Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M.,
Fischer U., Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N.,
Castelnau L., Rucci J., Montjean R., Dorseuil O., Billuart P.,
Stuhlmann T., Shaw M., Corbett M.A., Gardner A., Willis-Owen S.,
Tan C., Friend K.L., Belet S., van Roozendaal K.E.,
Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R., O'Keeffe S.,
Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
"X-exome sequencing of 405 unresolved families identifies seven novel
intellectual disability genes.";
Mol. Psychiatry 21:133-148(2016).
-!- FUNCTION: Largest component and core scaffold of the TFIID basal
transcription factor complex (PubMed:25412659, PubMed:27007846).
Contains novel N- and C-terminal Ser/Thr kinase domains which can
autophosphorylate or transphosphorylate other transcription
factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-
mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on
Ser residues. Possesses DNA-binding activity (PubMed:25412659).
Essential for progression of the G1 phase of the cell cycle
(PubMed:11278496, PubMed:15053879, PubMed:2038334, PubMed:8450888,
PubMed:8625415, PubMed:9660973, PubMed:9858607). Exhibits histone
acetyltransferase activity towards histones H3 and H4
(PubMed:15870300). {ECO:0000269|PubMed:11278496,
ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15870300,
ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:25412659,
ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:8450888,
ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9660973,
ECO:0000269|PubMed:9858607}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Autophosphorylates on Ser residues. Inhibited
by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1
or CIITA inhibits the histone acetyltransferase activity.
{ECO:0000269|PubMed:22711989}.
-!- SUBUNIT: TAF1 is the largest component of transcription factor
TFIID that is composed of TBP and a variety of TBP-associated
factors (PubMed:7680771). TAF1, when part of the TFIID complex,
interacts with C-terminus of TP53 (PubMed:15053879). Part of a
TFIID-containing RNA polymerase II pre-initiation complex that is
composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2,
GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2,
ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9,
TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846). Interacts with
TAF7; the interaction is direct (PubMed:25412659). Component of
some MLL1/MLL complex, at least composed of the core components
KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the
facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
and TEX10. RB1 interacts with the N-terminal domain of TAF1.
Interacts with ASF1A and ASF1B (PubMed:10759893, PubMed:12093919,
PubMed:12842904). Interacts (via bromo domains) with acetylated
lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3
and H4 (in vitro). Interacts with SV40 Large T antigen
(PubMed:8647434). Interacts with herpes simplex virus 1 ICP4
(PubMed:8649420). {ECO:0000269|PubMed:10759893,
ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:12842904,
ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:25412659,
ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:7680771,
ECO:0000269|PubMed:8647434, ECO:0000269|PubMed:8649420,
ECO:0000269|PubMed:9858607}.
-!- INTERACTION:
P03255:- (xeno); NbExp=3; IntAct=EBI-491289, EBI-2603114;
P35269:GTF2F1; NbExp=3; IntAct=EBI-491289, EBI-457886;
P20226:TBP; NbExp=5; IntAct=EBI-491289, EBI-355371;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2038334,
ECO:0000269|PubMed:27007846}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Comment=the TAF1/DYT3 multiple transcript system is composed of
38 evolutionary conserved exons plus 5 downstream exons referred
to as exons d1-d5 that are primate-specific. Multiple highly
polymorphic variants can be generated by splicing exons d3 and
d4 to various combinations of exons 1-37.;
Name=1;
IsoId=P21675-1; Sequence=Displayed;
Name=2;
IsoId=P21675-2; Sequence=VSP_012362;
Name=3;
IsoId=P21675-3; Sequence=VSP_053382, VSP_053383, VSP_053384;
Note=Contains a phosphoserine at position 1697.
{ECO:0000244|PubMed:20068231};
Name=4;
IsoId=P21675-4; Sequence=VSP_053383;
Note=Contains a phosphoserine at position 1700.
{ECO:0000244|PubMed:20068231};
Name=2a;
IsoId=P21675-5; Sequence=VSP_053383, VSP_053384;
Note=Contains a phosphoserine at position 1700.
{ECO:0000244|PubMed:20068231};
Name=2c;
IsoId=P21675-6; Sequence=VSP_053384;
Name=2d;
IsoId=P21675-7; Sequence=VSP_053381, VSP_053384;
Name=2e; Synonyms=2F;
IsoId=P21675-8; Sequence=VSP_053379, VSP_053380;
Name=2g;
IsoId=P21675-9; Sequence=VSP_053381, VSP_053383, VSP_053384;
Note=Contains a phosphoserine at position 1702.
{ECO:0000244|PubMed:20068231};
Name=2h;
IsoId=P21675-10; Sequence=VSP_053375, VSP_053377;
Name=2i;
IsoId=P21675-11; Sequence=VSP_053376, VSP_053378;
Name=N-TAF1; Synonyms=TA14-391;
IsoId=P21675-12; Sequence=VSP_012362, VSP_053381;
Note=Only detected in brain, highest expression in the caudate
nucleus.;
-!- PTM: Phosphorylated by casein kinase II in vitro.
{ECO:0000269|PubMed:8625415}.
-!- DISEASE: Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: A X-
linked dystonia-parkinsonism disorder. Dystonia is defined by the
presence of sustained involuntary muscle contractions, often
leading to abnormal postures. DYT3 is characterized by severe
progressive torsion dystonia followed by parkinsonism. It has a
well-defined pathology of extensive neuronal loss and mosaic
gliosis in the striatum (caudate nucleus and putamen) which
appears to resemble that in Huntington disease.
{ECO:0000269|PubMed:12928496, ECO:0000269|PubMed:17273961}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Mental retardation, X-linked, syndromic, 33 (MRXS33)
[MIM:300966]: A mental retardation syndrome characterized by
intellectual deficit, delayed psychomotor development, delayed
speech and language, and characteristic facial features. Mental
retardation is defined by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
{ECO:0000269|PubMed:26637982}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Isoforms including the downstream (d) exons are
preferentially expressed in brain, and may play a role in the
regulation of genes involved in dopamine processing and transport.
-!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/taf1/";
-----------------------------------------------------------------------
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EMBL; D90359; BAA14374.1; -; mRNA.
EMBL; X07024; CAA30073.1; ALT_SEQ; mRNA.
EMBL; AB300418; BAG15901.1; -; mRNA.
EMBL; AY623109; AAT38105.1; -; Genomic_DNA.
EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB209316; BAD92553.1; -; mRNA.
EMBL; AJ549247; CAD70490.1; -; mRNA.
EMBL; AJ549248; CAD70491.3; -; mRNA.
EMBL; AJ549249; CAD70492.2; -; mRNA.
EMBL; AJ549250; CAD70493.3; -; mRNA.
EMBL; AJ555148; CAD87527.2; -; mRNA.
EMBL; AJ555149; CAD87528.2; -; mRNA.
EMBL; AM711892; CAM98555.1; -; mRNA.
EMBL; AM711893; CAM98556.1; -; mRNA.
EMBL; AM711894; CAM98557.1; -; mRNA.
EMBL; AM711895; CAM98558.1; -; mRNA.
CCDS; CCDS14412.1; -. [P21675-2]
CCDS; CCDS35325.1; -. [P21675-1]
CCDS; CCDS69783.1; -. [P21675-12]
PIR; A40262; A40262.
RefSeq; NP_001273003.1; NM_001286074.1. [P21675-12]
RefSeq; NP_004597.2; NM_004606.4. [P21675-2]
RefSeq; NP_620278.1; NM_138923.3. [P21675-1]
RefSeq; XP_005262354.1; XM_005262297.4. [P21675-4]
UniGene; Hs.158560; -.
PDB; 1EQF; X-ray; 2.10 A; A=1359-1638.
PDB; 3AAD; X-ray; 3.30 A; A=1342-1629.
PDB; 3UV4; X-ray; 1.89 A; A/B=1501-1635.
PDB; 3UV5; X-ray; 2.03 A; A=1373-1635.
PDB; 4RGW; X-ray; 2.30 A; A=579-1215.
PDB; 4YYM; X-ray; 1.50 A; A/B=1497-1638.
PDB; 4YYN; X-ray; 1.85 A; A/B=1497-1638.
PDB; 5FUR; EM; 8.50 A; G=1-1872.
PDB; 5I1Q; X-ray; 1.50 A; A=1497-1638.
PDB; 5I29; X-ray; 1.21 A; A=1497-1638.
PDB; 5MG2; X-ray; 1.75 A; A=1501-1635.
PDBsum; 1EQF; -.
PDBsum; 3AAD; -.
PDBsum; 3UV4; -.
PDBsum; 3UV5; -.
PDBsum; 4RGW; -.
PDBsum; 4YYM; -.
PDBsum; 4YYN; -.
PDBsum; 5FUR; -.
PDBsum; 5I1Q; -.
PDBsum; 5I29; -.
PDBsum; 5MG2; -.
ProteinModelPortal; P21675; -.
SMR; P21675; -.
BioGrid; 112735; 74.
DIP; DIP-147N; -.
IntAct; P21675; 34.
MINT; MINT-1211825; -.
STRING; 9606.ENSP00000276072; -.
BindingDB; P21675; -.
ChEMBL; CHEMBL3217390; -.
GuidetoPHARMACOLOGY; 2231; -.
iPTMnet; P21675; -.
PhosphoSitePlus; P21675; -.
BioMuta; TAF1; -.
DMDM; 115942; -.
EPD; P21675; -.
MaxQB; P21675; -.
PaxDb; P21675; -.
PeptideAtlas; P21675; -.
PRIDE; P21675; -.
Ensembl; ENST00000276072; ENSP00000276072; ENSG00000147133. [P21675-2]
Ensembl; ENST00000373790; ENSP00000362895; ENSG00000147133. [P21675-1]
Ensembl; ENST00000423759; ENSP00000406549; ENSG00000147133. [P21675-12]
GeneID; 6872; -.
KEGG; hsa:6872; -.
UCSC; uc004dzt.6; human. [P21675-1]
CTD; 6872; -.
DisGeNET; 6872; -.
GeneCards; TAF1; -.
GeneReviews; TAF1; -.
HGNC; HGNC:11535; TAF1.
HPA; CAB016283; -.
HPA; HPA001075; -.
MalaCards; TAF1; -.
MIM; 300966; phenotype.
MIM; 313650; gene.
MIM; 314250; phenotype.
neXtProt; NX_P21675; -.
OpenTargets; ENSG00000147133; -.
Orphanet; 53351; X-linked dystonia-parkinsonism.
PharmGKB; PA36310; -.
eggNOG; KOG0008; Eukaryota.
eggNOG; COG5076; LUCA.
eggNOG; COG5179; LUCA.
GeneTree; ENSGT00390000012659; -.
HOGENOM; HOG000020066; -.
HOVERGEN; HBG050223; -.
InParanoid; P21675; -.
KO; K03125; -.
OMA; PTHMGPM; -.
OrthoDB; EOG091G00MO; -.
PhylomeDB; P21675; -.
TreeFam; TF313573; -.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNOR; P21675; -.
EvolutionaryTrace; P21675; -.
GeneWiki; TAF1; -.
GenomeRNAi; 6872; -.
PRO; PR:P21675; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147133; -.
ExpressionAtlas; P21675; baseline and differential.
Genevisible; P21675; HS.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0005667; C:transcription factor complex; IPI:ParkinsonsUK-UCL.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:BHF-UCL.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IPI:ParkinsonsUK-UCL.
GO; GO:0001129; F:RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0017025; F:TBP-class protein binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071318; P:cellular response to ATP; IDA:ParkinsonsUK-UCL.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:ParkinsonsUK-UCL.
GO; GO:0034644; P:cellular response to UV; IDA:ParkinsonsUK-UCL.
GO; GO:0006352; P:DNA-templated transcription, initiation; ISS:BHF-UCL.
GO; GO:0030901; P:midbrain development; IGI:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:1905524; P:negative regulation of protein autoubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:2000825; P:positive regulation of androgen receptor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; IGI:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0000209; P:protein polyubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; TAS:ParkinsonsUK-UCL.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0010767; P:regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; IDA:ParkinsonsUK-UCL.
GO; GO:0060260; P:regulation of transcription initiation from RNA polymerase II promoter; NAS:ParkinsonsUK-UCL.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; ISS:BHF-UCL.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0036369; P:transcription factor catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.1100.10; -; 1.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR011177; TAF1_animal.
InterPro; IPR009067; TAF_II_230-bd.
InterPro; IPR022591; TFIID_sub1_DUF3591.
Pfam; PF00439; Bromodomain; 2.
Pfam; PF12157; DUF3591; 1.
Pfam; PF09247; TBP-binding; 1.
PIRSF; PIRSF003047; TAF1_animal; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47055; SSF47055; 1.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS00633; BROMODOMAIN_1; 2.
PROSITE; PS50014; BROMODOMAIN_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative splicing;
ATP-binding; Bromodomain; Cell cycle; Complete proteome;
Disease mutation; DNA-binding; Dystonia; Host-virus interaction;
Isopeptide bond; Kinase; Mental retardation; Nucleotide-binding;
Nucleus; Parkinsonism; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 1872 Transcription initiation factor TFIID
subunit 1.
/FTId=PRO_0000211215.
DOMAIN 1 414 Protein kinase 1.
DOMAIN 1397 1467 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1425 1872 Protein kinase 2.
DOMAIN 1520 1590 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DNA_BIND 1195 1273 HMG box.
REGION 517 976 Histone acetyltransferase (HAT).
REGION 1342 1629 Interaction with ASF1A and ASF1B.
{ECO:0000269|PubMed:12842904}.
MOTIF 1351 1358 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 157 165 Pro-rich.
COMPBIAS 1627 1872 Asp/Glu-rich (acidic tail).
MOD_RES 137 137 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:8625415}.
MOD_RES 307 307 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:8625415}.
MOD_RES 544 544 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q80UV9}.
MOD_RES 1669 1669 Phosphoserine.
{ECO:0000250|UniProtKB:Q80UV9}.
MOD_RES 1672 1672 Phosphoserine.
{ECO:0000250|UniProtKB:Q80UV9}.
MOD_RES 1778 1778 Phosphoserine.
{ECO:0000250|UniProtKB:Q80UV9}.
MOD_RES 1781 1781 Phosphoserine.
{ECO:0000250|UniProtKB:Q80UV9}.
MOD_RES 1799 1799 Phosphoserine.
{ECO:0000250|UniProtKB:Q80UV9}.
MOD_RES 1826 1826 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
CROSSLNK 549 549 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 562 562 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 177 177 G -> GVSENGEGIILPSIIAPSSLAS (in isoform 2
and isoform N-TAF1).
{ECO:0000303|PubMed:17273961}.
/FTId=VSP_012362.
VAR_SEQ 1525 1540 SWPFHHPVNKKFVPDY -> VSCLCAKYFLAISSPS (in
isoform 2i).
{ECO:0000303|PubMed:17952504}.
/FTId=VSP_053376.
VAR_SEQ 1525 1528 SWPF -> IITK (in isoform 2h).
{ECO:0000303|PubMed:17952504}.
/FTId=VSP_053375.
VAR_SEQ 1529 1872 Missing (in isoform 2h).
{ECO:0000303|PubMed:17952504}.
/FTId=VSP_053377.
VAR_SEQ 1541 1872 Missing (in isoform 2i).
{ECO:0000303|PubMed:17952504}.
/FTId=VSP_053378.
VAR_SEQ 1585 1592 PESQYTKT -> YMCTTCRT (in isoform 2e).
{ECO:0000303|PubMed:12928496,
ECO:0000303|PubMed:17952504}.
/FTId=VSP_053379.
VAR_SEQ 1593 1872 Missing (in isoform 2e).
{ECO:0000303|PubMed:12928496,
ECO:0000303|PubMed:17952504}.
/FTId=VSP_053380.
VAR_SEQ 1645 1645 Q -> QAK (in isoform 2d, isoform 2g and
isoform N-TAF1).
{ECO:0000303|PubMed:12928496,
ECO:0000303|PubMed:17273961,
ECO:0000303|PubMed:17952504}.
/FTId=VSP_053381.
VAR_SEQ 1684 1686 Missing (in isoform 3).
{ECO:0000303|PubMed:12928496}.
/FTId=VSP_053382.
VAR_SEQ 1687 1687 Q -> QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
(in isoform 2g, isoform 2a, isoform 3 and
isoform 4). {ECO:0000303|PubMed:12928496,
ECO:0000303|PubMed:17952504,
ECO:0000303|Ref.7}.
/FTId=VSP_053383.
VAR_SEQ 1799 1872 SYGSYEEPDPKSNTQDTSFSSIGGYEVSEEEEDEEEEEQRS
GPSVLSQVHLSEDEEDSEDFHSIAGDSDLDSDE -> RYQ
(in isoform 2g, isoform 2a, isoform 2c,
isoform 2d and isoform 3).
{ECO:0000303|PubMed:12928496,
ECO:0000303|PubMed:17952504}.
/FTId=VSP_053384.
VARIANT 269 269 L -> V (in dbSNP:rs28382158).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.5}.
/FTId=VAR_020678.
VARIANT 297 297 A -> G (in dbSNP:rs35317750).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041930.
VARIANT 453 453 G -> D (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041931.
VARIANT 472 472 N -> D (found in a patient with X-linked
intellectual disability; unknown
pathological significance;
dbSNP:rs200177996).
{ECO:0000269|PubMed:25644381}.
/FTId=VAR_077838.
VARIANT 575 575 P -> S (in MRXS33; dbSNP:rs864321630).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076394.
VARIANT 651 651 E -> K (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041932.
VARIANT 691 691 M -> I (in a lung bronchoalveolar
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041933.
VARIANT 786 786 C -> R (in MRXS33; dbSNP:rs864321628).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076395.
VARIANT 955 955 D -> H (in MRXS33; dbSNP:rs864321631).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076396.
VARIANT 1169 1169 R -> C (found in a patient with X-linked
intellectual disability; unknown
pathological significance).
{ECO:0000269|PubMed:25644381}.
/FTId=VAR_077839.
VARIANT 1225 1225 R -> W (in MRXS33; dbSNP:rs864321629).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076397.
VARIANT 1316 1316 I -> T (in MRXS33; dbSNP:rs864321627).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076398.
VARIANT 1383 1383 V -> I (in dbSNP:rs7050748).
/FTId=VAR_048433.
VARIANT 1431 1431 R -> H (in MRXS33; unknown pathological
significance).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076399.
VARIANT 1496 1496 N -> H (in MRXS33; unknown pathological
significance).
{ECO:0000269|PubMed:26637982}.
/FTId=VAR_076400.
MUTAGEN 137 137 S->A: No decrease in kinase activity.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 145 145 D->A: Reduces kinase activity; when
associated with A-147; A-149; A-150; A-
152 and A-154.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 147 147 D->A: Reduces kinase activity; when
associated with A-145; A-149; A-150; A-
152 and A-154.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 149 149 E->A: Reduces kinase activity; when
associated with A-145; A-147; A-150; A-
152 and A-154.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 150 150 D->A: Reduces kinase activity; when
associated with A-145; A-147; A-149; A-
152 and A-154.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 152 152 D->A: Reduces kinase activity; when
associated with A-145; A-147; A-149; A-
150 and A-154.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 154 154 K->A: Reduces kinase activity; when
associated with A-145; A-147; A-149; A-
150 and A-152.
{ECO:0000269|PubMed:9660973}.
MUTAGEN 305 305 C->A: Reduces kinase activity; when
associated with A-307; A-308; A-309 and
A-310. {ECO:0000269|PubMed:9660973}.
MUTAGEN 307 307 S->A: Reduces kinase activity; when
associated with A-305; A-308; A-309 and
A-310. {ECO:0000269|PubMed:9660973}.
MUTAGEN 308 308 D->A: Reduces kinase activity; when
associated with A-305; A-307; A-309 and
A-310. {ECO:0000269|PubMed:9660973}.
MUTAGEN 309 309 D->A: Reduces kinase activity; when
associated with A-305; A-307; A-308 and
A-310. {ECO:0000269|PubMed:9660973}.
MUTAGEN 310 310 E->A: Reduces kinase activity; when
associated with A-305; A-307; A-308 and
A-309. {ECO:0000269|PubMed:9660973}.
MUTAGEN 721 721 E->Q: 25% decrease in histone
acetylation.
{ECO:0000269|PubMed:15870300}.
MUTAGEN 827 829 Missing: Dramatic decrease in histone
acetylation.
{ECO:0000269|PubMed:15870300}.
HELIX 593 596 {ECO:0000244|PDB:4RGW}.
TURN 600 602 {ECO:0000244|PDB:4RGW}.
HELIX 609 613 {ECO:0000244|PDB:4RGW}.
TURN 614 616 {ECO:0000244|PDB:4RGW}.
STRAND 624 626 {ECO:0000244|PDB:4RGW}.
HELIX 627 629 {ECO:0000244|PDB:4RGW}.
STRAND 630 632 {ECO:0000244|PDB:4RGW}.
STRAND 634 638 {ECO:0000244|PDB:4RGW}.
HELIX 640 655 {ECO:0000244|PDB:4RGW}.
TURN 656 658 {ECO:0000244|PDB:4RGW}.
HELIX 668 671 {ECO:0000244|PDB:4RGW}.
STRAND 675 685 {ECO:0000244|PDB:4RGW}.
STRAND 697 704 {ECO:0000244|PDB:4RGW}.
STRAND 708 710 {ECO:0000244|PDB:4RGW}.
STRAND 718 724 {ECO:0000244|PDB:4RGW}.
STRAND 729 732 {ECO:0000244|PDB:4RGW}.
STRAND 739 756 {ECO:0000244|PDB:4RGW}.
STRAND 761 767 {ECO:0000244|PDB:4RGW}.
STRAND 770 774 {ECO:0000244|PDB:4RGW}.
STRAND 778 782 {ECO:0000244|PDB:4RGW}.
HELIX 797 817 {ECO:0000244|PDB:4RGW}.
STRAND 820 822 {ECO:0000244|PDB:4RGW}.
STRAND 824 826 {ECO:0000244|PDB:4RGW}.
HELIX 827 833 {ECO:0000244|PDB:4RGW}.
HELIX 839 847 {ECO:0000244|PDB:4RGW}.
STRAND 850 853 {ECO:0000244|PDB:4RGW}.
STRAND 856 858 {ECO:0000244|PDB:4RGW}.
STRAND 861 864 {ECO:0000244|PDB:4RGW}.
HELIX 873 879 {ECO:0000244|PDB:4RGW}.
HELIX 882 900 {ECO:0000244|PDB:4RGW}.
HELIX 905 907 {ECO:0000244|PDB:4RGW}.
HELIX 925 928 {ECO:0000244|PDB:4RGW}.
HELIX 931 942 {ECO:0000244|PDB:4RGW}.
STRAND 947 952 {ECO:0000244|PDB:4RGW}.
STRAND 958 962 {ECO:0000244|PDB:4RGW}.
STRAND 964 968 {ECO:0000244|PDB:4RGW}.
HELIX 1055 1078 {ECO:0000244|PDB:4RGW}.
HELIX 1381 1397 {ECO:0000244|PDB:3UV5}.
HELIX 1403 1405 {ECO:0000244|PDB:3UV5}.
STRAND 1406 1408 {ECO:0000244|PDB:3AAD}.
TURN 1411 1413 {ECO:0000244|PDB:3UV5}.
HELIX 1417 1420 {ECO:0000244|PDB:3UV5}.
HELIX 1427 1435 {ECO:0000244|PDB:3UV5}.
HELIX 1442 1460 {ECO:0000244|PDB:3UV5}.
STRAND 1462 1464 {ECO:0000244|PDB:3AAD}.
HELIX 1465 1483 {ECO:0000244|PDB:3UV5}.
HELIX 1485 1495 {ECO:0000244|PDB:3UV5}.
TURN 1497 1500 {ECO:0000244|PDB:3UV5}.
HELIX 1502 1517 {ECO:0000244|PDB:5I29}.
TURN 1518 1521 {ECO:0000244|PDB:5I29}.
HELIX 1526 1528 {ECO:0000244|PDB:5I29}.
TURN 1534 1536 {ECO:0000244|PDB:5I29}.
HELIX 1540 1543 {ECO:0000244|PDB:5I29}.
HELIX 1550 1558 {ECO:0000244|PDB:5I29}.
HELIX 1565 1583 {ECO:0000244|PDB:5I29}.
HELIX 1588 1606 {ECO:0000244|PDB:5I29}.
HELIX 1608 1634 {ECO:0000244|PDB:5I29}.
SEQUENCE 1872 AA; 212677 MW; 93BE3D181A72ABEB CRC64;
MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD
ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVDY SDINEVAEDE
SRRYQQTMGS LQPLCHSDYD EDDYDADCED IDCKLMPPPP PPPGPMKKDK DQDSITGEKV
DFSSSSDSES EMGPQEATQA ESEDGKLTLP LAGIMQHDAT KLLPSVTELF PEFRPGKVLR
FLRLFGPGKN VPSVWRSARR KRKKKHRELI QEEQIQEVEC SVESEVSQKS LWNYDYAPPP
PPEQCLSDDE ITMMAPVESK FSQSTGDIDK VTDTKPRVAE WRYGPARLWY DMLGVPEDGS
GFDYGFKLRK TEHEPVIKSR MIEEFRKLEE NNGTDLLADE NFLMVTQLHW EDDIIWDGED
VKHKGTKPQR ASLAGWLPSS MTRNAMAYNV QQGFAATLDD DKPWYSIFPI DNEDLVYGRW
EDNIIWDAQA MPRLLEPPVL TLDPNDENLI LEIPDEKEEA TSNSPSKESK KESSLKKSRI
LLGKTGVIKE EPQQNMSQPE VKDPWNLSND EYYYPKQQGL RGTFGGNIIQ HSIPAVELRQ
PFFPTHMGPI KLRQFHRPPL KKYSFGALSQ PGPHSVQPLL KHIKKKAKMR EQERQASGGG
EMFFMRTPQD LTGKDGDLIL AEYSEENGPL MMQVGMATKI KNYYKRKPGK DPGAPDCKYG
ETVYCHTSPF LGSLHPGQLL QAFENNLFRA PIYLHKMPET DFLIIRTRQG YYIRELVDIF
VVGQQCPLFE VPGPNSKRAN THIRDFLQVF IYRLFWKSKD RPRRIRMEDI KKAFPSHSES
SIRKRLKLCA DFKRTGMDSN WWVLKSDFRL PTEEEIRAMV SPEQCCAYYS MIAAEQRLKD
AGYGEKSFFA PEEENEEDFQ MKIDDEVRTA PWNTTRAFIA AMKGKCLLEV TGVADPTGCG
EGFSYVKIPN KPTQQKDDKE PQPVKKTVTG TDADLRRLSL KNAKQLLRKF GVPEEEIKKL
SRWEVIDVVR TMSTEQARSG EGPMSKFARG SRFSVAEHQE RYKEECQRIF DLQNKVLSST
EVLSTDTDSS SAEDSDFEEM GKNIENMLQN KKTSSQLSRE REEQERKELQ RMLLAAGSAA
SGNNHRDDDT ASVTSLNSSA TGRCLKIYRT FRDEEGKEYV RCETVRKPAV IDAYVRIRTT
KDEEFIRKFA LFDEQHREEM RKERRRIQEQ LRRLKRNQEK EKLKGPPEKK PKKMKERPDL
KLKCGACGAI GHMRTNKFCP LYYQTNAPPS NPVAMTEEQE EELEKTVIHN DNEELIKVEG
TKIVLGKQLI ESADEVRRKS LVLKFPKQQL PPKKKRRVGT TVHCDYLNRP HKSIHRRRTD
PMVTLSSILE SIINDMRDLP NTYPFHTPVN AKVVKDYYKI ITRPMDLQTL RENVRKRLYP
SREEFREHLE LIVKNSATYN GPKHSLTQIS QSMLDLCDEK LKEKEDKLAR LEKAINPLLD
DDDQVAFSFI LDNIVTQKMM AVPDSWPFHH PVNKKFVPDY YKVIVNPMDL ETIRKNISKH
KYQSRESFLD DVNLILANSV KYNGPESQYT KTAQEIVNVC YQTLTEYDEH LTQLEKDICT
AKEAALEEAE LESLDPMTPG PYTPQPPDLY DTNTSLSMSR DASVFQDESN MSVLDIPSAT
PEKQVTQEGE DGDGDLADEE EGTVQQPQAS VLYEDLLMSE GEDDEEDAGS DEEGDNPFSA
IQLSESGSDS DVGSGGIRPK QPRMLQENTR MDMENEESMM SYEGDGGEAS HGLEDSNISY
GSYEEPDPKS NTQDTSFSSI GGYEVSEEEE DEEEEEQRSG PSVLSQVHLS EDEEDSEDFH
SIAGDSDLDS DE


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