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Bcl-2-associated transcription factor 1 (Btf) (BCLAF1 and THRAP3 family member 1)

 BCLF1_HUMAN             Reviewed;         920 AA.
Q9NYF8; A2RU75; B7ZM58; E1P586; Q14673; Q86WU6; Q86WY0;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 2.
12-SEP-2018, entry version 166.
RecName: Full=Bcl-2-associated transcription factor 1;
Short=Btf;
AltName: Full=BCLAF1 and THRAP3 family member 1;
Name=BCLAF1; Synonyms=BTF, KIAA0164;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
PubMed=10330179; DOI=10.1128/MCB.19.6.4390;
Kasof G.M., Goyal L., White E.;
"Btf, a novel death-promoting transcriptional repressor that interacts
with Bcl-2-related proteins.";
Mol. Cell. Biol. 19:4390-4404(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-676 (ISOFORM 4).
TISSUE=Brain, Pancreas, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
PROTEIN SEQUENCE OF 168-182; 189-204; 256-271; 284-298; 304-312;
319-332; 394-409; 422-439; 461-475; 505-517; 525-534; 537-548;
551-581; 587-593; 623-631; 654-664; 785-796; 832-842 AND 846-852,
PHOSPHORYLATION AT SER-177; SER-268; SER-290; SER-512; SER-531 AND
SER-658, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (APR-2008) to UniProtKB.
[7]
INTERACTION WITH EMD.
PubMed=15009215; DOI=10.1111/j.1432-1033.2004.04007.x;
Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N.,
Mori C., Wilson K.L., Hiraoka Y.;
"Emerin binding to Btf, a death-promoting transcriptional repressor,
is disrupted by a missense mutation that causes Emery-Dreifuss
muscular dystrophy.";
Eur. J. Biochem. 271:1035-1045(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-389; SER-397;
THR-402; SER-531 AND SER-648, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[11]
FUNCTION, AND IDENTIFICATION IN THE SNARP COMPLEX.
PubMed=18794151; DOI=10.1158/0008-5472.CAN-08-1217;
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M.,
Perkins N.D.;
"Regulation of cyclin D1 RNA stability by SNIP1.";
Cancer Res. 68:7621-7628(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-222; SER-264;
SER-268; TYR-284; SER-290; THR-341; SER-385; SER-389; SER-397;
THR-402; SER-512; SER-531; SER-578 AND SER-658, AND 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-397, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-222; SER-290;
SER-385; SER-397; THR-402 AND SER-512, 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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152 AND LYS-437, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-104; SER-177;
SER-196; SER-198; SER-222; SER-268; SER-290; SER-297; SER-385;
SER-397; THR-402; SER-472; SER-496; SER-502; SER-512; SER-531;
THR-566; SER-578; SER-658 AND SER-690, 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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-196; SER-198;
SER-222; SER-268; SER-285; SER-290; SER-385; SER-397; THR-494;
SER-496; SER-512; SER-531; SER-658; SER-660 AND SER-760, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=24100041; DOI=10.1074/jbc.M113.500397;
Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T.,
Hamakubo T.;
"Identification of Wilms' tumor 1-associating protein complex and its
role in alternative splicing and the cell cycle.";
J. Biol. Chem. 288:33292-33302(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-196; SER-198;
SER-222; SER-259; SER-262; SER-264; SER-268; SER-285; SER-290;
SER-300; SER-315; THR-341; THR-355; TYR-383; SER-385; SER-397;
THR-402; SER-422; SER-427; THR-431; SER-450; SER-472; SER-496;
SER-512; SER-525; SER-531; SER-559; SER-564; SER-578; SER-658;
SER-660; THR-661 AND SER-690, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; TYR-219; SER-222;
SER-259; SER-264; SER-285; SER-290; SER-385; SER-389; SER-397; SER-648
AND SER-658, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339
(ISOFORM 4), 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).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-809, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-332; LYS-413; LYS-437;
LYS-462; LYS-491; LYS-501; LYS-548; LYS-550; LYS-580; LYS-676; LYS-778
AND LYS-831, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-580 AND LYS-831, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-491; LYS-580; LYS-676 AND
LYS-831, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-421; LYS-437; LYS-457;
LYS-501; LYS-536; LYS-548; LYS-550; LYS-580 AND LYS-676, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-188; LYS-332; LYS-413;
LYS-421; LYS-437; LYS-457; LYS-462; LYS-491; LYS-492; LYS-501;
LYS-536; LYS-548; LYS-550; LYS-567; LYS-580; LYS-593; LYS-599;
LYS-622; LYS-676; LYS-778; LYS-784; LYS-831 AND LYS-911, 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).
-!- FUNCTION: Death-promoting transcriptional repressor. May be
involved in cyclin-D1/CCND1 mRNA stability through the SNARP
complex which associates with both the 3'end of the CCND1 gene and
its mRNA. {ECO:0000269|PubMed:18794151}.
-!- SUBUNIT: Interacts with Bcl-2 related proteins, EMD, with the
adenovirus E1B 19 kDa protein and with DNA. Component of the SNARP
complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and
PNN. Component of a MACOM-like complex, named WTAP complex,
composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and
THRAP3. {ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:18794151,
ECO:0000269|PubMed:24100041}.
-!- INTERACTION:
P10415:BCL2; NbExp=2; IntAct=EBI-437804, EBI-77694;
P50402:EMD; NbExp=3; IntAct=EBI-437804, EBI-489887;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus speckle
{ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:24100041}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9NYF8-1; Sequence=Displayed;
Name=2; Synonyms=Btf-l;
IsoId=Q9NYF8-2; Sequence=VSP_010369;
Name=3; Synonyms=Btf-s, BP-1;
IsoId=Q9NYF8-3; Sequence=VSP_010369, VSP_010370;
Name=4;
IsoId=Q9NYF8-4; Sequence=VSP_010371;
Note=Contains a phosphoserine at position 339.
{ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH47687.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH47887.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH56894.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH63846.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA11481.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCLAF1ID43164ch6q23.html";
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EMBL; AF249273; AAF64304.1; -; mRNA.
EMBL; D79986; BAA11481.2; ALT_INIT; mRNA.
EMBL; AL121713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47950.1; -; Genomic_DNA.
EMBL; CH471051; EAW47951.1; -; Genomic_DNA.
EMBL; BC047687; AAH47687.1; ALT_SEQ; mRNA.
EMBL; BC047887; AAH47887.1; ALT_SEQ; mRNA.
EMBL; BC056894; AAH56894.1; ALT_SEQ; mRNA.
EMBL; BC063846; AAH63846.1; ALT_SEQ; mRNA.
EMBL; BC132780; AAI32781.1; -; mRNA.
EMBL; BC144281; AAI44282.1; -; mRNA.
CCDS; CCDS47485.1; -. [Q9NYF8-4]
CCDS; CCDS47486.1; -. [Q9NYF8-3]
CCDS; CCDS5177.1; -. [Q9NYF8-1]
CCDS; CCDS75525.1; -. [Q9NYF8-2]
RefSeq; NP_001070908.1; NM_001077440.1. [Q9NYF8-3]
RefSeq; NP_001070909.1; NM_001077441.1. [Q9NYF8-4]
RefSeq; NP_001287967.1; NM_001301038.1. [Q9NYF8-2]
RefSeq; NP_055554.1; NM_014739.2. [Q9NYF8-1]
UniGene; Hs.486542; -.
ProteinModelPortal; Q9NYF8; -.
BioGrid; 115118; 120.
IntAct; Q9NYF8; 75.
MINT; Q9NYF8; -.
STRING; 9606.ENSP00000435210; -.
iPTMnet; Q9NYF8; -.
PhosphoSitePlus; Q9NYF8; -.
SwissPalm; Q9NYF8; -.
BioMuta; BCLAF1; -.
DMDM; 47605556; -.
EPD; Q9NYF8; -.
MaxQB; Q9NYF8; -.
PaxDb; Q9NYF8; -.
PeptideAtlas; Q9NYF8; -.
PRIDE; Q9NYF8; -.
ProteomicsDB; 83221; -.
ProteomicsDB; 83222; -. [Q9NYF8-2]
ProteomicsDB; 83223; -. [Q9NYF8-3]
ProteomicsDB; 83224; -. [Q9NYF8-4]
Ensembl; ENST00000353331; ENSP00000229446; ENSG00000029363. [Q9NYF8-3]
Ensembl; ENST00000392348; ENSP00000376159; ENSG00000029363. [Q9NYF8-3]
Ensembl; ENST00000527759; ENSP00000434826; ENSG00000029363. [Q9NYF8-2]
Ensembl; ENST00000530767; ENSP00000436501; ENSG00000029363. [Q9NYF8-4]
Ensembl; ENST00000531224; ENSP00000435210; ENSG00000029363. [Q9NYF8-1]
GeneID; 9774; -.
KEGG; hsa:9774; -.
UCSC; uc003qgw.2; human. [Q9NYF8-1]
CTD; 9774; -.
DisGeNET; 9774; -.
EuPathDB; HostDB:ENSG00000029363.15; -.
GeneCards; BCLAF1; -.
HGNC; HGNC:16863; BCLAF1.
HPA; HPA006484; -.
HPA; HPA006669; -.
HPA; HPA027770; -.
MIM; 612588; gene.
neXtProt; NX_Q9NYF8; -.
OpenTargets; ENSG00000029363; -.
PharmGKB; PA134868035; -.
eggNOG; ENOG410IJCD; Eukaryota.
eggNOG; ENOG4110X68; LUCA.
GeneTree; ENSGT00530000063211; -.
HOVERGEN; HBG050681; -.
InParanoid; Q9NYF8; -.
KO; K13087; -.
OMA; TSHRNTE; -.
OrthoDB; EOG091G03HU; -.
PhylomeDB; Q9NYF8; -.
TreeFam; TF335939; -.
ChiTaRS; BCLAF1; human.
GeneWiki; BCLAF1; -.
GenomeRNAi; 9774; -.
PRO; PR:Q9NYF8; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000029363; Expressed in 242 organ(s), highest expression level in substantia nigra.
CleanEx; HS_BCLAF1; -.
ExpressionAtlas; Q9NYF8; baseline and differential.
Genevisible; Q9NYF8; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026668; Bcl-2_assoc_TF1.
InterPro; IPR029199; THRAP3_BCLAF1.
PANTHER; PTHR15268; PTHR15268; 1.
PANTHER; PTHR15268:SF4; PTHR15268:SF4; 1.
Pfam; PF15440; THRAP3_BCLAF1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Citrullination; Complete proteome;
Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 920 Bcl-2-associated transcription factor 1.
/FTId=PRO_0000064888.
COMPBIAS 141 148 Poly-Ser.
COMPBIAS 749 763 Poly-Ser.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.6}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.6}.
MOD_RES 284 284 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.6}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 332 332 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K019}.
MOD_RES 341 341 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 402 402 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 421 421 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K019}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 431 431 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 475 475 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K019}.
MOD_RES 494 494 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.6}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.6}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 564 564 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 566 566 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 578 578 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 648 648 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:24275569}.
MOD_RES 658 658 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.6}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 661 661 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 760 760 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 803 803 Citrulline. {ECO:0000250}.
MOD_RES 809 809 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 188 188 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 413 413 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 421 421 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 437 437 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 457 457 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 491 491 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 492 492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 501 501 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 548 548 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 550 550 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 567 567 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 580 580 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 580 580 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 593 593 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 599 599 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 622 622 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 778 778 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 784 784 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 831 831 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 831 831 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 911 911 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 35 36 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10330179,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010369.
VAR_SEQ 339 511 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010371.
VAR_SEQ 800 848 Missing (in isoform 3).
{ECO:0000303|PubMed:10330179}.
/FTId=VSP_010370.
VARIANT 66 66 G -> A (in dbSNP:rs9942517).
/FTId=VAR_059591.
VARIANT 209 209 S -> C (in dbSNP:rs6940018).
/FTId=VAR_050692.
VARIANT 459 459 Y -> D (in dbSNP:rs1967446).
/FTId=VAR_050693.
VARIANT 461 461 L -> H (in dbSNP:rs1967445).
/FTId=VAR_050694.
VARIANT 629 629 N -> S (in dbSNP:rs7381749).
/FTId=VAR_050695.
VARIANT 875 875 R -> C (in dbSNP:rs34541670).
/FTId=VAR_050696.
CONFLICT 4 4 S -> A (in Ref. 1; AAF64304).
{ECO:0000305}.
SEQUENCE 920 AA; 106122 MW; 8892B98E54F52C20 CRC64;
MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD RMYSRDYRRD
YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR HSRSPRRGRS RSRSPKRRSV
SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY SKSPVSKRRG SQEKQTKKAE GEPQEESPLK
SKSQEEPKDT FEHDPSESID EFNKSSATSG DIWPGLSAYD NSPRSPHSPS PIATPPSQSS
SCSDAPMLST VHSAKNTPSQ HSHSIQHSPE RSGSGSVGNG SSRYSPSQNS PIHHIPSRRS
PAKTIAPQNA PRDESRGRSS FYPDGGDQET AKTGKFLKRF TDEESRVFLL DRGNTRDKEA
SKEKGSEKGR AEGEWEDQEA LDYFSDKESG KQKFNDSEGD DTEETEDYRQ FRKSVLADQG
KSFATASHRN TEEEGLKYKS KVSLKGNRES DGFREEKNYK LKETGYVVER PSTTKDKHKE
EDKNSERITV KKETQSPEQV KSEKLKDLFD YSPPLHKNLD AREKSTFREE SPLRIKMIAS
DSHRPEVKLK MAPVPLDDSN RPASLTKDRL LASTLVHSVK KEQEFRSIFD HIKLPQASKS
TSESFIQHIV SLVHHVKEQY FKSAAMTLNE RFTSYQKATE EHSTRQKSPE IHRRIDISPS
TLRKHTRLAG EERVFKEENQ KGDKKLRCDS ADLRHDIDRR RKERSKERGD SKGSRESSGS
RKQEKTPKDY KEYKSYKDDS KHKREQDHSR SSSSSASPSS PSSREEKESK KEREEEFKTH
HEMKEYSGFA GVSRPRGTFF RIRGRGRARG VFAGTNTGPN NSNTTFQKRP KEEEWDPEYT
PKSKKYFLHD DRDDGVDYWA KRGRGRGTFQ RGRGRFNFKK SGSSPKWTHD KYQGDGIVED
EEETMENNEE KKDRRKEEKE


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