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Methyl-CpG-binding domain protein 1 (CXXC-type zinc finger protein 3) (Methyl-CpG-binding protein MBD1) (Protein containing methyl-CpG-binding domain 1)

 MBD1_HUMAN              Reviewed;         605 AA.
Q9UIS9; A4UTZ0; B4DXJ5; E9PEC5; K7ELI2; K7EQZ4; K7ESN0; O15248;
O95241; Q7Z7B5; Q8N4W4; Q9UNZ6; Q9UNZ7; Q9UNZ8; Q9UNZ9;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
22-NOV-2017, entry version 168.
RecName: Full=Methyl-CpG-binding domain protein 1;
AltName: Full=CXXC-type zinc finger protein 3;
AltName: Full=Methyl-CpG-binding protein MBD1;
AltName: Full=Protein containing methyl-CpG-binding domain 1;
Name=MBD1; Synonyms=CXXC3, PCM1;
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 5), FUNCTION, INTERACTION WITH THE
MECP1 COMPLEX, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9207790; DOI=10.1038/ng0797-256;
Cross S.H., Meehan R.R., Nan X., Bird A.;
"A component of the transcriptional repressor MeCP1 shares a motif
with DNA methyltransferase and HRX proteins.";
Nat. Genet. 16:256-259(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-401.
PubMed=10441743; DOI=10.1007/s003359901112;
Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
"Genomic structure and chromosomal mapping of the murine and human
mbd1, mbd2, mbd3, and mbd4 genes.";
Mamm. Genome 10:906-912(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 7), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Fibroblast;
PubMed=10454587; DOI=10.1128/MCB.19.9.6415;
Fujita N., Takebayashi S., Okumura K., Kudo S., Chiba T., Saya H.,
Nakao M.;
"Methylation-mediated transcriptional silencing in euchromatin by
methyl-CpG binding protein MBD1 isoforms.";
Mol. Cell. Biol. 19:6415-6426(1999).
[4]
NUCLEOTIDE SEQUENCE (ISOFORM 6), INDUCTION BY INTERFERON, AND
INTERACTION WITH OASL.
TISSUE=Leukocyte;
PubMed=14728690; DOI=10.1046/j.1432-1033.2003.03966.x;
Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.;
"Interaction between the 2'-5' oligoadenylate synthetase-like protein
p59 OASL and the transcriptional repressor methyl CpG-binding protein
1.";
Eur. J. Biochem. 271:628-636(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
TISSUE=Cervix carcinoma;
Laget S.M., Xu S.-Y.;
"New splice variant of the methyl-CpG binding protein 1 (MBD1).";
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Prostate;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 169-220, AND FUNCTION.
PubMed=9774669; DOI=10.1128/MCB.18.11.6538;
Hendrich B., Bird A.;
"Identification and characterization of a family of mammalian methyl-
CpG binding proteins.";
Mol. Cell. Biol. 18:6538-6547(1998).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10648624; DOI=10.1128/MCB.20.4.1394-1406.2000;
Ng H.-H., Jeppesen P., Bird A.;
"Active repression of methylated genes by the chromosomal protein
MBD1.";
Mol. Cell. Biol. 20:1394-1406(2000).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE SUV39H1-CBX5
COMPLEX.
PubMed=12711603; DOI=10.1074/jbc.M302283200;
Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y.,
Tachibana M., Chiba T., Nakao M.;
"Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1
heterochromatic complex for DNA methylation-based transcriptional
repression.";
J. Biol. Chem. 278:24132-24138(2003).
[12]
FUNCTION, AND INTERACTION WITH AFT7IP.
PubMed=12665582; DOI=10.1128/MCB.23.8.2834-2843.2003;
Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H.,
Nakao M.;
"MCAF mediates MBD1-dependent transcriptional repression.";
Mol. Cell. Biol. 23:2834-2843(2003).
[13]
FUNCTION, AND INTERACTION WITH CHAF1A.
PubMed=12697822; DOI=10.1128/MCB.23.9.3226-3236.2003;
Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.;
"The methyl-CpG binding protein MBD1 interacts with the p150 subunit
of chromatin assembly factor 1.";
Mol. Cell. Biol. 23:3226-3236(2003).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14610093; DOI=10.1074/jbc.M309393200;
Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M.,
Frankel W., Jacob S.T.;
"Role of human ribosomal RNA (rRNA) promoter methylation and of
methyl-CpG-binding protein MBD2 in the suppression of rRNA gene
expression.";
J. Biol. Chem. 279:6783-6793(2004).
[15]
FUNCTION, AND INTERACTION WITH SETDB1 AND CHAF1A.
PubMed=15327775; DOI=10.1016/j.molcel.2004.06.043;
Sarraf S.A., Stancheva I.;
"Methyl-CpG binding protein MBD1 couples histone H3 methylation at
lysine 9 by SETDB1 to DNA replication and chromatin assembly.";
Mol. Cell 15:595-605(2004).
[16]
INTERACTION WITH AFT7IP AND AFT7IP2, AND MUTAGENESIS OF ILE-576.
PubMed=15691849; DOI=10.1074/jbc.M413654200;
Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.;
"Transcriptional repression and heterochromatin formation by MBD1 and
MCAF/AM family proteins.";
J. Biol. Chem. 280:13928-13935(2005).
[17]
INTERACTION WITH SETDB1, PHOSPHORYLATION, SUMOYLATION AT LYS-499 AND
LYS-538, AND MUTAGENESIS OF LYS-499; GLU-501; LYS-538 AND GLU-540.
PubMed=17066076; DOI=10.1038/sj.emboj.7601404;
Lyst M.J., Nan X., Stancheva I.;
"Regulation of MBD1-mediated transcriptional repression by SUMO and
PIAS proteins.";
EMBO J. 25:5317-5328(2006).
[18]
SUMOYLATION, AND INTERACTION WITH AFT7IP.
PubMed=16757475; DOI=10.1074/jbc.M602280200;
Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S.,
Nakao M., Saitoh H.;
"Involvement of SUMO modification in MBD1- and MCAF1-mediated
heterochromatin formation.";
J. Biol. Chem. 281:23180-23190(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, 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).
[20]
INTERACTION WITH BAHD1.
PubMed=19666599; DOI=10.1073/pnas.0901259106;
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C.,
Feunteun J., Cossart P.;
"Human BAHD1 promotes heterochromatic gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, 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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, 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).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-538, 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-538, 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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277 AND LYS-422, 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).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-277; LYS-422;
LYS-440; LYS-499; LYS-538 AND LYS-558, 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).
[29]
STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, AND
MUTAGENESIS OF ARG-30; ASP-32; TYR-34; ARG-44; SER-45; TYR-52 AND
PHE-64.
PubMed=10581239; DOI=10.1093/emboj/18.23.6653;
Ohki I., Shimotake N., Fujita N., Nakao M., Shirakawa M.;
"Solution structure of the methyl-CpG-binding domain of the
methylation-dependent transcriptional repressor MBD1.";
EMBO J. 18:6653-6661(1999).
[30]
STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, FUNCTION,
SUBCELLULAR LOCATION, AND INTERACTION WITH MPG.
PubMed=14555760; DOI=10.1073/pnas.2131819100;
Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I.,
Shirakawa M., Kawasuji M., Nakao M.;
"Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link
transcriptional repression and DNA repair in chromatin.";
Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003).
-!- FUNCTION: Transcriptional repressor that binds CpG islands in
promoters where the DNA is methylated at position 5 of cytosine
within CpG dinucleotides. Binding is abolished by the presence of
7-mG that is produced by DNA damage by methylmethanesulfonate
(MMS). Acts as transcriptional repressor and plays a role in gene
silencing by recruiting AFT7IP, which in turn recruits factors
such as the histone methyltransferase SETDB1. Probably forms a
complex with SETDB1 and ATF7IP that represses transcription and
couples DNA methylation and histone 'Lys-9' trimethylation.
Isoform 1 and isoform 2 can also repress transcription from
unmethylated promoters. {ECO:0000269|PubMed:10454587,
ECO:0000269|PubMed:10648624, ECO:0000269|PubMed:12665582,
ECO:0000269|PubMed:12697822, ECO:0000269|PubMed:12711603,
ECO:0000269|PubMed:14555760, ECO:0000269|PubMed:14610093,
ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:9207790,
ECO:0000269|PubMed:9774669}.
-!- SUBUNIT: Interacts with the Ten-1 ICD form of TENM1 (By
similarity). Interacts with OASL, AFT7IP, AFT7IP2 and BAHD1. Binds
CHAF1A and the SUV39H1-CBX5 complex via the MBD domain. Binds MGP
via the TRD domain. May be part of the MeCP1 complex. During DNA
replication, it recruits SETDB1 to form a S phase-specific complex
that facilitates methylation of H3 'Lys-9' during replication-
coupled chromatin assembly and is at least composed of the CAF-1
subunit CHAF1A, MBD1 and SETDB1. {ECO:0000250,
ECO:0000269|PubMed:10581239, ECO:0000269|PubMed:12665582,
ECO:0000269|PubMed:12697822, ECO:0000269|PubMed:12711603,
ECO:0000269|PubMed:14555760, ECO:0000269|PubMed:14728690,
ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:15691849,
ECO:0000269|PubMed:16757475, ECO:0000269|PubMed:17066076,
ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:9207790}.
-!- INTERACTION:
P45973:CBX5; NbExp=6; IntAct=EBI-867196, EBI-78219;
Q13111:CHAF1A; NbExp=3; IntAct=EBI-867196, EBI-1020839;
Q13547:HDAC1; NbExp=2; IntAct=EBI-867196, EBI-301834;
Q92769:HDAC2; NbExp=2; IntAct=EBI-867196, EBI-301821;
O15379:HDAC3; NbExp=3; IntAct=EBI-867196, EBI-607682;
P42858:HTT; NbExp=2; IntAct=EBI-867196, EBI-466029;
O75925:PIAS1; NbExp=3; IntAct=EBI-867196, EBI-629434;
Q9Y6X2:PIAS3; NbExp=3; IntAct=EBI-867196, EBI-2803703;
Q15156:PML-RAR; NbExp=4; IntAct=EBI-867196, EBI-867256;
Q15047:SETDB1; NbExp=3; IntAct=EBI-867196, EBI-79691;
P63165:SUMO1; NbExp=3; IntAct=EBI-867196, EBI-80140;
O43463:SUV39H1; NbExp=5; IntAct=EBI-867196, EBI-349968;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus matrix
{ECO:0000250}. Nucleus speckle. Chromosome. Note=Colocalizes with
the Ten-1 ICD form of TENM1 in foci associated with the nuclear
matrix (By similarity). Nuclear, in a punctate pattern. Associated
with euchromatic regions of the chromosomes, with pericentromeric
regions on chromosome 1 and with telomeric regions from several
chromosomes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Name=1; Synonyms=MBD1v1;
IsoId=Q9UIS9-1; Sequence=Displayed;
Name=2; Synonyms=MBD1v2;
IsoId=Q9UIS9-2; Sequence=VSP_011065, VSP_011068, VSP_011070;
Name=4; Synonyms=MBD1v3;
IsoId=Q9UIS9-4; Sequence=VSP_011066, VSP_011068;
Name=5; Synonyms=PCM1;
IsoId=Q9UIS9-5; Sequence=VSP_011064;
Name=6; Synonyms=MBD1v6;
IsoId=Q9UIS9-6; Sequence=VSP_011068, VSP_011069, VSP_011071;
Name=7;
IsoId=Q9UIS9-7; Sequence=VSP_011066;
Note=Ref.3 (AAD51444) sequence is in conflict in position:
327:K->Q. {ECO:0000305};
Name=8;
IsoId=Q9UIS9-8; Sequence=VSP_011065, VSP_011068;
Name=9;
IsoId=Q9UIS9-9; Sequence=VSP_042812;
Name=10;
IsoId=Q9UIS9-10; Sequence=VSP_011064, VSP_054737, VSP_054738;
Note=No experimental confirmation available.;
Name=11;
IsoId=Q9UIS9-11; Sequence=VSP_054736, VSP_011068, VSP_054739;
Note=No experimental confirmation available.;
Name=12;
IsoId=Q9UIS9-12; Sequence=VSP_011070;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9207790}.
-!- INDUCTION: Up-regulated by interferon.
{ECO:0000269|PubMed:14728690}.
-!- DOMAIN: The methyl-CpG-binding domain (MBD) functions both in
binding to methylated DNA and in protein interactions.
-!- DOMAIN: The third CXXC-type zinc finger mediates binding to non-
methylated CpG dinucleotides.
-!- DOMAIN: The transcriptional repression domain (TRD) is involved in
transcription repression and in protein interactions.
-!- PTM: Sumoylated with SUMO1 by PIAS1 and PIAS3. Sumoylation affects
transcriptional silencing by preventing the interaction with
SETDB1. In contrast, sumoylation may increase interaction with
AFT7IP. {ECO:0000269|PubMed:16757475,
ECO:0000269|PubMed:17066076}.
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EMBL; Y10746; CAA71735.1; -; mRNA.
EMBL; AF120981; AAD50371.1; -; Genomic_DNA.
EMBL; AF120980; AAD50371.1; JOINED; Genomic_DNA.
EMBL; AF078830; AAD51442.1; -; mRNA.
EMBL; AF078831; AAD51443.1; -; mRNA.
EMBL; AF078832; AAD51444.1; -; mRNA.
EMBL; AF078833; AAD51445.1; -; mRNA.
EMBL; EF488685; ABP02056.1; -; mRNA.
EMBL; AK302004; BAG63407.1; -; mRNA.
EMBL; AC090246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033242; AAH33242.1; -; mRNA.
EMBL; AJ564845; CAD92308.1; -; mRNA.
EMBL; AF072241; AAC68870.1; -; mRNA.
CCDS; CCDS11941.1; -. [Q9UIS9-4]
CCDS; CCDS11942.1; -. [Q9UIS9-7]
CCDS; CCDS11943.1; -. [Q9UIS9-1]
CCDS; CCDS11944.1; -. [Q9UIS9-5]
CCDS; CCDS32832.1; -. [Q9UIS9-2]
CCDS; CCDS56071.1; -. [Q9UIS9-8]
CCDS; CCDS56072.1; -. [Q9UIS9-6]
CCDS; CCDS56073.1; -. [Q9UIS9-9]
CCDS; CCDS59318.1; -. [Q9UIS9-10]
CCDS; CCDS59319.1; -. [Q9UIS9-11]
CCDS; CCDS59320.1; -. [Q9UIS9-12]
RefSeq; NP_001191065.1; NM_001204136.1. [Q9UIS9-12]
RefSeq; NP_001191066.1; NM_001204137.1. [Q9UIS9-9]
RefSeq; NP_001191067.1; NM_001204138.1.
RefSeq; NP_001191068.1; NM_001204139.1. [Q9UIS9-1]
RefSeq; NP_001191069.1; NM_001204140.1.
RefSeq; NP_001191070.1; NM_001204141.1. [Q9UIS9-10]
RefSeq; NP_001191071.1; NM_001204142.1. [Q9UIS9-6]
RefSeq; NP_001191072.1; NM_001204143.1. [Q9UIS9-11]
RefSeq; NP_001191080.1; NM_001204151.2. [Q9UIS9-8]
RefSeq; NP_002375.1; NM_002384.2. [Q9UIS9-4]
RefSeq; NP_056669.2; NM_015844.2. [Q9UIS9-7]
RefSeq; NP_056670.2; NM_015845.3. [Q9UIS9-2]
RefSeq; NP_056671.2; NM_015846.3. [Q9UIS9-1]
RefSeq; NP_056723.2; NM_015847.3. [Q9UIS9-5]
RefSeq; XP_005258328.1; XM_005258271.2. [Q9UIS9-1]
RefSeq; XP_011524295.1; XM_011525993.2. [Q9UIS9-9]
RefSeq; XP_011524296.1; XM_011525994.2. [Q9UIS9-9]
RefSeq; XP_011524308.1; XM_011526006.1. [Q9UIS9-11]
RefSeq; XP_016881249.1; XM_017025760.1. [Q9UIS9-1]
RefSeq; XP_016881259.1; XM_017025770.1. [Q9UIS9-7]
RefSeq; XP_016881260.1; XM_017025771.1. [Q9UIS9-7]
RefSeq; XP_016881265.1; XM_017025776.1. [Q9UIS9-4]
UniGene; Hs.405610; -.
PDB; 1D9N; NMR; -; A=1-75.
PDB; 1IG4; NMR; -; A=1-75.
PDB; 4D4W; NMR; -; A=167-222.
PDBsum; 1D9N; -.
PDBsum; 1IG4; -.
PDBsum; 4D4W; -.
ProteinModelPortal; Q9UIS9; -.
SMR; Q9UIS9; -.
BioGrid; 110322; 30.
CORUM; Q9UIS9; -.
IntAct; Q9UIS9; 19.
MINT; MINT-2860643; -.
STRING; 9606.ENSP00000405268; -.
iPTMnet; Q9UIS9; -.
PhosphoSitePlus; Q9UIS9; -.
BioMuta; MBD1; -.
DMDM; 50401200; -.
EPD; Q9UIS9; -.
PaxDb; Q9UIS9; -.
PeptideAtlas; Q9UIS9; -.
PRIDE; Q9UIS9; -.
DNASU; 4152; -.
Ensembl; ENST00000269468; ENSP00000269468; ENSG00000141644. [Q9UIS9-1]
Ensembl; ENST00000269471; ENSP00000269471; ENSG00000141644. [Q9UIS9-2]
Ensembl; ENST00000339998; ENSP00000339546; ENSG00000141644. [Q9UIS9-6]
Ensembl; ENST00000347968; ENSP00000285102; ENSG00000141644. [Q9UIS9-7]
Ensembl; ENST00000353909; ENSP00000269469; ENSG00000141644. [Q9UIS9-5]
Ensembl; ENST00000382948; ENSP00000372407; ENSG00000141644. [Q9UIS9-1]
Ensembl; ENST00000398488; ENSP00000381502; ENSG00000141644. [Q9UIS9-4]
Ensembl; ENST00000398493; ENSP00000381506; ENSG00000141644. [Q9UIS9-7]
Ensembl; ENST00000457839; ENSP00000405268; ENSG00000141644. [Q9UIS9-9]
Ensembl; ENST00000585595; ENSP00000468430; ENSG00000141644. [Q9UIS9-9]
Ensembl; ENST00000585672; ENSP00000466092; ENSG00000141644. [Q9UIS9-10]
Ensembl; ENST00000587605; ENSP00000468042; ENSG00000141644. [Q9UIS9-11]
Ensembl; ENST00000588937; ENSP00000467763; ENSG00000141644. [Q9UIS9-2]
Ensembl; ENST00000590208; ENSP00000468785; ENSG00000141644. [Q9UIS9-12]
Ensembl; ENST00000591416; ENSP00000467017; ENSG00000141644. [Q9UIS9-1]
Ensembl; ENST00000591535; ENSP00000465923; ENSG00000141644. [Q9UIS9-8]
GeneID; 4152; -.
KEGG; hsa:4152; -.
UCSC; uc002leg.4; human. [Q9UIS9-1]
CTD; 4152; -.
DisGeNET; 4152; -.
EuPathDB; HostDB:ENSG00000141644.17; -.
GeneCards; MBD1; -.
HGNC; HGNC:6916; MBD1.
HPA; CAB009017; -.
HPA; CAB036003; -.
MIM; 156535; gene.
neXtProt; NX_Q9UIS9; -.
OpenTargets; ENSG00000141644; -.
PharmGKB; PA30659; -.
eggNOG; ENOG410IIBG; Eukaryota.
eggNOG; ENOG4111S3X; LUCA.
GeneTree; ENSGT00730000111257; -.
HOVERGEN; HBG052416; -.
InParanoid; Q9UIS9; -.
KO; K11589; -.
OMA; CQTREDC; -.
OrthoDB; EOG091G0I05; -.
PhylomeDB; Q9UIS9; -.
SIGNOR; Q9UIS9; -.
ChiTaRS; MBD1; human.
EvolutionaryTrace; Q9UIS9; -.
GeneWiki; MBD1; -.
GenomeRNAi; 4152; -.
PRO; PR:Q9UIS9; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141644; -.
CleanEx; HS_PCM1; -.
ExpressionAtlas; Q9UIS9; baseline and differential.
Genevisible; Q9UIS9; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:MGI.
GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
InterPro; IPR002857; Znf_CXXC.
Pfam; PF01429; MBD; 1.
Pfam; PF02008; zf-CXXC; 3.
SMART; SM00391; MBD; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
PROSITE; PS51058; ZF_CXXC; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 605 Methyl-CpG-binding domain protein 1.
/FTId=PRO_0000096258.
DOMAIN 1 69 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
ZN_FING 169 216 CXXC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 217 263 CXXC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 330 378 CXXC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 529 592 TRD.
MOTIF 84 88 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 284 313 Pro-rich.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 440 440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 499 499 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:17066076}.
CROSSLNK 499 499 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 538 538 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 538 538 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 173 221 Missing (in isoform 5 and isoform 10).
{ECO:0000303|PubMed:9207790}.
/FTId=VSP_011064.
VAR_SEQ 264 264 R -> RHLAHRLRRRHQRCQRRTPLAVAPPT (in
isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042812.
VAR_SEQ 304 326 Missing (in isoform 2 and isoform 8).
{ECO:0000303|PubMed:10454587,
ECO:0000303|Ref.5}.
/FTId=VSP_011065.
VAR_SEQ 326 382 LQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSN
QKRQKCRWRQCLQFAM -> L (in isoform 11).
{ECO:0000305}.
/FTId=VSP_054736.
VAR_SEQ 327 382 Missing (in isoform 4 and isoform 7).
{ECO:0000303|PubMed:10454587,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011066.
VAR_SEQ 327 327 Missing (in isoform 10). {ECO:0000305}.
/FTId=VSP_054737.
VAR_SEQ 483 528 Missing (in isoform 2, isoform 4, isoform
6, isoform 8 and isoform 11).
{ECO:0000303|PubMed:10454587,
ECO:0000303|Ref.5}.
/FTId=VSP_011068.
VAR_SEQ 573 596 ITEIFSLGGTRFRDTAVWLPRSKD -> EPTTQPQYSGNFD
NDLYEIYLIDI (in isoform 6).
{ECO:0000305}.
/FTId=VSP_011069.
VAR_SEQ 593 605 RSKDLKKPGARKQ -> SLQGRHSGREDGCKVWETEDTVEP
TSTSWNPRGWPGTHVSLSPPPASMMWVSCRRSWCPSSQS
(in isoform 2 and isoform 12).
{ECO:0000303|PubMed:10454587}.
/FTId=VSP_011070.
VAR_SEQ 594 605 SKDLKKPGARKQ -> YYHLALDWKCNCGYHLCCRSVLVP
(in isoform 10). {ECO:0000305}.
/FTId=VSP_054738.
VAR_SEQ 594 605 SKDLKKPGARKQ -> AGTREGKMDVKCGRPRTQWSPRARA
GTHEDGLEPMSVSHHLQLR (in isoform 11).
{ECO:0000305}.
/FTId=VSP_054739.
VAR_SEQ 597 605 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_011071.
VARIANT 401 401 P -> A (in dbSNP:rs125555).
{ECO:0000269|PubMed:10441743}.
/FTId=VAR_019513.
MUTAGEN 22 22 R->A: Abolishes binding to methylated
DNA.
MUTAGEN 30 30 R->A: Strongly reduces binding to
methylated DNA.
{ECO:0000269|PubMed:10581239}.
MUTAGEN 32 32 D->A: Strongly reduces binding to
methylated DNA.
{ECO:0000269|PubMed:10581239}.
MUTAGEN 34 34 Y->A: Reduces binding to methylated DNA.
{ECO:0000269|PubMed:10581239}.
MUTAGEN 44 44 R->A: Abolishes binding to methylated
DNA. {ECO:0000269|PubMed:10581239}.
MUTAGEN 45 45 S->A: Slightly reduces binding to
methylated DNA.
{ECO:0000269|PubMed:10581239}.
MUTAGEN 52 52 Y->A: No effect.
{ECO:0000269|PubMed:10581239}.
MUTAGEN 64 64 F->A: Disrupts tertiary structure and
abolishes DNA binding.
{ECO:0000269|PubMed:10581239}.
MUTAGEN 499 499 K->A: Abolishes sumoylation; when
associated with A-538.
{ECO:0000269|PubMed:17066076}.
MUTAGEN 501 501 E->A: Abolishes sumoylation; when
associated with A-540.
{ECO:0000269|PubMed:17066076}.
MUTAGEN 538 538 K->A: Abolishes sumoylation; when
associated with A-499.
{ECO:0000269|PubMed:17066076}.
MUTAGEN 540 540 E->A: Abolishes sumoylation; when
associated with A-501.
{ECO:0000269|PubMed:17066076}.
MUTAGEN 576 576 I->R: Abolishes interaction with AFT7IP
and subsequent transcription repression
activity. {ECO:0000269|PubMed:15691849}.
CONFLICT 239 239 H -> R (in Ref. 5; ABP02056).
{ECO:0000305}.
CONFLICT 330 330 T -> M (in Ref. 5; ABP02056).
{ECO:0000305}.
CONFLICT 348 349 MD -> NG (in Ref. 1; CAA71735 and 3;
AAD51442/AAD51443). {ECO:0000305}.
CONFLICT 489 489 L -> M (in Ref. 1; CAA71735).
{ECO:0000305}.
STRAND 5 7 {ECO:0000244|PDB:1IG4}.
TURN 9 11 {ECO:0000244|PDB:1D9N}.
STRAND 16 19 {ECO:0000244|PDB:1D9N}.
STRAND 21 25 {ECO:0000244|PDB:1D9N}.
STRAND 33 36 {ECO:0000244|PDB:1D9N}.
STRAND 38 40 {ECO:0000244|PDB:1D9N}.
HELIX 47 53 {ECO:0000244|PDB:1D9N}.
STRAND 55 57 {ECO:0000244|PDB:1IG4}.
TURN 64 66 {ECO:0000244|PDB:1D9N}.
STRAND 177 179 {ECO:0000244|PDB:4D4W}.
HELIX 180 183 {ECO:0000244|PDB:4D4W}.
HELIX 194 196 {ECO:0000244|PDB:4D4W}.
SEQUENCE 605 AA; 66607 MW; 665732782CC6A32A CRC64;
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT
LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT
DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA
ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC
PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC GRCDFCCDKP
KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP PPYRRRKRPS SARRHHLGPT
LKPTLATRTA QPDHTQAPTK QEAGGGFVLP PPGTDLVFLR EGASSPVQVP GPVAASTEAL
LQEAQCSGLS WVVALPQVKQ EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE
PPDPEEDKEE NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPRSKDLKKP
GARKQ


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