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DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37) (DNA MTase RnoIP) (M.RnoIP) (DNA methyltransferase I) (MCMT)

 DNMT1_RAT               Reviewed;        1622 AA.
Q9Z330; P70487; Q9R252; Q9WTX3; Q9WU57;
21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
21-FEB-2002, sequence version 2.
23-MAY-2018, entry version 157.
RecName: Full=DNA (cytosine-5)-methyltransferase 1;
Short=Dnmt1;
EC=2.1.1.37;
AltName: Full=DNA MTase RnoIP;
Short=M.RnoIP;
AltName: Full=DNA methyltransferase I;
AltName: Full=MCMT;
Name=Dnmt1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Brain, and Placenta;
PubMed=9878564; DOI=10.1006/bbrc.1998.9802;
Kimura H., Takeda T., Tanaka S., Ogawa T., Shiota K.;
"Expression of rat DNA (cytosine-5) methyltransferase (DNA MTase) in
rodent trophoblast giant cells: molecular cloning and characterization
of rat DNA MTase.";
Biochem. Biophys. Res. Commun. 253:495-501(1998).
[2]
NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 9).
TISSUE=Brain;
Deng J., Szyf M.;
"Multiple N-terminal isoforms of DNA (cytosine-5-)-methyltransferase
in vivo.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-356, AND IN VITRO BINDING TO ANNEXIN
V.
STRAIN=Wistar; TISSUE=Brain;
PubMed=8667030;
Ohsawa K., Imai Y., Ito D., Kohsaka S.;
"Molecular cloning and characterization of annexin V-binding proteins
with highly hydrophilic peptide structure.";
J. Neurochem. 67:89-97(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1169-1517 (ISOFORMS 1; 2; 3; 4;
5; 6; 7 AND 8).
PubMed=9722504; DOI=10.1074/jbc.273.36.22869;
Deng J., Szyf M.;
"Multiple isoforms of DNA methyltransferase are encoded by the
vertebrate cytosine DNA methyltransferase gene.";
J. Biol. Chem. 273:22869-22872(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-304; SER-718 AND
SER-1436, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Methylates CpG residues. Preferentially methylates
hemimethylated DNA. Associates with DNA replication sites in S
phase maintaining the methylation pattern in the newly synthesized
strand, that is essential for epigenetic inheritance. Associates
with chromatin during G2 and M phases to maintain DNA methylation
independently of replication. It is responsible for maintaining
methylation patterns established in development. DNA methylation
is coordinated with methylation of histones. Mediates
transcriptional repression by direct binding to HDAC2. In
association with DNMT3B and via the recruitment of CTCFL/BORIS,
involved in activation of BAG1 gene expression by modulating
dimethylation of promoter histone H3 at H3K4 and H3K9. Probably
forms a corepressor complex required for activated KRAS-mediated
promoter hypermethylation and transcriptional silencing of tumor
suppressor genes (TSGs) or other tumor-related genes in colorectal
cancer (CRC) cells. Also required to maintain a transcriptionally
repressive state of genes in undifferentiated embryonic stem cells
(ESCs). Associates at promoter regions of tumor suppressor genes
(TSGs) leading to their gene silencing. Promotes tumor growth.
{ECO:0000250|UniProtKB:P26358}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
homocysteine + DNA containing 5-methylcytosine.
{ECO:0000255|PROSITE-ProRule:PRU10018}.
-!- SUBUNIT: Homodimer. Forms a stable complex with E2F1, BB1 and
HDAC1. Forms a complex with DMAP1 and HDAC2, with direct
interaction. Interacts with the PRC2/EED-EZH2 complex. Probably
part of a corepressor complex containing ZNF304, TRIM28, SETDB1
and DNMT1. Interacts with UHRF1; promoting its recruitment to
hemimethylated DNA. Interacts with USP7, promoting its
deubiquitination. Interacts with BAZ2A/TIP5. Interacts with PCNA.
Interacts with MBD2 and MBD3. Interacts with DNMT3A and DNMT3B.
Interacts with UBC9. Interacts with HDAC1. Interacts with CSNK1D.
{ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9Z330-1; Sequence=Displayed;
Name=2; Synonyms=SF1;
IsoId=Q9Z330-2; Sequence=VSP_005627;
Name=3; Synonyms=SF2;
IsoId=Q9Z330-3; Sequence=VSP_005625;
Name=4; Synonyms=SF3;
IsoId=Q9Z330-4; Sequence=VSP_005624;
Name=5; Synonyms=SF4;
IsoId=Q9Z330-5; Sequence=VSP_005621;
Name=6; Synonyms=SF5;
IsoId=Q9Z330-6; Sequence=VSP_005622;
Name=7; Synonyms=SF6;
IsoId=Q9Z330-7; Sequence=VSP_005626;
Name=8; Synonyms=SF7;
IsoId=Q9Z330-8; Sequence=VSP_005623;
Name=9; Synonyms=short;
IsoId=Q9Z330-9; Sequence=VSP_005620;
-!- TISSUE SPECIFICITY: Isoforms 0 and 8 are highly expressed in
placenta, brain, lung, spleen, kidney, heart, and at much lower
levels in liver. Isoform 1 is expressed in cerebellum, isoform 2
in muscle and testis, isoform 3 in lung, isoform 4 in spleen and
brain, and isoform 5 in brain.
-!- DOMAIN: The N-terminal part is required for homodimerization and
acts as a regulatory domain.
-!- DOMAIN: The CXXC-type zinc finger specifically binds to
unmethylated CpG dinucleotides, positioning the autoinhibitory
linker between the DNA and the active site, thus providing a
mechanism to ensure that only hemimethylated CpG dinucleotides
undergo methylation. {ECO:0000250}.
-!- PTM: Sumoylated. {ECO:0000250}.
-!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF,
regulates cell cycle G(2)/M transition. Deacetylation of Lys-1116
and Lys-1354 by SIRT1 increases methyltransferase activity (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylation of Ser-151 by CDKs is important for enzymatic
activity and protein stability. Phosphorylation of Ser-140 by AKT1
prevents methylation by SETD7 therebye increasing DNMT1 stability
(By similarity). {ECO:0000250}.
-!- PTM: Methylation at Lys-139 by SETD7 promotes DNMT1 proteasomal
degradation. {ECO:0000250}.
-!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
ubiquitination by UHRF1 by promoting deubiquitination and
preventing degradation by the proteasome. {ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. C5-methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
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EMBL; AB012214; BAA37118.1; -; mRNA.
EMBL; AF116344; AAD32541.1; -; mRNA.
EMBL; AF116345; AAD32542.1; -; Genomic_DNA.
EMBL; D64060; BAA20854.1; -; mRNA.
EMBL; AH007612; AAD28102.1; -; Genomic_DNA.
PIR; JE0378; JE0378.
UniGene; Rn.6955; -.
ProteinModelPortal; Q9Z330; -.
SMR; Q9Z330; -.
IntAct; Q9Z330; 2.
STRING; 10116.ENSRNOP00000063831; -.
REBASE; 3019; M.RnoDnmt1.
CarbonylDB; Q9Z330; -.
iPTMnet; Q9Z330; -.
PhosphoSitePlus; Q9Z330; -.
PaxDb; Q9Z330; -.
PRIDE; Q9Z330; -.
UCSC; RGD:620979; rat. [Q9Z330-1]
RGD; 620979; Dnmt1.
eggNOG; ENOG410IF68; Eukaryota.
eggNOG; COG0270; LUCA.
HOGENOM; HOG000082497; -.
HOVERGEN; HBG051384; -.
InParanoid; Q9Z330; -.
PhylomeDB; Q9Z330; -.
BioCyc; MetaCyc:MONOMER-8581; -.
BRENDA; 2.1.1.37; 5301.
PRO; PR:Q9Z330; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:RGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:RGD.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0044026; P:DNA hypermethylation; IMP:RGD.
GO; GO:0006306; P:DNA methylation; TAS:RGD.
GO; GO:0032776; P:DNA methylation on cytosine; IDA:RGD.
GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IDA:RGD.
GO; GO:0010216; P:maintenance of DNA methylation; IDA:RGD.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0031000; P:response to caffeine; IEP:RGD.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR001025; BAH_dom.
InterPro; IPR018117; C5_DNA_meth_AS.
InterPro; IPR001525; C5_MeTfrase.
InterPro; IPR031303; C5_meth_CS.
InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
InterPro; IPR010506; DMAP1-bd.
InterPro; IPR017198; DNMT1-like.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR002857; Znf_CXXC.
Pfam; PF01426; BAH; 2.
Pfam; PF06464; DMAP_binding; 1.
Pfam; PF00145; DNA_methylase; 1.
Pfam; PF12047; DNMT1-RFD; 1.
Pfam; PF02008; zf-CXXC; 1.
PIRSF; PIRSF037404; DNMT1; 1.
PRINTS; PR00105; C5METTRFRASE.
SMART; SM00439; BAH; 2.
SMART; SM01137; DMAP_binding; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51038; BAH; 2.
PROSITE; PS00094; C5_MTASE_1; 1.
PROSITE; PS00095; C5_MTASE_2; 1.
PROSITE; PS51679; SAM_MT_C5; 1.
PROSITE; PS51058; ZF_CXXC; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
Methylation; Methyltransferase; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 1622 DNA (cytosine-5)-methyltransferase 1.
/FTId=PRO_0000088036.
DOMAIN 18 105 DMAP-interaction.
DOMAIN 759 884 BAH 1. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
DOMAIN 977 1105 BAH 2. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
REPEAT 1114 1115 1.
REPEAT 1116 1117 2.
REPEAT 1118 1119 3.
REPEAT 1120 1121 4.
REPEAT 1122 1123 5.
REPEAT 1124 1125 6.
REPEAT 1126 1127 7; approximate.
DOMAIN 1144 1603 SAM-dependent MTase C5-type.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
ZN_FING 650 696 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 1 342 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 1 145 Interaction with DNMT3A. {ECO:0000250}.
REGION 146 213 Interaction with DNMT3B. {ECO:0000250}.
REGION 304 610 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 327 556 DNA replication foci-targeting sequence.
REGION 697 758 Autoinhibitory linker.
REGION 1114 1127 7 X 2 AA tandem repeats of K-G.
REGION 1126 1622 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 1144 1622 Catalytic.
REGION 1155 1156 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P13864}.
REGION 1173 1174 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P26358}.
REGION 1195 1196 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P13864}.
MOTIF 173 200 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 149 152 Poly-Ser.
COMPBIAS 269 274 Poly-Asp.
COMPBIAS 726 729 Poly-Lys.
ACT_SITE 1231 1231 {ECO:0000255|PROSITE-ProRule:PRU01016,
ECO:0000255|PROSITE-ProRule:PRU10018}.
METAL 359 359 Zinc. {ECO:0000250}.
METAL 362 362 Zinc. {ECO:0000250}.
METAL 420 420 Zinc. {ECO:0000250}.
METAL 424 424 Zinc. {ECO:0000250}.
BINDING 1151 1151 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P13864}.
BINDING 1196 1196 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:P26358}.
BINDING 1582 1582 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P26358}.
BINDING 1584 1584 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250|UniProtKB:P13864}.
SITE 515 515 Important for activity. {ECO:0000250}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 70 70 N6,N6-dimethyllysine; by EHMT2.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 139 139 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 140 140 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 163 163 Phosphothreonine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 169 169 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 304 304 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 372 372 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 555 555 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 753 753 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 895 895 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 961 961 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 980 980 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1116 1116 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1118 1118 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1120 1120 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1122 1122 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1124 1124 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 1126 1126 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 1354 1354 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1436 1436 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CROSSLNK 1613 1613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P26358}.
VAR_SEQ 1 118 Missing (in isoform 9). {ECO:0000305}.
/FTId=VSP_005620.
VAR_SEQ 1202 1410 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_005622.
VAR_SEQ 1216 1504 Missing (in isoform 8). {ECO:0000305}.
/FTId=VSP_005623.
VAR_SEQ 1218 1430 QKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLS
YCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQC
TFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFA
PRACQLSVVVDDKKFVSNITRLSSGPFRTITMRDTMSDLPE
IQNGASAPEISYKWRATVLVPEAAARVALPAHPQGPYPQVH
ERAGGCRM -> VC (in isoform 5).
{ECO:0000305}.
/FTId=VSP_005621.
VAR_SEQ 1226 1477 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_005624.
VAR_SEQ 1252 1482 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_005625.
VAR_SEQ 1259 1481 Missing (in isoform 7). {ECO:0000305}.
/FTId=VSP_005626.
VAR_SEQ 1323 1403 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_005627.
CONFLICT 17 25 AGSLPDHVR -> RQARPRPCP (in Ref. 3;
BAA20854). {ECO:0000305}.
CONFLICT 189 189 A -> V (in Ref. 3; BAA20854).
{ECO:0000305}.
CONFLICT 1276 1276 F -> S (in Ref. 1; BAA37118).
{ECO:0000305}.
CONFLICT 1300 1300 T -> I (in Ref. 4; AAD28102).
{ECO:0000305}.
CONFLICT 1372 1372 M -> V (in Ref. 1; BAA37118).
{ECO:0000305}.
CONFLICT 1394 1428 KWRATVLVPEAAARVALPAHPQGPYPQVHERAGGC -> NG
EPQSWFQRQLRGSHYQPILRDHICKDMSALVAA (in
Ref. 1; BAA37118). {ECO:0000305}.
SEQUENCE 1622 AA; 182774 MW; FCFA4AAA69E234BA CRC64;
MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVKEKLNLLH EFLQTEIKSQ
LCDLETKLHK EELSEEGYLA KVKTLLNKDL CLENGTLSLT QKANGCPANG SRPTWKAEMA
DSNRSPRSRP KPRGPRRSKS DSETMIEASS SSVATRRTTR QTTITSHFKG PAKRKPKEDS
EKGNANESAA EERDQDKKRR VAGTESRASR AGESVEKPER VRPGTQLCQE EQGEQEDDRR
PRRQTRELAS RRKSREDPDR EARPGTHLDV DDDDEKDKRS SRPRSQPRDL ATKRRPKEEV
EQITPEPPEG KDEDEREEKR RKTTRKKPEP LSIPVQSRVE RKASQGKASA IPKLNPPQCP
ECGQYLDDPD LKYQQHPVDA VDEPQMLTNE ALSVFDSNSS WFETYDSSPM HKFTFFSVYC
SRGHLCPVDT GLIEKNVELY FSGVAKAIHE ENPSVEGGVN GKNLGPINQW WISGFDGGEK
ALIGFSTAFA EYFLMEPSPE YAPIFGLMQE KIYISKIVVE FLQSNPDAVY EDLINKIETT
VPPSAINVNR FTEDSLLRHA QFVVSQVESY DDAKDDDETP IFLSPCMRSL IHLAGVSLGQ
RRATRRTVIN SAKVKRKGPT KATTTKLVYQ IFDTFFSEQI EKDDKEDKEN TMKRRRCGVC
EVCQQPECGK CKACKDMVKF GGTGRSKQAC LKRRCPNLAV KEADEDEEAD DDIPELPSPK
KLHQGKKKKQ NKDRISWLGE PVKIEENRTY YWKVSIDEET LEVGDCVSVI PDDPSKPLYL
ARVTALWEDK NGQMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYR
GPSPNWAMEG GMDPEAMLPG AEDGKTYFYQ FWYSQDYARF ESPPKTQPAE DNKHKFCLSC
IRLAELRQKE MPKVLEQLEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKMASPM
KRSKRDPVNE NPVPRDTYRK YSDYIKGSNL DAPEPYRIGR IKEIYCGKKK GGKVNEADIK
IRLYKFYRPE NTHKSIQATY HADINLLYWS DEEAVVDFSD VQGRCTVEYG EDLLESIQDY
SQGGPDRFYF LEAYNSKTKS FEDPPNHARS PGNKGKGKGK GKGKGKPQVS EPKEPEAAIK
LPKLRTLDVF SGCGGLTEGF HQAGISETLW AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL
KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN SLVVSFLSYC
DYYRPRFFLL ENVRNFVSFR RSMVLKLTLR CLVRMGYQCT FGVLQAGQYG VAQTRRRAII
LAAAPGEKLP LFPEPLHVFA PRACQLSVVV DDKKFVSNIT RLSSGPFRTI TMRDTMSDLP
EIQNGASAPE ISYKWRATVL VPEAAARVAL PAHPQGPYPQ VHERAGGCRM RHIPLSPGSD
WRDLPNIQVR LRDGVITNKL RYTFHDTKNG CSSTGALRGV CSCAEGKTCD PASRQFNTLI
PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR VVSVRECARS
QGFPDTYRLF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL LASAQESASA AVKGKEETTT
ED


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EIAAB11614 DNA (cytosine-5)-methyltransferase 1,DNA methyltransferase I,DNA MTase RnoIP,Dnmt1,Dnmt1,M.RnoIP,MCMT,Rat,Rattus norvegicus
EIAAB11615 AIM,CXXC9,CXXC-type zinc finger protein 9,DNA (cytosine-5)-methyltransferase 1,DNA methyltransferase HsaI,DNA MTase HsaI,DNMT,Dnmt1,DNMT1,Homo sapiens,Human,M.HsaI,MCMT
EIAAB11613 DNA (cytosine-5)-methyltransferase 1,DNA methyltransferase MmuI,DNA MTase MmuI,Dnmt,Dnmt1,Dnmt1,M.MmuI,MCMT,Met1,Met-1,Mouse,Mus musculus,Uim
15-288-22659 DNA (cytosine-5)-methyltransferase 1 - EC 2.1.1.37; Dnmt1; DNA methyltransferase HsaI; DNA MTase HsaI; MCMT; M.HsaI Polyclonal 0.05 mg
15-288-22659 DNA (cytosine-5)-methyltransferase 1 - EC 2.1.1.37; Dnmt1; DNA methyltransferase HsaI; DNA MTase HsaI; MCMT; M.HsaI Polyclonal 0.1 mg
EIAAB11616 AIM,Chicken,DNA (cytosine-5)-methyltransferase 1,DNA methyltransferase GgaI,DNA MTase GgaI,DNMT,Dnmt1,DNMT1,Gallus gallus,M.GgaI,MCMT
MD002* Monkey DNA (cytosine-5)-methyltransferase 1,DNMT1 per AIM per CXXC9 per HSN1E per MCMT per mta ELISA Kit 96T
PD001 Porcine DNA (cytosine-5)-methyltransferase 1,DNMT1 per AIM per CXXC9 per HSN1E per MCMT per mta ELISA Kit 96T
20-272-190888 Dnmt1 - Mouse monoclonal [60B1220] to Dnmt1; EC 2.1.1.37; Dnmt1; DNA methyltransferase HsaI; DNA MTase HsaI; MCMT; M.HsaI Monoclonal 0.1 mg
18-272-195557 Dnmt1 - Rabbit polyclonal to Dnmt1; EC 2.1.1.37; Dnmt1; DNA methyltransferase HsaI; DNA MTase HsaI; MCMT; M.HsaI Polyclonal 0.05 mg
18-272-195555 Dnmt1 - Rabbit polyclonal to Dnmt1; EC 2.1.1.37; Dnmt1; DNA methyltransferase HsaI; DNA MTase HsaI; MCMT; M.HsaI Polyclonal 0.05 mg
18-272-195556 Dnmt1 - Rabbit polyclonal to Dnmt1; EC 2.1.1.37; Dnmt1; DNA methyltransferase HsaI; DNA MTase HsaI; MCMT; M.HsaI Polyclonal 0.05 mg
EIAAB43807 DNA (cytosine-5)-methyltransferase-like protein 2,DNA methyltransferase homolog HsaIIP,DNA MTase homolog HsaIIP,Dnmt2,DNMT2,Homo sapiens,Human,M.HsaIIP,PuMet,TRDMT1,tRNA (cytosine(38)-C(5))-methyltran
EIAAB43809 DNA (cytosine-5)-methyltransferase-like protein 2,DNA methyltransferase homolog MmuIIP,DNA MTase homolog MmuIIP,Dnmt2,Dnmt2,M.MmuIIP,Met2,Met-2,Mouse,Mus musculus,Trdmt1,tRNA (cytosine(38)-C(5))-methy
EIAAB08636 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase,3-demethylubiquinone-10 3-methyltransferase,COQ3,DHHB methyltransferase,DHHB-MT,DHHB-MTase,Dihydroxyhexaprenylbenzoate methyltransferase,Hexaprenyl
EIAAB08638 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase,3-demethylubiquinone-9 3-methyltransferase,Coq3,DHHB methyltransferase,DHHB-MT,DHHB-MTase,Dihydroxyhexaprenylbenzoate methyltransferase,Hexaprenyld
EIAAB08637 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase,3-demethylubiquinone-9 3-methyltransferase,Coq3,DHHB methyltransferase,DHHB-MT,DHHB-MTase,Dihydroxyhexaprenylbenzoate methyltransferase,Hexaprenyld
EIAAB11605 DNA (cytosine-5)-methyltransferase 3A,DNA methyltransferase HsaIIIA,DNA MTase HsaIIIA,Dnmt3a,DNMT3A,Homo sapiens,Human,M.HsaIIIA
EIAAB11606 DNA (cytosine-5)-methyltransferase 3B,DNA methyltransferase HsaIIIB,DNA MTase HsaIIIB,Dnmt3b,DNMT3B,Homo sapiens,Human,M.HsaIIIB
EIAAB11617 Bos taurus,Bovine,DNA (cytosine-5)-methyltransferase 1,Dnmt1,DNMT1
EIAAB11607 DNA (cytosine-5)-methyltransferase 3B,DNA methyltransferase MmuIIIB,DNA MTase MmuIIIB,Dnmt3b,Dnmt3b,M.MmuIIIB,Mouse,Mus musculus
EIAAB11602 DNA (cytosine-5)-methyltransferase 3A,DNA methyltransferase MmuIIIA,DNA MTase MmuIIIA,Dnmt3a,Dnmt3a,M.MmuIIIA,Mouse,Mus musculus
EIAAB08635 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase,3-demethylubiquinone-n 3-methyltransferase,Bos taurus,Bovine,COQ3,DHHB methyltransferase,DHHB-MT,DHHB-MTase,Dihydroxyhexaprenylbenzoate methyltrans
10-201 DNA (cytosine-5) methyltransferase 1 (Dnmt1), Active 300 units
CSB-E15849r Rat DNA (cytosine-5)-methyltransferase 1(DNMT1) ELISA Kit 96T


 

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