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DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37)

 DNMT1_BOVIN             Reviewed;        1611 AA.
Q24K09; Q6Y856; Q7YS60;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
18-APR-2006, sequence version 1.
23-MAY-2018, entry version 106.
RecName: Full=DNA (cytosine-5)-methyltransferase 1;
Short=Dnmt1;
EC=2.1.1.37;
Name=DNMT1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12971987; DOI=10.1016/S1567-133X(03)00121-2;
Golding M.C., Westhusin M.E.;
"Analysis of DNA (cytosine 5) methyltransferase mRNA sequence and
expression in bovine preimplantation embryos, fetal and adult
tissues.";
Gene Expr. Patterns 3:551-558(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Lee P., Min K.S., Seong H.H., Park J.K., Lee Y.K., Kim S.W., Kim S.J.,
Lee H.G., Chung H.K., Chang Y.M., Chang W.K., Kwon M.;
"Bovine (Bos taurus) cytosine-5-methyltransferase (Dnmt1) cDNA.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Hypothalamus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
-!- 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:P13864, 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 {ECO:0000250}.
-!- 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-1346
and Lys-1412 by SIRT1 increases methyltransferase activity (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylation of Ser-154 by CDKs is important for enzymatic
activity and protein stability. Phosphorylation of Ser-143 by AKT1
prevents methylation by SETD7 therebye increasing DNMT1 stability
(By similarity). {ECO:0000250}.
-!- PTM: Methylation at Lys-142 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; AY244709; AAP20551.1; -; mRNA.
EMBL; AY173048; AAO44952.1; -; mRNA.
EMBL; BC114063; AAI14064.1; -; mRNA.
RefSeq; NP_872592.2; NM_182651.2.
UniGene; Bt.108052; -.
UniGene; Bt.48560; -.
ProteinModelPortal; Q24K09; -.
SMR; Q24K09; -.
BioGrid; 158481; 1.
STRING; 9913.ENSBTAP00000003549; -.
REBASE; 7406; M.BtaDnmt1AP.
PaxDb; Q24K09; -.
PRIDE; Q24K09; -.
Ensembl; ENSBTAT00000003549; ENSBTAP00000003549; ENSBTAG00000002736.
GeneID; 281119; -.
KEGG; bta:281119; -.
CTD; 1786; -.
VGNC; VGNC:28145; DNMT1.
eggNOG; ENOG410IF68; Eukaryota.
eggNOG; COG0270; LUCA.
GeneTree; ENSGT00390000005100; -.
HOGENOM; HOG000082497; -.
HOVERGEN; HBG051384; -.
InParanoid; Q24K09; -.
KO; K00558; -.
OMA; WAMEGGM; -.
OrthoDB; EOG091G02YU; -.
TreeFam; TF328926; -.
BRENDA; 2.1.1.37; 908.
Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
Proteomes; UP000009136; Chromosome 7.
Bgee; ENSBTAG00000002736; -.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
GO; GO:0005657; C:replication fork; IEA:Ensembl.
GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0043045; P:DNA methylation involved in embryo development; IEA:Ensembl.
GO; GO:0016458; P:gene silencing; IEA:Ensembl.
GO; GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
GO; GO:1905931; P:negative regulation of vascular smooth muscle cell differentiation involved in phenotypic switching; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
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.
2: Evidence at transcript level;
Acetylation; Activator; 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 1611 DNA (cytosine-5)-methyltransferase 1.
/FTId=PRO_0000239845.
DOMAIN 18 106 DMAP-interaction.
DOMAIN 752 877 BAH 1. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
DOMAIN 969 1097 BAH 2. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
REPEAT 1106 1107 1.
REPEAT 1108 1109 2.
REPEAT 1110 1111 3.
REPEAT 1112 1113 4.
REPEAT 1114 1115 5; approximate.
DOMAIN 1136 1595 SAM-dependent MTase C5-type.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
ZN_FING 643 689 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 1 334 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 1 148 Interaction with DNMT3A. {ECO:0000250}.
REGION 1 120 Interaction with DMAP1. {ECO:0000250}.
REGION 149 216 Interaction with DNMT3B. {ECO:0000250}.
REGION 163 174 Interaction with PCNA. {ECO:0000250}.
REGION 306 603 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 329 548 DNA replication foci-targeting sequence.
{ECO:0000250}.
REGION 690 751 Autoinhibitory linker.
REGION 1106 1115 5 X 2 AA tandem repeats of K-G.
REGION 1118 1611 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 1136 1611 Catalytic. {ECO:0000250}.
REGION 1147 1148 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P13864}.
REGION 1165 1166 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P26358}.
REGION 1187 1188 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P13864}.
MOTIF 177 204 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 1223 1223 {ECO:0000255|PROSITE-ProRule:PRU01016,
ECO:0000255|PROSITE-ProRule:PRU10018}.
METAL 351 351 Zinc. {ECO:0000250}.
METAL 354 354 Zinc. {ECO:0000250}.
METAL 412 412 Zinc. {ECO:0000250}.
METAL 416 416 Zinc. {ECO:0000250}.
BINDING 1143 1143 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P13864}.
BINDING 1188 1188 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:P26358}.
BINDING 1574 1574 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P26358}.
BINDING 1576 1576 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250|UniProtKB:P13864}.
SITE 507 507 Important for activity. {ECO:0000250}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 70 70 N6,N6-dimethyllysine; by EHMT2.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 137 137 Phosphothreonine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 142 142 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 143 143 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 160 160 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 166 166 Phosphothreonine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 188 188 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 257 257 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 711 711 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 746 746 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 875 875 Phosphoserine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 888 888 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 954 954 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 958 958 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 972 972 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1051 1051 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1108 1108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1110 1110 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1112 1112 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1114 1114 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1118 1118 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 1346 1346 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
MOD_RES 1412 1412 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26358}.
CROSSLNK 257 257 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P26358}.
CROSSLNK 1605 1605 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P26358}.
CONFLICT 655 655 I -> V (in Ref. 2; AAO44952).
{ECO:0000305}.
CONFLICT 716 716 H -> R (in Ref. 2; AAO44952).
{ECO:0000305}.
CONFLICT 777 777 T -> A (in Ref. 2; AAO44952).
{ECO:0000305}.
CONFLICT 1176 1176 L -> F (in Ref. 1; AAP20551).
{ECO:0000305}.
CONFLICT 1186 1186 E -> K (in Ref. 1; AAP20551).
{ECO:0000305}.
CONFLICT 1192 1192 L -> V (in Ref. 1; AAP20551).
{ECO:0000305}.
CONFLICT 1209 1209 P -> L (in Ref. 1; AAP20551).
{ECO:0000305}.
CONFLICT 1287 1287 M -> R (in Ref. 1; AAP20551).
{ECO:0000305}.
CONFLICT 1387 1387 G -> R (in Ref. 1; AAP20551).
{ECO:0000305}.
CONFLICT 1405 1405 I -> T (in Ref. 2; AAO44952).
{ECO:0000305}.
CONFLICT 1466 1466 S -> T (in Ref. 2; AAO44952).
{ECO:0000305}.
SEQUENCE 1611 AA; 182842 MW; A7F0D9B24A18771C CRC64;
MPARTAPARV PALASRAFSL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLRTEIKNQ
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHAFS REANGCLENG SQTSGEDCRV
VMAEKGKPPK PVSRLYTPRR SKSDGETKSE VSSSPRITRK TTRQTTITSH FPRGPAKRKP
EEEPEKVKSD DSVDEEKDQE EKRRRVTSRE RVAGLLPAEE PGRVRPGTHM EEEGRDDKEE
KRLRSQTKEP TPKHKAKEEP DRDVRPGGAQ AEMNEGEDKD EKRHRSQPKD LASKRRPEEK
EPERVKPQVS DEKDEDEKEE KRRRTTYREL TEKKMTRTKI AVVSKTNPPK CTECLQYLDD
PELRYEQHPP DAVEEIQILT NERLSIFDAN ESGFESYEDL PQHKLTCFSV YCKRGHLCPI
DTGLIEKDVE LLFSGSAKPI YEDDPSPEGG INGKNFGPIN EWWIAGFDGG EKALLGFSTS
FAEYILMDPS PEYAPLFSVM QEKIYISKIV VEFLQSNPDS TYEDLINKIE TTVPPCMLNL
NRFTEDSLLR HAQFVVEQVE SYDRAGDSDE QPIFLSPCMR DLIKLAGVTL GKRRAERRQT
IRQPAKEKDK GPTKATTTKL VYQIFDTFFA EQIEKDDKED KENAFKRRRC GVCEICQQPE
CGKCKACKDM VKFGGSGRSK QACQKRRCPN MAMKEADDDE EVDDNIPEMP SPKKMHQGKK
KKQNKNRISW VGDAVKTDGK KSYYKKVCID SETLEVGDCV SVIPDDSSKP LYLARVTALW
EDSSNGQMFH AHWFCAGTDT VLGATSDPLE LFLVDECEDM QLSYIHSKVQ VIYKAPSENW
AMEGGVDPEA LMSEDDGKTY FYQLWYDQDY ARFESPPKTQ PTEDNKYKFC ASCARLAEMR
QKEIPRVVEQ LQDLEGRVLY SLATKNGVQY RVGDGVYLPP EAFTFNIKLS SPVKRPRKEP
VDEALYPEHY RKYSDYIKGS NLDAPEPYRI GRIKEIFCSK KSNGRPNETD IKIRVNKFYR
PENTHKSTPA SYHADINLLY WSDEEAVVDF KAVQGRCTVE YGEDLPQCLQ DFSAGGPDRF
YFLEAYNAKS KSFEDPPNHA RSTGNKGKGK GKGKNRTKSQ TCEPSELETE IKLPKLRTLD
VFSGCGGLSE GFHQAGISET LWAIEMWDPA AQAFRLNNPG STVFTEDCNV LLKLVMAGEV
TNSRGQKLPQ KGDVEMLCGG PPCQGFSGMN RFNSRTYSKF KNSLVVSFLS YCDYYRPRYF
LLENVRNFVS FKRSMVLKLT LRCLVRMGYQ CTFGVLQAGQ YGVAQTRRRA IILAAAPGEP
LPLFPEPLHV FAPRACQLSV VVDDKKFVSN ITRLSSGPFR TITVRDTMSD LPEIRNGASA
LEISYNGEPQ SWFQRQLRGS QYQPILRDHI CKDMSALVAA RMRHIPLAPG SDWRDLPNIE
VRLSDGTLAR KLRYNYHDKK NGCSSSGALR GVCSCVEGKP CEPAARQFNT LIPWCLPHTG
NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR
LFGNILDKHR QVGNAVPPPL AKAIGLEIKR CMLAKARESA SAKIKEEAAK D


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