Reviewed, UniProtKB/Swiss-Prot P13864 (DNMT1_MOUSE)

Names and origin

Protein names

Recommended name:
    DNA (cytosine-5)-methyltransferase 1
      Short name=Dnmt1
      Short name=Met-1
    EC=2.1.1.37
Alternative name(s):
    MCMT
    DNA methyltransferase MmuI
      Short name=DNA MTase MmuI
      Short name=M.MmuI

Gene names

Name:	Dnmt1
Synonyms:	Dnmt, Met1, Uim

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1620 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Methylates CpG residues. Preferentially methylates hemimethylated DNA. 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. Ref.14
Catalytic activity	S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
Enzyme regulation	Allosterically regulated. The binding of 5-methylcytosine-containing DNA to the N-terminal parts of DNMT1 causes an allosteric activation of the catalytic domain by a direct interaction of its Zn-binding domain with the catalytic domain. Ref.10
Subunit structure	Interacts with HDAC1 and with PCNA. Binds MBD2 and MBD3. Component of complexes containing SUV39H1. Interacts with DNMT3A and DNMT3B By similarity. Forms a complex with DMAP1 and HDAC2, with direct interaction. Interacts with the PRC2/EED-EZH2 complex.
Subcellular location	Nucleus. Cytoplasm. Note: It is nucleoplasmic through most of the cell cycle and associates with replication foci during S-phase. In germ cells, spermatogonia, preleptotene and leptotene spermatocytes all express high levels of nuclear protein, while the protein is not detected in pachytene spermatocytes, despite the fact they expressed high levels of mRNA. In females, the protein is not detected in non-growing oocytes, in contrast to the growing oocytes. During the growing, the protein is no longer detectable in nuclei but accumulates to very high levels first throughout the cytoplasm. At the time of ovulation, all the protein is cytoplasmic and is actively associated with the oocyte cortex. After fecondation, in the preimplantation embryo, the protein remains cytoplasmic and after implantation, it is exclusively nuclear in all tissue types. Isoform 2 is sequestered in the cytoplasm of maturing oocytes and of preimplantation embryos, except for the 8-cell stage, while isoform 1 is exclusively nuclear. Ref.14
Tissue specificity	Isoform 1 is expressed in embryonic stem cells and in somatic tissues. Isoform 2 is expressed in oocytes, preimplantation embryos, testis and in skeletal muscle during myogenesis.
Developmental stage	In germ cells, it is present at high levels in spermatogonia and spermatocytes until the pachytene stage, where it falls to undetectable levels. The transient drop at the pachytene stage coincides with the disappearance of the 5.2 kb mRNA and the accumulation of a larger 6.0 kb mRNA. Oocytes accumulate very large amounts of Dnmt1 protein during the growth phase.
Miscellaneous	There are three 5' exons, one specific to the oocyte (1c), one specific to the pachytene spermatocyte and also found in skeletal muscle (1b) and one found in somatic cells (1a). Three differents mRNAs can be produced which give rise to two different translation products: isoform 1 (mRNAs-1a) and isoform 2 (mRNA-1b or -1c).
Sequence similarities	Belongs to the C5-methyltransferase family. Contains 2 BAH domains. Contains 1 CXXC-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Methyltransferase Repressor Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA methylation Ref.15 Inferred from direct assay. Source: MGI gene silencing Ref.12 Inferred from direct assay. Source: UniProtKB negative regulation of transcription, DNA-dependent Ref.13 Inferred from direct assay. Source: MGI regulation of cell proliferation Inferred from genetic interaction. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell heterochromatin Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI replication fork Ref.13 Inferred from direct assay. Source: MGI
Molecular function	DNA (cytosine-5-)-methyltransferase activity Ref.15 Inferred from direct assay. Source: MGI DNA binding Ref.15 Inferred from direct assay. Source: MGI transcription factor binding Inferred from electronic annotation. Source: InterPro transcription repressor activity Ref.13 Inferred from direct assay. Source: MGI zinc ion binding Ref.15 Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hdac1	O09106	2	EBI-301927,EBI-301912

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P13864-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P13864-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1620	1620	DNA (cytosine-5)-methyltransferase 1		PRO_0000088035
Regions
	Domain	758 – 884	127	BAH 1
	Domain	976 – 1103	128	BAH 2
	Repeat	1112 – 1113	2	1
	Repeat	1114 – 1115	2	2
	Repeat	1116 – 1117	2	3
	Repeat	1118 – 1119	2	4
	Repeat	1120 – 1121	2	5
	Repeat	1122 – 1123	2	6
	Repeat	1124 – 1125	2	7; approximate
	Zinc finger	649 – 695	47	CXXC-type
	Region	1 – 343	343	Interaction with the PRC2/EED-EZH2 complex
	Region	1 – 145	145	Interaction with DNMT3A By similarity
	Region	1 – 120	120	Interaction with DMAP1
	Region	147 – 217	71	Interaction with DNMT3B By similarity
	Region	161 – 172	12	Interaction with PCNA
	Region	305 – 609	305	Interaction with the PRC2/EED-EZH2 complex
	Region	328 – 556	229	DNA replication foci-targeting sequence By similarity
	Region	696 – 813	118	Interaction with HDAC1
	Region	1112 – 1125	14	7 X 2 AA tandem repeats of K-G
	Region	1124 – 1620	497	Interaction with the PRC2/EED-EZH2 complex
	Region	1142 – 1620	479	Catalytic
	Motif	175 – 202	28	Nuclear localization signal Potential
Sites
	Active site	1229	1	By similarity
Amino acid modifications
	Modified residue	150	1	Phosphoserine By similarity
	Modified residue	152	1	Phosphoserine By similarity
	Modified residue	515	1	Phosphoserine Ref.11
	Modified residue	717	1	Phosphoserine By similarity
	Modified residue	735	1	Phosphoserine By similarity
	Modified residue	958	1	Phosphoserine By similarity
	Modified residue	973	1	Phosphotyrosine By similarity
	Modified residue	1108	1	Phosphoserine By similarity
	Modified residue	1116	1	N6-acetyllysine By similarity
	Modified residue	1118	1	N6-acetyllysine By similarity
	Modified residue	1120	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 118	118	Missing in isoform 2.		VSP_005619
Experimental info
	Sequence conflict	146 – 147	2	SV → F Ref.1
	Sequence conflict	146 – 147	2	SV → F Ref.2
	Sequence conflict	146 – 147	2	SV → F Ref.6
	Sequence conflict	299 – 309	11	AEPEQVAPETP → VRARAGSSRDS Ref.1
	Sequence conflict	299 – 309	11	AEPEQVAPETP → VRARAGSSRDS Ref.6
	Sequence conflict	936	1	V → C Ref.1
	Sequence conflict	936	1	V → C Ref.6
	Sequence conflict	947	1	P → R Ref.1
	Sequence conflict	947	1	P → R Ref.6
	Sequence conflict	969 – 976	8	NETLYPEH → KENPVPRDT Ref.1
	Sequence conflict	969 – 976	8	NETLYPEH → KENPVPRDT Ref.6
	Sequence conflict	987	1	S → R Ref.1
	Sequence conflict	987	1	S → R Ref.6
	Sequence conflict	1046	1	Y → C Ref.1
	Sequence conflict	1046	1	Y → C Ref.6
	Sequence conflict	1068	1	G → R Ref.1
	Sequence conflict	1068	1	G → R Ref.6
	Sequence conflict	1429	1	R → P Ref.1
	Sequence conflict	1429	1	R → P Ref.6
	Sequence conflict	1456	1	H → D Ref.1
	Sequence conflict	1456	1	H → D Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified February 21, 2002. Version 5. Checksum: 4F9A98CEAF09F037	FASTA	1,620	183,189
	10 20 30 40 50 60 MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVREKLNLLH EFLQTEIKSQ 70 80 90 100 110 120 LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGTHTLT QKANGCPANG SRPTWRAEMA 130 140 150 160 170 180 DSNRSPRSRP KPRGPRRSKS DSDTLSVETS PSSVATRRTT RQTTITAHFT KGPTKRKPKE 190 200 210 220 230 240 ESEEGNSAES AAEERDQDKK RRVVDTESGA AAAVEKLEEV TAGTQLGPEE PCEQEDDNRS 250 260 270 280 290 300 LRRHTRELSL RRKSKEDPDR EARPETHLDE DEDGKKDKRS SRPRSQPRDP AAKRRPKEAE 310 320 330 340 350 360 PEQVAPETPE DRDEDEREEK RRKTTRKKLE SHTVPVQSRS ERKAAQSKSV IPKINSPKCP 370 380 390 400 410 420 ECGQHLDDPN LKYQQHPEDA VDEPQMLTSE KLSIYDSTST WFDTYEDSPM HRFTSFSVYC 430 440 450 460 470 480 SRGHLCPVDT GLIEKNVELY FSGCAKAIHD ENPSMEGGIN GKNLGPINQW WLSGFDGGEK 490 500 510 520 530 540 VLIGFSTAFA EYILMEPSKE YEPIFGLMQE KIYISKIVVE FLQNNPDAVY EDLINKIETT 550 560 570 580 590 600 VPPSTINVNR FTEDSLLRHA QFVVSQVESY DEAKDDDETP IFLSPCMRAL IHLAGVSLGQ 610 620 630 640 650 660 RRATRRVMGA TKEKDKAPTK ATTTKLVYQI FDTFFSEQIE KYDKEDKENA MKRRRCGVCE 670 680 690 700 710 720 VCQQPECGKC KACKDMVKFG GTGRSKQACL KRRCPNLAVK EADDDEEADD DVSEMPSPKK 730 740 750 760 770 780 LHQGKKKKQN KDRISWLGQP MKIEENRTYY QKVSIDEEML EVGDCVSVIP DDSSKPLYLA 790 800 810 820 830 840 RVTALWEDKN GQMMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYK 850 860 870 880 890 900 APSENWAMEG GTDPETTLPG AEDGKTYFFQ LWYNQEYARF ESPPKTQPTE DNKHKFCLSC 910 920 930 940 950 960 IRLAELRQKE MPKVLEQIEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKVASPV 970 980 990 1000 1010 1020 KRPKKDPVNE TLYPEHYRKY SDYIKGSNLD APEPYRIGRI KEIHCGKKKG KVNEADIKLR 1030 1040 1050 1060 1070 1080 LYKFYRPENT HRSYNGSYHT DINMLYWSDE EAVVNFSDVQ GRCTVEYGED LLESIQDYSQ 1090 1100 1110 1120 1130 1140 GGPDRFYFLE AYNSKTKNFE DPPNHARSPG NKGKGKGKGK GKGKHQVSEP KEPEAAIKLP 1150 1160 1170 1180 1190 1200 KLRTLDVFSG CGGLSEGFHQ AGISETLWAI EMWDPAAQAF RLNNPGTTVF TEDCNVLLKL 1210 1220 1230 1240 1250 1260 VMAGEVTNSL GQRLPQKGDV EMLCGGPPCQ GFSGMNRFNS RTYSKFKNSL VVSFLSYCDY 1270 1280 1290 1300 1310 1320 YRPRFFLLEN VRNFVSYRRS MVLKLTLRCL VRMGYQCTFG VLQAGQYGVA QTRRRAIILA 1330 1340 1350 1360 1370 1380 AAPGEKLPLF PEPLHVFAPR ACQLSVVVDD KKFVSNITRL SSGPFRTITV RDTMSDLPEI 1390 1400 1410 1420 1430 1440 QNGASNSEIP YNGEPLSWFQ RQLRGSHYQP ILRDHICKDM SPLVAARMRH IPLFPGSDWR 1450 1460 1470 1480 1490 1500 DLPNIQVRLG DGVIAHKLQY TFHDVKNGYS STGALRGVCS CAEGKACDPE SRQFSTLIPW 1510 1520 1530 1540 1550 1560 CLPHTGNRHN HWAGLYGRLE WDGFFSTTVT NPEPMGKQGR VLHPEQHRVV SVRECARSQG 1570 1580 1590 1600 1610 1620 FPDSYRFFGN ILDRHRQVGN AVPPPLAKAI GLEIKLCLLS SARESASAAV KAKEEAATKD
	Isoform 2 (Short). Checksum: 4364F6D494EA67E4	FASTA	1,502	169,996
	10 20 30 40 50 60 MADSNRSPRS RPKPRGPRRS KSDSDTLSVE TSPSSVATRR TTRQTTITAH FTKGPTKRKP 70 80 90 100 110 120 KEESEEGNSA ESAAEERDQD KKRRVVDTES GAAAAVEKLE EVTAGTQLGP EEPCEQEDDN 130 140 150 160 170 180 RSLRRHTREL SLRRKSKEDP DREARPETHL DEDEDGKKDK RSSRPRSQPR DPAAKRRPKE 190 200 210 220 230 240 AEPEQVAPET PEDRDEDERE EKRRKTTRKK LESHTVPVQS RSERKAAQSK SVIPKINSPK 250 260 270 280 290 300 CPECGQHLDD PNLKYQQHPE DAVDEPQMLT SEKLSIYDST STWFDTYEDS PMHRFTSFSV 310 320 330 340 350 360 YCSRGHLCPV DTGLIEKNVE LYFSGCAKAI HDENPSMEGG INGKNLGPIN QWWLSGFDGG 370 380 390 400 410 420 EKVLIGFSTA FAEYILMEPS KEYEPIFGLM QEKIYISKIV VEFLQNNPDA VYEDLINKIE 430 440 450 460 470 480 TTVPPSTINV NRFTEDSLLR HAQFVVSQVE SYDEAKDDDE TPIFLSPCMR ALIHLAGVSL 490 500 510 520 530 540 GQRRATRRVM GATKEKDKAP TKATTTKLVY QIFDTFFSEQ IEKYDKEDKE NAMKRRRCGV 550 560 570 580 590 600 CEVCQQPECG KCKACKDMVK FGGTGRSKQA CLKRRCPNLA VKEADDDEEA DDDVSEMPSP 610 620 630 640 650 660 KKLHQGKKKK QNKDRISWLG QPMKIEENRT YYQKVSIDEE MLEVGDCVSV IPDDSSKPLY 670 680 690 700 710 720 LARVTALWED KNGQMMFHAH WFCAGTDTVL GATSDPLELF LVGECENMQL SYIHSKVKVI 730 740 750 760 770 780 YKAPSENWAM EGGTDPETTL PGAEDGKTYF FQLWYNQEYA RFESPPKTQP TEDNKHKFCL 790 800 810 820 830 840 SCIRLAELRQ KEMPKVLEQI EEVDGRVYCS SITKNGVVYR LGDSVYLPPE AFTFNIKVAS 850 860 870 880 890 900 PVKRPKKDPV NETLYPEHYR KYSDYIKGSN LDAPEPYRIG RIKEIHCGKK KGKVNEADIK 910 920 930 940 950 960 LRLYKFYRPE NTHRSYNGSY HTDINMLYWS DEEAVVNFSD VQGRCTVEYG EDLLESIQDY 970 980 990 1000 1010 1020 SQGGPDRFYF LEAYNSKTKN FEDPPNHARS PGNKGKGKGK GKGKGKHQVS EPKEPEAAIK 1030 1040 1050 1060 1070 1080 LPKLRTLDVF SGCGGLSEGF HQAGISETLW AIEMWDPAAQ AFRLNNPGTT VFTEDCNVLL 1090 1100 1110 1120 1130 1140 KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN SLVVSFLSYC 1150 1160 1170 1180 1190 1200 DYYRPRFFLL ENVRNFVSYR RSMVLKLTLR CLVRMGYQCT FGVLQAGQYG VAQTRRRAII 1210 1220 1230 1240 1250 1260 LAAAPGEKLP LFPEPLHVFA PRACQLSVVV DDKKFVSNIT RLSSGPFRTI TVRDTMSDLP 1270 1280 1290 1300 1310 1320 EIQNGASNSE IPYNGEPLSW FQRQLRGSHY QPILRDHICK DMSPLVAARM RHIPLFPGSD 1330 1340 1350 1360 1370 1380 WRDLPNIQVR LGDGVIAHKL QYTFHDVKNG YSSTGALRGV CSCAEGKACD PESRQFSTLI 1390 1400 1410 1420 1430 1440 PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR VVSVRECARS 1450 1460 1470 1480 1490 1500 QGFPDSYRFF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL LSSARESASA AVKAKEEAAT KD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells. The carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases." Bestor T.H., Laudano A., Mattaliano R., Ingram V. J. Mol. Biol. 203:971-983(1988) [PubMed: 3210246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"New 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase." Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B. J. Biol. Chem. 271:31092-31097(1996) [PubMed: 8940105] [Abstract] Cited for: SEQUENCE REVISION TO N-TERMINUS. Tissue: Embryo.
[3]	"Expression of an alternative Dnmt1 isoform during muscle differentiation." Aguirre-Arteta A.M., Grunewald I., Cardoso M.C., Leonhardt H. Cell Growth Differ. 11:551-559(2000) [PubMed: 11063128] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Skeletal muscle.
[4]	"Structure and function of the mouse DNA methyltransferase gene: Dnmt1 shows a tripartite structure." Margot J.B., Aguirre-Arteta A.M., Di Giacco B.V., Pradhan S., Roberts R.J., Cardoso M.C., Leonhardt H. J. Mol. Biol. 297:293-300(2000) [PubMed: 10715201] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[6]	"Sex-specific exons control DNA methyltransferase in mammalian germ cells." Mertineit C., Yoder J.A., Taketo T., Laird D.W., Trasler J.M., Bestor T.H. Development 125:889-897(1998) [PubMed: 9449671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-27 AND 119-1619 (ISOFORMS 1 AND 2).
[7]	"A short DNA methyltransferase isoform restores methylation in vivo." Gaudet F., Talbot D., Leonhardt H., Jaenisch R. J. Biol. Chem. 273:32725-32729(1998) [PubMed: 9830015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 3-6. Strain: 129/Sv and BALB/c. Tissue: Embryonic stem cell.
[8]	"Complementation of methylation deficiency in embryonic stem cells by a DNA methyltransferase minigene." Tucker K.L., Talbot D., Lee M.A., Leonhardt H., Jaenisch R. Proc. Natl. Acad. Sci. U.S.A. 93:12920-12925(1996) [PubMed: 8917520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-119 (ISOFORM 1). Strain: 129/Sv. Tissue: Embryonic stem cell and Kidney.
[9]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-272 (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryo.
[10]	"Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain." Bestor T.H. EMBO J. 11:2611-2617(1992) [PubMed: 1628623] [Abstract] Cited for: PROTEIN SEQUENCE OF 1108-1154, ENZYME REGULATION.
[11]	"Peptide mapping of the murine DNA methyltransferase reveals a major phosphorylation site and the start of translation." Glickman J.F., Pavlovich J.G., Reich N.O. J. Biol. Chem. 272:17851-17857(1997) [PubMed: 9211941] [Abstract] Cited for: PHOSPHORYLATION AT SER-515, MASS SPECTROMETRY. Tissue: Erythroleukemia.
[12]	"DNA methyltransferase Dnmt1 associates with histone deacetylase activity." Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T. Nat. Genet. 24:88-91(2000) [PubMed: 10615135] [Abstract] Cited for: INTERACTION WITH HDAC1.
[13]	"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci." Rountree M.R., Bachman K.E., Baylin S.B. Nat. Genet. 25:269-277(2000) [PubMed: 10888872] [Abstract] Cited for: INTERACTION WITH HDAC2 AND DMAP1.
[14]	"Genomic imprinting disrupted by a maternal effect mutation in the Dnmt1 gene." Howell C.Y., Bestor T.H., Ding F., Latham K.E., Mertineit C., Trasler J.M., Chaillet J.R. Cell 104:829-838(2001) [PubMed: 11290321] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"The activity of the murine DNA methyltransferase Dnmt1 is controlled by interaction of the catalytic domain with the N-terminal part of the enzyme leading to an allosteric activation of the enzyme after binding to methylated DNA." Fatemi M., Hermann A., Pradhan S., Jeltsch A. J. Mol. Biol. 309:1189-1199(2001) [PubMed: 11399088] [Abstract] Cited for: ALLOSTERIC REGULATION.
[16]	"The Polycomb group protein EZH2 directly controls DNA methylation." Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F. Nature 439:871-874(2006) [PubMed: 16357870] [Abstract] Cited for: INTERACTION WITH THE PRC2 COMPLEX.
[17]	Erratum Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F. Nature 446:824-824(2006)
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X14805 mRNA. Translation: CAA32910.1. AF175432 mRNA. Translation: AAF97695.1. AF162282 mRNA. Translation: AAF19352.1. AF175431 , AF175412, AF175413, AF175414, AF244089, AF244090, AF175416, AF175417, AF175418, AF175419, AF175420, AF175421, AF175422, AF175423, AF234317, AF175424, AF175425, AF175426, AF234318, AF175427, AF175428, AF175429, AF175430 Genomic DNA. Translation: AAF60965.1. BC048148 mRNA. Translation: AAH48148.2. AF036007 mRNA. Translation: AAC40061.1. AF036008 Genomic DNA. Translation: AAC53551.1. U70051 mRNA. Translation: AAC52900.1. Different initiation. AK013247 mRNA. Translation: BAB28743.1.
IPI	IPI00469323. IPI00474974.
PIR	S01845.
UniGene	Mm.128580
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P13864. 1 interaction.
Protein family/group databases
REBASE	2844. M.MmuDnmt1.
PTM databases
PhosphoSite	P13864.
Genome annotation databases
Ensembl	ENSMUSG00000004099. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:94912. Dnmt1.
Phylogenomic databases
HOVERGEN	P13864.
Enzyme and pathway databases
BRENDA	2.1.1.37. 244.
Gene expression databases
ArrayExpress	P13864.
Bgee	P13864.
CleanEx	MM_DNMT1.
GermOnline	ENSMUSG00000004099. Mus musculus.
Family and domain databases
InterPro	IPR001025. BAH. IPR001525. C5_DNA_meth. IPR018117. C5_DNA_meth_AS. IPR010506. DMAP1_bd. IPR017198. DNA_C5-MeTrfase_1. IPR002857. Znf_CXXC. [Graphical view]
PANTHER	PTHR10629. C5_DNA_meth. 1 hit.
Pfam	PF01426. BAH. 2 hits. PF06464. DMAP_binding. 1 hit. PF00145. DNA_methylase. 3 hits. PF02008. zf-CXXC. 1 hit. [Graphical view]
PIRSF	PIRSF037404. DNMT1. 1 hit.
PRINTS	PR00105. C5METTRFRASE.
SMART	SM00439. BAH. 2 hits. [Graphical view]
TIGRFAMs	TIGR00675. dcm. 1 hit.
PROSITE	PS51038. BAH. 2 hits. PS00094. C5_MTASE_1. 1 hit. PS00095. C5_MTASE_2. 1 hit. PS51058. ZF_CXXC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

DNMT1_MOUSE

Accession

Primary (citable) accession number: P13864
Secondary accession number(s): P97413 , Q80ZU3, Q9CSC6, Q9QXX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 21, 2002
Last modified:	June 16, 2009
This is version 114 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)