P26358 (DNMT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA (cytosine-5)-methyltransferase 1
Short name=Dnmt1
EC=2.1.1.37

Alternative name(s):
CXXC-type zinc finger protein 9
DNA methyltransferase HsaI
Short name=DNA MTase HsaI
Short name=M.HsaI
MCMT

Gene names

Name:	DNMT1
Synonyms:	AIM, CXXC9, DNMT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1616 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.15 Ref.18 Ref.19
Catalytic activity	S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
Subunit structure	Binds to CSNK1D By similarity. Homodimer. Interacts with HDAC1 and with PCNA. Forms a complex with DMAP1 and HDAC2, with direct interaction. Forms also a stable complex with E2F1, BB1 and HDAC1. Binds MBD2 and MBD3. Component of complexes containing SUV39H1. Interacts with DNMT3A and DNMT3B. Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9 and BAZ2A/TIP5. Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. Interacts with USP7, promoting its deubiquitination. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.23 Ref.24 Ref.32
Subcellular location	Nucleus Ref.13.
Tissue specificity	Ubiquitous; highly expressed in fetal tissues, heart, kidney, placenta, peripheral blood mononuclear cells, and expressed at lower levels in spleen, lung, brain, small intestine, colon, liver, and skeletal muscle. Isoform 2 is less expressed than isoform 1. Ref.12
Induction	Its abundance is reduced to non detectable levels at the G0 phase of the cell cycle and is dramatically induced upon entrance into the S-phase of the cell cycle.
Domain	The N-terminal part is required for homodimerization and acts as a regulatory 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 (Ref.35).
Post-translational modification	Sumoylated; sumoylation increases activity. Ref.23 Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G2/M transition. Deacetylation of Lys-1349 and Lys-1415 by SIRT1 increases methyltransferase activity. 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. Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal degradation. Ref.17 Ref.21 Ref.31 Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome By similarity.
Involvement in disease	Hereditary sensory neuropathy 1E (HSN1E) [MIM:614116]: A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36
Sequence similarities	Belongs to the C5-methyltransferase family. Contains 2 BAH domains. Contains 1 CXXC-type zinc finger.
Sequence caution	The sequence AAD54507.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Neuropathy
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Activator Chromatin regulator Methyltransferase Repressor Transferase
PTM	Acetylation Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW gene silencing Inferred from electronic annotation. Source: Compara maintenance of DNA methylation Inferred from direct assay Ref.18Ref.32. Source: UniProtKB negative regulation of histone H3-K9 methylation Inferred from mutant phenotype Ref.19. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.10. Source: ProtInc positive regulation of gene expression Inferred from mutant phenotype Ref.19. Source: UniProtKB positive regulation of histone H3-K4 methylation Inferred from mutant phenotype Ref.19. Source: UniProtKB regulation of cell proliferation Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centromeric heterochromatin Inferred from electronic annotation. Source: Compara nucleus Traceable author statement Ref.2. Source: ProtInc replication fork Inferred from electronic annotation. Source: Compara
Molecular_function	DNA (cytosine-5-)-methyltransferase activity Inferred from direct assay Ref.32. Source: UniProtKB DNA binding Inferred from direct assay Ref.18. Source: UniProtKB RNA binding Inferred from electronic annotation. Source: Compara methyl-CpG binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EED	O75530	3	EBI-719459,EBI-923794
EZH2	Q15910	8	EBI-719459,EBI-530054
SIRT1	Q96EB6	11	EBI-719459,EBI-1802965
UHRF1	Q96T88	10	EBI-719459,EBI-1548946

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P26358-1)

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: P26358-2)

Also known as: Dnmt1b;

The sequence of this isoform differs from the canonical sequence as follows:
     149-149: P → RSRDPPASASQVTGIRA

Isoform 3 (identifier: P26358-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-336: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1616

1616

DNA (cytosine-5)-methyltransferase 1

PRO_0000088034

Regions

Domain

755 – 880

126

BAH 1

Domain

972 – 1100

129

BAH 2

Repeat

1109 – 1110

2

1

Repeat

1111 – 1112

2

2

Repeat

1113 – 1114

2

3

Repeat

1115 – 1116

2

4

Repeat

1117 – 1118

2

5

Repeat

1119 – 1120

2

6; approximate

Zinc finger

646 – 692

47

CXXC-type

Region

1 – 336

336

Interaction with the PRC2/EED-EZH2 complex By similarity

Region

1 – 148

148

Interaction with DNMT3A

Region

1 – 120

120

Interaction with DMAP1

Region

149 – 217

69

Interaction with DNMT3B

Region

163 – 174

12

Interaction with PCNA

Region

308 – 606

299

Interaction with the PRC2/EED-EZH2 complex By similarity

Region

310 – 502

193

Homodimerization

Region

331 – 550

220

DNA replication foci-targeting sequence By similarity

Region

651 – 697

47

Required for activity

Region

693 – 754

62

Autoinhibitory linker

Region

1109 – 1120

12

6 X 2 AA tandem repeats of K-G

Region

1121 – 1616

496

Interaction with the PRC2/EED-EZH2 complex By similarity

Region

1139 – 1616

478

Catalytic

Motif

177 – 205

29

Nuclear localization signal Potential

Sites

Active site

1226

1

Metal binding

353

1

Zinc

Metal binding

356

1

Zinc

Metal binding

414

1

Zinc

Metal binding

418

1

Zinc

Site

509

1

Important for activity By similarity

Amino acid modifications

Modified residue

70

1

N6,N6-dimethyllysine Ref.21

Modified residue

127

1

Phosphoserine Ref.14 Ref.22 Ref.25 Ref.33

Modified residue

133

1

Phosphoserine Ref.33

Modified residue

142

1

N6-methyllysine; by SETD7 Ref.31

Modified residue

143

1

Phosphoserine; by PKB/AKT1 Ref.22 Ref.31

Modified residue

152

1

Phosphoserine Ref.22

Modified residue

154

1

Phosphoserine Ref.22 Ref.29

Modified residue

160

1

N6-acetyllysine Ref.30

Modified residue

173

1

N6-acetyllysine Ref.26

Modified residue

188

1

N6-acetyllysine Ref.30

Modified residue

259

1

N6-acetyllysine Ref.30

Modified residue

288

1

Phosphoserine By similarity

Modified residue

366

1

N6-acetyllysine Ref.30

Modified residue

394

1

Phosphoserine Ref.22 Ref.27

Modified residue

509

1

Phosphoserine By similarity

Modified residue

714

1

Phosphoserine Ref.14 Ref.27 Ref.33

Modified residue

732

1

Phosphoserine Ref.20

Modified residue

749

1

N6-acetyllysine Ref.30

Modified residue

891

1

N6-acetyllysine Ref.30

Modified residue

957

1

N6-acetyllysine Ref.30

Modified residue

961

1

N6-acetyllysine Ref.30

Modified residue

975

1

N6-acetyllysine Ref.30

Modified residue

1054

1

N6-acetyllysine Ref.30

Modified residue

1111

1

N6-acetyllysine Ref.26 Ref.30

Modified residue

1113

1

N6-acetyllysine Ref.26 Ref.30

Modified residue

1115

1

N6-acetyllysine Ref.26 Ref.30

Modified residue

1117

1

N6-acetyllysine; by EHMT2 Ref.30

Modified residue

1349

1

N6-acetyllysine Ref.30

Modified residue

1415

1

N6-acetyllysine Ref.30

Natural variations

Alternative sequence

1 – 336

336

Missing in isoform 3.

VSP_005617

Alternative sequence

149

1

P → RSRDPPASASQVTGIRA in isoform 2.

VSP_005618

Natural variant

97

1

H → R.
Corresponds to variant rs16999593 [ dbSNP | Ensembl ].

VAR_024605

Natural variant

311

1

I → V.
Corresponds to variant rs2228612 [ dbSNP | Ensembl ].

VAR_051960

Natural variant

490 – 491

2

DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase.

VAR_065965

Natural variant

495

1

Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. Ref.36

VAR_065966

Experimental info

Mutagenesis

163

1

R → A: Abolishes interaction with PCNA.

Mutagenesis

164

1

Q → A: Abolishes interaction with PCNA.

Mutagenesis

166

1

T → A: Abolishes interaction with PCNA.

Mutagenesis

167

1

I → A: Abolishes interaction with PCNA.

Mutagenesis

169

1

S → A: No loss of interaction with PCNA.

Mutagenesis

170

1

H → V: Abolishes interaction with PCNA.

Mutagenesis

171

1

F → V: Abolishes interaction with PCNA.

Mutagenesis

172

1

A → S: No loss of interaction with PCNA.

Mutagenesis

173

1

K → A: No loss of interaction with PCNA.

Mutagenesis

653

1

C → G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670. Ref.18

Mutagenesis

656

1

C → G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670. Ref.18

Mutagenesis

659

1

C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670. Ref.18

Mutagenesis

664

1

C → F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670. Ref.18

Mutagenesis

667

1

C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670. Ref.18

Mutagenesis

670

1

C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667. Ref.18

Mutagenesis

1226

1

C → A: Loss of activity. Ref.23

Secondary structure

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1616

Helix Strand Turn

Details...

Turn

354 – 356

3

Helix

377 – 389

13

Beta strand

405 – 413

9

Beta strand

422 – 425

4

Turn

426 – 430

5

Beta strand

434 – 441

8

Beta strand

453 – 458

6

Beta strand

462 – 467

6

Beta strand

476 – 480

5

Beta strand

485 – 488

4

Turn

493 – 495

3

Helix

496 – 499

4

Helix

504 – 518

15

Helix

524 – 533

10

Helix

538 – 540

3

Helix

547 – 551

5

Helix

554 – 567

14

Helix

575 – 577

3

Helix

579 – 587

9

Helix

592 – 598

7

Helix

622 – 629

8

Turn

657 – 659

3

Helix

670 – 672

3

Helix

687 – 689

3

Beta strand

731 – 735

5

Beta strand

744 – 746

3

Beta strand

748 – 752

5

Beta strand

755 – 758

4

Beta strand

762 – 765

4

Beta strand

767 – 769

3

Beta strand

775 – 785

11

Turn

786 – 788

3

Beta strand

789 – 799

11

Helix

800 – 802

3

Helix

806 – 808

3

Beta strand

813 – 824

12

Helix

825 – 827

3

Beta strand

828 – 832

5

Beta strand

834 – 836

3

Helix

843 – 845

3

Helix

856 – 860

5

Beta strand

862 – 870

9

Turn

871 – 874

4

Beta strand

875 – 877

3

Turn

889 – 891

3

Helix

894 – 905

12

Beta strand

912 – 916

5

Beta strand

921 – 928

8

Beta strand

931 – 934

4

Beta strand

938 – 941

4

Turn

966 – 968

3

Helix

973 – 975

3

Helix

976 – 980

5

Beta strand

992 – 1001

10

Beta strand

1005 – 1008

4

Beta strand

1015 – 1020

6

Helix

1024 – 1026

3

Helix

1031 – 1034

4

Beta strand

1035 – 1037

3

Beta strand

1041 – 1044

4

Beta strand

1048 – 1052

5

Helix

1053 – 1055

3

Beta strand

1058 – 1064

7

Helix

1065 – 1067

3

Helix

1072 – 1077

6

Beta strand

1079 – 1090

12

Turn

1091 – 1094

4

Beta strand

1095 – 1097

3

Beta strand

1139 – 1145

7

Helix

1150 – 1158

9

Beta strand

1160 – 1167

8

Helix

1171 – 1180

10

Beta strand

1184 – 1187

4

Helix

1191 – 1200

10

Turn

1214 – 1216

3

Beta strand

1218 – 1222

5

Beta strand

1231 – 1233

3

Helix

1237 – 1243

7

Helix

1247 – 1258

12

Beta strand

1261 – 1268

8

Helix

1269 – 1272

4

Helix

1275 – 1277

3

Helix

1278 – 1289

12

Beta strand

1293 – 1300

8

Helix

1301 – 1304

4

Beta strand

1311 – 1318

8

Helix

1336 – 1338

3

Beta strand

1343 – 1345

3

Beta strand

1348 – 1350

3

Helix

1367 – 1371

5

Beta strand

1384 – 1386

3

Helix

1395 – 1401

7

Helix

1419 – 1426

8

Helix

1436 – 1438

3

Beta strand

1451 – 1453

3

Turn

1462 – 1464

3

Helix

1477 – 1479

3

Beta strand

1480 – 1482

3

Helix

1487 – 1489

3

Beta strand

1493 – 1496

4

Helix

1499 – 1503

5

Helix

1504 – 1506

3

Helix

1508 – 1510

3

Turn

1511 – 1514

4

Beta strand

1523 – 1525

3

Beta strand

1542 – 1547

6

Helix

1550 – 1556

7

Helix

1569 – 1578

10

Helix

1582 – 1598

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 1E833192D22AFA5B	FASTA	1,616	183,165
	10 20 30 40 50 60 MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ 70 80 90 100 110 120 LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN REVNGRLENG NQARSEARRV 130 140 150 160 170 180 GMADANSPPK PLSKPRTPRR SKSDGEAKPE PSPSPRITRK STRQTTITSH FAKGPAKRKP 190 200 210 220 230 240 QEESERAKSD ESIKEEDKDQ DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK 250 260 270 280 290 300 EEKRLRSQTK EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE 310 320 330 340 350 360 EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP PKCIQCGQYL 370 380 390 400 410 420 DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE ALPQHKLTCF SVYCKHGHLC 430 440 450 460 470 480 PIDTGLIEKN IELFFSGSAK PIYDDDPSLE GGVNGKNLGP INEWWITGFD GGEKALIGFS 490 500 510 520 530 540 TSFAEYILMD PSPEYAPIFG LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL 550 560 570 580 590 600 NLNRFTEDSL LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR 610 620 630 640 650 660 RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR RRCGVCEVCQ 670 680 690 700 710 720 QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD DDEEVDDNIP EMPSPKKMHQ 730 740 750 760 770 780 GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV CIDAETLEVG DCVSVIPDDS SKPLYLARVT 790 800 810 820 830 840 ALWEDSSNGQ MFHAHWFCAG TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS 850 860 870 880 890 900 ENWAMEGGMD PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA 910 920 930 940 950 960 EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI KLSSPVKRPR 970 980 990 1000 1010 1020 KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF CPKKSNGRPN ETDIKIRVNK 1030 1040 1050 1060 1070 1080 FYRPENTHKS TPASYHADIN LLYWSDEEAV VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP 1090 1100 1110 1120 1130 1140 NRFYFLEAYN AKSKSFEDPP NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR 1150 1160 1170 1180 1190 1200 TLDVFSGCGG LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA 1210 1220 1230 1240 1250 1260 GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS FLSYCDYYRP 1270 1280 1290 1300 1310 1320 RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ AGQYGVAQTR RRAIILAAAP 1330 1340 1350 1360 1370 1380 GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF VSNITRLSSG PFRTITVRDT MSDLPEVRNG 1390 1400 1410 1420 1430 1440 ASALEISYNG EPQSWFQRQL RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP 1450 1460 1470 1480 1490 1500 NIEVRLSDGT MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL 1510 1520 1530 1540 1550 1560 PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV RECARSQGFP 1570 1580 1590 1600 1610 DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA RESASAKIKE EEAAKD
	Isoform 2 (Dnmt1b) [UniParc]. Checksum: 650AA14F73A75649	FASTA	1,632	184,819
	10 20 30 40 50 60 MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ 70 80 90 100 110 120 LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN REVNGRLENG NQARSEARRV 130 140 150 160 170 180 GMADANSPPK PLSKPRTPRR SKSDGEAKRS RDPPASASQV TGIRAEPSPS PRITRKSTRQ 190 200 210 220 230 240 TTITSHFAKG PAKRKPQEES ERAKSDESIK EEDKDQDEKR RRVTSRERVA RPLPAEEPER 250 260 270 280 290 300 AKSGTRTEKE EERDEKEEKR LRSQTKEPTP KQKLKEEPDR EARAGVQADE DEDGDEKDEK 310 320 330 340 350 360 KHRSQPKDLA AKRRPEEKEP EKVNPQISDE KDEDEKEEKR RKTTPKEPTE KKMARAKTVM 370 380 390 400 410 420 NSKTHPPKCI QCGQYLDDPD LKYGQHPPDA VDEPQMLTNE KLSIFDANES GFESYEALPQ 430 440 450 460 470 480 HKLTCFSVYC KHGHLCPIDT GLIEKNIELF FSGSAKPIYD DDPSLEGGVN GKNLGPINEW 490 500 510 520 530 540 WITGFDGGEK ALIGFSTSFA EYILMDPSPE YAPIFGLMQE KIYISKIVVE FLQSNSDSTY 550 560 570 580 590 600 EDLINKIETT VPPSGLNLNR FTEDSLLRHA QFVVEQVESY DEAGDSDEQP IFLTPCMRDL 610 620 630 640 650 660 IKLAGVTLGQ RRAQARRQTI RHSTREKDRG PTKATTTKLV YQIFDTFFAE QIEKDDREDK 670 680 690 700 710 720 ENAFKRRRCG VCEVCQQPEC GKCKACKDMV KFGGSGRSKQ ACQERRCPNM AMKEADDDEE 730 740 750 760 770 780 VDDNIPEMPS PKKMHQGKKK KQNKNRISWV GEAVKTDGKK SYYKKVCIDA ETLEVGDCVS 790 800 810 820 830 840 VIPDDSSKPL YLARVTALWE DSSNGQMFHA HWFCAGTDTV LGATSDPLEL FLVDECEDMQ 850 860 870 880 890 900 LSYIHSKVKV IYKAPSENWA MEGGMDPESL LEGDDGKTYF YQLWYDQDYA RFESPPKTQP 910 920 930 940 950 960 TEDNKFKFCV SCARLAEMRQ KEIPRVLEQL EDLDSRVLYY SATKNGILYR VGDGVYLPPE 970 980 990 1000 1010 1020 AFTFNIKLSS PVKRPRKEPV DEDLYPEHYR KYSDYIKGSN LDAPEPYRIG RIKEIFCPKK 1030 1040 1050 1060 1070 1080 SNGRPNETDI KIRVNKFYRP ENTHKSTPAS YHADINLLYW SDEEAVVDFK AVQGRCTVEY 1090 1100 1110 1120 1130 1140 GEDLPECVQV YSMGGPNRFY FLEAYNAKSK SFEDPPNHAR SPGNKGKGKG KGKGKPKSQA 1150 1160 1170 1180 1190 1200 CEPSEPEIEI KLPKLRTLDV FSGCGGLSEG FHQAGISDTL WAIEMWDPAA QAFRLNNPGS 1210 1220 1230 1240 1250 1260 TVFTEDCNIL LKLVMAGETT NSRGQRLPQK GDVEMLCGGP PCQGFSGMNR FNSRTYSKFK 1270 1280 1290 1300 1310 1320 NSLVVSFLSY CDYYRPRFFL LENVRNFVSF KRSMVLKLTL RCLVRMGYQC TFGVLQAGQY 1330 1340 1350 1360 1370 1380 GVAQTRRRAI ILAAAPGEKL PLFPEPLHVF APRACQLSVV VDDKKFVSNI TRLSSGPFRT 1390 1400 1410 1420 1430 1440 ITVRDTMSDL PEVRNGASAL EISYNGEPQS WFQRQLRGAQ YQPILRDHIC KDMSALVAAR 1450 1460 1470 1480 1490 1500 MRHIPLAPGS DWRDLPNIEV RLSDGTMARK LRYTHHDRKN GRSSSGALRG VCSCVEAGKA 1510 1520 1530 1540 1550 1560 CDPAARQFNT LIPWCLPHTG NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ 1570 1580 1590 1600 1610 1620 HRVVSVRECA RSQGFPDTYR LFGNILDKHR QVGNAVPPPL AKAIGLEIKL CMLAKARESA 1630 SAKIKEEEAA KD
	Isoform 3 [UniParc]. Checksum: 70ECEE72AE313EE9	FASTA	1,280	144,465
	10 20 30 40 50 60 MARAKTVMNS KTHPPKCIQC GQYLDDPDLK YGQHPPDAVD EPQMLTNEKL SIFDANESGF 70 80 90 100 110 120 ESYEALPQHK LTCFSVYCKH GHLCPIDTGL IEKNIELFFS GSAKPIYDDD PSLEGGVNGK 130 140 150 160 170 180 NLGPINEWWI TGFDGGEKAL IGFSTSFAEY ILMDPSPEYA PIFGLMQEKI YISKIVVEFL 190 200 210 220 230 240 QSNSDSTYED LINKIETTVP PSGLNLNRFT EDSLLRHAQF VVEQVESYDE AGDSDEQPIF 250 260 270 280 290 300 LTPCMRDLIK LAGVTLGQRR AQARRQTIRH STREKDRGPT KATTTKLVYQ IFDTFFAEQI 310 320 330 340 350 360 EKDDREDKEN AFKRRRCGVC EVCQQPECGK CKACKDMVKF GGSGRSKQAC QERRCPNMAM 370 380 390 400 410 420 KEADDDEEVD DNIPEMPSPK KMHQGKKKKQ NKNRISWVGE AVKTDGKKSY YKKVCIDAET 430 440 450 460 470 480 LEVGDCVSVI PDDSSKPLYL ARVTALWEDS SNGQMFHAHW FCAGTDTVLG ATSDPLELFL 490 500 510 520 530 540 VDECEDMQLS YIHSKVKVIY KAPSENWAME GGMDPESLLE GDDGKTYFYQ LWYDQDYARF 550 560 570 580 590 600 ESPPKTQPTE DNKFKFCVSC ARLAEMRQKE IPRVLEQLED LDSRVLYYSA TKNGILYRVG 610 620 630 640 650 660 DGVYLPPEAF TFNIKLSSPV KRPRKEPVDE DLYPEHYRKY SDYIKGSNLD APEPYRIGRI 670 680 690 700 710 720 KEIFCPKKSN GRPNETDIKI RVNKFYRPEN THKSTPASYH ADINLLYWSD EEAVVDFKAV 730 740 750 760 770 780 QGRCTVEYGE DLPECVQVYS MGGPNRFYFL EAYNAKSKSF EDPPNHARSP GNKGKGKGKG 790 800 810 820 830 840 KGKPKSQACE PSEPEIEIKL PKLRTLDVFS GCGGLSEGFH QAGISDTLWA IEMWDPAAQA 850 860 870 880 890 900 FRLNNPGSTV FTEDCNILLK LVMAGETTNS RGQRLPQKGD VEMLCGGPPC QGFSGMNRFN 910 920 930 940 950 960 SRTYSKFKNS LVVSFLSYCD YYRPRFFLLE NVRNFVSFKR SMVLKLTLRC LVRMGYQCTF 970 980 990 1000 1010 1020 GVLQAGQYGV AQTRRRAIIL AAAPGEKLPL FPEPLHVFAP RACQLSVVVD DKKFVSNITR 1030 1040 1050 1060 1070 1080 LSSGPFRTIT VRDTMSDLPE VRNGASALEI SYNGEPQSWF QRQLRGAQYQ PILRDHICKD 1090 1100 1110 1120 1130 1140 MSALVAARMR HIPLAPGSDW RDLPNIEVRL SDGTMARKLR YTHHDRKNGR SSSGALRGVC 1150 1160 1170 1180 1190 1200 SCVEAGKACD PAARQFNTLI PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ 1210 1220 1230 1240 1250 1260 GRVLHPEQHR VVSVRECARS QGFPDTYRLF GNILDKHRQV GNAVPPPLAK AIGLEIKLCM 1270 1280 LAKARESASA KIKEEEAAKD

References

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[1]	"Isolation and characterization of the cDNA encoding human DNA methyltransferase." Yen R.-W.C., Vertino P.M., Nelkin B.D., Yu J.J., Deiry W.E., Cumaraswamy A., Lennon G.G., Trask B.J., Celano P., Baylin S.B. Nucleic Acids Res. 20:2287-2291(1992) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]	"Human DNA methyltransferase (DNMT1) is alternatively spliced." Li L.C., Au H., Chui R., Dahiya R. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Prostatic carcinoma.
[4]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"Two major forms of DNA (cytosine-5) methyltransferase in human somatic tissues." Hsu D.-W., Lin M.-J., Lee T.-L., Wen S.-C., Chen X., Shen C.-K.J. Proc. Natl. Acad. Sci. U.S.A. 96:9751-9756(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[7]	"Characterization of the human DNA methyltransferase splice variant Dnmt1b." Bonfils C., Beaulieu N., Chan E., Cotton-Montpetit J., MacLeod A.R. J. Biol. Chem. 275:10754-10760(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[8]	"Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1." Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L. Science 277:1996-2000(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCNA, MUTAGENESIS.
[9]	"MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase." Tatematsu K., Yamazaki T., Ishikawa F. Genes Cells 5:677-688(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MBD2 AND MBD3.
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC2 AND DMAP1.
[11]	"DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters." Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P. Nat. Genet. 25:338-342(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RB1; E2F1 AND HDAC1.
[12]	"The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors." Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J., Gonzales F.A., Jones P.A. Nucleic Acids Res. 27:2291-2298(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[13]	"Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases." Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S. EMBO J. 21:4183-4195(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNMT3A AND DNMT3B, SUBCELLULAR LOCATION.
[14]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-714, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EED AND EZH2.
[16]	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)
[17]	"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer." Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H. Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DE NOVO DNA METHYLATION OF TARGET GENES.
[18]	"CXXC domain of human DNMT1 is essential for enzymatic activity." Pradhan M., Esteve P.-O., Chin H.G., Samaranayke M., Kim G.-D., Pradhan S. Biochemistry 47:10000-10009(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-653; CYS-656; CYS-659; CYS-664; CYS-667 AND CYS-670.
[19]	"DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation." Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S., Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P., Gius D. Cancer Res. 68:2726-2735(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Protein lysine methyltransferase G9a acts on non-histone targets." Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A. Nat. Chem. Biol. 4:344-346(2008) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-70, MASS SPECTROMETRY.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-143; SER-152; SER-154 AND SER-394, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"SUMOylation enhances DNA methyltransferase 1 activity." Lee B., Muller M.T. Biochem. J. 421:449-461(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, INTERACTION WITH UBC9, MUTAGENESIS OF CYS-1226.
[24]	"Dimerization of DNA methyltransferase 1 is mediated by its regulatory domain." Fellinger K., Rothbauer U., Felle M., Laengst G., Leonhardt H. J. Cell. Biochem. 106:521-528(2009) [PubMed] [Europe PMC] [Abstract] Cited for: HOMODIMERIZATION.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-1111; LYS-1113 AND LYS-1115, MASS SPECTROMETRY.
[27]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-714, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"Phosphorylation of human DNMT1: implication of cyclin-dependent kinases." Lavoie G., St-Pierre Y. Biochem. Biophys. Res. Commun. 409:187-192(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-154.
[30]	"SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities." Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N., Koomen J., Chen J., Lane W.S., Seto E. Mol. Cell. Biol. 31:4720-4734(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-160; LYS-188; LYS-259; LYS-366; LYS-749; LYS-891; LYS-957; LYS-961; LYS-975; LYS-1054; LYS-1111; LYS-1113; LYS-1115; LYS-1117; LYS-1349 AND LYS-1415, DEACETYLATION BY SIRT1.
[31]	"A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability." Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R., Feehery G.R., Cheng X., Pradhan S. Nat. Struct. Mol. Biol. 18:42-48(2011) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-142, PHOSPHORYLATION AT SER-143.
[32]	"The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1." Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T., Kremmer E., Kappler R., Langst G. Nucleic Acids Res. 39:8355-8365(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH USP7 AND UHRF1.
[33]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-133 AND SER-714, MASS SPECTROMETRY.
[34]	"The replication focus targeting sequence (RFTS) domain is a DNA-competitive inhibitor of Dnmt1." Syeda F., Fagan R.L., Wean M., Avvakumov G.V., Walker J.R., Xue S., Dhe-Paganon S., Brenner C. J. Biol. Chem. 286:15344-15351(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 351-600 IN COMPLEX WITH ZINC IONS.
[35]	"Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation." Song J., Rechkoblit O., Bestor T.H., Patel D.J. Science 331:1036-1040(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 646-1600 IN COMPLEX WITH SAH AND DNA, AUTOINHIBITORY LINKER.
[36]	"Mutations in DNMT1 cause hereditary sensory neuropathy with dementia and hearing loss." Klein C.J., Botuyan M.V., Wu Y., Ward C.J., Nicholson G.A., Hammans S., Hojo K., Yamanishi H., Karpf A.R., Wallace D.C., Simon M., Lander C., Boardman L.A., Cunningham J.M., Smith G.E., Litchy W.J., Boes B., Atkinson E.J. , Middha S., Dyck P.J.B., Parisi J.E., Mer G., Smith D.I., Dyck P.J. Nat. Genet. 43:595-600(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495, CHARACTERIZATION OF VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X63692 mRNA. Translation: CAA45219.1.
AF180682 mRNA. Translation: AAF23609.1.
AC010077 Genomic DNA. Translation: AAD54507.1. Sequence problems.
AC011511 Genomic DNA. No translation available.
AC020931 Genomic DNA. No translation available.
BC126227 mRNA. Translation: AAI26228.1.
BC144093 mRNA. Translation: AAI44094.1.
AH008119 Genomic DNA. Translation: AAD51619.1.

IPI

IPI00031519.
IPI00220918.
IPI00220919.

PIR

S22610.

RefSeq

NP_001124295.1. NM_001130823.1.
NP_001370.1. NM_001379.2.

UniGene

Hs.202672.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EPZ	X-ray	2.31	A/B	351-600	[»]
3PTA	X-ray	3.60	A	646-1600	[»]
3SWR	X-ray	2.49	A	601-1600	[»]

ProteinModelPortal

P26358.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39693N.

IntAct

P26358. 16 interactions.

MINT

MINT-232346.

STRING

9606.ENSP00000352516.

Protein family/group databases

REBASE

1161. M.HsaDnmt1A.

PTM databases

PhosphoSite

P26358.

Polymorphism databases

DMDM

12231019.

Proteomic databases

PaxDb

P26358.

PRIDE

P26358.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340748; ENSP00000345739; ENSG00000130816.
ENST00000359526; ENSP00000352516; ENSG00000130816.

GeneID

1786.

KEGG

hsa:1786.

UCSC

uc002mng.3. human.
uc002mnh.3. human.

Organism-specific databases

CTD

1786.

GeneCards

GC19M010244.

HGNC

HGNC:2976. DNMT1.

HPA

CAB005876.
HPA002694.

MIM

126375. gene.
614116. phenotype.

neXtProt

NX_P26358.

Orphanet

36386. Hereditary sensory and autonomic neuropathy type 1.

PharmGKB

PA27443.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0270.

HOGENOM

HOG000082497.

HOVERGEN

HBG051384.

KO

K00558.

OMA

SENWAME.

OrthoDB

EOG4T1HKN.

Enzyme and pathway databases

BRENDA

2.1.1.37. 2681.

Gene expression databases

ArrayExpress

P26358.

Bgee

P26358.

CleanEx

HS_DNMT1.

Genevestigator

P26358.

GermOnline

ENSG00000130816. Homo sapiens.

Family and domain databases

InterPro

IPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNA_C5-MeTrfase_1_euk.
IPR002857. Znf_CXXC.
[Graphical view]

PANTHER

PTHR10629. PTHR10629. 1 hit.

Pfam

PF01426. BAH. 2 hits.
PF06464. DMAP_binding. 1 hit.
PF00145. DNA_methylase. 1 hit.
PF12047. DNMT1-RFD. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]

PIRSF

PIRSF037404. DNMT1. 1 hit.

PRINTS

PR00105. C5METTRFRASE.

SMART

SM00439. BAH. 2 hits.
[Graphical view]

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

BindingDB

P26358.

ChEMBL

CHEMBL1993.

ChiTaRS

DNMT1. human.

DrugBank

DB00928. Azacitidine.
DB01262. Decitabine.
DB01099. Flucytosine.
DB01181. Ifosfamide.
DB01035. Procainamide.

EvolutionaryTrace

P26358.

GenomeRNAi

1786.

NextBio

7267.

SOURCE

Search...

Entry information

Entry name

DNMT1_HUMAN

Accession

Primary (citable) accession number: P26358
Secondary accession number(s): A0AV63 , B7ZLW6, Q9UHG5, Q9ULA2, Q9UMZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 11, 2001
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.