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P26358

- DNMT1_HUMAN

UniProt

P26358 - DNMT1_HUMAN

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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

DNMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 H3K9.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi353 – 3531Zinc
Metal bindingi356 – 3561Zinc
Metal bindingi414 – 4141Zinc
Metal bindingi418 – 4181Zinc
Sitei509 – 5091Important for activityBy similarity
Active sitei1226 – 12261

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri646 – 69247CXXC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. DNA-methyltransferase activity Source: UniProtKB
  5. methyl-CpG binding Source: Ensembl
  6. RNA binding Source: Ensembl
  7. zinc ion binding Source: Ensembl

GO - Biological processi

  1. cellular response to amino acid stimulus Source: Ensembl
  2. chromatin modification Source: UniProtKB-KW
  3. DNA methylation Source: ProtInc
  4. gene silencing Source: Ensembl
  5. maintenance of DNA methylation Source: UniProtKB
  6. negative regulation of histone H3-K9 methylation Source: UniProtKB
  7. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  8. positive regulation of gene expression Source: UniProtKB
  9. positive regulation of histone H3-K4 methylation Source: UniProtKB
  10. regulation of cell proliferation Source: Ensembl
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAi2.1.1.37. 2681.
ReactomeiREACT_200808. PRC2 methylates histones and DNA.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_267652. DNA methylation.

Protein family/group databases

REBASEi1161. M.HsaDnmt1A.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37)
Short name:
Dnmt1
Alternative name(s):
CXXC-type zinc finger protein 9
DNA methyltransferase HsaI
Short name:
DNA MTase HsaI
Short name:
M.HsaI
MCMT
Gene namesi
Name:DNMT1
Synonyms:AIM, CXXC9, DNMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:2976. DNMT1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: ProtInc
  2. pericentric heterochromatin Source: Ensembl
  3. replication fork Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary sensory, 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti490 – 4912DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase.
VAR_065965
Natural varianti495 – 4951Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 Publication
VAR_065966
Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic disorder characterized by adult onset of progressive cerebellar ataxia, narcolepsy, cataplexy, sensorineural deafness, and dementia. More variable features include optic atrophy, sensory neuropathy, psychosis, and depression.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti554 – 5541A → V in ADCADN. 1 Publication
VAR_070055
Natural varianti589 – 5891G → A in ADCADN. 1 Publication
VAR_070056
Natural varianti590 – 5901V → F in ADCADN. 1 Publication
VAR_070057

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1631R → A: Abolishes interaction with PCNA. 1 Publication
Mutagenesisi164 – 1641Q → A: Abolishes interaction with PCNA. 1 Publication
Mutagenesisi166 – 1661T → A: Abolishes interaction with PCNA. 1 Publication
Mutagenesisi167 – 1671I → A: Abolishes interaction with PCNA. 1 Publication
Mutagenesisi169 – 1691S → A: No loss of interaction with PCNA. 1 Publication
Mutagenesisi170 – 1701H → V: Abolishes interaction with PCNA. 1 Publication
Mutagenesisi171 – 1711F → V: Abolishes interaction with PCNA. 1 Publication
Mutagenesisi172 – 1721A → S: No loss of interaction with PCNA. 1 Publication
Mutagenesisi173 – 1731K → A: No loss of interaction with PCNA. 1 Publication
Mutagenesisi653 – 6531C → G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670. 1 Publication
Mutagenesisi656 – 6561C → G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670. 1 Publication
Mutagenesisi659 – 6591C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670. 1 Publication
Mutagenesisi664 – 6641C → F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670. 1 Publication
Mutagenesisi667 – 6671C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670. 1 Publication
Mutagenesisi670 – 6701C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667. 1 Publication
Mutagenesisi1226 – 12261C → A: Loss of activity. 1 Publication

Keywords - Diseasei

Deafness, Disease mutation, Neuropathy

Organism-specific databases

MIMi604121. phenotype.
614116. phenotype.
Orphaneti314404. Autosomal dominant cerebellar ataxia, deafness and narcolepsy.
PharmGKBiPA27443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16161616DNA (cytosine-5)-methyltransferase 1PRO_0000088034Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6,N6-dimethyllysine1 Publication
Modified residuei127 – 1271Phosphoserine4 Publications
Modified residuei133 – 1331Phosphoserine1 Publication
Modified residuei142 – 1421N6-methyllysine; by SETD71 Publication
Modified residuei143 – 1431Phosphoserine; by PKB/AKT12 Publications
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei154 – 1541Phosphoserine2 Publications
Modified residuei160 – 1601N6-acetyllysine1 Publication
Modified residuei173 – 1731N6-acetyllysine1 Publication
Modified residuei188 – 1881N6-acetyllysine1 Publication
Modified residuei259 – 2591N6-acetyllysine1 Publication
Modified residuei366 – 3661N6-acetyllysine1 Publication
Modified residuei394 – 3941Phosphoserine2 Publications
Modified residuei509 – 5091PhosphoserineBy similarity
Modified residuei714 – 7141Phosphoserine3 Publications
Modified residuei732 – 7321Phosphoserine1 Publication
Modified residuei749 – 7491N6-acetyllysine1 Publication
Modified residuei891 – 8911N6-acetyllysine1 Publication
Modified residuei957 – 9571N6-acetyllysine1 Publication
Modified residuei961 – 9611N6-acetyllysine1 Publication
Modified residuei975 – 9751N6-acetyllysine1 Publication
Modified residuei1054 – 10541N6-acetyllysine1 Publication
Modified residuei1111 – 11111N6-acetyllysine2 Publications
Modified residuei1113 – 11131N6-acetyllysine2 Publications
Modified residuei1115 – 11151N6-acetyllysine2 Publications
Modified residuei1117 – 11171N6-acetyllysine; by EHMT21 Publication
Modified residuei1119 – 11191N6-acetyllysineBy similarity
Modified residuei1121 – 11211N6-acetyllysineBy similarity
Modified residuei1349 – 13491N6-acetyllysine1 Publication
Modified residuei1415 – 14151N6-acetyllysine1 Publication

Post-translational modificationi

Sumoylated; sumoylation increases activity.1 Publication
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.2 Publications
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.8 Publications
Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal degradation.2 Publications
Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26358.
PaxDbiP26358.
PRIDEiP26358.

PTM databases

PhosphoSiteiP26358.

Expressioni

Tissue specificityi

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 1.1 Publication

Inductioni

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.

Gene expression databases

BgeeiP26358.
CleanExiHS_DNMT1.
ExpressionAtlasiP26358. baseline and differential.
GenevestigatoriP26358.

Organism-specific databases

HPAiCAB005876.
HPA002694.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EEDO755303EBI-719459,EBI-923794
EZH2Q159108EBI-719459,EBI-530054
NRIP1P485523EBI-719459,EBI-746484
SIRT1Q96EB611EBI-719459,EBI-1802965
UHRF1Q96T8812EBI-719459,EBI-1548946

Protein-protein interaction databases

BioGridi108123. 78 interactions.
DIPiDIP-39693N.
IntActiP26358. 21 interactions.
MINTiMINT-232346.
STRINGi9606.ENSP00000352516.

Structurei

Secondary structure

1
1616
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni354 – 3563Combined sources
Helixi377 – 38913Combined sources
Beta strandi405 – 4139Combined sources
Beta strandi422 – 4254Combined sources
Turni426 – 4305Combined sources
Beta strandi434 – 4418Combined sources
Beta strandi453 – 4586Combined sources
Beta strandi462 – 4676Combined sources
Beta strandi476 – 4805Combined sources
Beta strandi485 – 4884Combined sources
Turni493 – 4953Combined sources
Helixi496 – 4994Combined sources
Helixi504 – 51815Combined sources
Helixi524 – 53310Combined sources
Helixi538 – 5403Combined sources
Helixi547 – 5515Combined sources
Helixi554 – 56714Combined sources
Helixi575 – 5773Combined sources
Helixi579 – 5879Combined sources
Helixi592 – 5987Combined sources
Helixi622 – 6298Combined sources
Turni657 – 6593Combined sources
Helixi670 – 6723Combined sources
Helixi687 – 6893Combined sources
Beta strandi731 – 7355Combined sources
Beta strandi744 – 7463Combined sources
Beta strandi748 – 7525Combined sources
Beta strandi755 – 7584Combined sources
Beta strandi762 – 7654Combined sources
Beta strandi767 – 7693Combined sources
Beta strandi775 – 78511Combined sources
Turni786 – 7883Combined sources
Beta strandi789 – 79911Combined sources
Helixi800 – 8023Combined sources
Helixi806 – 8083Combined sources
Beta strandi813 – 82412Combined sources
Helixi825 – 8273Combined sources
Beta strandi828 – 8325Combined sources
Beta strandi834 – 8363Combined sources
Helixi843 – 8453Combined sources
Helixi856 – 8605Combined sources
Beta strandi862 – 8709Combined sources
Turni871 – 8744Combined sources
Beta strandi875 – 8773Combined sources
Turni889 – 8913Combined sources
Helixi894 – 90512Combined sources
Beta strandi912 – 9165Combined sources
Beta strandi921 – 9288Combined sources
Beta strandi931 – 9344Combined sources
Beta strandi938 – 9414Combined sources
Turni966 – 9683Combined sources
Helixi973 – 9753Combined sources
Helixi976 – 9805Combined sources
Beta strandi992 – 100110Combined sources
Beta strandi1005 – 10084Combined sources
Beta strandi1015 – 10206Combined sources
Helixi1024 – 10263Combined sources
Helixi1031 – 10344Combined sources
Beta strandi1035 – 10373Combined sources
Beta strandi1041 – 10444Combined sources
Beta strandi1048 – 10525Combined sources
Helixi1053 – 10553Combined sources
Beta strandi1058 – 10647Combined sources
Helixi1065 – 10673Combined sources
Helixi1072 – 10776Combined sources
Beta strandi1079 – 109012Combined sources
Turni1091 – 10944Combined sources
Beta strandi1095 – 10973Combined sources
Beta strandi1139 – 11457Combined sources
Helixi1150 – 11589Combined sources
Beta strandi1160 – 11678Combined sources
Helixi1171 – 118010Combined sources
Beta strandi1184 – 11874Combined sources
Helixi1191 – 120010Combined sources
Turni1214 – 12163Combined sources
Beta strandi1218 – 12225Combined sources
Beta strandi1231 – 12333Combined sources
Helixi1237 – 12437Combined sources
Helixi1247 – 125812Combined sources
Beta strandi1261 – 12688Combined sources
Helixi1269 – 12724Combined sources
Helixi1275 – 12773Combined sources
Helixi1278 – 128912Combined sources
Beta strandi1293 – 13008Combined sources
Helixi1301 – 13044Combined sources
Beta strandi1311 – 13188Combined sources
Helixi1336 – 13383Combined sources
Beta strandi1343 – 13453Combined sources
Beta strandi1348 – 13503Combined sources
Helixi1367 – 13715Combined sources
Beta strandi1384 – 13863Combined sources
Helixi1395 – 14017Combined sources
Helixi1419 – 14268Combined sources
Helixi1436 – 14383Combined sources
Beta strandi1451 – 14533Combined sources
Turni1462 – 14643Combined sources
Helixi1477 – 14793Combined sources
Beta strandi1480 – 14823Combined sources
Helixi1487 – 14893Combined sources
Beta strandi1493 – 14964Combined sources
Helixi1499 – 15035Combined sources
Helixi1504 – 15063Combined sources
Helixi1508 – 15103Combined sources
Turni1511 – 15144Combined sources
Beta strandi1523 – 15253Combined sources
Beta strandi1542 – 15476Combined sources
Helixi1550 – 15567Combined sources
Helixi1569 – 157810Combined sources
Helixi1582 – 159817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EPZX-ray2.31A/B351-600[»]
3PTAX-ray3.60A646-1600[»]
3SWRX-ray2.49A601-1600[»]
ProteinModelPortaliP26358.
SMRiP26358. Positions 351-599, 601-1600.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26358.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 10386DMAP-interactionAdd
BLAST
Domaini755 – 880126BAH 1PROSITE-ProRule annotationAdd
BLAST
Domaini972 – 1100129BAH 2PROSITE-ProRule annotationAdd
BLAST
Repeati1109 – 111021
Repeati1111 – 111222
Repeati1113 – 111423
Repeati1115 – 111624
Repeati1117 – 111825
Repeati1119 – 112026; approximate
Domaini1139 – 1599461SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 336336Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
BLAST
Regioni1 – 148148Interaction with DNMT3AAdd
BLAST
Regioni1 – 120120Interaction with DMAP1Add
BLAST
Regioni149 – 21769Interaction with DNMT3BAdd
BLAST
Regioni163 – 17412Interaction with PCNAAdd
BLAST
Regioni308 – 606299Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
BLAST
Regioni310 – 502193HomodimerizationAdd
BLAST
Regioni331 – 550220DNA replication foci-targeting sequenceBy similarityAdd
BLAST
Regioni651 – 69747Required for activityAdd
BLAST
Regioni693 – 75462Autoinhibitory linkerAdd
BLAST
Regioni1109 – 1120126 X 2 AA tandem repeats of K-GAdd
BLAST
Regioni1121 – 1616496Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
BLAST
Regioni1139 – 1616478CatalyticAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi177 – 20529Nuclear localization signalSequence AnalysisAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 2 BAH domains.PROSITE-ProRule annotation
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 DMAP-interaction domain.Curated
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri646 – 69247CXXC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0270.
GeneTreeiENSGT00390000005100.
HOGENOMiHOG000082497.
HOVERGENiHBG051384.
InParanoidiP26358.
KOiK00558.
OMAiCPNLAVK.
OrthoDBiEOG77WWBH.
PhylomeDBiP26358.
TreeFamiTF328926.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNA_C5-MeTrfase_1_euk.
IPR029063. SAM-dependent_MTases-like.
IPR002857. Znf_CXXC.
[Graphical view]
PANTHERiPTHR10629. PTHR10629. 1 hit.
PfamiPF01426. 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]
PIRSFiPIRSF037404. DNMT1. 1 hit.
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00439. BAH. 2 hits.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51038. BAH. 2 hits.
PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
PS51058. ZF_CXXC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26358-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH
60 70 80 90 100
EFLQTEIKNQ LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN
110 120 130 140 150
REVNGRLENG NQARSEARRV GMADANSPPK PLSKPRTPRR SKSDGEAKPE
160 170 180 190 200
PSPSPRITRK STRQTTITSH FAKGPAKRKP QEESERAKSD ESIKEEDKDQ
210 220 230 240 250
DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK EEKRLRSQTK
260 270 280 290 300
EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE
310 320 330 340 350
EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP
360 370 380 390 400
PKCIQCGQYL DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE
410 420 430 440 450
ALPQHKLTCF SVYCKHGHLC PIDTGLIEKN IELFFSGSAK PIYDDDPSLE
460 470 480 490 500
GGVNGKNLGP INEWWITGFD GGEKALIGFS TSFAEYILMD PSPEYAPIFG
510 520 530 540 550
LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL NLNRFTEDSL
560 570 580 590 600
LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR
610 620 630 640 650
RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR
660 670 680 690 700
RRCGVCEVCQ QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD
710 720 730 740 750
DDEEVDDNIP EMPSPKKMHQ GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV
760 770 780 790 800
CIDAETLEVG DCVSVIPDDS SKPLYLARVT ALWEDSSNGQ MFHAHWFCAG
810 820 830 840 850
TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS ENWAMEGGMD
860 870 880 890 900
PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA
910 920 930 940 950
EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI
960 970 980 990 1000
KLSSPVKRPR KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF
1010 1020 1030 1040 1050
CPKKSNGRPN ETDIKIRVNK FYRPENTHKS TPASYHADIN LLYWSDEEAV
1060 1070 1080 1090 1100
VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP NRFYFLEAYN AKSKSFEDPP
1110 1120 1130 1140 1150
NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR TLDVFSGCGG
1160 1170 1180 1190 1200
LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA
1210 1220 1230 1240 1250
GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS
1260 1270 1280 1290 1300
FLSYCDYYRP RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ
1310 1320 1330 1340 1350
AGQYGVAQTR RRAIILAAAP GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF
1360 1370 1380 1390 1400
VSNITRLSSG PFRTITVRDT MSDLPEVRNG ASALEISYNG EPQSWFQRQL
1410 1420 1430 1440 1450
RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP NIEVRLSDGT
1460 1470 1480 1490 1500
MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL
1510 1520 1530 1540 1550
PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV
1560 1570 1580 1590 1600
RECARSQGFP DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA
1610
RESASAKIKE EEAAKD
Length:1,616
Mass (Da):183,165
Last modified:January 11, 2001 - v2
Checksum:i1E833192D22AFA5B
GO
Isoform 2 (identifier: P26358-2) [UniParc]FASTAAdd to Basket

Also known as: Dnmt1b

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

Show »
Length:1,632
Mass (Da):184,819
Checksum:i650AA14F73A75649
GO
Isoform 3 (identifier: P26358-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,280
Mass (Da):144,465
Checksum:i70ECEE72AE313EE9
GO

Sequence cautioni

The sequence AAD54507.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti97 – 971H → R.
Corresponds to variant rs16999593 [ dbSNP | Ensembl ].
VAR_024605
Natural varianti311 – 3111I → V.
Corresponds to variant rs2228612 [ dbSNP | Ensembl ].
VAR_051960
Natural varianti490 – 4912DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase.
VAR_065965
Natural varianti495 – 4951Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 Publication
VAR_065966
Natural varianti554 – 5541A → V in ADCADN. 1 Publication
VAR_070055
Natural varianti589 – 5891G → A in ADCADN. 1 Publication
VAR_070056
Natural varianti590 – 5901V → F in ADCADN. 1 Publication
VAR_070057

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 336336Missing in isoform 3. 1 PublicationVSP_005617Add
BLAST
Alternative sequencei149 – 1491P → RSRDPPASASQVTGIRA in isoform 2. 1 PublicationVSP_005618

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12228.1. [P26358-1]
CCDS45958.1. [P26358-2]
PIRiS22610.
RefSeqiNP_001124295.1. NM_001130823.1. [P26358-2]
NP_001370.1. NM_001379.2. [P26358-1]
UniGeneiHs.202672.

Genome annotation databases

EnsembliENST00000340748; ENSP00000345739; ENSG00000130816. [P26358-1]
ENST00000359526; ENSP00000352516; ENSG00000130816. [P26358-2]
ENST00000540357; ENSP00000440457; ENSG00000130816. [P26358-3]
GeneIDi1786.
KEGGihsa:1786.
UCSCiuc002mng.3. human. [P26358-1]
uc010xlc.2. human. [P26358-2]

Polymorphism databases

DMDMi12231019.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS12228.1. [P26358-1 ]
CCDS45958.1. [P26358-2 ]
PIRi S22610.
RefSeqi NP_001124295.1. NM_001130823.1. [P26358-2 ]
NP_001370.1. NM_001379.2. [P26358-1 ]
UniGenei Hs.202672.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P26358.
SMRi P26358. Positions 351-599, 601-1600.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108123. 78 interactions.
DIPi DIP-39693N.
IntActi P26358. 21 interactions.
MINTi MINT-232346.
STRINGi 9606.ENSP00000352516.

Chemistry

BindingDBi P26358.
ChEMBLi CHEMBL1993.
DrugBanki DB00928. Azacitidine.
DB01262. Decitabine.
DB01099. Flucytosine.
DB01035. Procainamide.

Protein family/group databases

REBASEi 1161. M.HsaDnmt1A.

PTM databases

PhosphoSitei P26358.

Polymorphism databases

DMDMi 12231019.

Proteomic databases

MaxQBi P26358.
PaxDbi P26358.
PRIDEi P26358.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340748 ; ENSP00000345739 ; ENSG00000130816 . [P26358-1 ]
ENST00000359526 ; ENSP00000352516 ; ENSG00000130816 . [P26358-2 ]
ENST00000540357 ; ENSP00000440457 ; ENSG00000130816 . [P26358-3 ]
GeneIDi 1786.
KEGGi hsa:1786.
UCSCi uc002mng.3. human. [P26358-1 ]
uc010xlc.2. human. [P26358-2 ]

Organism-specific databases

CTDi 1786.
GeneCardsi GC19M010244.
GeneReviewsi DNMT1.
HGNCi HGNC:2976. DNMT1.
HPAi CAB005876.
HPA002694.
MIMi 126375. gene.
604121. phenotype.
614116. phenotype.
neXtProti NX_P26358.
Orphaneti 314404. Autosomal dominant cerebellar ataxia, deafness and narcolepsy.
PharmGKBi PA27443.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0270.
GeneTreei ENSGT00390000005100.
HOGENOMi HOG000082497.
HOVERGENi HBG051384.
InParanoidi P26358.
KOi K00558.
OMAi CPNLAVK.
OrthoDBi EOG77WWBH.
PhylomeDBi P26358.
TreeFami TF328926.

Enzyme and pathway databases

BRENDAi 2.1.1.37. 2681.
Reactomei REACT_200808. PRC2 methylates histones and DNA.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_267652. DNA methylation.

Miscellaneous databases

ChiTaRSi DNMT1. human.
EvolutionaryTracei P26358.
GeneWikii DNMT1.
GenomeRNAii 1786.
NextBioi 7267.
PROi P26358.
SOURCEi Search...

Gene expression databases

Bgeei P26358.
CleanExi HS_DNMT1.
ExpressionAtlasi P26358. baseline and differential.
Genevestigatori P26358.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNA_C5-MeTrfase_1_euk.
IPR029063. SAM-dependent_MTases-like.
IPR002857. Znf_CXXC.
[Graphical view ]
PANTHERi PTHR10629. PTHR10629. 1 hit.
Pfami 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 ]
PIRSFi PIRSF037404. DNMT1. 1 hit.
PRINTSi PR00105. C5METTRFRASE.
SMARTi SM00439. BAH. 2 hits.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 2 hits.
PROSITEi PS51038. BAH. 2 hits.
PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
PS51058. ZF_CXXC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: FUNCTION, INTERACTION WITH EED AND EZH2.
  16. "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.
  17. "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.
  18. "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.
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: METHYLATION AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-143; SER-152; SER-154 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. Cited for: VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495, CHARACTERIZATION OF VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495.
  37. Cited for: VARIANTS ADCADN VAL-554; ALA-589 AND PHE-590.

Entry informationi

Entry nameiDNMT1_HUMAN
AccessioniPrimary (citable) accession number: P26358
Secondary accession number(s): A0AV63
, B7ZLW6, Q9UHG5, Q9ULA2, Q9UMZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 11, 2001
Last modified: November 26, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3