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UniProtKB - P26358 (DNMT1_HUMAN)

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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

DNMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). Promotes tumor growth (PubMed:24623306).4 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi353Zinc1
Metal bindingi356Zinc1
Metal bindingi414Zinc1
Metal bindingi418Zinc1
Sitei509Important for activityBy similarity1
Binding sitei1146S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1191S-adenosyl-L-methionineCombined sources1 Publication1
Active sitei12261
Binding sitei1578S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Binding sitei1580S-adenosyl-L-methionine; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri646 – 692CXXC-typePROSITE-ProRule annotationAdd BLAST47

GO - Molecular functioni

  • DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-methyltransferase activity Source: UniProtKB
  • methyl-CpG binding Source: Ensembl
  • promoter-specific chromatin binding Source: UniProtKB
  • RNA binding Source: Ensembl
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • zinc ion binding Source: Ensembl
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cellular response to amino acid stimulus Source: Ensembl
  • chromatin organization Source: UniProtKB-KW
  • DNA methylation Source: ProtInc
  • DNA methylation involved in embryo development Source: Ensembl
  • gene silencing Source: Ensembl
  • maintenance of DNA methylation Source: UniProtKB
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of gene expression, epigenetic Source: Reactome
  • negative regulation of histone H3-K9 methylation Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: ProtInc
  • negative regulation of vascular associated smooth muscle cell apoptotic process Source: BHF-UCL
  • negative regulation of vascular smooth muscle cell differentiation involved in phenotypic switching Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of histone H3-K4 methylation Source: UniProtKB
  • positive regulation of methylation-dependent chromatin silencing Source: UniProtKB
  • positive regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • Ras protein signal transduction Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, Chromatin regulator, DNA-binding, Methyltransferase, Repressor, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAi2.1.1.37 2681
ReactomeiR-HSA-212300 PRC2 methylates histones and DNA
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5334118 DNA methylation
SIGNORiP26358

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000130816.14
HGNCiHGNC:2976 DNMT1
MIMi126375 gene
neXtProtiNX_P26358

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary sensory, 1E (HSN1E)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia.
See also OMIM:614116
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065965490 – 491DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. Corresponds to variant dbSNP:rs199473691Ensembl.2
Natural variantiVAR_065966495Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 PublicationCorresponds to variant dbSNP:rs199473690Ensembl.1
Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:604121
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070055554A → V in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509392Ensembl.1
Natural variantiVAR_070056589G → A in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509393Ensembl.1
Natural variantiVAR_070057590V → F in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509391Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163R → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi164Q → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi166T → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi167I → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi169S → A: No loss of interaction with PCNA. 1 Publication1
Mutagenesisi170H → V: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi171F → V: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi172A → S: No loss of interaction with PCNA. 1 Publication1
Mutagenesisi173K → A: No loss of interaction with PCNA. 1 Publication1
Mutagenesisi653C → G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670. 1 Publication1
Mutagenesisi656C → G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670. 1 Publication1
Mutagenesisi659C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670. 1 Publication1
Mutagenesisi664C → F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670. 1 Publication1
Mutagenesisi667C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670. 1 Publication1
Mutagenesisi670C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667. 1 Publication1
Mutagenesisi1226C → A: Loss of activity. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Neuropathy

Organism-specific databases

DisGeNETi1786
GeneReviewsiDNMT1
MalaCardsiDNMT1
MIMi604121 phenotype
614116 phenotype
OpenTargetsiENSG00000130816
Orphaneti314404 Autosomal dominant cerebellar ataxia, deafness and narcolepsy
PharmGKBiPA27443

Chemistry databases

ChEMBLiCHEMBL1993
DrugBankiDB00928 Azacitidine
DB01262 Decitabine
DB01099 Flucytosine
DB01035 Procainamide
GuidetoPHARMACOLOGYi2605

Polymorphism and mutation databases

BioMutaiDNMT1
DMDMi12231019

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880341 – 1616DNA (cytosine-5)-methyltransferase 1Add BLAST1616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei70N6,N6-dimethyllysine1 Publication1
Modified residuei127PhosphoserineCombined sources1
Modified residuei133PhosphoserineCombined sources1
Modified residuei137PhosphothreonineCombined sources1
Modified residuei141PhosphoserineBy similarity1
Modified residuei142N6-methyllysine; by SETD71 Publication1
Modified residuei143Phosphoserine; by PKB/AKT1Combined sources1 Publication1
Modified residuei152PhosphoserineCombined sources1
Modified residuei154PhosphoserineCombined sources1 Publication1
Modified residuei160N6-acetyllysine1 Publication1
Modified residuei166PhosphothreonineCombined sources1
Modified residuei173N6-acetyllysineCombined sources1
Modified residuei188N6-acetyllysine1 Publication1
Modified residuei259N6-acetyllysine; alternate1 Publication1
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei312PhosphoserineCombined sources1
Modified residuei366N6-acetyllysine1 Publication1
Modified residuei394PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei509PhosphoserineBy similarity1
Modified residuei549PhosphoserineCombined sources1
Modified residuei714PhosphoserineCombined sources1
Modified residuei732PhosphoserineCombined sources1
Modified residuei749N6-acetyllysine1 Publication1
Modified residuei878PhosphoserineCombined sources1
Modified residuei891N6-acetyllysine1 Publication1
Modified residuei957N6-acetyllysine1 Publication1
Modified residuei961N6-acetyllysine1 Publication1
Modified residuei975N6-acetyllysine1 Publication1
Modified residuei1054N6-acetyllysine1 Publication1
Modified residuei1111N6-acetyllysineCombined sources1 Publication1
Modified residuei1113N6-acetyllysineCombined sources1 Publication1
Modified residuei1115N6-acetyllysineCombined sources1 Publication1
Modified residuei1117N6-acetyllysine; by EHMT21 Publication1
Modified residuei1119N6-acetyllysineBy similarity1
Modified residuei1121N6-acetyllysineBy similarity1
Modified residuei1349N6-acetyllysine1 Publication1
Modified residuei1415N6-acetyllysine1 Publication1
Cross-linki1609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

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.1 Publication
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.2 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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP26358
MaxQBiP26358
PaxDbiP26358
PeptideAtlasiP26358
PRIDEiP26358
ProteomicsDBi54320
54321 [P26358-2]
54322 [P26358-3]

PTM databases

iPTMnetiP26358
PhosphoSitePlusiP26358

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

BgeeiENSG00000130816
CleanExiHS_DNMT1
ExpressionAtlasiP26358 baseline and differential
GenevisibleiP26358 HS

Organism-specific databases

HPAiCAB005876
HPA002694

Interactioni

Subunit structurei

Homodimer (PubMed:19173286). Forms a stable complex with E2F1, BB1 and HDAC1 (PubMed:10888886). Forms a complex with DMAP1 and HDAC2, with direct interaction (PubMed:10888872). Interacts with the PRC2/EED-EZH2 complex (PubMed:16357870). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306). Interacts with UHRF1; promoting its recruitment to hemimethylated DNA (PubMed:21745816). Interacts with USP7, promoting its deubiquitination (PubMed:21745816). Interacts with PCNA (PubMed:9302295). Interacts with MBD2 and MBD3 (PubMed:10947852). Interacts with DNMT3A and DNMT3B (PubMed:12145218). Interacts with UBC9 (PubMed:19450230). Interacts with CSNK1D (By similarity). Interacts with HDAC1 (By similarity). Interacts with BAZ2A/TIP5 (By similarity).By similarity10 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi108123, 98 interactors
CORUMiP26358
DIPiDIP-39693N
ELMiP26358
IntActiP26358, 36 interactors
MINTiP26358
STRINGi9606.ENSP00000352516

Chemistry databases

BindingDBiP26358

Structurei

Secondary structure

11616
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni354 – 356Combined sources3
Beta strandi359 – 361Combined sources3
Helixi363 – 365Combined sources3
Helixi377 – 381Combined sources5
Helixi384 – 386Combined sources3
Beta strandi392 – 394Combined sources3
Beta strandi404 – 414Combined sources11
Beta strandi417 – 419Combined sources3
Beta strandi422 – 425Combined sources4
Turni426 – 430Combined sources5
Beta strandi433 – 440Combined sources8
Beta strandi453 – 458Combined sources6
Beta strandi463 – 467Combined sources5
Beta strandi470 – 473Combined sources4
Beta strandi476 – 480Combined sources5
Beta strandi485 – 488Combined sources4
Turni493 – 495Combined sources3
Helixi496 – 518Combined sources23
Helixi524 – 533Combined sources10
Helixi538 – 540Combined sources3
Helixi547 – 551Combined sources5
Helixi554 – 566Combined sources13
Beta strandi575 – 578Combined sources4
Helixi579 – 588Combined sources10
Helixi592 – 597Combined sources6
Helixi622 – 629Combined sources8
Turni657 – 659Combined sources3
Helixi670 – 672Combined sources3
Turni674 – 677Combined sources4
Helixi687 – 689Combined sources3
Helixi692 – 703Combined sources12
Beta strandi731 – 735Combined sources5
Beta strandi738 – 740Combined sources3
Beta strandi744 – 746Combined sources3
Beta strandi748 – 752Combined sources5
Beta strandi755 – 758Combined sources4
Beta strandi762 – 765Combined sources4
Beta strandi767 – 769Combined sources3
Beta strandi775 – 785Combined sources11
Turni786 – 788Combined sources3
Beta strandi789 – 799Combined sources11
Helixi800 – 802Combined sources3
Beta strandi803 – 805Combined sources3
Helixi806 – 808Combined sources3
Beta strandi813 – 824Combined sources12
Helixi825 – 827Combined sources3
Beta strandi828 – 832Combined sources5
Beta strandi834 – 836Combined sources3
Helixi843 – 845Combined sources3
Turni851 – 853Combined sources3
Helixi856 – 860Combined sources5
Beta strandi862 – 870Combined sources9
Turni871 – 874Combined sources4
Beta strandi875 – 877Combined sources3
Beta strandi886 – 888Combined sources3
Turni889 – 891Combined sources3
Helixi894 – 905Combined sources12
Beta strandi912 – 916Combined sources5
Beta strandi921 – 928Combined sources8
Beta strandi931 – 934Combined sources4
Beta strandi938 – 941Combined sources4
Turni966 – 968Combined sources3
Helixi973 – 975Combined sources3
Helixi976 – 980Combined sources5
Beta strandi992 – 1001Combined sources10
Beta strandi1005 – 1008Combined sources4
Beta strandi1015 – 1020Combined sources6
Helixi1024 – 1026Combined sources3
Helixi1031 – 1034Combined sources4
Beta strandi1035 – 1037Combined sources3
Beta strandi1041 – 1044Combined sources4
Beta strandi1048 – 1052Combined sources5
Helixi1053 – 1055Combined sources3
Beta strandi1058 – 1064Combined sources7
Helixi1065 – 1067Combined sources3
Helixi1072 – 1077Combined sources6
Beta strandi1079 – 1090Combined sources12
Turni1091 – 1094Combined sources4
Beta strandi1095 – 1097Combined sources3
Helixi1101 – 1103Combined sources3
Beta strandi1139 – 1145Combined sources7
Helixi1150 – 1158Combined sources9
Beta strandi1160 – 1167Combined sources8
Helixi1171 – 1180Combined sources10
Beta strandi1184 – 1187Combined sources4
Helixi1191 – 1200Combined sources10
Turni1214 – 1216Combined sources3
Beta strandi1218 – 1222Combined sources5
Beta strandi1231 – 1233Combined sources3
Helixi1237 – 1243Combined sources7
Helixi1247 – 1258Combined sources12
Beta strandi1261 – 1268Combined sources8
Helixi1269 – 1272Combined sources4
Helixi1275 – 1277Combined sources3
Helixi1278 – 1289Combined sources12
Beta strandi1293 – 1300Combined sources8
Helixi1301 – 1304Combined sources4
Beta strandi1311 – 1318Combined sources8
Helixi1336 – 1338Combined sources3
Beta strandi1343 – 1345Combined sources3
Beta strandi1348 – 1350Combined sources3
Helixi1367 – 1371Combined sources5
Beta strandi1384 – 1386Combined sources3
Helixi1395 – 1401Combined sources7
Helixi1419 – 1426Combined sources8
Helixi1436 – 1438Combined sources3
Beta strandi1451 – 1453Combined sources3
Turni1462 – 1464Combined sources3
Beta strandi1474 – 1476Combined sources3
Helixi1477 – 1479Combined sources3
Beta strandi1480 – 1482Combined sources3
Helixi1487 – 1489Combined sources3
Beta strandi1493 – 1496Combined sources4
Helixi1499 – 1503Combined sources5
Helixi1504 – 1506Combined sources3
Helixi1508 – 1510Combined sources3
Turni1511 – 1514Combined sources4
Beta strandi1523 – 1525Combined sources3
Beta strandi1534 – 1536Combined sources3
Beta strandi1542 – 1547Combined sources6
Helixi1550 – 1556Combined sources7
Helixi1569 – 1578Combined sources10
Helixi1582 – 1598Combined sources17

3D structure databases

ProteinModelPortaliP26358
SMRiP26358
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26358

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 103DMAP-interactionAdd BLAST86
Domaini755 – 880BAH 1PROSITE-ProRule annotationAdd BLAST126
Domaini972 – 1100BAH 2PROSITE-ProRule annotationAdd BLAST129
Repeati1109 – 111012
Repeati1111 – 111222
Repeati1113 – 111432
Repeati1115 – 111642
Repeati1117 – 111852
Repeati1119 – 11206; approximate2
Domaini1139 – 1599SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST461

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 336Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST336
Regioni1 – 148Interaction with DNMT3A1 PublicationAdd BLAST148
Regioni1 – 120Interaction with DMAP11 PublicationAdd BLAST120
Regioni149 – 217Interaction with DNMT3B1 PublicationAdd BLAST69
Regioni163 – 174Interaction with PCNA1 PublicationAdd BLAST12
Regioni308 – 606Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST299
Regioni310 – 502HomodimerizationAdd BLAST193
Regioni331 – 550DNA replication foci-targeting sequenceBy similarityAdd BLAST220
Regioni651 – 697Required for activityAdd BLAST47
Regioni693 – 754Autoinhibitory linkerAdd BLAST62
Regioni1109 – 11206 X 2 AA tandem repeats of K-GAdd BLAST12
Regioni1121 – 1616Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST496
Regioni1139 – 1616CatalyticAdd BLAST478
Regioni1150 – 1151S-adenosyl-L-methionine bindingBy similarity2
Regioni1168 – 1169S-adenosyl-L-methionine bindingCombined sources1 Publication2
Regioni1190 – 1191S-adenosyl-L-methionine bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi177 – 205Nuclear localization signalSequence analysisAdd BLAST29

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri646 – 692CXXC-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IF68 Eukaryota
COG0270 LUCA
GeneTreeiENSGT00390000005100
HOGENOMiHOG000082497
HOVERGENiHBG051384
InParanoidiP26358
KOiK00558
OMAiWAMEGGM
OrthoDBiEOG091G02YU
PhylomeDBiP26358
TreeFamiTF328926

Family and domain databases

InterProiView protein in InterPro
IPR001025 BAH_dom
IPR018117 C5_DNA_meth_AS
IPR001525 C5_MeTfrase
IPR031303 C5_meth_CS
IPR022702 Cytosine_MeTrfase1_RFD
IPR010506 DMAP1-bd
IPR017198 DNMT1-like
IPR029063 SAM-dependent_MTases
IPR002857 Znf_CXXC
PfamiView protein in 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
PIRSFiPIRSF037404 DNMT1, 1 hit
PRINTSiPR00105 C5METTRFRASE
SMARTiView protein in SMART
SM00439 BAH, 2 hits
SM01137 DMAP_binding, 1 hit
SUPFAMiSSF53335 SSF53335, 2 hits
PROSITEiView protein in PROSITE
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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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.

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        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 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02460597H → R. Corresponds to variant dbSNP:rs16999593EnsemblClinVar.1
Natural variantiVAR_051960311I → V. Corresponds to variant dbSNP:rs2228612Ensembl.1
Natural variantiVAR_065965490 – 491DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. Corresponds to variant dbSNP:rs199473691Ensembl.2
Natural variantiVAR_065966495Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 PublicationCorresponds to variant dbSNP:rs199473690Ensembl.1
Natural variantiVAR_070055554A → V in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509392Ensembl.1
Natural variantiVAR_070056589G → A in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509393Ensembl.1
Natural variantiVAR_070057590V → F in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509391Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0056171 – 336Missing in isoform 3. 1 PublicationAdd BLAST336
Alternative sequenceiVSP_005618149P → RSRDPPASASQVTGIRA in isoform 2. 1 Publication1

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_001130823.2 [P26358-2]
NP_001305659.1, NM_001318730.1
NP_001305660.1, NM_001318731.1
NP_001370.1, NM_001379.3 [P26358-1]
UniGeneiHs.202672

Genome annotation databases

EnsembliENST00000340748; ENSP00000345739; ENSG00000130816 [P26358-1]
ENST00000359526; ENSP00000352516; ENSG00000130816 [P26358-2]
GeneIDi1786
KEGGihsa:1786
UCSCiuc002mng.4 human [P26358-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiDNMT1_HUMAN
AccessioniPrimary (citable) accession number: P26358
Secondary accession number(s): A0AV63
, B7ZLW6, Q9UHG5, Q9ULA2, Q9UMZ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 11, 2001
Last modified: June 20, 2018
This is version 207 of the entry and version 2 of the sequence. See 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

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