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Q24K09 (DNMT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA (cytosine-5)-methyltransferase 1
Short name=Dnmt1
EC=2.1.1.37
Gene names
Name:DNMT1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length1611 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Subunit structure

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 By similarity. Interacts with the PRC2/EED-EZH2. complex. Interacts with UBC9 and BAZ2A/TIP5 By similarity. Binds to CSNK1D. Interacts with BAZ2A/TIP5. Binds to CSNK1D. Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. Interacts with USP7, promoting its deubiquitination By similarity.

Subcellular location

Nucleus By similarity.

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 By similarity.

Post-translational modification

Sumoylated By similarity.

Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G2/M transition. Deacetylation of Lys-1346 and Lys-1412 by SIRT1 increases methyltransferase activity By similarity.

Phosphorylation of Ser-154 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-143 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability By similarity.

Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal degradation By similarity.

Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome By similarity.

Sequence similarities

Belongs to the C5-methyltransferase family.

Contains 2 BAH domains.

Contains 1 CXXC-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionActivator
Chromatin regulator
Methyltransferase
Repressor
Transferase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular 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 sequence or structural similarity. Source: UniProtKB

negative regulation of histone H3-K9 methylation

Inferred from electronic annotation. Source: Compara

negative regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: Compara

positive regulation of gene expression

Inferred from electronic annotation. Source: Compara

positive regulation of histone H3-K4 methylation

Inferred from electronic annotation. Source: Compara

regulation of cell proliferation

Inferred from electronic annotation. Source: Compara

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentromeric heterochromatin

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

replication fork

Inferred from electronic annotation. Source: Compara

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from sequence or structural similarity. 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16111611DNA (cytosine-5)-methyltransferase 1
PRO_0000239845

Regions

Domain752 – 877126BAH 1
Domain969 – 1097129BAH 2
Repeat1106 – 110721
Repeat1108 – 110922
Repeat1110 – 111123
Repeat1112 – 111324
Repeat1114 – 111525; approximate
Zinc finger643 – 68947CXXC-type
Region1 – 334334Interaction with the PRC2/EED-EZH2 complex By similarity
Region1 – 148148Interaction with DNMT3A By similarity
Region1 – 120120Interaction with DMAP1 By similarity
Region149 – 21668Interaction with DNMT3B By similarity
Region163 – 17412Interaction with PCNA By similarity
Region306 – 603298Interaction with the PRC2/EED-EZH2 complex By similarity
Region329 – 548220DNA replication foci-targeting sequence By similarity
Region690 – 75162Autoinhibitory linker
Region1106 – 1115105 X 2 AA tandem repeats of K-G
Region1118 – 1611494Interaction with the PRC2/EED-EZH2 complex By similarity
Region1136 – 1611476Catalytic By similarity
Motif177 – 20428Nuclear localization signal Potential

Sites

Active site12231 By similarity
Metal binding3511Zinc By similarity
Metal binding3541Zinc By similarity
Metal binding4121Zinc By similarity
Metal binding4161Zinc By similarity
Site5071Important for activity By similarity

Amino acid modifications

Modified residue701N6,N6-dimethyllysine; by EHMT2 By similarity
Modified residue1331Phosphoserine By similarity
Modified residue1421N6-methyllysine; by SETD7 By similarity
Modified residue1431Phosphoserine; by PKB/AKT1 By similarity
Modified residue1521Phosphoserine By similarity
Modified residue1541Phosphoserine By similarity
Modified residue1601N6-acetyllysine By similarity
Modified residue1881N6-acetyllysine By similarity
Modified residue2571N6-acetyllysine By similarity
Modified residue2861Phosphoserine By similarity
Modified residue3921Phosphoserine By similarity
Modified residue5071Phosphoserine By similarity
Modified residue7111Phosphoserine By similarity
Modified residue7291Phosphoserine By similarity
Modified residue7461N6-acetyllysine By similarity
Modified residue8881N6-acetyllysine By similarity
Modified residue9541N6-acetyllysine By similarity
Modified residue9581N6-acetyllysine By similarity
Modified residue9721N6-acetyllysine By similarity
Modified residue10511N6-acetyllysine By similarity
Modified residue11081N6-acetyllysine By similarity
Modified residue11101N6-acetyllysine By similarity
Modified residue11121N6-acetyllysine By similarity
Modified residue11141N6-acetyllysine By similarity
Modified residue13461N6-acetyllysine By similarity
Modified residue14121N6-acetyllysine By similarity

Experimental info

Sequence conflict6551I → V in AAO44952. Ref.2
Sequence conflict7161H → R in AAO44952. Ref.2
Sequence conflict7771T → A in AAO44952. Ref.2
Sequence conflict11761L → F in AAP20551. Ref.1
Sequence conflict11861E → K in AAP20551. Ref.1
Sequence conflict11921L → V in AAP20551. Ref.1
Sequence conflict12091P → L in AAP20551. Ref.1
Sequence conflict12871M → R in AAP20551. Ref.1
Sequence conflict13871G → R in AAP20551. Ref.1
Sequence conflict14051I → T in AAO44952. Ref.2
Sequence conflict14661S → T in AAO44952. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q24K09 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: A7F0D9B24A18771C

FASTA1,611182,842
        10         20         30         40         50         60 
MPARTAPARV PALASRAFSL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLRTEIKNQ 

        70         80         90        100        110        120 
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHAFS REANGCLENG SQTSGEDCRV 

       130        140        150        160        170        180 
VMAEKGKPPK PVSRLYTPRR SKSDGETKSE VSSSPRITRK TTRQTTITSH FPRGPAKRKP 

       190        200        210        220        230        240 
EEEPEKVKSD DSVDEEKDQE EKRRRVTSRE RVAGLLPAEE PGRVRPGTHM EEEGRDDKEE 

       250        260        270        280        290        300 
KRLRSQTKEP TPKHKAKEEP DRDVRPGGAQ AEMNEGEDKD EKRHRSQPKD LASKRRPEEK 

       310        320        330        340        350        360 
EPERVKPQVS DEKDEDEKEE KRRRTTYREL TEKKMTRTKI AVVSKTNPPK CTECLQYLDD 

       370        380        390        400        410        420 
PELRYEQHPP DAVEEIQILT NERLSIFDAN ESGFESYEDL PQHKLTCFSV YCKRGHLCPI 

       430        440        450        460        470        480 
DTGLIEKDVE LLFSGSAKPI YEDDPSPEGG INGKNFGPIN EWWIAGFDGG EKALLGFSTS 

       490        500        510        520        530        540 
FAEYILMDPS PEYAPLFSVM QEKIYISKIV VEFLQSNPDS TYEDLINKIE TTVPPCMLNL 

       550        560        570        580        590        600 
NRFTEDSLLR HAQFVVEQVE SYDRAGDSDE QPIFLSPCMR DLIKLAGVTL GKRRAERRQT 

       610        620        630        640        650        660 
IRQPAKEKDK GPTKATTTKL VYQIFDTFFA EQIEKDDKED KENAFKRRRC GVCEICQQPE 

       670        680        690        700        710        720 
CGKCKACKDM VKFGGSGRSK QACQKRRCPN MAMKEADDDE EVDDNIPEMP SPKKMHQGKK 

       730        740        750        760        770        780 
KKQNKNRISW VGDAVKTDGK KSYYKKVCID SETLEVGDCV SVIPDDSSKP LYLARVTALW 

       790        800        810        820        830        840 
EDSSNGQMFH AHWFCAGTDT VLGATSDPLE LFLVDECEDM QLSYIHSKVQ VIYKAPSENW 

       850        860        870        880        890        900 
AMEGGVDPEA LMSEDDGKTY FYQLWYDQDY ARFESPPKTQ PTEDNKYKFC ASCARLAEMR 

       910        920        930        940        950        960 
QKEIPRVVEQ LQDLEGRVLY SLATKNGVQY RVGDGVYLPP EAFTFNIKLS SPVKRPRKEP 

       970        980        990       1000       1010       1020 
VDEALYPEHY RKYSDYIKGS NLDAPEPYRI GRIKEIFCSK KSNGRPNETD IKIRVNKFYR 

      1030       1040       1050       1060       1070       1080 
PENTHKSTPA SYHADINLLY WSDEEAVVDF KAVQGRCTVE YGEDLPQCLQ DFSAGGPDRF 

      1090       1100       1110       1120       1130       1140 
YFLEAYNAKS KSFEDPPNHA RSTGNKGKGK GKGKNRTKSQ TCEPSELETE IKLPKLRTLD 

      1150       1160       1170       1180       1190       1200 
VFSGCGGLSE GFHQAGISET LWAIEMWDPA AQAFRLNNPG STVFTEDCNV LLKLVMAGEV 

      1210       1220       1230       1240       1250       1260 
TNSRGQKLPQ KGDVEMLCGG PPCQGFSGMN RFNSRTYSKF KNSLVVSFLS YCDYYRPRYF 

      1270       1280       1290       1300       1310       1320 
LLENVRNFVS FKRSMVLKLT LRCLVRMGYQ CTFGVLQAGQ YGVAQTRRRA IILAAAPGEP 

      1330       1340       1350       1360       1370       1380 
LPLFPEPLHV FAPRACQLSV VVDDKKFVSN ITRLSSGPFR TITVRDTMSD LPEIRNGASA 

      1390       1400       1410       1420       1430       1440 
LEISYNGEPQ SWFQRQLRGS QYQPILRDHI CKDMSALVAA RMRHIPLAPG SDWRDLPNIE 

      1450       1460       1470       1480       1490       1500 
VRLSDGTLAR KLRYNYHDKK NGCSSSGALR GVCSCVEGKP CEPAARQFNT LIPWCLPHTG 

      1510       1520       1530       1540       1550       1560 
NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR 

      1570       1580       1590       1600       1610 
LFGNILDKHR QVGNAVPPPL AKAIGLEIKR CMLAKARESA SAKIKEEAAK D

« Hide

References

« Hide 'large scale' references
[1]"Analysis of DNA (cytosine 5) methyltransferase mRNA sequence and expression in bovine preimplantation embryos, fetal and adult tissues."
Golding M.C., Westhusin M.E.
Gene Expr. Patterns 3:551-558(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Bovine (Bos taurus) cytosine-5-methyltransferase (Dnmt1) cDNA."
Lee P., Min K.S., Seong H.H., Park J.K., Lee Y.K., Kim S.W., Kim S.J., Lee H.G., Chung H.K., Chang Y.M., Chang W.K., Kwon M.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY244709 mRNA. Translation: AAP20551.1.
AY173048 mRNA. Translation: AAO44952.1.
BC114063 mRNA. Translation: AAI14064.1.
IPIIPI00711805.
RefSeqNP_872592.2. NM_182651.2.
UniGeneBt.108052.
Bt.48560.

3D structure databases

ProteinModelPortalQ24K09.
ModBaseSearch...

Protein family/group databases

REBASE7406. M.BtaDnmt1AP.

Proteomic databases

PRIDEQ24K09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000003549; ENSBTAP00000003549; ENSBTAG00000002736.
GeneID281119.
KEGGbta:281119.

Organism-specific databases

CTD1786.

Phylogenomic databases

eggNOGCOG0270.
GeneTreeENSGT00390000005100.
HOGENOMHOG000082497.
HOVERGENHBG051384.
InParanoidQ24K09.
KOK00558.
OMASENWAME.
OrthoDBEOG4T1HKN.

Family and domain databases

InterProIPR001025. 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]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF01426. 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]
PIRSFPIRSF037404. DNMT1. 1 hit.
PRINTSPR00105. C5METTRFRASE.
SMARTSM00439. BAH. 2 hits.
[Graphical view]
PROSITEPS51038. BAH. 2 hits.
PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51058. ZF_CXXC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805188.

Entry information

Entry nameDNMT1_BOVIN
AccessionPrimary (citable) accession number: Q24K09
Secondary accession number(s): Q6Y856, Q7YS60
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: April 18, 2006
Last modified: April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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