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Q24K09

- DNMT1_BOVIN

UniProt

Q24K09 - DNMT1_BOVIN

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Protein

DNA (cytosine-5)-methyltransferase 1

Gene
DNMT1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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 By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi351 – 3511Zinc By similarity
Metal bindingi354 – 3541Zinc By similarity
Metal bindingi412 – 4121Zinc By similarity
Metal bindingi416 – 4161Zinc By similarity
Sitei507 – 5071Important for activity By similarity
Active sitei1223 – 12231 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri643 – 68947CXXC-typeAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

ReactomeiREACT_207393. PRC2 methylates histones and DNA.
REACT_214253. NoRC negatively regulates rRNA expression.

Protein family/group databases

REBASEi7406. M.BtaDnmt1AP.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37)
Short name:
Dnmt1
Gene namesi
Name:DNMT1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 7

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. centromeric heterochromatin Source: Ensembl
  2. nucleus Source: UniProtKB-SubCell
  3. replication fork Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16111611DNA (cytosine-5)-methyltransferase 1PRO_0000239845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6,N6-dimethyllysine; by EHMT2 By similarity
Modified residuei133 – 1331Phosphoserine By similarity
Modified residuei142 – 1421N6-methyllysine; by SETD7 By similarity
Modified residuei143 – 1431Phosphoserine; by PKB/AKT1 By similarity
Modified residuei152 – 1521Phosphoserine By similarity
Modified residuei154 – 1541Phosphoserine By similarity
Modified residuei160 – 1601N6-acetyllysine By similarity
Modified residuei188 – 1881N6-acetyllysine By similarity
Modified residuei257 – 2571N6-acetyllysine By similarity
Modified residuei392 – 3921Phosphoserine By similarity
Modified residuei507 – 5071Phosphoserine By similarity
Modified residuei711 – 7111Phosphoserine By similarity
Modified residuei729 – 7291Phosphoserine By similarity
Modified residuei746 – 7461N6-acetyllysine By similarity
Modified residuei888 – 8881N6-acetyllysine By similarity
Modified residuei954 – 9541N6-acetyllysine By similarity
Modified residuei958 – 9581N6-acetyllysine By similarity
Modified residuei972 – 9721N6-acetyllysine By similarity
Modified residuei1051 – 10511N6-acetyllysine By similarity
Modified residuei1108 – 11081N6-acetyllysine By similarity
Modified residuei1110 – 11101N6-acetyllysine By similarity
Modified residuei1112 – 11121N6-acetyllysine By similarity
Modified residuei1114 – 11141N6-acetyllysine By similarity
Modified residuei1118 – 11181N6-acetyllysine By similarity
Modified residuei1346 – 13461N6-acetyllysine By similarity
Modified residuei1412 – 14121N6-acetyllysine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ24K09.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi158481. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ24K09.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 10689DMAP-interactionAdd
BLAST
Domaini752 – 877126BAH 1Add
BLAST
Domaini969 – 1097129BAH 2Add
BLAST
Repeati1106 – 110721
Repeati1108 – 110922
Repeati1110 – 111123
Repeati1112 – 111324
Repeati1114 – 111525; approximate
Domaini1136 – 1595460SAM-dependent MTase C5-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 334334Interaction with the PRC2/EED-EZH2 complex By similarityAdd
BLAST
Regioni1 – 148148Interaction with DNMT3A By similarityAdd
BLAST
Regioni1 – 120120Interaction with DMAP1 By similarityAdd
BLAST
Regioni149 – 21668Interaction with DNMT3B By similarityAdd
BLAST
Regioni163 – 17412Interaction with PCNA By similarityAdd
BLAST
Regioni306 – 603298Interaction with the PRC2/EED-EZH2 complex By similarityAdd
BLAST
Regioni329 – 548220DNA replication foci-targeting sequence By similarityAdd
BLAST
Regioni690 – 75162Autoinhibitory linkerAdd
BLAST
Regioni1106 – 1115105 X 2 AA tandem repeats of K-G
Regioni1118 – 1611494Interaction with the PRC2/EED-EZH2 complex By similarityAdd
BLAST
Regioni1136 – 1611476Catalytic By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi177 – 20428Nuclear localization signal Reviewed predictionAdd
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 By similarity.

Sequence similaritiesi

Contains 2 BAH domains.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri643 – 68947CXXC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0270.
GeneTreeiENSGT00390000005100.
HOGENOMiHOG000082497.
HOVERGENiHBG051384.
InParanoidiQ24K09.
KOiK00558.
OMAiCPNLAVK.
OrthoDBiEOG77WWBH.
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]

Sequencei

Sequence statusi: Complete.

Q24K09-1 [UniParc]FASTAAdd to Basket

« Hide

MPARTAPARV PALASRAFSL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH     50
EFLRTEIKNQ LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHAFS 100
REANGCLENG SQTSGEDCRV VMAEKGKPPK PVSRLYTPRR SKSDGETKSE 150
VSSSPRITRK TTRQTTITSH FPRGPAKRKP EEEPEKVKSD DSVDEEKDQE 200
EKRRRVTSRE RVAGLLPAEE PGRVRPGTHM EEEGRDDKEE KRLRSQTKEP 250
TPKHKAKEEP DRDVRPGGAQ AEMNEGEDKD EKRHRSQPKD LASKRRPEEK 300
EPERVKPQVS DEKDEDEKEE KRRRTTYREL TEKKMTRTKI AVVSKTNPPK 350
CTECLQYLDD PELRYEQHPP DAVEEIQILT NERLSIFDAN ESGFESYEDL 400
PQHKLTCFSV YCKRGHLCPI DTGLIEKDVE LLFSGSAKPI YEDDPSPEGG 450
INGKNFGPIN EWWIAGFDGG EKALLGFSTS FAEYILMDPS PEYAPLFSVM 500
QEKIYISKIV VEFLQSNPDS TYEDLINKIE TTVPPCMLNL NRFTEDSLLR 550
HAQFVVEQVE SYDRAGDSDE QPIFLSPCMR DLIKLAGVTL GKRRAERRQT 600
IRQPAKEKDK GPTKATTTKL VYQIFDTFFA EQIEKDDKED KENAFKRRRC 650
GVCEICQQPE CGKCKACKDM VKFGGSGRSK QACQKRRCPN MAMKEADDDE 700
EVDDNIPEMP SPKKMHQGKK KKQNKNRISW VGDAVKTDGK KSYYKKVCID 750
SETLEVGDCV SVIPDDSSKP LYLARVTALW EDSSNGQMFH AHWFCAGTDT 800
VLGATSDPLE LFLVDECEDM QLSYIHSKVQ VIYKAPSENW AMEGGVDPEA 850
LMSEDDGKTY FYQLWYDQDY ARFESPPKTQ PTEDNKYKFC ASCARLAEMR 900
QKEIPRVVEQ LQDLEGRVLY SLATKNGVQY RVGDGVYLPP EAFTFNIKLS 950
SPVKRPRKEP VDEALYPEHY RKYSDYIKGS NLDAPEPYRI GRIKEIFCSK 1000
KSNGRPNETD IKIRVNKFYR PENTHKSTPA SYHADINLLY WSDEEAVVDF 1050
KAVQGRCTVE YGEDLPQCLQ DFSAGGPDRF YFLEAYNAKS KSFEDPPNHA 1100
RSTGNKGKGK GKGKNRTKSQ TCEPSELETE IKLPKLRTLD VFSGCGGLSE 1150
GFHQAGISET LWAIEMWDPA AQAFRLNNPG STVFTEDCNV LLKLVMAGEV 1200
TNSRGQKLPQ KGDVEMLCGG PPCQGFSGMN RFNSRTYSKF KNSLVVSFLS 1250
YCDYYRPRYF LLENVRNFVS FKRSMVLKLT LRCLVRMGYQ CTFGVLQAGQ 1300
YGVAQTRRRA IILAAAPGEP LPLFPEPLHV FAPRACQLSV VVDDKKFVSN 1350
ITRLSSGPFR TITVRDTMSD LPEIRNGASA LEISYNGEPQ SWFQRQLRGS 1400
QYQPILRDHI CKDMSALVAA RMRHIPLAPG SDWRDLPNIE VRLSDGTLAR 1450
KLRYNYHDKK NGCSSSGALR GVCSCVEGKP CEPAARQFNT LIPWCLPHTG 1500
NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA 1550
RSQGFPDTYR LFGNILDKHR QVGNAVPPPL AKAIGLEIKR CMLAKARESA 1600
SAKIKEEAAK D 1611
Length:1,611
Mass (Da):182,842
Last modified:April 18, 2006 - v1
Checksum:iA7F0D9B24A18771C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti655 – 6551I → V in AAO44952. 1 Publication
Sequence conflicti716 – 7161H → R in AAO44952. 1 Publication
Sequence conflicti777 – 7771T → A in AAO44952. 1 Publication
Sequence conflicti1176 – 11761L → F in AAP20551. 1 Publication
Sequence conflicti1186 – 11861E → K in AAP20551. 1 Publication
Sequence conflicti1192 – 11921L → V in AAP20551. 1 Publication
Sequence conflicti1209 – 12091P → L in AAP20551. 1 Publication
Sequence conflicti1287 – 12871M → R in AAP20551. 1 Publication
Sequence conflicti1387 – 13871G → R in AAP20551. 1 Publication
Sequence conflicti1405 – 14051I → T in AAO44952. 1 Publication
Sequence conflicti1466 – 14661S → T in AAO44952. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY244709 mRNA. Translation: AAP20551.1.
AY173048 mRNA. Translation: AAO44952.1.
BC114063 mRNA. Translation: AAI14064.1.
RefSeqiNP_872592.2. NM_182651.2.
UniGeneiBt.108052.
Bt.48560.

Genome annotation databases

EnsembliENSBTAT00000003549; ENSBTAP00000003549; ENSBTAG00000002736.
GeneIDi281119.
KEGGibta:281119.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY244709 mRNA. Translation: AAP20551.1 .
AY173048 mRNA. Translation: AAO44952.1 .
BC114063 mRNA. Translation: AAI14064.1 .
RefSeqi NP_872592.2. NM_182651.2.
UniGenei Bt.108052.
Bt.48560.

3D structure databases

ProteinModelPortali Q24K09.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158481. 1 interaction.

Protein family/group databases

REBASEi 7406. M.BtaDnmt1AP.

Proteomic databases

PRIDEi Q24K09.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000003549 ; ENSBTAP00000003549 ; ENSBTAG00000002736 .
GeneIDi 281119.
KEGGi bta:281119.

Organism-specific databases

CTDi 1786.

Phylogenomic databases

eggNOGi COG0270.
GeneTreei ENSGT00390000005100.
HOGENOMi HOG000082497.
HOVERGENi HBG051384.
InParanoidi Q24K09.
KOi K00558.
OMAi CPNLAVK.
OrthoDBi EOG77WWBH.
TreeFami TF328926.

Enzyme and pathway databases

Reactomei REACT_207393. PRC2 methylates histones and DNA.
REACT_214253. NoRC negatively regulates rRNA expression.

Miscellaneous databases

NextBioi 20805188.

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. "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.

Entry informationi

Entry nameiDNMT1_BOVIN
AccessioniPrimary (citable) accession number: Q24K09
Secondary accession number(s): Q6Y856, Q7YS60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: April 18, 2006
Last modified: September 3, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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