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Q24K09

- DNMT1_BOVIN

UniProt

Q24K09 - DNMT1_BOVIN

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
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (18 Apr 2006)
      Previous versions | rss
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    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.By similarity

    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 bindingi351 – 3511ZincBy similarity
    Metal bindingi354 – 3541ZincBy similarity
    Metal bindingi412 – 4121ZincBy similarity
    Metal bindingi416 – 4161ZincBy similarity
    Sitei507 – 5071Important for activityBy similarity
    Active sitei1223 – 12231PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri643 – 68947CXXC-typePROSITE-ProRule annotationAdd
    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

    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. nucleus Source: UniProtKB-SubCell
    2. pericentric heterochromatin Source: Ensembl
    3. replication fork Source: Ensembl

    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 EHMT2By similarity
    Modified residuei133 – 1331PhosphoserineBy similarity
    Modified residuei142 – 1421N6-methyllysine; by SETD7By similarity
    Modified residuei143 – 1431Phosphoserine; by PKB/AKT1By similarity
    Modified residuei152 – 1521PhosphoserineBy similarity
    Modified residuei154 – 1541PhosphoserineBy similarity
    Modified residuei160 – 1601N6-acetyllysineBy similarity
    Modified residuei188 – 1881N6-acetyllysineBy similarity
    Modified residuei257 – 2571N6-acetyllysineBy similarity
    Modified residuei392 – 3921PhosphoserineBy similarity
    Modified residuei507 – 5071PhosphoserineBy similarity
    Modified residuei711 – 7111PhosphoserineBy similarity
    Modified residuei729 – 7291PhosphoserineBy similarity
    Modified residuei746 – 7461N6-acetyllysineBy similarity
    Modified residuei888 – 8881N6-acetyllysineBy similarity
    Modified residuei954 – 9541N6-acetyllysineBy similarity
    Modified residuei958 – 9581N6-acetyllysineBy similarity
    Modified residuei972 – 9721N6-acetyllysineBy similarity
    Modified residuei1051 – 10511N6-acetyllysineBy similarity
    Modified residuei1108 – 11081N6-acetyllysineBy similarity
    Modified residuei1110 – 11101N6-acetyllysineBy similarity
    Modified residuei1112 – 11121N6-acetyllysineBy similarity
    Modified residuei1114 – 11141N6-acetyllysineBy similarity
    Modified residuei1118 – 11181N6-acetyllysineBy similarity
    Modified residuei1346 – 13461N6-acetyllysineBy similarity
    Modified residuei1412 – 14121N6-acetyllysineBy 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.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.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.By similarity

    Protein-protein interaction databases

    BioGridi158481. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ24K09.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 334334Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni1 – 148148Interaction with DNMT3ABy similarityAdd
    BLAST
    Regioni1 – 120120Interaction with DMAP1By similarityAdd
    BLAST
    Regioni149 – 21668Interaction with DNMT3BBy similarityAdd
    BLAST
    Regioni163 – 17412Interaction with PCNABy similarityAdd
    BLAST
    Regioni306 – 603298Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni329 – 548220DNA replication foci-targeting sequenceBy similarityAdd
    BLAST
    Regioni690 – 75162Autoinhibitory linkerAdd
    BLAST
    Regioni1106 – 1115105 X 2 AA tandem repeats of K-G
    Regioni1118 – 1611494Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni1136 – 1611476CatalyticBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi177 – 20428Nuclear 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.By similarity

    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 fingeri643 – 68947CXXC-typePROSITE-ProRule annotationAdd
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti655 – 6551I → V in AAO44952. 1 PublicationCurated
    Sequence conflicti716 – 7161H → R in AAO44952. 1 PublicationCurated
    Sequence conflicti777 – 7771T → A in AAO44952. 1 PublicationCurated
    Sequence conflicti1176 – 11761L → F in AAP20551. (PubMed:12971987)Curated
    Sequence conflicti1186 – 11861E → K in AAP20551. (PubMed:12971987)Curated
    Sequence conflicti1192 – 11921L → V in AAP20551. (PubMed:12971987)Curated
    Sequence conflicti1209 – 12091P → L in AAP20551. (PubMed:12971987)Curated
    Sequence conflicti1287 – 12871M → R in AAP20551. (PubMed:12971987)Curated
    Sequence conflicti1387 – 13871G → R in AAP20551. (PubMed:12971987)Curated
    Sequence conflicti1405 – 14051I → T in AAO44952. 1 PublicationCurated
    Sequence conflicti1466 – 14661S → T in AAO44952. 1 PublicationCurated

    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

    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: October 1, 2014
    This is version 75 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