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Q9Z330

- DNMT1_RAT

UniProt

Q9Z330 - DNMT1_RAT

Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (21 Feb 2002)
      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 bindingi359 – 3591ZincBy similarity
    Metal bindingi362 – 3621ZincBy similarity
    Metal bindingi420 – 4201ZincBy similarity
    Metal bindingi424 – 4241ZincBy similarity
    Sitei515 – 5151Important for activityBy similarity
    Active sitei1231 – 12311PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri650 – 69647CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. DNA (cytosine-5-)-methyltransferase activity Source: RGD
    3. DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates Source: RGD
    4. double-stranded DNA binding Source: RGD
    5. histone deacetylase binding Source: RGD
    6. methyl-CpG binding Source: RGD
    7. protein domain specific binding Source: RGD
    8. S-adenosylmethionine-dependent methyltransferase activity Source: RGD
    9. unmethylated CpG binding Source: RGD
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. DNA methylation Source: RGD
    3. DNA methylation on cytosine within a CG sequence Source: RGD
    4. maintenance of DNA methylation Source: RGD
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. S-adenosylhomocysteine metabolic process Source: RGD
    7. S-adenosylmethioninamine metabolic process Source: RGD
    8. S-adenosylmethionine metabolic process Source: RGD
    9. 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

    BioCyciMetaCyc:MONOMER-8581.

    Protein family/group databases

    REBASEi3019. M.RnoDnmt1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37)
    Short name:
    Dnmt1
    Alternative name(s):
    DNA MTase RnoIP
    Short name:
    M.RnoIP
    DNA methyltransferase I
    MCMT
    Gene namesi
    Name:Dnmt1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620979. Dnmt1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: RGD
    2. protein complex Source: RGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16221622DNA (cytosine-5)-methyltransferase 1PRO_0000088036Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6,N6-dimethyllysine; by EHMT2By similarity
    Modified residuei139 – 1391N6-methyllysine; by SETD7By similarity
    Modified residuei140 – 1401Phosphoserine; by PKB/AKT1By similarity
    Modified residuei149 – 1491PhosphoserineBy similarity
    Modified residuei151 – 1511PhosphoserineBy similarity
    Modified residuei169 – 1691N6-acetyllysineBy similarity
    Modified residuei372 – 3721N6-acetyllysineBy similarity
    Modified residuei400 – 4001PhosphoserineBy similarity
    Modified residuei515 – 5151PhosphoserineBy similarity
    Modified residuei718 – 7181PhosphoserineBy similarity
    Modified residuei736 – 7361PhosphoserineBy similarity
    Modified residuei753 – 7531N6-acetyllysineBy similarity
    Modified residuei895 – 8951N6-acetyllysineBy similarity
    Modified residuei961 – 9611N6-acetyllysineBy similarity
    Modified residuei980 – 9801N6-acetyllysineBy similarity
    Modified residuei1116 – 11161N6-acetyllysineBy similarity
    Modified residuei1118 – 11181N6-acetyllysineBy similarity
    Modified residuei1120 – 11201N6-acetyllysineBy similarity
    Modified residuei1122 – 11221N6-acetyllysineBy similarity
    Modified residuei1124 – 11241N6-acetyllysineBy similarity
    Modified residuei1126 – 11261N6-acetyllysineBy similarity
    Modified residuei1354 – 13541N6-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-1116 and Lys-1354 by SIRT1 increases methyltransferase activity By similarity.By similarity
    Phosphorylation of Ser-151 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-140 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability By similarity.By similarity
    Methylation at Lys-139 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

    PaxDbiQ9Z330.
    PRIDEiQ9Z330.

    PTM databases

    PhosphoSiteiQ9Z330.

    Expressioni

    Tissue specificityi

    Isoforms 0 and 8 are highly expressed in placenta, brain, lung, spleen, kidney, heart, and at much lower levels in liver. Isoform 1 is expressed in cerebellum, isoform 2 in muscle and testis, isoform 3 in lung, isoform 4 in spleen and brain, and isoform 5 in brain.

    Gene expression databases

    GenevestigatoriQ9Z330.

    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. Binds annexin V Potential. 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 similarityCurated

    Protein-protein interaction databases

    IntActiQ9Z330. 2 interactions.
    STRINGi10116.ENSRNOP00000063029.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z330.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 10588DMAP-interactionAdd
    BLAST
    Domaini759 – 884126BAH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini977 – 1105129BAH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati1114 – 111521
    Repeati1116 – 111722
    Repeati1118 – 111923
    Repeati1120 – 112124
    Repeati1122 – 112325
    Repeati1124 – 112526
    Repeati1126 – 112727; approximate
    Domaini1144 – 1603460SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 342342Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni1 – 145145Interaction with DNMT3ABy similarityAdd
    BLAST
    Regioni146 – 21368Interaction with DNMT3BBy similarityAdd
    BLAST
    Regioni304 – 610307Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni327 – 556230DNA replication foci-targeting sequenceAdd
    BLAST
    Regioni697 – 75862Autoinhibitory linkerAdd
    BLAST
    Regioni1114 – 1127147 X 2 AA tandem repeats of K-GAdd
    BLAST
    Regioni1126 – 1622497Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni1144 – 1622479CatalyticAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi173 – 20028Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi149 – 1524Poly-Ser
    Compositional biasi269 – 2746Poly-Asp
    Compositional biasi726 – 7294Poly-Lys

    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 fingeri650 – 69647CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0270.
    HOGENOMiHOG000082497.
    HOVERGENiHBG051384.
    PhylomeDBiQ9Z330.

    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 (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9Z330-1) [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

    MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVKEKLNLLH     50
    EFLQTEIKSQ LCDLETKLHK EELSEEGYLA KVKTLLNKDL CLENGTLSLT 100
    QKANGCPANG SRPTWKAEMA DSNRSPRSRP KPRGPRRSKS DSETMIEASS 150
    SSVATRRTTR QTTITSHFKG PAKRKPKEDS EKGNANESAA EERDQDKKRR 200
    VAGTESRASR AGESVEKPER VRPGTQLCQE EQGEQEDDRR PRRQTRELAS 250
    RRKSREDPDR EARPGTHLDV DDDDEKDKRS SRPRSQPRDL ATKRRPKEEV 300
    EQITPEPPEG KDEDEREEKR RKTTRKKPEP LSIPVQSRVE RKASQGKASA 350
    IPKLNPPQCP ECGQYLDDPD LKYQQHPVDA VDEPQMLTNE ALSVFDSNSS 400
    WFETYDSSPM HKFTFFSVYC SRGHLCPVDT GLIEKNVELY FSGVAKAIHE 450
    ENPSVEGGVN GKNLGPINQW WISGFDGGEK ALIGFSTAFA EYFLMEPSPE 500
    YAPIFGLMQE KIYISKIVVE FLQSNPDAVY EDLINKIETT VPPSAINVNR 550
    FTEDSLLRHA QFVVSQVESY DDAKDDDETP IFLSPCMRSL IHLAGVSLGQ 600
    RRATRRTVIN SAKVKRKGPT KATTTKLVYQ IFDTFFSEQI EKDDKEDKEN 650
    TMKRRRCGVC EVCQQPECGK CKACKDMVKF GGTGRSKQAC LKRRCPNLAV 700
    KEADEDEEAD DDIPELPSPK KLHQGKKKKQ NKDRISWLGE PVKIEENRTY 750
    YWKVSIDEET LEVGDCVSVI PDDPSKPLYL ARVTALWEDK NGQMFHAHWF 800
    CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYR GPSPNWAMEG 850
    GMDPEAMLPG AEDGKTYFYQ FWYSQDYARF ESPPKTQPAE DNKHKFCLSC 900
    IRLAELRQKE MPKVLEQLEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF 950
    TFNIKMASPM KRSKRDPVNE NPVPRDTYRK YSDYIKGSNL DAPEPYRIGR 1000
    IKEIYCGKKK GGKVNEADIK IRLYKFYRPE NTHKSIQATY HADINLLYWS 1050
    DEEAVVDFSD VQGRCTVEYG EDLLESIQDY SQGGPDRFYF LEAYNSKTKS 1100
    FEDPPNHARS PGNKGKGKGK GKGKGKPQVS EPKEPEAAIK LPKLRTLDVF 1150
    SGCGGLTEGF HQAGISETLW AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL 1200
    KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN 1250
    SLVVSFLSYC DYYRPRFFLL ENVRNFVSFR RSMVLKLTLR CLVRMGYQCT 1300
    FGVLQAGQYG VAQTRRRAII LAAAPGEKLP LFPEPLHVFA PRACQLSVVV 1350
    DDKKFVSNIT RLSSGPFRTI TMRDTMSDLP EIQNGASAPE ISYKWRATVL 1400
    VPEAAARVAL PAHPQGPYPQ VHERAGGCRM RHIPLSPGSD WRDLPNIQVR 1450
    LRDGVITNKL RYTFHDTKNG CSSTGALRGV CSCAEGKTCD PASRQFNTLI 1500
    PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR 1550
    VVSVRECARS QGFPDTYRLF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL 1600
    LASAQESASA AVKGKEETTT ED 1622
    Length:1,622
    Mass (Da):182,774
    Last modified:February 21, 2002 - v2
    Checksum:iFCFA4AAA69E234BA
    GO
    Isoform 2 (identifier: Q9Z330-2) [UniParc]FASTAAdd to Basket

    Also known as: SF1

    The sequence of this isoform differs from the canonical sequence as follows:
         1323-1403: Missing.

    Show »
    Length:1,541
    Mass (Da):173,853
    Checksum:i9F1B86D1D13B45AB
    GO
    Isoform 3 (identifier: Q9Z330-3) [UniParc]FASTAAdd to Basket

    Also known as: SF2

    The sequence of this isoform differs from the canonical sequence as follows:
         1252-1482: Missing.

    Show »
    Length:1,391
    Mass (Da):156,880
    Checksum:i7F92F4E446BBD358
    GO
    Isoform 4 (identifier: Q9Z330-4) [UniParc]FASTAAdd to Basket

    Also known as: SF3

    The sequence of this isoform differs from the canonical sequence as follows:
         1226-1477: Missing.

    Show »
    Length:1,370
    Mass (Da):154,529
    Checksum:i9137E151ED3EED0B
    GO
    Isoform 5 (identifier: Q9Z330-5) [UniParc]FASTAAdd to Basket

    Also known as: SF4

    The sequence of this isoform differs from the canonical sequence as follows:
         1218-1430: QKGDVEMLCG...VHERAGGCRM → VC

    Show »
    Length:1,411
    Mass (Da):159,119
    Checksum:i961F53E307E2447E
    GO
    Isoform 6 (identifier: Q9Z330-6) [UniParc]FASTAAdd to Basket

    Also known as: SF5

    The sequence of this isoform differs from the canonical sequence as follows:
         1202-1410: Missing.

    Show »
    Length:1,413
    Mass (Da):159,421
    Checksum:iAE3F0037058D8167
    GO
    Isoform 7 (identifier: Q9Z330-7) [UniParc]FASTAAdd to Basket

    Also known as: SF6

    The sequence of this isoform differs from the canonical sequence as follows:
         1259-1481: Missing.

    Show »
    Length:1,399
    Mass (Da):157,713
    Checksum:i28C6F61C3085A7ED
    GO
    Isoform 8 (identifier: Q9Z330-8) [UniParc]FASTAAdd to Basket

    Also known as: SF7

    The sequence of this isoform differs from the canonical sequence as follows:
         1216-1504: Missing.

    Show »
    Length:1,333
    Mass (Da):150,479
    Checksum:iD8713CC5B748BFC2
    GO
    Isoform 9 (identifier: Q9Z330-9) [UniParc]FASTAAdd to Basket

    Also known as: short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.

    Show »
    Length:1,504
    Mass (Da):169,645
    Checksum:iC880386135929522
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 259AGSLPDHVR → RQARPRPCP in BAA20854. (PubMed:8667030)Curated
    Sequence conflicti189 – 1891A → V in BAA20854. (PubMed:8667030)Curated
    Sequence conflicti1276 – 12761F → S in BAA37118. (PubMed:9878564)Curated
    Sequence conflicti1300 – 13001T → I in AAD28102. (PubMed:9722504)Curated
    Sequence conflicti1372 – 13721M → V in BAA37118. (PubMed:9878564)Curated
    Sequence conflicti1394 – 142835KWRAT…RAGGC → NGEPQSWFQRQLRGSHYQPI LRDHICKDMSALVAA in BAA37118. (PubMed:9878564)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 9. CuratedVSP_005620Add
    BLAST
    Alternative sequencei1202 – 1410209Missing in isoform 6. CuratedVSP_005622Add
    BLAST
    Alternative sequencei1216 – 1504289Missing in isoform 8. CuratedVSP_005623Add
    BLAST
    Alternative sequencei1218 – 1430213QKGDV…GGCRM → VC in isoform 5. CuratedVSP_005621Add
    BLAST
    Alternative sequencei1226 – 1477252Missing in isoform 4. CuratedVSP_005624Add
    BLAST
    Alternative sequencei1252 – 1482231Missing in isoform 3. CuratedVSP_005625Add
    BLAST
    Alternative sequencei1259 – 1481223Missing in isoform 7. CuratedVSP_005626Add
    BLAST
    Alternative sequencei1323 – 140381Missing in isoform 2. CuratedVSP_005627Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012214 mRNA. Translation: BAA37118.1.
    AF116344 mRNA. Translation: AAD32541.1.
    AF116345 Genomic DNA. Translation: AAD32542.1.
    D64060 mRNA. Translation: BAA20854.1.
    AH007612 Genomic DNA. Translation: AAD28102.1.
    PIRiJE0378.
    UniGeneiRn.6955.

    Genome annotation databases

    UCSCiRGD:620979. rat. [Q9Z330-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012214 mRNA. Translation: BAA37118.1 .
    AF116344 mRNA. Translation: AAD32541.1 .
    AF116345 Genomic DNA. Translation: AAD32542.1 .
    D64060 mRNA. Translation: BAA20854.1 .
    AH007612 Genomic DNA. Translation: AAD28102.1 .
    PIRi JE0378.
    UniGenei Rn.6955.

    3D structure databases

    ProteinModelPortali Q9Z330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z330. 2 interactions.
    STRINGi 10116.ENSRNOP00000063029.

    Protein family/group databases

    REBASEi 3019. M.RnoDnmt1.

    PTM databases

    PhosphoSitei Q9Z330.

    Proteomic databases

    PaxDbi Q9Z330.
    PRIDEi Q9Z330.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:620979. rat. [Q9Z330-1 ]

    Organism-specific databases

    RGDi 620979. Dnmt1.

    Phylogenomic databases

    eggNOGi COG0270.
    HOGENOMi HOG000082497.
    HOVERGENi HBG051384.
    PhylomeDBi Q9Z330.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-8581.

    Miscellaneous databases

    PROi Q9Z330.

    Gene expression databases

    Genevestigatori Q9Z330.

    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. "Expression of rat DNA (cytosine-5) methyltransferase (DNA MTase) in rodent trophoblast giant cells: molecular cloning and characterization of rat DNA MTase."
      Kimura H., Takeda T., Tanaka S., Ogawa T., Shiota K.
      Biochem. Biophys. Res. Commun. 253:495-501(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
      Tissue: Brain and Placenta.
    2. "Multiple N-terminal isoforms of DNA (cytosine-5-)-methyltransferase in vivo."
      Deng J., Szyf M.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 9).
      Tissue: Brain.
    3. "Molecular cloning and characterization of annexin V-binding proteins with highly hydrophilic peptide structure."
      Ohsawa K., Imai Y., Ito D., Kohsaka S.
      J. Neurochem. 67:89-97(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-356, IN VITRO BINDING TO ANNEXIN V.
      Strain: Wistar.
      Tissue: Brain.
    4. "Multiple isoforms of DNA methyltransferase are encoded by the vertebrate cytosine DNA methyltransferase gene."
      Deng J., Szyf M.
      J. Biol. Chem. 273:22869-22872(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1169-1517 (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8).

    Entry informationi

    Entry nameiDNMT1_RAT
    AccessioniPrimary (citable) accession number: Q9Z330
    Secondary accession number(s): P70487
    , Q9R252, Q9WTX3, Q9WU57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2002
    Last sequence update: February 21, 2002
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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