CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004183
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA (cytosine-5)-methyltransferase 1 
Protein Synonyms/Alias
 Dnmt1; Met-1; DNA methyltransferase MmuI; DNA MTase MmuI; M.MmuI; MCMT 
Gene Name
 Dnmt1 
Gene Synonyms/Alias
 Dnmt; Met1; Uim 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
81SEEGYLAKVKSLLNKacetylation[1]
669CQQPECGKCKACKDMubiquitination[2]
671QPECGKCKACKDMVKubiquitination[2]
674CGKCKACKDMVKFGGubiquitination[2]
1326LAAAPGEKLPLFPEPubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 758 884 BAH 1.
 DOMAIN 976 1103 BAH 2.
 REPEAT 1112 1113 1.
 REPEAT 1114 1115 2.
 REPEAT 1116 1117 3.
 REPEAT 1118 1119 4.
 REPEAT 1120 1121 5.
 REPEAT 1122 1123 6.
 REPEAT 1124 1125 7; approximate.
 ZN_FING 649 695 CXXC-type.
 REGION 1 343 Interaction with the PRC2/EED-EZH2
 REGION 1 145 Interaction with DNMT3A (By similarity).
 REGION 1 120 Interaction with DMAP1.
 REGION 147 217 Interaction with DNMT3B (By similarity).
 REGION 161 172 Interaction with PCNA.
 REGION 305 609 Interaction with the PRC2/EED-EZH2
 REGION 328 556 DNA replication foci-targeting sequence
 REGION 696 813 Interaction with HDAC1.
 REGION 696 757 Autoinhibitory linker.
 REGION 1112 1125 7 X 2 AA tandem repeats of K-G.
 REGION 1124 1620 Interaction with the PRC2/EED-EZH2
 REGION 1142 1620 Catalytic.
 MOTIF 175 202 Nuclear localization signal (Potential).
 ACT_SITE 1229 1229
 METAL 359 359 Zinc (By similarity).
 METAL 362 362 Zinc (By similarity).
 METAL 420 420 Zinc (By similarity).
 METAL 424 424 Zinc (By similarity).
 MOD_RES 70 70 N6,N6-dimethyllysine; by EHMT2 (By
 MOD_RES 139 139 N6-methyllysine; by SETD7 (By
 MOD_RES 140 140 Phosphoserine; by PKB/AKT1 (By
 MOD_RES 146 146 Phosphoserine; by CK1.
 MOD_RES 150 150 Phosphoserine (By similarity).
 MOD_RES 152 152 Phosphoserine (By similarity).
 MOD_RES 171 171 N6-acetyllysine (By similarity).
 MOD_RES 255 255 N6-acetyllysine (By similarity).
 MOD_RES 285 285 Phosphoserine.
 MOD_RES 372 372 N6-acetyllysine (By similarity).
 MOD_RES 515 515 Phosphoserine.
 MOD_RES 717 717 Phosphoserine (By similarity).
 MOD_RES 735 735 Phosphoserine (By similarity).
 MOD_RES 752 752 N6-acetyllysine (By similarity).
 MOD_RES 895 895 N6-acetyllysine (By similarity).
 MOD_RES 961 961 N6-acetyllysine (By similarity).
 MOD_RES 965 965 N6-acetyllysine (By similarity).
 MOD_RES 979 979 N6-acetyllysine (By similarity).
 MOD_RES 1114 1114 N6-acetyllysine (By similarity).
 MOD_RES 1116 1116 N6-acetyllysine (By similarity).
 MOD_RES 1118 1118 N6-acetyllysine (By similarity).
 MOD_RES 1120 1120 N6-acetyllysine (By similarity).
 MOD_RES 1352 1352 N6-acetyllysine (By similarity).
 MOD_RES 1418 1418 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; Activator; Allosteric enzyme; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Metal-binding; Methylation; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1620 AA 
Protein Sequence
MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVREKLNLLH EFLQTEIKSQ 60
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGTHTLT QKANGCPANG SRPTWRAEMA 120
DSNRSPRSRP KPRGPRRSKS DSDTLSVETS PSSVATRRTT RQTTITAHFT KGPTKRKPKE 180
ESEEGNSAES AAEERDQDKK RRVVDTESGA AAAVEKLEEV TAGTQLGPEE PCEQEDDNRS 240
LRRHTRELSL RRKSKEDPDR EARPETHLDE DEDGKKDKRS SRPRSQPRDP AAKRRPKEAE 300
PEQVAPETPE DRDEDEREEK RRKTTRKKLE SHTVPVQSRS ERKAAQSKSV IPKINSPKCP 360
ECGQHLDDPN LKYQQHPEDA VDEPQMLTSE KLSIYDSTST WFDTYEDSPM HRFTSFSVYC 420
SRGHLCPVDT GLIEKNVELY FSGCAKAIHD ENPSMEGGIN GKNLGPINQW WLSGFDGGEK 480
VLIGFSTAFA EYILMEPSKE YEPIFGLMQE KIYISKIVVE FLQNNPDAVY EDLINKIETT 540
VPPSTINVNR FTEDSLLRHA QFVVSQVESY DEAKDDDETP IFLSPCMRAL IHLAGVSLGQ 600
RRATRRVMGA TKEKDKAPTK ATTTKLVYQI FDTFFSEQIE KYDKEDKENA MKRRRCGVCE 660
VCQQPECGKC KACKDMVKFG GTGRSKQACL KRRCPNLAVK EADDDEEADD DVSEMPSPKK 720
LHQGKKKKQN KDRISWLGQP MKIEENRTYY QKVSIDEEML EVGDCVSVIP DDSSKPLYLA 780
RVTALWEDKN GQMMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYK 840
APSENWAMEG GTDPETTLPG AEDGKTYFFQ LWYNQEYARF ESPPKTQPTE DNKHKFCLSC 900
IRLAELRQKE MPKVLEQIEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKVASPV 960
KRPKKDPVNE TLYPEHYRKY SDYIKGSNLD APEPYRIGRI KEIHCGKKKG KVNEADIKLR 1020
LYKFYRPENT HRSYNGSYHT DINMLYWSDE EAVVNFSDVQ GRCTVEYGED LLESIQDYSQ 1080
GGPDRFYFLE AYNSKTKNFE DPPNHARSPG NKGKGKGKGK GKGKHQVSEP KEPEAAIKLP 1140
KLRTLDVFSG CGGLSEGFHQ AGISETLWAI EMWDPAAQAF RLNNPGTTVF TEDCNVLLKL 1200
VMAGEVTNSL GQRLPQKGDV EMLCGGPPCQ GFSGMNRFNS RTYSKFKNSL VVSFLSYCDY 1260
YRPRFFLLEN VRNFVSYRRS MVLKLTLRCL VRMGYQCTFG VLQAGQYGVA QTRRRAIILA 1320
AAPGEKLPLF PEPLHVFAPR ACQLSVVVDD KKFVSNITRL SSGPFRTITV RDTMSDLPEI 1380
QNGASNSEIP YNGEPLSWFQ RQLRGSHYQP ILRDHICKDM SPLVAARMRH IPLFPGSDWR 1440
DLPNIQVRLG DGVIAHKLQY TFHDVKNGYS STGALRGVCS CAEGKACDPE SRQFSTLIPW 1500
CLPHTGNRHN HWAGLYGRLE WDGFFSTTVT NPEPMGKQGR VLHPEQHRVV SVRECARSQG 1560
FPDSYRFFGN ILDRHRQVGN AVPPPLAKAI GLEIKLCLLS SARESASAAV KAKEEAATKD 1620 
Gene Ontology
 GO:0005721; C:centromeric heterochromatin; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0005657; C:replication fork; IDA:MGI.
 GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
 GO:0008327; F:methyl-CpG binding; IDA:MGI.
 GO:0003723; F:RNA binding; IDA:MGI.
 GO:0008270; F:zinc ion binding; IDA:MGI.
 GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0016458; P:gene silencing; IDA:UniProtKB.
 GO:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
 GO:0051573; P:negative regulation of histone H3-K9 methylation; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
 GO:0010628; P:positive regulation of gene expression; IEA:Compara.
 GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Compara.
 GO:0042127; P:regulation of cell proliferation; IGI:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001025; 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. 
Pfam
 PF01426; BAH
 PF06464; DMAP_binding
 PF00145; DNA_methylase
 PF12047; DNMT1-RFD
 PF02008; zf-CXXC 
SMART
 SM00439; BAH 
PROSITE
 PS51038; BAH
 PS00094; C5_MTASE_1
 PS00095; C5_MTASE_2
 PS51058; ZF_CXXC 
PRINTS
 PR00105; C5METTRFRASE.