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DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37) (CXXC-type zinc finger protein 9) (DNA methyltransferase HsaI) (DNA MTase HsaI) (M.HsaI) (MCMT)

 DNMT1_HUMAN             Reviewed;        1616 AA.
P26358; A0AV63; B7ZLW6; Q9UHG5; Q9ULA2; Q9UMZ6;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
25-OCT-2017, entry version 201.
RecName: Full=DNA (cytosine-5)-methyltransferase 1;
Short=Dnmt1;
EC=2.1.1.37;
AltName: Full=CXXC-type zinc finger protein 9;
AltName: Full=DNA methyltransferase HsaI;
Short=DNA MTase HsaI;
Short=M.HsaI;
AltName: Full=MCMT;
Name=DNMT1; Synonyms=AIM, CXXC9, DNMT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1594447; DOI=10.1093/nar/20.9.2287;
Yen R.-W.C., Vertino P.M., Nelkin B.D., Yu J.J., Deiry W.E.,
Cumaraswamy A., Lennon G.G., Trask B.J., Celano P., Baylin S.B.;
"Isolation and characterization of the cDNA encoding human DNA
methyltransferase.";
Nucleic Acids Res. 20:2287-2291(1992).
[2]
SEQUENCE REVISION TO N-TERMINUS.
PubMed=8940105; DOI=10.1074/jbc.271.49.31092;
Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.;
"New 5' regions of the murine and human genes for DNA (cytosine-5)-
methyltransferase.";
J. Biol. Chem. 271:31092-31097(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Prostatic carcinoma;
Li L.C., Au H., Chui R., Dahiya R.;
"Human DNA methyltransferase (DNMT1) is alternatively spliced.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=10449766; DOI=10.1073/pnas.96.17.9751;
Hsu D.-W., Lin M.-J., Lee T.-L., Wen S.-C., Chen X., Shen C.-K.J.;
"Two major forms of DNA (cytosine-5) methyltransferase in human
somatic tissues.";
Proc. Natl. Acad. Sci. U.S.A. 96:9751-9756(1999).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
PubMed=10753866; DOI=10.1074/jbc.275.15.10754;
Bonfils C., Beaulieu N., Chan E., Cotton-Montpetit J., MacLeod A.R.;
"Characterization of the human DNA methyltransferase splice variant
Dnmt1b.";
J. Biol. Chem. 275:10754-10760(2000).
[8]
INTERACTION WITH PCNA, AND MUTAGENESIS.
PubMed=9302295; DOI=10.1126/science.277.5334.1996;
Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
"Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
p21WAF1.";
Science 277:1996-2000(1997).
[9]
INTERACTION WITH MBD2 AND MBD3.
PubMed=10947852; DOI=10.1046/j.1365-2443.2000.00359.x;
Tatematsu K., Yamazaki T., Ishikawa F.;
"MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex
containing DNMT1 at the replication foci in late S phase.";
Genes Cells 5:677-688(2000).
[10]
INTERACTION WITH HDAC2 AND DMAP1.
PubMed=10888872; DOI=10.1038/77023;
Rountree M.R., Bachman K.E., Baylin S.B.;
"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
replication foci.";
Nat. Genet. 25:269-277(2000).
[11]
INTERACTION WITH RB1; E2F1 AND HDAC1.
PubMed=10888886; DOI=10.1038/77124;
Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
Wolffe A.P.;
"DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses
transcription from E2F-responsive promoters.";
Nat. Genet. 25:338-342(2000).
[12]
TISSUE SPECIFICITY.
PubMed=10325416; DOI=10.1093/nar/27.11.2291;
Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J.,
Gonzales F.A., Jones P.A.;
"The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate
mRNA expression in normal tissues and overexpression in tumors.";
Nucleic Acids Res. 27:2291-2298(1999).
[13]
INTERACTION WITH DNMT3A AND DNMT3B, AND SUBCELLULAR LOCATION.
PubMed=12145218; DOI=10.1093/emboj/cdf401;
Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.;
"Co-operation and communication between the human maintenance and de
novo DNA (cytosine-5) methyltransferases.";
EMBO J. 21:4183-4195(2002).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-714, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
FUNCTION, AND INTERACTION WITH EED AND EZH2.
PubMed=16357870; DOI=10.1038/nature04431;
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
"The Polycomb group protein EZH2 directly controls DNA methylation.";
Nature 439:871-874(2006).
[16]
ERRATUM.
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
Nature 446:824-824(2006).
[17]
DE NOVO DNA METHYLATION OF TARGET GENES.
PubMed=17200670; DOI=10.1038/ng1950;
Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M.,
Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E.,
Bergman Y., Simon I., Cedar H.;
"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes
for de novo methylation in cancer.";
Nat. Genet. 39:232-236(2007).
[18]
FUNCTION, AND MUTAGENESIS OF CYS-653; CYS-656; CYS-659; CYS-664;
CYS-667 AND CYS-670.
PubMed=18754681; DOI=10.1021/bi8011725;
Pradhan M., Esteve P.-O., Chin H.G., Samaranayke M., Kim G.-D.,
Pradhan S.;
"CXXC domain of human DNMT1 is essential for enzymatic activity.";
Biochemistry 47:10000-10009(2008).
[19]
FUNCTION.
PubMed=18413740; DOI=10.1158/0008-5472.CAN-07-6654;
Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S.,
Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P.,
Gius D.;
"DNA methyltransferase 1 and 3B activate BAG-1 expression via
recruitment of CTCFL/BORIS and modulation of promoter histone
methylation.";
Cancer Res. 68:2726-2735(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[21]
METHYLATION AT LYS-70, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18438403; DOI=10.1038/nchembio.88;
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Nat. Chem. Biol. 4:344-346(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-143; SER-152;
SER-154 AND SER-394, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[24]
SUMOYLATION, INTERACTION WITH UBC9, AND MUTAGENESIS OF CYS-1226.
PubMed=19450230; DOI=10.1042/BJ20090142;
Lee B., Muller M.T.;
"SUMOylation enhances DNA methyltransferase 1 activity.";
Biochem. J. 421:449-461(2009).
[25]
HOMODIMERIZATION.
PubMed=19173286; DOI=10.1002/jcb.22071;
Fellinger K., Rothbauer U., Felle M., Laengst G., Leonhardt H.;
"Dimerization of DNA methyltransferase 1 is mediated by its regulatory
domain.";
J. Cell. Biochem. 106:521-528(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-1111; LYS-1113 AND
LYS-1115, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-714, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
PHOSPHORYLATION AT SER-154.
PubMed=21565170; DOI=10.1016/j.bbrc.2011.04.115;
Lavoie G., St-Pierre Y.;
"Phosphorylation of human DNMT1: implication of cyclin-dependent
kinases.";
Biochem. Biophys. Res. Commun. 409:187-192(2011).
[31]
ACETYLATION AT LYS-160; LYS-188; LYS-259; LYS-366; LYS-749; LYS-891;
LYS-957; LYS-961; LYS-975; LYS-1054; LYS-1111; LYS-1113; LYS-1115;
LYS-1117; LYS-1349 AND LYS-1415, AND DEACETYLATION BY SIRT1.
PubMed=21947282; DOI=10.1128/MCB.06147-11;
Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N.,
Koomen J., Chen J., Lane W.S., Seto E.;
"SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and
alters its activities.";
Mol. Cell. Biol. 31:4720-4734(2011).
[32]
METHYLATION AT LYS-142, AND PHOSPHORYLATION AT SER-143.
PubMed=21151116; DOI=10.1038/nsmb.1939;
Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R.,
Feehery G.R., Cheng X., Pradhan S.;
"A methylation and phosphorylation switch between an adjacent lysine
and serine determines human DNMT1 stability.";
Nat. Struct. Mol. Biol. 18:42-48(2011).
[33]
INTERACTION WITH USP7 AND UHRF1.
PubMed=21745816; DOI=10.1093/nar/gkr528;
Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V.,
Dobner T., Kremmer E., Kappler R., Langst G.;
"The USP7/Dnmt1 complex stimulates the DNA methylation activity of
Dnmt1 and regulates the stability of UHRF1.";
Nucleic Acids Res. 39:8355-8365(2011).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-133 AND
SER-714, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; THR-137; SER-143;
SER-154; THR-166; SER-312; SER-394; SER-398; SER-549; SER-714 AND
SER-878, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
FUNCTION, POSSIBLE IDENTIFICATION IN A COREPRESSOR COMPLEX, AND
CHROMATIN-BINDING.
PubMed=24623306; DOI=10.7554/eLife.02313;
Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
"A KRAS-directed transcriptional silencing pathway that mediates the
CpG island methylator phenotype.";
Elife 3:E02313-E02313(2014).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1609, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-259 AND LYS-1609, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[40]
X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 351-600 IN COMPLEX WITH ZINC
IONS.
PubMed=21389349; DOI=10.1074/jbc.M110.209882;
Syeda F., Fagan R.L., Wean M., Avvakumov G.V., Walker J.R., Xue S.,
Dhe-Paganon S., Brenner C.;
"The replication focus targeting sequence (RFTS) domain is a DNA-
competitive inhibitor of Dnmt1.";
J. Biol. Chem. 286:15344-15351(2011).
[41]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 646-1600 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE AND DNA, AND AUTOINHIBITORY LINKER.
PubMed=21163962; DOI=10.1126/science.1195380;
Song J., Rechkoblit O., Bestor T.H., Patel D.J.;
"Structure of DNMT1-DNA complex reveals a role for autoinhibition in
maintenance DNA methylation.";
Science 331:1036-1040(2011).
[42]
VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495, AND CHARACTERIZATION OF
VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495.
PubMed=21532572; DOI=10.1038/ng.830;
Klein C.J., Botuyan M.V., Wu Y., Ward C.J., Nicholson G.A.,
Hammans S., Hojo K., Yamanishi H., Karpf A.R., Wallace D.C., Simon M.,
Lander C., Boardman L.A., Cunningham J.M., Smith G.E., Litchy W.J.,
Boes B., Atkinson E.J., Middha S., Dyck P.J.B., Parisi J.E., Mer G.,
Smith D.I., Dyck P.J.;
"Mutations in DNMT1 cause hereditary sensory neuropathy with dementia
and hearing loss.";
Nat. Genet. 43:595-600(2011).
[43]
VARIANTS ADCADN VAL-554; ALA-589 AND PHE-590.
PubMed=22328086; DOI=10.1093/hmg/dds035;
Winkelmann J., Lin L., Schormair B., Kornum B.R., Faraco J.,
Plazzi G., Melberg A., Cornelio F., Urban A.E., Pizza F., Poli F.,
Grubert F., Wieland T., Graf E., Hallmayer J., Strom T.M., Mignot E.;
"Mutations in DNMT1 cause autosomal dominant cerebellar ataxia,
deafness and narcolepsy.";
Hum. Mol. Genet. 21:2205-2210(2012).
-!- 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. Probably
forms a corepressor complex required for activated KRAS-mediated
promoter hypermethylation and transcriptional silencing of tumor
suppressor genes (TSGs) or other tumor-related genes in colorectal
cancer (CRC) cells (PubMed:24623306). Also required to maintain a
transcriptionally repressive state of genes in undifferentiated
embryonic stem cells (ESCs) (PubMed:24623306). Associates at
promoter regions of tumor suppressor genes (TSGs) leading to their
gene silencing (PubMed:24623306). Promotes tumor growth
(PubMed:24623306). {ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18754681,
ECO:0000269|PubMed:24623306}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
homocysteine + DNA containing 5-methylcytosine.
{ECO:0000255|PROSITE-ProRule:PRU10018}.
-!- SUBUNIT: Homodimer (PubMed:19173286). Forms a stable complex with
E2F1, BB1 and HDAC1 (PubMed:10888886). Forms a complex with DMAP1
and HDAC2, with direct interaction (PubMed:10888872). Interacts
with the PRC2/EED-EZH2 complex (PubMed:16357870). Probably part of
a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1
(PubMed:24623306). Interacts with UHRF1; promoting its recruitment
to hemimethylated DNA (PubMed:21745816). Interacts with USP7,
promoting its deubiquitination (PubMed:21745816). Interacts with
PCNA (PubMed:9302295). Interacts with MBD2 and MBD3
(PubMed:10947852). Interacts with DNMT3A and DNMT3B
(PubMed:12145218). Interacts with UBC9 (PubMed:19450230).
Interacts with CSNK1D (By similarity). Interacts with HDAC1 (By
similarity). Interacts with BAZ2A/TIP5 (By similarity).
{ECO:0000250|UniProtKB:P13864, ECO:0000269|PubMed:10888872,
ECO:0000269|PubMed:10888886, ECO:0000269|PubMed:10947852,
ECO:0000269|PubMed:12145218, ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:19173286, ECO:0000269|PubMed:19450230,
ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:24623306,
ECO:0000269|PubMed:9302295}.
-!- INTERACTION:
P31749:AKT1; NbExp=6; IntAct=EBI-719459, EBI-296087;
O75530:EED; NbExp=3; IntAct=EBI-719459, EBI-923794;
Q15910:EZH2; NbExp=8; IntAct=EBI-719459, EBI-530054;
Q77UV9:KIE-2 (xeno); NbExp=2; IntAct=EBI-719459, EBI-2608731;
P48552:NRIP1; NbExp=3; IntAct=EBI-719459, EBI-746484;
Q9QR71:ORF73 (xeno); NbExp=2; IntAct=EBI-719459, EBI-15602554;
P09874:PARP1; NbExp=6; IntAct=EBI-719459, EBI-355676;
Q8WTS6:SETD7; NbExp=9; IntAct=EBI-719459, EBI-1268586;
Q96EB6:SIRT1; NbExp=11; IntAct=EBI-719459, EBI-1802965;
Q96T88:UHRF1; NbExp=12; IntAct=EBI-719459, EBI-1548946;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12145218}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P26358-1; Sequence=Displayed;
Name=2; Synonyms=Dnmt1b;
IsoId=P26358-2; Sequence=VSP_005618;
Name=3;
IsoId=P26358-3; Sequence=VSP_005617;
-!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal tissues,
heart, kidney, placenta, peripheral blood mononuclear cells, and
expressed at lower levels in spleen, lung, brain, small intestine,
colon, liver, and skeletal muscle. Isoform 2 is less expressed
than isoform 1. {ECO:0000269|PubMed:10325416}.
-!- INDUCTION: Its abundance is reduced to non detectable levels at
the G0 phase of the cell cycle and is dramatically induced upon
entrance into the S-phase of the cell cycle.
-!- DOMAIN: The N-terminal part is required for homodimerization and
acts as a regulatory domain.
-!- 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. {ECO:0000269|PubMed:21163962}.
-!- PTM: Sumoylated; sumoylation increases activity.
{ECO:0000269|PubMed:19450230}.
-!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF,
regulates cell cycle G(2)/M transition. Deacetylation of Lys-1349
and Lys-1415 by SIRT1 increases methyltransferase activity.
{ECO:0000269|PubMed:21947282}.
-!- PTM: 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.
{ECO:0000269|PubMed:21151116, ECO:0000269|PubMed:21565170}.
-!- PTM: Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal
degradation. {ECO:0000269|PubMed:18438403,
ECO:0000269|PubMed:21151116}.
-!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
ubiquitination by UHRF1 by promoting deubiquitination and
preventing degradation by the proteasome. {ECO:0000250}.
-!- DISEASE: Neuropathy, hereditary sensory, 1E (HSN1E) [MIM:614116]:
A neurodegenerative disorder characterized by adult onset of
progressive peripheral sensory loss associated with progressive
hearing impairment and early-onset dementia.
{ECO:0000269|PubMed:21532572}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cerebellar ataxia, deafness, and narcolepsy, autosomal
dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic
disorder characterized by adult onset of progressive cerebellar
ataxia, narcolepsy, cataplexy, sensorineural deafness, and
dementia. More variable features include optic atrophy, sensory
neuropathy, psychosis, and depression.
{ECO:0000269|PubMed:22328086}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. C5-methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
-!- SEQUENCE CAUTION:
Sequence=AAD54507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DNMT1ID40347ch19p13.html";
-----------------------------------------------------------------------
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EMBL; X63692; CAA45219.1; -; mRNA.
EMBL; AF180682; AAF23609.1; -; mRNA.
EMBL; AC010077; AAD54507.1; ALT_SEQ; Genomic_DNA.
EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC126227; AAI26228.1; -; mRNA.
EMBL; BC144093; AAI44094.1; -; mRNA.
EMBL; AH008119; AAD51619.1; -; Genomic_DNA.
CCDS; CCDS12228.1; -. [P26358-1]
CCDS; CCDS45958.1; -. [P26358-2]
PIR; S22610; S22610.
RefSeq; NP_001124295.1; NM_001130823.2. [P26358-2]
RefSeq; NP_001305659.1; NM_001318730.1.
RefSeq; NP_001305660.1; NM_001318731.1.
RefSeq; NP_001370.1; NM_001379.3. [P26358-1]
UniGene; Hs.202672; -.
PDB; 3EPZ; X-ray; 2.31 A; A/B=351-600.
PDB; 3PTA; X-ray; 3.60 A; A=646-1600.
PDB; 3SWR; X-ray; 2.49 A; A=601-1600.
PDB; 4WXX; X-ray; 2.62 A; A/B=351-1600.
PDB; 4YOC; X-ray; 2.92 A; A=600-1600.
PDB; 4Z96; X-ray; 2.85 A; C=1098-1129.
PDB; 4Z97; X-ray; 3.00 A; C=1098-1129.
PDBsum; 3EPZ; -.
PDBsum; 3PTA; -.
PDBsum; 3SWR; -.
PDBsum; 4WXX; -.
PDBsum; 4YOC; -.
PDBsum; 4Z96; -.
PDBsum; 4Z97; -.
ProteinModelPortal; P26358; -.
SMR; P26358; -.
BioGrid; 108123; 92.
CORUM; P26358; -.
DIP; DIP-39693N; -.
ELM; P26358; -.
IntAct; P26358; 33.
MINT; MINT-232346; -.
STRING; 9606.ENSP00000352516; -.
BindingDB; P26358; -.
ChEMBL; CHEMBL1993; -.
DrugBank; DB00928; Azacitidine.
DrugBank; DB01262; Decitabine.
DrugBank; DB01099; Flucytosine.
DrugBank; DB01035; Procainamide.
GuidetoPHARMACOLOGY; 2605; -.
REBASE; 1161; M.HsaDnmt1A.
iPTMnet; P26358; -.
PhosphoSitePlus; P26358; -.
BioMuta; DNMT1; -.
DMDM; 12231019; -.
EPD; P26358; -.
MaxQB; P26358; -.
PaxDb; P26358; -.
PeptideAtlas; P26358; -.
PRIDE; P26358; -.
Ensembl; ENST00000340748; ENSP00000345739; ENSG00000130816. [P26358-1]
Ensembl; ENST00000359526; ENSP00000352516; ENSG00000130816. [P26358-2]
Ensembl; ENST00000540357; ENSP00000440457; ENSG00000130816. [P26358-3]
GeneID; 1786; -.
KEGG; hsa:1786; -.
UCSC; uc002mng.4; human. [P26358-1]
CTD; 1786; -.
DisGeNET; 1786; -.
EuPathDB; HostDB:ENSG00000130816.14; -.
GeneCards; DNMT1; -.
GeneReviews; DNMT1; -.
HGNC; HGNC:2976; DNMT1.
HPA; CAB005876; -.
HPA; HPA002694; -.
MalaCards; DNMT1; -.
MIM; 126375; gene.
MIM; 604121; phenotype.
MIM; 614116; phenotype.
neXtProt; NX_P26358; -.
OpenTargets; ENSG00000130816; -.
Orphanet; 314404; Autosomal dominant cerebellar ataxia, deafness and narcolepsy.
PharmGKB; PA27443; -.
eggNOG; ENOG410IF68; Eukaryota.
eggNOG; COG0270; LUCA.
GeneTree; ENSGT00390000005100; -.
HOGENOM; HOG000082497; -.
HOVERGEN; HBG051384; -.
InParanoid; P26358; -.
KO; K00558; -.
OMA; WAMEGGM; -.
OrthoDB; EOG091G02YU; -.
PhylomeDB; P26358; -.
TreeFam; TF328926; -.
BRENDA; 2.1.1.37; 2681.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5334118; DNA methylation.
SIGNOR; P26358; -.
ChiTaRS; DNMT1; human.
EvolutionaryTrace; P26358; -.
GeneWiki; DNMT1; -.
GenomeRNAi; 1786; -.
PRO; PR:P26358; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130816; -.
CleanEx; HS_DNMT1; -.
ExpressionAtlas; P26358; baseline and differential.
Genevisible; P26358; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
GO; GO:0005657; C:replication fork; IEA:Ensembl.
GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0009008; F:DNA-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
GO; GO:0043045; P:DNA methylation involved in embryo development; IEA:Ensembl.
GO; GO:0016458; P:gene silencing; IEA:Ensembl.
GO; GO:0010216; P:maintenance of DNA methylation; IDA:UniProtKB.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR001025; BAH_dom.
InterPro; IPR018117; C5_DNA_meth_AS.
InterPro; IPR001525; C5_MeTfrase.
InterPro; IPR031303; C5_meth_CS.
InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
InterPro; IPR010506; DMAP1-bd.
InterPro; IPR017198; DNMT1-like.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR002857; Znf_CXXC.
Pfam; PF01426; BAH; 2.
Pfam; PF06464; DMAP_binding; 1.
Pfam; PF12047; DNMT1-RFD; 1.
Pfam; PF02008; zf-CXXC; 1.
PIRSF; PIRSF037404; DNMT1; 1.
PRINTS; PR00105; C5METTRFRASE.
SMART; SM00439; BAH; 2.
SMART; SM01137; DMAP_binding; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51038; BAH; 2.
PROSITE; PS00094; C5_MTASE_1; 1.
PROSITE; PS00095; C5_MTASE_2; 1.
PROSITE; PS51679; SAM_MT_C5; 1.
PROSITE; PS51058; ZF_CXXC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Chromatin regulator; Complete proteome; Deafness; Disease mutation;
DNA-binding; Isopeptide bond; Metal-binding; Methylation;
Methyltransferase; Neuropathy; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 1616 DNA (cytosine-5)-methyltransferase 1.
/FTId=PRO_0000088034.
DOMAIN 18 103 DMAP-interaction.
DOMAIN 755 880 BAH 1. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
DOMAIN 972 1100 BAH 2. {ECO:0000255|PROSITE-
ProRule:PRU00370}.
REPEAT 1109 1110 1.
REPEAT 1111 1112 2.
REPEAT 1113 1114 3.
REPEAT 1115 1116 4.
REPEAT 1117 1118 5.
REPEAT 1119 1120 6; approximate.
DOMAIN 1139 1599 SAM-dependent MTase C5-type.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
ZN_FING 646 692 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
REGION 1 336 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 1 148 Interaction with DNMT3A.
{ECO:0000269|PubMed:12145218}.
REGION 1 120 Interaction with DMAP1.
{ECO:0000269|PubMed:10888872}.
REGION 149 217 Interaction with DNMT3B.
{ECO:0000269|PubMed:12145218}.
REGION 163 174 Interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
REGION 308 606 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 310 502 Homodimerization.
REGION 331 550 DNA replication foci-targeting sequence.
{ECO:0000250}.
REGION 651 697 Required for activity.
REGION 693 754 Autoinhibitory linker.
REGION 1109 1120 6 X 2 AA tandem repeats of K-G.
REGION 1121 1616 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 1139 1616 Catalytic.
REGION 1150 1151 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P13864}.
REGION 1168 1169 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3PTA,
ECO:0000269|PubMed:21163962}.
REGION 1190 1191 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:P13864}.
MOTIF 177 205 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 1226 1226
METAL 353 353 Zinc.
METAL 356 356 Zinc.
METAL 414 414 Zinc.
METAL 418 418 Zinc.
BINDING 1146 1146 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P13864}.
BINDING 1191 1191 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3PTA,
ECO:0000269|PubMed:21163962}.
BINDING 1578 1578 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3PTA,
ECO:0000269|PubMed:21163962}.
BINDING 1580 1580 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250|UniProtKB:P13864}.
SITE 509 509 Important for activity. {ECO:0000250}.
MOD_RES 70 70 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:18438403}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 137 137 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 142 142 N6-methyllysine; by SETD7.
{ECO:0000269|PubMed:21151116}.
MOD_RES 143 143 Phosphoserine; by PKB/AKT1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21151116}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21565170}.
MOD_RES 160 160 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 166 166 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 173 173 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 188 188 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 259 259 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:21947282}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 366 366 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 749 749 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 878 878 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 891 891 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 957 957 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 961 961 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 975 975 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 1054 1054 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 1111 1111 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:21947282}.
MOD_RES 1113 1113 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:21947282}.
MOD_RES 1115 1115 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:21947282}.
MOD_RES 1117 1117 N6-acetyllysine; by EHMT2.
{ECO:0000269|PubMed:21947282}.
MOD_RES 1119 1119 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 1121 1121 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13864}.
MOD_RES 1349 1349 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
MOD_RES 1415 1415 N6-acetyllysine.
{ECO:0000269|PubMed:21947282}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 1609 1609 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 336 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_005617.
VAR_SEQ 149 149 P -> RSRDPPASASQVTGIRA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_005618.
VARIANT 97 97 H -> R (in dbSNP:rs16999593).
/FTId=VAR_024605.
VARIANT 311 311 I -> V (in dbSNP:rs2228612).
/FTId=VAR_051960.
VARIANT 490 491 DP -> EY (in HSN1E; unstable protein with
decreased enzymatic activity and impaired
heterochromatin binding ability after the
S phase; dbSNP:rs199473691).
/FTId=VAR_065965.
VARIANT 495 495 Y -> C (in HSN1E; unstable protein with
decreased enzymatic activity and impaired
heterochromatin binding ability after the
S phase; dbSNP:rs199473690).
{ECO:0000269|PubMed:21532572}.
/FTId=VAR_065966.
VARIANT 554 554 A -> V (in ADCADN; dbSNP:rs397509392).
{ECO:0000269|PubMed:22328086}.
/FTId=VAR_070055.
VARIANT 589 589 G -> A (in ADCADN; dbSNP:rs397509393).
{ECO:0000269|PubMed:22328086}.
/FTId=VAR_070056.
VARIANT 590 590 V -> F (in ADCADN; dbSNP:rs397509391).
{ECO:0000269|PubMed:22328086}.
/FTId=VAR_070057.
MUTAGEN 163 163 R->A: Abolishes interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 164 164 Q->A: Abolishes interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 166 166 T->A: Abolishes interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 167 167 I->A: Abolishes interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 169 169 S->A: No loss of interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 170 170 H->V: Abolishes interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 171 171 F->V: Abolishes interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 172 172 A->S: No loss of interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 173 173 K->A: No loss of interaction with PCNA.
{ECO:0000269|PubMed:9302295}.
MUTAGEN 653 653 C->G: Reduces activity about 10-fold;
when associated with G-656; G-659; G-664;
G-667 and G-670.
{ECO:0000269|PubMed:18754681}.
MUTAGEN 656 656 C->G: Reduces activity about 10-fold;
when associated with G-653; G-659; G-664;
G-667 and G-670.
{ECO:0000269|PubMed:18754681}.
MUTAGEN 659 659 C->G: Reduces activity about 10-fold;
when associated with G-653; G-656; G-664;
G-667 and G-670.
{ECO:0000269|PubMed:18754681}.
MUTAGEN 664 664 C->F: Reduces activity about 10-fold;
when associated with G-653; G-656; G-659;
G-667 and G-670.
{ECO:0000269|PubMed:18754681}.
MUTAGEN 667 667 C->G: Reduces activity about 10-fold;
when associated with G-653; G-656; G-659;
G-664 and G-670.
{ECO:0000269|PubMed:18754681}.
MUTAGEN 670 670 C->G: Reduces activity about 10-fold;
when associated with G-653; G-656; G-659;
G-664 and G-667.
{ECO:0000269|PubMed:18754681}.
MUTAGEN 1226 1226 C->A: Loss of activity.
{ECO:0000269|PubMed:19450230}.
TURN 354 356 {ECO:0000244|PDB:3EPZ}.
STRAND 359 364 {ECO:0000244|PDB:4WXX}.
HELIX 377 389 {ECO:0000244|PDB:3EPZ}.
STRAND 405 413 {ECO:0000244|PDB:3EPZ}.
STRAND 422 425 {ECO:0000244|PDB:3EPZ}.
TURN 426 430 {ECO:0000244|PDB:3EPZ}.
STRAND 434 441 {ECO:0000244|PDB:3EPZ}.
STRAND 453 458 {ECO:0000244|PDB:3EPZ}.
STRAND 462 467 {ECO:0000244|PDB:3EPZ}.
STRAND 476 480 {ECO:0000244|PDB:3EPZ}.
STRAND 485 488 {ECO:0000244|PDB:3EPZ}.
TURN 493 495 {ECO:0000244|PDB:3EPZ}.
HELIX 496 499 {ECO:0000244|PDB:3EPZ}.
HELIX 504 518 {ECO:0000244|PDB:3EPZ}.
HELIX 524 533 {ECO:0000244|PDB:3EPZ}.
HELIX 538 540 {ECO:0000244|PDB:3EPZ}.
HELIX 547 551 {ECO:0000244|PDB:3EPZ}.
HELIX 554 567 {ECO:0000244|PDB:3EPZ}.
HELIX 575 577 {ECO:0000244|PDB:3EPZ}.
HELIX 579 587 {ECO:0000244|PDB:3EPZ}.
HELIX 592 598 {ECO:0000244|PDB:3EPZ}.
HELIX 622 629 {ECO:0000244|PDB:3SWR}.
TURN 657 659 {ECO:0000244|PDB:3SWR}.
HELIX 670 672 {ECO:0000244|PDB:3SWR}.
TURN 674 677 {ECO:0000244|PDB:4WXX}.
HELIX 687 689 {ECO:0000244|PDB:3SWR}.
HELIX 692 703 {ECO:0000244|PDB:4WXX}.
STRAND 731 735 {ECO:0000244|PDB:3SWR}.
STRAND 738 740 {ECO:0000244|PDB:4WXX}.
STRAND 744 746 {ECO:0000244|PDB:3SWR}.
STRAND 748 752 {ECO:0000244|PDB:3SWR}.
STRAND 755 758 {ECO:0000244|PDB:3SWR}.
STRAND 762 765 {ECO:0000244|PDB:3SWR}.
STRAND 767 769 {ECO:0000244|PDB:3SWR}.
STRAND 775 785 {ECO:0000244|PDB:3SWR}.
TURN 786 788 {ECO:0000244|PDB:3SWR}.
STRAND 789 799 {ECO:0000244|PDB:3SWR}.
HELIX 800 802 {ECO:0000244|PDB:3SWR}.
STRAND 803 805 {ECO:0000244|PDB:4YOC}.
HELIX 806 808 {ECO:0000244|PDB:3SWR}.
STRAND 813 824 {ECO:0000244|PDB:3SWR}.
HELIX 825 827 {ECO:0000244|PDB:3SWR}.
STRAND 828 832 {ECO:0000244|PDB:3SWR}.
STRAND 834 836 {ECO:0000244|PDB:3SWR}.
HELIX 843 845 {ECO:0000244|PDB:3SWR}.
TURN 851 853 {ECO:0000244|PDB:4WXX}.
HELIX 856 860 {ECO:0000244|PDB:3SWR}.
STRAND 862 870 {ECO:0000244|PDB:3SWR}.
TURN 871 874 {ECO:0000244|PDB:3SWR}.
STRAND 875 877 {ECO:0000244|PDB:3SWR}.
STRAND 886 888 {ECO:0000244|PDB:4YOC}.
TURN 889 891 {ECO:0000244|PDB:3SWR}.
HELIX 894 905 {ECO:0000244|PDB:3SWR}.
STRAND 912 916 {ECO:0000244|PDB:3SWR}.
STRAND 921 928 {ECO:0000244|PDB:3SWR}.
STRAND 931 934 {ECO:0000244|PDB:3SWR}.
STRAND 938 941 {ECO:0000244|PDB:3SWR}.
TURN 966 968 {ECO:0000244|PDB:3SWR}.
HELIX 973 975 {ECO:0000244|PDB:3SWR}.
HELIX 976 980 {ECO:0000244|PDB:3SWR}.
STRAND 992 1001 {ECO:0000244|PDB:3SWR}.
STRAND 1005 1008 {ECO:0000244|PDB:3SWR}.
STRAND 1015 1020 {ECO:0000244|PDB:3SWR}.
HELIX 1024 1026 {ECO:0000244|PDB:3SWR}.
HELIX 1031 1034 {ECO:0000244|PDB:3SWR}.
STRAND 1035 1037 {ECO:0000244|PDB:3SWR}.
STRAND 1041 1044 {ECO:0000244|PDB:3SWR}.
STRAND 1048 1052 {ECO:0000244|PDB:3SWR}.
HELIX 1053 1055 {ECO:0000244|PDB:3SWR}.
STRAND 1058 1064 {ECO:0000244|PDB:3SWR}.
HELIX 1065 1067 {ECO:0000244|PDB:3SWR}.
HELIX 1072 1077 {ECO:0000244|PDB:3SWR}.
STRAND 1079 1090 {ECO:0000244|PDB:3SWR}.
TURN 1091 1094 {ECO:0000244|PDB:3SWR}.
STRAND 1095 1097 {ECO:0000244|PDB:3SWR}.
HELIX 1101 1103 {ECO:0000244|PDB:4WXX}.
STRAND 1139 1145 {ECO:0000244|PDB:3SWR}.
HELIX 1150 1158 {ECO:0000244|PDB:3SWR}.
STRAND 1160 1167 {ECO:0000244|PDB:3SWR}.
HELIX 1171 1180 {ECO:0000244|PDB:3SWR}.
STRAND 1184 1187 {ECO:0000244|PDB:3SWR}.
HELIX 1191 1200 {ECO:0000244|PDB:3SWR}.
TURN 1214 1216 {ECO:0000244|PDB:3SWR}.
STRAND 1218 1222 {ECO:0000244|PDB:3SWR}.
STRAND 1231 1233 {ECO:0000244|PDB:3SWR}.
HELIX 1237 1243 {ECO:0000244|PDB:3SWR}.
HELIX 1247 1258 {ECO:0000244|PDB:3SWR}.
STRAND 1261 1268 {ECO:0000244|PDB:3SWR}.
HELIX 1269 1272 {ECO:0000244|PDB:3SWR}.
HELIX 1275 1277 {ECO:0000244|PDB:3SWR}.
HELIX 1278 1289 {ECO:0000244|PDB:3SWR}.
STRAND 1293 1300 {ECO:0000244|PDB:3SWR}.
HELIX 1301 1304 {ECO:0000244|PDB:3SWR}.
STRAND 1311 1318 {ECO:0000244|PDB:3SWR}.
HELIX 1336 1338 {ECO:0000244|PDB:3SWR}.
STRAND 1343 1345 {ECO:0000244|PDB:3SWR}.
STRAND 1348 1350 {ECO:0000244|PDB:3SWR}.
HELIX 1367 1371 {ECO:0000244|PDB:3SWR}.
STRAND 1384 1386 {ECO:0000244|PDB:3SWR}.
HELIX 1395 1401 {ECO:0000244|PDB:3SWR}.
HELIX 1419 1426 {ECO:0000244|PDB:3SWR}.
HELIX 1436 1438 {ECO:0000244|PDB:3SWR}.
STRAND 1451 1453 {ECO:0000244|PDB:3SWR}.
TURN 1462 1464 {ECO:0000244|PDB:3SWR}.
STRAND 1474 1476 {ECO:0000244|PDB:4YOC}.
HELIX 1477 1479 {ECO:0000244|PDB:3SWR}.
STRAND 1480 1482 {ECO:0000244|PDB:3SWR}.
HELIX 1487 1489 {ECO:0000244|PDB:3SWR}.
STRAND 1493 1496 {ECO:0000244|PDB:3SWR}.
HELIX 1499 1503 {ECO:0000244|PDB:3SWR}.
HELIX 1504 1506 {ECO:0000244|PDB:3SWR}.
HELIX 1508 1510 {ECO:0000244|PDB:3SWR}.
TURN 1511 1514 {ECO:0000244|PDB:3SWR}.
STRAND 1523 1525 {ECO:0000244|PDB:3SWR}.
STRAND 1534 1536 {ECO:0000244|PDB:4WXX}.
STRAND 1542 1547 {ECO:0000244|PDB:3SWR}.
HELIX 1550 1556 {ECO:0000244|PDB:3SWR}.
HELIX 1569 1578 {ECO:0000244|PDB:3SWR}.
HELIX 1582 1598 {ECO:0000244|PDB:3SWR}.
SEQUENCE 1616 AA; 183165 MW; 1E833192D22AFA5B CRC64;
MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ
LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN REVNGRLENG NQARSEARRV
GMADANSPPK PLSKPRTPRR SKSDGEAKPE PSPSPRITRK STRQTTITSH FAKGPAKRKP
QEESERAKSD ESIKEEDKDQ DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK
EEKRLRSQTK EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE
EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP PKCIQCGQYL
DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE ALPQHKLTCF SVYCKHGHLC
PIDTGLIEKN IELFFSGSAK PIYDDDPSLE GGVNGKNLGP INEWWITGFD GGEKALIGFS
TSFAEYILMD PSPEYAPIFG LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL
NLNRFTEDSL LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR
RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR RRCGVCEVCQ
QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD DDEEVDDNIP EMPSPKKMHQ
GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV CIDAETLEVG DCVSVIPDDS SKPLYLARVT
ALWEDSSNGQ MFHAHWFCAG TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS
ENWAMEGGMD PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA
EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI KLSSPVKRPR
KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF CPKKSNGRPN ETDIKIRVNK
FYRPENTHKS TPASYHADIN LLYWSDEEAV VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP
NRFYFLEAYN AKSKSFEDPP NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR
TLDVFSGCGG LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA
GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS FLSYCDYYRP
RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ AGQYGVAQTR RRAIILAAAP
GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF VSNITRLSSG PFRTITVRDT MSDLPEVRNG
ASALEISYNG EPQSWFQRQL RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP
NIEVRLSDGT MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL
PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV RECARSQGFP
DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA RESASAKIKE EEAAKD


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