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Database: UniProt
Entry: P26358
LinkDB: P26358
Original site: P26358 
ID   DNMT1_HUMAN             Reviewed;        1616 AA.
AC   P26358; A0AV63; B7ZLW6; Q9UHG5; Q9ULA2; Q9UMZ6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   02-JUN-2021, entry version 230.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE            Short=Dnmt1;
DE            EC=2.1.1.37;
DE   AltName: Full=CXXC-type zinc finger protein 9;
DE   AltName: Full=DNA methyltransferase HsaI;
DE            Short=DNA MTase HsaI;
DE            Short=M.HsaI;
DE   AltName: Full=MCMT;
GN   Name=DNMT1; Synonyms=AIM, CXXC9, DNMT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1594447; DOI=10.1093/nar/20.9.2287;
RA   Yen R.-W.C., Vertino P.M., Nelkin B.D., Yu J.J., Deiry W.E.,
RA   Cumaraswamy A., Lennon G.G., Trask B.J., Celano P., Baylin S.B.;
RT   "Isolation and characterization of the cDNA encoding human DNA
RT   methyltransferase.";
RL   Nucleic Acids Res. 20:2287-2291(1992).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=8940105; DOI=10.1074/jbc.271.49.31092;
RA   Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.;
RT   "New 5' regions of the murine and human genes for DNA (cytosine-5)-
RT   methyltransferase.";
RL   J. Biol. Chem. 271:31092-31097(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Prostatic carcinoma;
RA   Li L.C., Au H., Chui R., Dahiya R.;
RT   "Human DNA methyltransferase (DNMT1) is alternatively spliced.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=10449766; DOI=10.1073/pnas.96.17.9751;
RA   Hsu D.-W., Lin M.-J., Lee T.-L., Wen S.-C., Chen X., Shen C.-K.J.;
RT   "Two major forms of DNA (cytosine-5) methyltransferase in human somatic
RT   tissues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9751-9756(1999).
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=10753866; DOI=10.1074/jbc.275.15.10754;
RA   Bonfils C., Beaulieu N., Chan E., Cotton-Montpetit J., MacLeod A.R.;
RT   "Characterization of the human DNA methyltransferase splice variant
RT   Dnmt1b.";
RL   J. Biol. Chem. 275:10754-10760(2000).
RN   [8]
RP   INTERACTION WITH PCNA, AND MUTAGENESIS OF ARG-163; GLN-164; THR-166;
RP   ILE-167; SER-169; HIS-170; PHE-171; ALA-172 AND LYS-173.
RX   PubMed=9302295; DOI=10.1126/science.277.5334.1996;
RA   Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
RT   "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
RT   p21WAF1.";
RL   Science 277:1996-2000(1997).
RN   [9]
RP   INTERACTION WITH MBD2 AND MBD3.
RX   PubMed=10947852; DOI=10.1046/j.1365-2443.2000.00359.x;
RA   Tatematsu K., Yamazaki T., Ishikawa F.;
RT   "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex
RT   containing DNMT1 at the replication foci in late S phase.";
RL   Genes Cells 5:677-688(2000).
RN   [10]
RP   INTERACTION WITH HDAC2 AND DMAP1.
RX   PubMed=10888872; DOI=10.1038/77023;
RA   Rountree M.R., Bachman K.E., Baylin S.B.;
RT   "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT   replication foci.";
RL   Nat. Genet. 25:269-277(2000).
RN   [11]
RP   INTERACTION WITH RB1; E2F1 AND HDAC1.
RX   PubMed=10888886; DOI=10.1038/77124;
RA   Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
RA   Wolffe A.P.;
RT   "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription
RT   from E2F-responsive promoters.";
RL   Nat. Genet. 25:338-342(2000).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=10325416; DOI=10.1093/nar/27.11.2291;
RA   Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J.,
RA   Gonzales F.A., Jones P.A.;
RT   "The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA
RT   expression in normal tissues and overexpression in tumors.";
RL   Nucleic Acids Res. 27:2291-2298(1999).
RN   [13]
RP   INTERACTION WITH DNMT3A AND DNMT3B, AND SUBCELLULAR LOCATION.
RX   PubMed=12145218; DOI=10.1093/emboj/cdf401;
RA   Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.;
RT   "Co-operation and communication between the human maintenance and de novo
RT   DNA (cytosine-5) methyltransferases.";
RL   EMBO J. 21:4183-4195(2002).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-714, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH EED AND EZH2.
RX   PubMed=16357870; DOI=10.1038/nature04431;
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RT   "The Polycomb group protein EZH2 directly controls DNA methylation.";
RL   Nature 439:871-874(2006).
RN   [16]
RP   ERRATUM OF PUBMED:16357870.
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RL   Nature 446:824-824(2006).
RN   [17]
RP   DE NOVO DNA METHYLATION OF TARGET GENES.
RX   PubMed=17200670; DOI=10.1038/ng1950;
RA   Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M.,
RA   Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E.,
RA   Bergman Y., Simon I., Cedar H.;
RT   "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for
RT   de novo methylation in cancer.";
RL   Nat. Genet. 39:232-236(2007).
RN   [18]
RP   FUNCTION, AND MUTAGENESIS OF CYS-653; CYS-656; CYS-659; CYS-664; CYS-667
RP   AND CYS-670.
RX   PubMed=18754681; DOI=10.1021/bi8011725;
RA   Pradhan M., Esteve P.-O., Chin H.G., Samaranayke M., Kim G.-D., Pradhan S.;
RT   "CXXC domain of human DNMT1 is essential for enzymatic activity.";
RL   Biochemistry 47:10000-10009(2008).
RN   [19]
RP   FUNCTION.
RX   PubMed=18413740; DOI=10.1158/0008-5472.can-07-6654;
RA   Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S.,
RA   Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P., Gius D.;
RT   "DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment
RT   of CTCFL/BORIS and modulation of promoter histone methylation.";
RL   Cancer Res. 68:2726-2735(2008).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [21]
RP   METHYLATION AT LYS-70, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18438403; DOI=10.1038/nchembio.88;
RA   Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R.,
RA   Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
RT   "Protein lysine methyltransferase G9a acts on non-histone targets.";
RL   Nat. Chem. Biol. 4:344-346(2008).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-143; SER-152;
RP   SER-154 AND SER-394, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [24]
RP   SUMOYLATION, INTERACTION WITH UBC9, AND MUTAGENESIS OF CYS-1226.
RX   PubMed=19450230; DOI=10.1042/bj20090142;
RA   Lee B., Muller M.T.;
RT   "SUMOylation enhances DNA methyltransferase 1 activity.";
RL   Biochem. J. 421:449-461(2009).
RN   [25]
RP   HOMODIMERIZATION.
RX   PubMed=19173286; DOI=10.1002/jcb.22071;
RA   Fellinger K., Rothbauer U., Felle M., Laengst G., Leonhardt H.;
RT   "Dimerization of DNA methyltransferase 1 is mediated by its regulatory
RT   domain.";
RL   J. Cell. Biochem. 106:521-528(2009).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-1111; LYS-1113 AND
RP   LYS-1115, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-714, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [29]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [30]
RP   PHOSPHORYLATION AT SER-154.
RX   PubMed=21565170; DOI=10.1016/j.bbrc.2011.04.115;
RA   Lavoie G., St-Pierre Y.;
RT   "Phosphorylation of human DNMT1: implication of cyclin-dependent kinases.";
RL   Biochem. Biophys. Res. Commun. 409:187-192(2011).
RN   [31]
RP   ACETYLATION AT LYS-160; LYS-188; LYS-259; LYS-366; LYS-749; LYS-891;
RP   LYS-957; LYS-961; LYS-975; LYS-1054; LYS-1111; LYS-1113; LYS-1115;
RP   LYS-1117; LYS-1349 AND LYS-1415, AND DEACETYLATION BY SIRT1.
RX   PubMed=21947282; DOI=10.1128/mcb.06147-11;
RA   Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N.,
RA   Koomen J., Chen J., Lane W.S., Seto E.;
RT   "SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters
RT   its activities.";
RL   Mol. Cell. Biol. 31:4720-4734(2011).
RN   [32]
RP   METHYLATION AT LYS-142, AND PHOSPHORYLATION AT SER-143.
RX   PubMed=21151116; DOI=10.1038/nsmb.1939;
RA   Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R.,
RA   Feehery G.R., Cheng X., Pradhan S.;
RT   "A methylation and phosphorylation switch between an adjacent lysine and
RT   serine determines human DNMT1 stability.";
RL   Nat. Struct. Mol. Biol. 18:42-48(2011).
RN   [33]
RP   INTERACTION WITH USP7 AND UHRF1.
RX   PubMed=21745816; DOI=10.1093/nar/gkr528;
RA   Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T.,
RA   Kremmer E., Kappler R., Langst G.;
RT   "The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1
RT   and regulates the stability of UHRF1.";
RL   Nucleic Acids Res. 39:8355-8365(2011).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-133 AND SER-714, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [35]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; THR-137; SER-143;
RP   SER-154; THR-166; SER-312; SER-394; SER-398; SER-549; SER-714 AND SER-878,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [36]
RP   FUNCTION, POSSIBLE IDENTIFICATION IN A COREPRESSOR COMPLEX, AND
RP   CHROMATIN-BINDING.
RX   PubMed=24623306; DOI=10.7554/elife.02313;
RA   Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
RT   "A KRAS-directed transcriptional silencing pathway that mediates the CpG
RT   island methylator phenotype.";
RL   Elife 3:E02313-E02313(2014).
RN   [37]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [38]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1609, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [39]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-259 AND LYS-1609, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [40]
RP   INTERACTION WITH ZNF263.
RX   PubMed=32051553; DOI=10.1038/s41388-020-1206-7;
RA   Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C.,
RA   Liu Q., Chen S., Wu M.;
RT   "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma
RT   epigenetically.";
RL   Oncogene 39:3163-3178(2020).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 351-600 IN COMPLEX WITH ZINC
RP   IONS.
RX   PubMed=21389349; DOI=10.1074/jbc.m110.209882;
RA   Syeda F., Fagan R.L., Wean M., Avvakumov G.V., Walker J.R., Xue S.,
RA   Dhe-Paganon S., Brenner C.;
RT   "The replication focus targeting sequence (RFTS) domain is a DNA-
RT   competitive inhibitor of Dnmt1.";
RL   J. Biol. Chem. 286:15344-15351(2011).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 646-1600 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND DNA, AND AUTOINHIBITORY LINKER.
RX   PubMed=21163962; DOI=10.1126/science.1195380;
RA   Song J., Rechkoblit O., Bestor T.H., Patel D.J.;
RT   "Structure of DNMT1-DNA complex reveals a role for autoinhibition in
RT   maintenance DNA methylation.";
RL   Science 331:1036-1040(2011).
RN   [43]
RP   VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495, AND CHARACTERIZATION OF
RP   VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495.
RX   PubMed=21532572; DOI=10.1038/ng.830;
RA   Klein C.J., Botuyan M.V., Wu Y., Ward C.J., Nicholson G.A., Hammans S.,
RA   Hojo K., Yamanishi H., Karpf A.R., Wallace D.C., Simon M., Lander C.,
RA   Boardman L.A., Cunningham J.M., Smith G.E., Litchy W.J., Boes B.,
RA   Atkinson E.J., Middha S., Dyck P.J.B., Parisi J.E., Mer G., Smith D.I.,
RA   Dyck P.J.;
RT   "Mutations in DNMT1 cause hereditary sensory neuropathy with dementia and
RT   hearing loss.";
RL   Nat. Genet. 43:595-600(2011).
RN   [44]
RP   VARIANTS ADCADN VAL-554; ALA-589 AND PHE-590.
RX   PubMed=22328086; DOI=10.1093/hmg/dds035;
RA   Winkelmann J., Lin L., Schormair B., Kornum B.R., Faraco J., Plazzi G.,
RA   Melberg A., Cornelio F., Urban A.E., Pizza F., Poli F., Grubert F.,
RA   Wieland T., Graf E., Hallmayer J., Strom T.M., Mignot E.;
RT   "Mutations in DNMT1 cause autosomal dominant cerebellar ataxia, deafness
RT   and narcolepsy.";
RL   Hum. Mol. Genet. 21:2205-2210(2012).
CC   -!- FUNCTION: Methylates CpG residues. Preferentially methylates
CC       hemimethylated DNA. Associates with DNA replication sites in S phase
CC       maintaining the methylation pattern in the newly synthesized strand,
CC       that is essential for epigenetic inheritance. Associates with chromatin
CC       during G2 and M phases to maintain DNA methylation independently of
CC       replication. It is responsible for maintaining methylation patterns
CC       established in development. DNA methylation is coordinated with
CC       methylation of histones. Mediates transcriptional repression by direct
CC       binding to HDAC2. In association with DNMT3B and via the recruitment of
CC       CTCFL/BORIS, involved in activation of BAG1 gene expression by
CC       modulating dimethylation of promoter histone H3 at H3K4 and H3K9.
CC       Probably forms a corepressor complex required for activated KRAS-
CC       mediated promoter hypermethylation and transcriptional silencing of
CC       tumor suppressor genes (TSGs) or other tumor-related genes in
CC       colorectal cancer (CRC) cells (PubMed:24623306). Also required to
CC       maintain a transcriptionally repressive state of genes in
CC       undifferentiated embryonic stem cells (ESCs) (PubMed:24623306).
CC       Associates at promoter regions of tumor suppressor genes (TSGs) leading
CC       to their gene silencing (PubMed:24623306). Promotes tumor growth
CC       (PubMed:24623306). {ECO:0000269|PubMed:16357870,
CC       ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18754681,
CC       ECO:0000269|PubMed:24623306}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SUBUNIT: Homodimer (PubMed:19173286). Forms a stable complex with E2F1,
CC       BB1 and HDAC1 (PubMed:10888886). Forms a complex with DMAP1 and HDAC2,
CC       with direct interaction (PubMed:10888872). Interacts with the PRC2/EED-
CC       EZH2 complex (PubMed:16357870). Probably part of a corepressor complex
CC       containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306).
CC       Interacts with UHRF1; promoting its recruitment to hemimethylated DNA
CC       (PubMed:21745816). Interacts with USP7, promoting its deubiquitination
CC       (PubMed:21745816). Interacts with PCNA (PubMed:9302295). Interacts with
CC       MBD2 and MBD3 (PubMed:10947852). Interacts with DNMT3A and DNMT3B
CC       (PubMed:12145218). Interacts with UBC9 (PubMed:19450230). Interacts
CC       with CSNK1D (By similarity). Interacts with HDAC1 (By similarity).
CC       Interacts with BAZ2A/TIP5 (By similarity). Interacts with SIRT7 (By
CC       similarity). Interacts with ZNF263; recruited to the SIX3 promoter
CC       along with other proteins involved in chromatin modification and
CC       transcriptional corepression where it contributes to transcriptional
CC       repression (PubMed:32051553). {ECO:0000250|UniProtKB:P13864,
CC       ECO:0000269|PubMed:10888872, ECO:0000269|PubMed:10888886,
CC       ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12145218,
CC       ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:19173286,
CC       ECO:0000269|PubMed:19450230, ECO:0000269|PubMed:21745816,
CC       ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:32051553,
CC       ECO:0000269|PubMed:9302295}.
CC   -!- INTERACTION:
CC       P26358; P31749: AKT1; NbExp=6; IntAct=EBI-719459, EBI-296087;
CC       P26358; P35222: CTNNB1; NbExp=8; IntAct=EBI-719459, EBI-491549;
CC       P26358; O75530: EED; NbExp=3; IntAct=EBI-719459, EBI-923794;
CC       P26358; Q15910: EZH2; NbExp=8; IntAct=EBI-719459, EBI-530054;
CC       P26358; P48552: NRIP1; NbExp=3; IntAct=EBI-719459, EBI-746484;
CC       P26358; P09874: PARP1; NbExp=6; IntAct=EBI-719459, EBI-355676;
CC       P26358; Q9NRD5: PICK1; NbExp=2; IntAct=EBI-719459, EBI-79165;
CC       P26358; Q8WTS6: SETD7; NbExp=9; IntAct=EBI-719459, EBI-1268586;
CC       P26358; Q96EB6: SIRT1; NbExp=11; IntAct=EBI-719459, EBI-1802965;
CC       P26358; Q96T88: UHRF1; NbExp=12; IntAct=EBI-719459, EBI-1548946;
CC       P26358; Q77UV9: KIE-2; Xeno; NbExp=2; IntAct=EBI-719459, EBI-2608731;
CC       P26358; Q9QR71: LANA1; Xeno; NbExp=2; IntAct=EBI-719459, EBI-15602554;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12145218}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P26358-1; Sequence=Displayed;
CC       Name=2; Synonyms=Dnmt1b;
CC         IsoId=P26358-2; Sequence=VSP_005618;
CC       Name=3;
CC         IsoId=P26358-3; Sequence=VSP_005617;
CC   -!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal tissues,
CC       heart, kidney, placenta, peripheral blood mononuclear cells, and
CC       expressed at lower levels in spleen, lung, brain, small intestine,
CC       colon, liver, and skeletal muscle. Isoform 2 is less expressed than
CC       isoform 1. {ECO:0000269|PubMed:10325416}.
CC   -!- INDUCTION: Its abundance is reduced to non detectable levels at the G0
CC       phase of the cell cycle and is dramatically induced upon entrance into
CC       the S-phase of the cell cycle.
CC   -!- DOMAIN: The N-terminal part is required for homodimerization and acts
CC       as a regulatory domain.
CC   -!- DOMAIN: The CXXC-type zinc finger specifically binds to unmethylated
CC       CpG dinucleotides, positioning the autoinhibitory linker between the
CC       DNA and the active site, thus providing a mechanism to ensure that only
CC       hemimethylated CpG dinucleotides undergo methylation.
CC       {ECO:0000269|PubMed:21163962}.
CC   -!- PTM: Sumoylated; sumoylation increases activity.
CC       {ECO:0000269|PubMed:19450230}.
CC   -!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates
CC       cell cycle G(2)/M transition. Deacetylation of Lys-1349 and Lys-1415 by
CC       SIRT1 increases methyltransferase activity.
CC       {ECO:0000269|PubMed:21947282}.
CC   -!- PTM: Phosphorylation of Ser-154 by CDKs is important for enzymatic
CC       activity and protein stability. Phosphorylation of Ser-143 by AKT1
CC       prevents methylation by SETD7 therebye increasing DNMT1 stability.
CC       {ECO:0000269|PubMed:21151116, ECO:0000269|PubMed:21565170}.
CC   -!- PTM: Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal
CC       degradation. {ECO:0000269|PubMed:18438403,
CC       ECO:0000269|PubMed:21151116}.
CC   -!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
CC       ubiquitination by UHRF1 by promoting deubiquitination and preventing
CC       degradation by the proteasome. {ECO:0000250|UniProtKB:P13864}.
CC   -!- DISEASE: Neuropathy, hereditary sensory, 1E (HSN1E) [MIM:614116]: A
CC       neurodegenerative disorder characterized by adult onset of progressive
CC       peripheral sensory loss associated with progressive hearing impairment
CC       and early-onset dementia. {ECO:0000269|PubMed:21532572}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Cerebellar ataxia, deafness, and narcolepsy, autosomal
CC       dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic
CC       disorder characterized by adult onset of progressive cerebellar ataxia,
CC       narcolepsy, cataplexy, sensorineural deafness, and dementia. More
CC       variable features include optic atrophy, sensory neuropathy, psychosis,
CC       and depression. {ECO:0000269|PubMed:22328086}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD54507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/DNMT1ID40347ch19p13.html";
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DR   EMBL; X63692; CAA45219.1; -; mRNA.
DR   EMBL; AF180682; AAF23609.1; -; mRNA.
DR   EMBL; AC010077; AAD54507.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC020931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126227; AAI26228.1; -; mRNA.
DR   EMBL; BC144093; AAI44094.1; -; mRNA.
DR   EMBL; AH008119; AAD51619.1; -; Genomic_DNA.
DR   CCDS; CCDS12228.1; -. [P26358-1]
DR   CCDS; CCDS45958.1; -. [P26358-2]
DR   PIR; S22610; S22610.
DR   RefSeq; NP_001124295.1; NM_001130823.2. [P26358-2]
DR   RefSeq; NP_001305659.1; NM_001318730.1.
DR   RefSeq; NP_001305660.1; NM_001318731.1.
DR   RefSeq; NP_001370.1; NM_001379.3. [P26358-1]
DR   PDB; 3EPZ; X-ray; 2.31 A; A/B=351-600.
DR   PDB; 3PTA; X-ray; 3.60 A; A=646-1600.
DR   PDB; 3SWR; X-ray; 2.49 A; A=601-1600.
DR   PDB; 4WXX; X-ray; 2.62 A; A/B=351-1600.
DR   PDB; 4YOC; X-ray; 2.92 A; A=600-1600.
DR   PDB; 4Z96; X-ray; 2.85 A; C=1098-1129.
DR   PDB; 4Z97; X-ray; 3.00 A; C=1098-1129.
DR   PDB; 5WVO; X-ray; 2.00 A; C=351-600.
DR   PDB; 5YDR; X-ray; 2.00 A; B=351-599.
DR   PDB; 6K3A; X-ray; 2.30 A; B/D/F=161-180.
DR   PDBsum; 3EPZ; -.
DR   PDBsum; 3PTA; -.
DR   PDBsum; 3SWR; -.
DR   PDBsum; 4WXX; -.
DR   PDBsum; 4YOC; -.
DR   PDBsum; 4Z96; -.
DR   PDBsum; 4Z97; -.
DR   PDBsum; 5WVO; -.
DR   PDBsum; 5YDR; -.
DR   PDBsum; 6K3A; -.
DR   SMR; P26358; -.
DR   BioGRID; 108123; 150.
DR   CORUM; P26358; -.
DR   DIP; DIP-39693N; -.
DR   ELM; P26358; -.
DR   IntAct; P26358; 51.
DR   MINT; P26358; -.
DR   STRING; 9606.ENSP00000352516; -.
DR   BindingDB; P26358; -.
DR   ChEMBL; CHEMBL1993; -.
DR   DrugBank; DB00928; Azacitidine.
DR   DrugBank; DB01262; Decitabine.
DR   DrugBank; DB12116; Epigallocatechin gallate.
DR   DrugBank; DB01099; Flucytosine.
DR   DrugBank; DB05668; Palifosfamide.
DR   DrugBank; DB01035; Procainamide.
DR   DrugBank; DB00721; Procaine.
DR   DrugCentral; P26358; -.
DR   GuidetoPHARMACOLOGY; 2605; -.
DR   REBASE; 1161; M.HsaDnmt1A.
DR   REBASE; 4240; M.HsaDnmt1B.
DR   iPTMnet; P26358; -.
DR   PhosphoSitePlus; P26358; -.
DR   SwissPalm; P26358; -.
DR   BioMuta; DNMT1; -.
DR   DMDM; 12231019; -.
DR   EPD; P26358; -.
DR   jPOST; P26358; -.
DR   MassIVE; P26358; -.
DR   MaxQB; P26358; -.
DR   PaxDb; P26358; -.
DR   PeptideAtlas; P26358; -.
DR   PRIDE; P26358; -.
DR   ProteomicsDB; 54320; -. [P26358-1]
DR   ProteomicsDB; 54321; -. [P26358-2]
DR   ProteomicsDB; 54322; -. [P26358-3]
DR   ABCD; P26358; 1 sequenced antibody.
DR   Antibodypedia; 1052; 1576 antibodies.
DR   DNASU; 1786; -.
DR   Ensembl; ENST00000340748; ENSP00000345739; ENSG00000130816. [P26358-1]
DR   Ensembl; ENST00000359526; ENSP00000352516; ENSG00000130816. [P26358-2]
DR   GeneID; 1786; -.
DR   KEGG; hsa:1786; -.
DR   UCSC; uc002mng.4; human. [P26358-1]
DR   CTD; 1786; -.
DR   DisGeNET; 1786; -.
DR   GeneCards; DNMT1; -.
DR   GeneReviews; DNMT1; -.
DR   HGNC; HGNC:2976; DNMT1.
DR   HPA; ENSG00000130816; Low tissue specificity.
DR   MalaCards; DNMT1; -.
DR   MIM; 126375; gene.
DR   MIM; 604121; phenotype.
DR   MIM; 614116; phenotype.
DR   neXtProt; NX_P26358; -.
DR   OpenTargets; ENSG00000130816; -.
DR   Orphanet; 314404; Autosomal dominant cerebellar ataxia-deafness-narcolepsy syndrome.
DR   Orphanet; 456318; Hereditary sensory neuropathy-deafness-dementia syndrome.
DR   PharmGKB; PA27443; -.
DR   VEuPathDB; HostDB:ENSG00000130816.14; -.
DR   eggNOG; ENOG502QPKK; Eukaryota.
DR   GeneTree; ENSGT00390000005100; -.
DR   HOGENOM; CLU_003040_0_0_1; -.
DR   InParanoid; P26358; -.
DR   OMA; IPRVMEQ; -.
DR   PhylomeDB; P26358; -.
DR   TreeFam; TF328926; -.
DR   BRENDA; 2.1.1.37; 2681.
DR   PathwayCommons; P26358; -.
DR   Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR   Reactome; R-HSA-5334118; DNA methylation.
DR   SIGNOR; P26358; -.
DR   BioGRID-ORCS; 1786; 324 hits in 1009 CRISPR screens.
DR   ChiTaRS; DNMT1; human.
DR   EvolutionaryTrace; P26358; -.
DR   GeneWiki; DNMT1; -.
DR   GenomeRNAi; 1786; -.
DR   Pharos; P26358; Tclin.
DR   PRO; PR:P26358; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P26358; protein.
DR   Bgee; ENSG00000130816; Expressed in oocyte and 227 other tissues.
DR   ExpressionAtlas; P26358; baseline and differential.
DR   Genevisible; P26358; HS.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0009008; F:DNA-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
DR   GO; GO:0010216; P:maintenance of DNA methylation; IDA:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IMP:BHF-UCL.
DR   GO; GO:1905931; P:negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; IMP:BHF-UCL.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
DR   Gene3D; 2.30.30.490; -; 2.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR   InterPro; IPR010506; DMAP1-bd.
DR   InterPro; IPR017198; DNMT1-like.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR002857; Znf_CXXC.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF12047; DNMT1-RFD; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PIRSF; PIRSF037404; DNMT1; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
DR   SMART; SM01137; DMAP_binding; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51912; DMAP1_BIND; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   Chromatin regulator; Deafness; Disease variant; DNA-binding;
KW   Isopeptide bond; Metal-binding; Methylation; Methyltransferase; Neuropathy;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1616
FT                   /note="DNA (cytosine-5)-methyltransferase 1"
FT                   /id="PRO_0000088034"
FT   DOMAIN          16..109
FT                   /note="DMAP1-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT   DOMAIN          755..880
FT                   /note="BAH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          972..1100
FT                   /note="BAH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   REPEAT          1109..1110
FT                   /note="1"
FT   REPEAT          1111..1112
FT                   /note="2"
FT   REPEAT          1113..1114
FT                   /note="3"
FT   REPEAT          1115..1116
FT                   /note="4"
FT   REPEAT          1117..1118
FT                   /note="5"
FT   REPEAT          1119..1120
FT                   /note="6; approximate"
FT   DOMAIN          1139..1599
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ZN_FING         646..692
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT   REGION          1..336
FT                   /note="Interaction with the PRC2/EED-EZH2 complex"
FT                   /evidence="ECO:0000250"
FT   REGION          1..148
FT                   /note="Interaction with DNMT3A"
FT                   /evidence="ECO:0000269|PubMed:12145218"
FT   REGION          1..120
FT                   /note="Interaction with DMAP1"
FT                   /evidence="ECO:0000269|PubMed:10888872"
FT   REGION          103..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..217
FT                   /note="Interaction with DNMT3B"
FT                   /evidence="ECO:0000269|PubMed:12145218"
FT   REGION          163..174
FT                   /note="Interaction with PCNA"
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   REGION          308..606
FT                   /note="Interaction with the PRC2/EED-EZH2 complex"
FT                   /evidence="ECO:0000250"
FT   REGION          310..502
FT                   /note="Homodimerization"
FT   REGION          331..550
FT                   /note="DNA replication foci-targeting sequence"
FT                   /evidence="ECO:0000250"
FT   REGION          651..697
FT                   /note="Required for activity"
FT   REGION          693..754
FT                   /note="Autoinhibitory linker"
FT   REGION          699..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1120
FT                   /note="6 X 2 AA tandem repeats of K-G"
FT   REGION          1121..1616
FT                   /note="Interaction with the PRC2/EED-EZH2 complex"
FT                   /evidence="ECO:0000250"
FT   REGION          1139..1616
FT                   /note="Catalytic"
FT   REGION          1150..1151
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   REGION          1168..1169
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000269|PubMed:21163962,
FT                   ECO:0007744|PDB:3PTA"
FT   REGION          1190..1191
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   MOTIF           177..205
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        155..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1226
FT   METAL           353
FT                   /note="Zinc"
FT   METAL           356
FT                   /note="Zinc"
FT   METAL           414
FT                   /note="Zinc"
FT   METAL           418
FT                   /note="Zinc"
FT   BINDING         1146
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   BINDING         1191
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000269|PubMed:21163962,
FT                   ECO:0007744|PDB:3PTA"
FT   BINDING         1578
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:21163962,
FT                   ECO:0007744|PDB:3PTA"
FT   BINDING         1580
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   SITE            509
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         70
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:18438403"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   MOD_RES         142
FT                   /note="N6-methyllysine; by SETD7"
FT                   /evidence="ECO:0000269|PubMed:21151116"
FT   MOD_RES         143
FT                   /note="Phosphoserine; by PKB/AKT1"
FT                   /evidence="ECO:0000269|PubMed:21151116,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:21565170,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         160
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         166
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         173
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         188
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         259
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         366
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         732
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336"
FT   MOD_RES         749
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         878
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         891
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         957
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         961
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         975
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         1054
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         1111
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282,
FT                   ECO:0007744|PubMed:19608861"
FT   MOD_RES         1113
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282,
FT                   ECO:0007744|PubMed:19608861"
FT   MOD_RES         1115
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282,
FT                   ECO:0007744|PubMed:19608861"
FT   MOD_RES         1117
FT                   /note="N6-acetyllysine; by EHMT2"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         1119
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   MOD_RES         1121
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13864"
FT   MOD_RES         1349
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   MOD_RES         1415
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21947282"
FT   CROSSLNK        259
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1609
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..336
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_005617"
FT   VAR_SEQ         149
FT                   /note="P -> RSRDPPASASQVTGIRA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_005618"
FT   VARIANT         97
FT                   /note="H -> R (in dbSNP:rs16999593)"
FT                   /id="VAR_024605"
FT   VARIANT         311
FT                   /note="I -> V (in dbSNP:rs2228612)"
FT                   /id="VAR_051960"
FT   VARIANT         490..491
FT                   /note="DP -> EY (in HSN1E; unstable protein with decreased
FT                   enzymatic activity and impaired heterochromatin binding
FT                   ability after the S phase; dbSNP:rs199473691)"
FT                   /id="VAR_065965"
FT   VARIANT         495
FT                   /note="Y -> C (in HSN1E; unstable protein with decreased
FT                   enzymatic activity and impaired heterochromatin binding
FT                   ability after the S phase; dbSNP:rs199473690)"
FT                   /evidence="ECO:0000269|PubMed:21532572"
FT                   /id="VAR_065966"
FT   VARIANT         554
FT                   /note="A -> V (in ADCADN; dbSNP:rs397509392)"
FT                   /evidence="ECO:0000269|PubMed:22328086"
FT                   /id="VAR_070055"
FT   VARIANT         589
FT                   /note="G -> A (in ADCADN; dbSNP:rs397509393)"
FT                   /evidence="ECO:0000269|PubMed:22328086"
FT                   /id="VAR_070056"
FT   VARIANT         590
FT                   /note="V -> F (in ADCADN; dbSNP:rs397509391)"
FT                   /evidence="ECO:0000269|PubMed:22328086"
FT                   /id="VAR_070057"
FT   MUTAGEN         163
FT                   /note="R->A: Abolishes interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         164
FT                   /note="Q->A: Abolishes interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         166
FT                   /note="T->A: Abolishes interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         167
FT                   /note="I->A: Abolishes interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         169
FT                   /note="S->A: No loss of interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         170
FT                   /note="H->V: Abolishes interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         171
FT                   /note="F->V: Abolishes interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         172
FT                   /note="A->S: No loss of interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         173
FT                   /note="K->A: No loss of interaction with PCNA."
FT                   /evidence="ECO:0000269|PubMed:9302295"
FT   MUTAGEN         653
FT                   /note="C->G: Reduces activity about 10-fold; when
FT                   associated with G-656; G-659; G-664; G-667 and G-670."
FT                   /evidence="ECO:0000269|PubMed:18754681"
FT   MUTAGEN         656
FT                   /note="C->G: Reduces activity about 10-fold; when
FT                   associated with G-653; G-659; G-664; G-667 and G-670."
FT                   /evidence="ECO:0000269|PubMed:18754681"
FT   MUTAGEN         659
FT                   /note="C->G: Reduces activity about 10-fold; when
FT                   associated with G-653; G-656; G-664; G-667 and G-670."
FT                   /evidence="ECO:0000269|PubMed:18754681"
FT   MUTAGEN         664
FT                   /note="C->F: Reduces activity about 10-fold; when
FT                   associated with G-653; G-656; G-659; G-667 and G-670."
FT                   /evidence="ECO:0000269|PubMed:18754681"
FT   MUTAGEN         667
FT                   /note="C->G: Reduces activity about 10-fold; when
FT                   associated with G-653; G-656; G-659; G-664 and G-670."
FT                   /evidence="ECO:0000269|PubMed:18754681"
FT   MUTAGEN         670
FT                   /note="C->G: Reduces activity about 10-fold; when
FT                   associated with G-653; G-656; G-659; G-664 and G-667."
FT                   /evidence="ECO:0000269|PubMed:18754681"
FT   MUTAGEN         1226
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19450230"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:6K3A"
FT   TURN            354..356
FT                   /evidence="ECO:0007829|PDB:5YDR"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:5YDR"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:5YDR"
FT   HELIX           377..381
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           384..386
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          392..394
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          404..414
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          417..419
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          422..425
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   TURN            426..430
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          433..440
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          453..458
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          463..467
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          470..473
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          476..480
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          485..488
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   TURN            493..495
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           496..518
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           524..533
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           538..540
FT                   /evidence="ECO:0007829|PDB:3EPZ"
FT   HELIX           547..551
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           554..566
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   STRAND          575..578
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           579..588
FT                   /evidence="ECO:0007829|PDB:5WVO"
FT   HELIX           592..597
FT                   /evidence="ECO:0007829|PDB:5YDR"
FT   HELIX           622..629
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            657..659
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           670..672
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            674..677
FT                   /evidence="ECO:0007829|PDB:4WXX"
FT   HELIX           687..689
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           692..703
FT                   /evidence="ECO:0007829|PDB:4WXX"
FT   STRAND          731..735
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          738..740
FT                   /evidence="ECO:0007829|PDB:4WXX"
FT   STRAND          744..746
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          748..752
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          755..758
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          762..765
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          767..769
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          775..785
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            786..788
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          789..799
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           800..802
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          803..805
FT                   /evidence="ECO:0007829|PDB:4YOC"
FT   HELIX           806..808
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          813..824
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           825..827
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          828..832
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          834..836
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           843..845
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            851..853
FT                   /evidence="ECO:0007829|PDB:4WXX"
FT   HELIX           856..860
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          862..870
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            871..874
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          875..877
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          886..888
FT                   /evidence="ECO:0007829|PDB:4YOC"
FT   TURN            889..891
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           894..905
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          912..916
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          921..928
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          931..934
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          938..941
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            966..968
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           973..975
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           976..980
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          992..1001
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1005..1008
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1015..1020
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1024..1026
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1031..1034
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1035..1037
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1041..1044
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1048..1052
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1053..1055
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1058..1064
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1065..1067
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1072..1077
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1079..1090
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            1091..1094
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1095..1097
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1101..1103
FT                   /evidence="ECO:0007829|PDB:4WXX"
FT   STRAND          1139..1145
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1150..1158
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1160..1167
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1171..1180
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1184..1187
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1191..1200
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            1214..1216
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1218..1222
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1231..1233
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1237..1243
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1247..1258
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1261..1268
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1269..1272
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1275..1277
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1278..1289
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1293..1300
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1301..1304
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1311..1318
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1336..1338
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1343..1345
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1348..1350
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1367..1371
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1384..1386
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1395..1401
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1419..1426
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1436..1438
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1451..1453
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            1462..1464
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1474..1476
FT                   /evidence="ECO:0007829|PDB:4YOC"
FT   HELIX           1477..1479
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1480..1482
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1487..1489
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1493..1496
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1499..1503
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1504..1506
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1508..1510
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   TURN            1511..1514
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1523..1525
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   STRAND          1534..1536
FT                   /evidence="ECO:0007829|PDB:4WXX"
FT   STRAND          1542..1547
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1550..1556
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1569..1578
FT                   /evidence="ECO:0007829|PDB:3SWR"
FT   HELIX           1582..1598
FT                   /evidence="ECO:0007829|PDB:3SWR"
SQ   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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