MBD1_HUMAN
ID MBD1_HUMAN Reviewed; 605 AA.
AC Q9UIS9; A4UTZ0; B4DXJ5; E9PEC5; K7ELI2; K7EQZ4; K7ESN0; O15248; O95241;
AC Q7Z7B5; Q8N4W4; Q9UNZ6; Q9UNZ7; Q9UNZ8; Q9UNZ9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Methyl-CpG-binding domain protein 1 {ECO:0000305};
DE AltName: Full=CXXC-type zinc finger protein 3;
DE AltName: Full=Methyl-CpG-binding protein MBD1;
DE AltName: Full=Protein containing methyl-CpG-binding domain 1;
GN Name=MBD1 {ECO:0000312|HGNC:HGNC:6916}; Synonyms=CXXC3, PCM1;
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 5), FUNCTION, INTERACTION WITH THE
RP MECP1 COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=9207790; DOI=10.1038/ng0797-256;
RA Cross S.H., Meehan R.R., Nan X., Bird A.;
RT "A component of the transcriptional repressor MeCP1 shares a motif with DNA
RT methyltransferase and HRX proteins.";
RL Nat. Genet. 16:256-259(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-401.
RX PubMed=10441743; DOI=10.1007/s003359901112;
RA Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
RT "Genomic structure and chromosomal mapping of the murine and human mbd1,
RT mbd2, mbd3, and mbd4 genes.";
RL Mamm. Genome 10:906-912(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 7), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fibroblast;
RX PubMed=10454587; DOI=10.1128/mcb.19.9.6415;
RA Fujita N., Takebayashi S., Okumura K., Kudo S., Chiba T., Saya H.,
RA Nakao M.;
RT "Methylation-mediated transcriptional silencing in euchromatin by methyl-
RT CpG binding protein MBD1 isoforms.";
RL Mol. Cell. Biol. 19:6415-6426(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 6), INDUCTION BY INTERFERON, AND INTERACTION
RP WITH OASL.
RC TISSUE=Leukocyte;
RX PubMed=14728690; DOI=10.1046/j.1432-1033.2003.03966.x;
RA Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.;
RT "Interaction between the 2'-5' oligoadenylate synthetase-like protein p59
RT OASL and the transcriptional repressor methyl CpG-binding protein 1.";
RL Eur. J. Biochem. 271:628-636(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
RC TISSUE=Cervix carcinoma;
RA Laget S.M., Xu S.-Y.;
RT "New splice variant of the methyl-CpG binding protein 1 (MBD1).";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Prostate;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 169-220, AND FUNCTION.
RX PubMed=9774669; DOI=10.1128/mcb.18.11.6538;
RA Hendrich B., Bird A.;
RT "Identification and characterization of a family of mammalian methyl-CpG
RT binding proteins.";
RL Mol. Cell. Biol. 18:6538-6547(1998).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10648624; DOI=10.1128/mcb.20.4.1394-1406.2000;
RA Ng H.-H., Jeppesen P., Bird A.;
RT "Active repression of methylated genes by the chromosomal protein MBD1.";
RL Mol. Cell. Biol. 20:1394-1406(2000).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE SUV39H1-CBX5
RP COMPLEX.
RX PubMed=12711603; DOI=10.1074/jbc.m302283200;
RA Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M.,
RA Chiba T., Nakao M.;
RT "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1
RT heterochromatic complex for DNA methylation-based transcriptional
RT repression.";
RL J. Biol. Chem. 278:24132-24138(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH ATF7IP.
RX PubMed=12665582; DOI=10.1128/mcb.23.8.2834-2843.2003;
RA Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H.,
RA Nakao M.;
RT "MCAF mediates MBD1-dependent transcriptional repression.";
RL Mol. Cell. Biol. 23:2834-2843(2003).
RN [13]
RP FUNCTION, AND INTERACTION WITH CHAF1A.
RX PubMed=12697822; DOI=10.1128/mcb.23.9.3226-3236.2003;
RA Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.;
RT "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of
RT chromatin assembly factor 1.";
RL Mol. Cell. Biol. 23:3226-3236(2003).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14610093; DOI=10.1074/jbc.m309393200;
RA Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M.,
RA Frankel W., Jacob S.T.;
RT "Role of human ribosomal RNA (rRNA) promoter methylation and of methyl-CpG-
RT binding protein MBD2 in the suppression of rRNA gene expression.";
RL J. Biol. Chem. 279:6783-6793(2004).
RN [15]
RP RETRACTED PAPER.
RX PubMed=15327775; DOI=10.1016/j.molcel.2004.06.043;
RA Sarraf S.A., Stancheva I.;
RT "Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9
RT by SETDB1 to DNA replication and chromatin assembly.";
RL Mol. Cell 15:595-605(2004).
RN [16]
RP RETRACTION NOTICE OF PUBMED:15327775.
RX PubMed=30849389; DOI=10.1016/j.molcel.2019.02.023;
RA Sarraf S.A., Stancheva I.;
RT "Retraction Notice to: Methyl-CpG Binding Protein MBD1 Couples Histone H3
RT Methylation at Lysine 9 by SETDB1 to DNA Replication and Chromatin
RT Assembly.";
RL Mol. Cell 73:1084-1084(2019).
RN [17]
RP INTERACTION WITH ATF7IP AND ATF7IP2, AND MUTAGENESIS OF ILE-576.
RX PubMed=15691849; DOI=10.1074/jbc.m413654200;
RA Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.;
RT "Transcriptional repression and heterochromatin formation by MBD1 and
RT MCAF/AM family proteins.";
RL J. Biol. Chem. 280:13928-13935(2005).
RN [18]
RP RETRACTED PAPER.
RX PubMed=17066076; DOI=10.1038/sj.emboj.7601404;
RA Lyst M.J., Nan X., Stancheva I.;
RT "Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS
RT proteins.";
RL EMBO J. 25:5317-5328(2006).
RN [19]
RP RETRACTION NOTICE OF PUBMED:17066076.
RX PubMed=31612521; DOI=10.15252/embj.2019103220;
RA Lyst M.J., Nan X., Stancheva I.;
RT "Retraction: Regulation of MBD1-mediated transcriptional repression by SUMO
RT and PIAS proteins.";
RL EMBO J. 38:e103220-e103220(2019).
RN [20]
RP SUMOYLATION, AND INTERACTION WITH ATF7IP.
RX PubMed=16757475; DOI=10.1074/jbc.m602280200;
RA Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S., Nakao M.,
RA Saitoh H.;
RT "Involvement of SUMO modification in MBD1- and MCAF1-mediated
RT heterochromatin formation.";
RL J. Biol. Chem. 281:23180-23190(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [22]
RP INTERACTION WITH BAHD1.
RX PubMed=19666599; DOI=10.1073/pnas.0901259106;
RA Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
RA Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J.,
RA Cossart P.;
RT "Human BAHD1 promotes heterochromatic gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP 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 [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-538, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-538, 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 [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277 AND LYS-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-277; LYS-422; LYS-440;
RP LYS-499; LYS-538 AND LYS-558, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [31]
RP STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, AND MUTAGENESIS OF
RP ARG-22; ARG-30; ASP-32; TYR-34; ARG-44; SER-45; TYR-52 AND PHE-64.
RX PubMed=10581239; DOI=10.1093/emboj/18.23.6653;
RA Ohki I., Shimotake N., Fujita N., Nakao M., Shirakawa M.;
RT "Solution structure of the methyl-CpG-binding domain of the methylation-
RT dependent transcriptional repressor MBD1.";
RL EMBO J. 18:6653-6661(1999).
RN [32] {ECO:0007744|PDB:1IG4}
RP STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, DOMAIN MBD, AND
RP MUTAGENESIS OF ARG-22; ARG-30; ASP-32; TYR-34; ARG-44; SER-45; LYS-46;
RP TYR-52 AND LYS-65.
RX PubMed=11371345; DOI=10.1016/s0092-8674(01)00324-5;
RA Ohki I., Shimotake N., Fujita N., Jee J., Ikegami T., Nakao M.,
RA Shirakawa M.;
RT "Solution structure of the methyl-CpG binding domain of human MBD1 in
RT complex with methylated DNA.";
RL Cell 105:487-497(2001).
RN [33]
RP STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, FUNCTION,
RP SUBCELLULAR LOCATION, INTERACTION WITH MPG, AND DOMAIN TRD.
RX PubMed=14555760; DOI=10.1073/pnas.2131819100;
RA Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M.,
RA Kawasuji M., Nakao M.;
RT "Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link
RT transcriptional repression and DNA repair in chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003).
RN [34] {ECO:0007744|PDB:4D4W}
RP STRUCTURE BY NMR OF 167-222, AND DOMAIN CXXC-TYPE 1 ZINC-FINGER.
RX PubMed=26354109; DOI=10.1007/s10858-015-9986-8;
RA Thomson R., Smith B.O.;
RT "Solution structure of human MBD1 CXXC1.";
RL J. Biomol. NMR 63:309-314(2015).
RN [35] {ECO:0007744|PDB:5W9Q}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 330-388 IN COMPLEX WITH CPG DNA,
RP DOMAIN CXXC-TYPE 3 ZINC-FINGER, AND ZINC-BINDING.
RX PubMed=29276034; DOI=10.1016/j.str.2017.11.022;
RA Xu C., Liu K., Lei M., Yang A., Li Y., Hughes T.R., Min J.;
RT "DNA Sequence Recognition of Human CXXC Domains and Their Structural
RT Determinants.";
RL Structure 26:85-95.e3(2018).
RN [36] {ECO:0007744|PDB:6D1T}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-77 IN COMPLEX WITH METHYLATED
RP DNA, AND DOMAIN MBD.
RG Structural genomics consortium (SGC);
RT "Complex of MBD1-MBD and methylated DNA.";
RL Submitted (APR-2018) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor that binds CpG islands in promoters
CC where the DNA is methylated at position 5 of cytosine within CpG
CC dinucleotides. Binding is abolished by the presence of 7-mG that is
CC produced by DNA damage by methylmethanesulfonate (MMS). Acts as
CC transcriptional repressor and plays a role in gene silencing by
CC recruiting ATF7IP, which in turn recruits factors such as the histone
CC methyltransferase SETDB1. Probably forms a complex with SETDB1 and
CC ATF7IP that represses transcription and couples DNA methylation and
CC histone 'Lys-9' trimethylation. Isoform 1 and isoform 2 can also
CC repress transcription from unmethylated promoters.
CC {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624,
CC ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:12697822,
CC ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14555760,
CC ECO:0000269|PubMed:14610093, ECO:0000269|PubMed:9207790,
CC ECO:0000269|PubMed:9774669}.
CC -!- SUBUNIT: Interacts with OASL, ATF7IP, ATF7IP2 and BAHD1
CC (PubMed:12665582, PubMed:14728690, PubMed:15691849, PubMed:16757475,
CC PubMed:19666599). Binds CHAF1A and the SUV39H1-CBX5 complex via the MBD
CC domain (PubMed:12697822, PubMed:12711603). Binds MGP via the TRD domain
CC (PubMed:14555760). May be part of the MeCP1 complex (PubMed:9207790).
CC {ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:12697822,
CC ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14555760,
CC ECO:0000269|PubMed:14728690, ECO:0000269|PubMed:15691849,
CC ECO:0000269|PubMed:16757475, ECO:0000269|PubMed:19666599,
CC ECO:0000269|PubMed:9207790}.
CC -!- INTERACTION:
CC Q9UIS9; P45973: CBX5; NbExp=6; IntAct=EBI-867196, EBI-78219;
CC Q9UIS9; Q13111: CHAF1A; NbExp=3; IntAct=EBI-867196, EBI-1020839;
CC Q9UIS9; Q13547: HDAC1; NbExp=2; IntAct=EBI-867196, EBI-301834;
CC Q9UIS9; Q92769: HDAC2; NbExp=2; IntAct=EBI-867196, EBI-301821;
CC Q9UIS9; O15379: HDAC3; NbExp=3; IntAct=EBI-867196, EBI-607682;
CC Q9UIS9; P42858: HTT; NbExp=2; IntAct=EBI-867196, EBI-466029;
CC Q9UIS9; Q99435: NELL2; NbExp=2; IntAct=EBI-867196, EBI-946274;
CC Q9UIS9; O75925: PIAS1; NbExp=3; IntAct=EBI-867196, EBI-629434;
CC Q9UIS9; Q9Y6X2: PIAS3; NbExp=3; IntAct=EBI-867196, EBI-2803703;
CC Q9UIS9; Q15156: PML-RAR; NbExp=4; IntAct=EBI-867196, EBI-867256;
CC Q9UIS9; Q15047: SETDB1; NbExp=3; IntAct=EBI-867196, EBI-79691;
CC Q9UIS9; P63165: SUMO1; NbExp=3; IntAct=EBI-867196, EBI-80140;
CC Q9UIS9; O43463: SUV39H1; NbExp=5; IntAct=EBI-867196, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12711603,
CC ECO:0000269|PubMed:14610093}. Nucleus matrix
CC {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624}. Nucleus
CC speckle {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624}.
CC Chromosome {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624,
CC ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14555760}.
CC Note=Nuclear, in a punctate pattern (PubMed:12711603). Associated with
CC euchromatic regions of the chromosomes, with pericentromeric regions on
CC chromosome 1 and with telomeric regions from several chromosomes
CC (PubMed:10648624, PubMed:10454587). {ECO:0000269|PubMed:10454587,
CC ECO:0000269|PubMed:10648624, ECO:0000269|PubMed:12711603}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=MBD1v1;
CC IsoId=Q9UIS9-1; Sequence=Displayed;
CC Name=2; Synonyms=MBD1v2;
CC IsoId=Q9UIS9-2; Sequence=VSP_011065, VSP_011068, VSP_011070;
CC Name=4; Synonyms=MBD1v3;
CC IsoId=Q9UIS9-4; Sequence=VSP_011066, VSP_011068;
CC Name=5; Synonyms=PCM1;
CC IsoId=Q9UIS9-5; Sequence=VSP_011064;
CC Name=6; Synonyms=MBD1v6;
CC IsoId=Q9UIS9-6; Sequence=VSP_011068, VSP_011069, VSP_011071;
CC Name=7;
CC IsoId=Q9UIS9-7; Sequence=VSP_011066;
CC Name=8;
CC IsoId=Q9UIS9-8; Sequence=VSP_011065, VSP_011068;
CC Name=9;
CC IsoId=Q9UIS9-9; Sequence=VSP_042812;
CC Name=10;
CC IsoId=Q9UIS9-10; Sequence=VSP_011064, VSP_054737, VSP_054738;
CC Name=11;
CC IsoId=Q9UIS9-11; Sequence=VSP_054736, VSP_011068, VSP_054739;
CC Name=12;
CC IsoId=Q9UIS9-12; Sequence=VSP_011070;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9207790}.
CC -!- INDUCTION: Up-regulated by interferon. {ECO:0000269|PubMed:14728690}.
CC -!- DOMAIN: The methyl-CpG-binding domain (MBD) functions both in binding
CC to methylated DNA and in protein interactions.
CC {ECO:0000269|PubMed:10581239}.
CC -!- DOMAIN: The third CXXC-type zinc finger mediates binding to DNA
CC containing unmethylated CpG dinucleotides.
CC {ECO:0000269|PubMed:29276034}.
CC -!- DOMAIN: The transcriptional repression domain (TRD) is involved in
CC transcription repression and in protein interactions.
CC {ECO:0000269|PubMed:14555760}.
CC -!- PTM: Sumoylated, sumoylation may increase interaction with ATF7IP.
CC {ECO:0000269|PubMed:16757475}.
CC -!- CAUTION: Was reported to recruit SETDB1 during DNA replication, to form
CC a S phase-specific complex that would facilitate methylation of H3
CC 'Lys-9' during replication-coupled chromatin assembly and vould be at
CC least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1
CC (PubMed:15327775). The interaction with SETDB1 was also reported to be
CC inhibited by sumoylation at Lys-499 and Lys-538 (PubMed:17066076).
CC However, these papers have been retracted because some data, results
CC and conclusions are not reliable (PubMed:30849389, PubMed:31612521).
CC {ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:17066076,
CC ECO:0000269|PubMed:30849389, ECO:0000269|PubMed:31612521}.
CC ---------------------------------------------------------------------------
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DR EMBL; Y10746; CAA71735.1; -; mRNA.
DR EMBL; AF120981; AAD50371.1; -; Genomic_DNA.
DR EMBL; AF120980; AAD50371.1; JOINED; Genomic_DNA.
DR EMBL; AF078830; AAD51442.1; -; mRNA.
DR EMBL; AF078831; AAD51443.1; -; mRNA.
DR EMBL; AF078832; AAD51444.1; -; mRNA.
DR EMBL; AF078833; AAD51445.1; -; mRNA.
DR EMBL; EF488685; ABP02056.1; -; mRNA.
DR EMBL; AK302004; BAG63407.1; -; mRNA.
DR EMBL; AC090246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033242; AAH33242.1; -; mRNA.
DR EMBL; AJ564845; CAD92308.1; -; mRNA.
DR EMBL; AF072241; AAC68870.1; -; mRNA.
DR CCDS; CCDS11941.1; -. [Q9UIS9-4]
DR CCDS; CCDS11942.1; -. [Q9UIS9-7]
DR CCDS; CCDS11943.1; -. [Q9UIS9-1]
DR CCDS; CCDS11944.1; -. [Q9UIS9-5]
DR CCDS; CCDS32832.1; -. [Q9UIS9-2]
DR CCDS; CCDS56071.1; -. [Q9UIS9-8]
DR CCDS; CCDS56072.1; -. [Q9UIS9-6]
DR CCDS; CCDS56073.1; -. [Q9UIS9-9]
DR CCDS; CCDS59318.1; -. [Q9UIS9-10]
DR CCDS; CCDS59319.1; -. [Q9UIS9-11]
DR CCDS; CCDS59320.1; -. [Q9UIS9-12]
DR RefSeq; NP_001191065.1; NM_001204136.1. [Q9UIS9-12]
DR RefSeq; NP_001191066.1; NM_001204137.1. [Q9UIS9-9]
DR RefSeq; NP_001191067.1; NM_001204138.1.
DR RefSeq; NP_001191068.1; NM_001204139.1. [Q9UIS9-1]
DR RefSeq; NP_001191069.1; NM_001204140.1.
DR RefSeq; NP_001191070.1; NM_001204141.1. [Q9UIS9-10]
DR RefSeq; NP_001191071.1; NM_001204142.1. [Q9UIS9-6]
DR RefSeq; NP_001191072.1; NM_001204143.1. [Q9UIS9-11]
DR RefSeq; NP_001191080.1; NM_001204151.2. [Q9UIS9-8]
DR RefSeq; NP_002375.1; NM_002384.2. [Q9UIS9-4]
DR RefSeq; NP_056669.2; NM_015844.2. [Q9UIS9-7]
DR RefSeq; NP_056670.2; NM_015845.3. [Q9UIS9-2]
DR RefSeq; NP_056671.2; NM_015846.3. [Q9UIS9-1]
DR RefSeq; NP_056723.2; NM_015847.3. [Q9UIS9-5]
DR RefSeq; XP_005258328.1; XM_005258271.2. [Q9UIS9-1]
DR RefSeq; XP_011524295.1; XM_011525993.2. [Q9UIS9-9]
DR RefSeq; XP_011524296.1; XM_011525994.2.
DR RefSeq; XP_011524308.1; XM_011526006.1. [Q9UIS9-11]
DR RefSeq; XP_016881249.1; XM_017025760.1. [Q9UIS9-1]
DR RefSeq; XP_016881259.1; XM_017025770.1. [Q9UIS9-7]
DR RefSeq; XP_016881260.1; XM_017025771.1.
DR RefSeq; XP_016881265.1; XM_017025776.1. [Q9UIS9-4]
DR PDB; 1D9N; NMR; -; A=1-75.
DR PDB; 1IG4; NMR; -; A=1-75.
DR PDB; 4D4W; NMR; -; A=167-222.
DR PDB; 5W9Q; X-ray; 1.80 A; A/B=330-388.
DR PDB; 6D1T; X-ray; 2.25 A; A=1-77.
DR PDBsum; 1D9N; -.
DR PDBsum; 1IG4; -.
DR PDBsum; 4D4W; -.
DR PDBsum; 5W9Q; -.
DR PDBsum; 6D1T; -.
DR AlphaFoldDB; Q9UIS9; -.
DR BMRB; Q9UIS9; -.
DR SMR; Q9UIS9; -.
DR BioGRID; 110322; 65.
DR CORUM; Q9UIS9; -.
DR IntAct; Q9UIS9; 42.
DR MINT; Q9UIS9; -.
DR STRING; 9606.ENSP00000468785; -.
DR iPTMnet; Q9UIS9; -.
DR PhosphoSitePlus; Q9UIS9; -.
DR BioMuta; MBD1; -.
DR DMDM; 50401200; -.
DR EPD; Q9UIS9; -.
DR jPOST; Q9UIS9; -.
DR MassIVE; Q9UIS9; -.
DR MaxQB; Q9UIS9; -.
DR PaxDb; Q9UIS9; -.
DR PeptideAtlas; Q9UIS9; -.
DR PRIDE; Q9UIS9; -.
DR ProteomicsDB; 84560; -. [Q9UIS9-1]
DR ProteomicsDB; 84561; -. [Q9UIS9-2]
DR ProteomicsDB; 84562; -. [Q9UIS9-4]
DR ProteomicsDB; 84563; -. [Q9UIS9-5]
DR ProteomicsDB; 84564; -. [Q9UIS9-6]
DR ProteomicsDB; 84565; -. [Q9UIS9-7]
DR ProteomicsDB; 84566; -. [Q9UIS9-8]
DR ProteomicsDB; 84567; -. [Q9UIS9-9]
DR Antibodypedia; 3959; 435 antibodies from 33 providers.
DR CPTC; Q9UIS9; 3 antibodies.
DR DNASU; 4152; -.
DR Ensembl; ENST00000269468.10; ENSP00000269468.5; ENSG00000141644.18. [Q9UIS9-1]
DR Ensembl; ENST00000269471.9; ENSP00000269471.5; ENSG00000141644.18. [Q9UIS9-2]
DR Ensembl; ENST00000339998.10; ENSP00000339546.5; ENSG00000141644.18. [Q9UIS9-6]
DR Ensembl; ENST00000347968.7; ENSP00000285102.5; ENSG00000141644.18. [Q9UIS9-7]
DR Ensembl; ENST00000353909.7; ENSP00000269469.5; ENSG00000141644.18. [Q9UIS9-5]
DR Ensembl; ENST00000382948.9; ENSP00000372407.5; ENSG00000141644.18. [Q9UIS9-1]
DR Ensembl; ENST00000398488.5; ENSP00000381502.1; ENSG00000141644.18. [Q9UIS9-4]
DR Ensembl; ENST00000398493.5; ENSP00000381506.1; ENSG00000141644.18. [Q9UIS9-7]
DR Ensembl; ENST00000457839.6; ENSP00000405268.2; ENSG00000141644.18. [Q9UIS9-9]
DR Ensembl; ENST00000585595.5; ENSP00000468430.1; ENSG00000141644.18. [Q9UIS9-9]
DR Ensembl; ENST00000585672.5; ENSP00000466092.1; ENSG00000141644.18. [Q9UIS9-10]
DR Ensembl; ENST00000587605.5; ENSP00000468042.1; ENSG00000141644.18. [Q9UIS9-11]
DR Ensembl; ENST00000588937.5; ENSP00000467763.1; ENSG00000141644.18. [Q9UIS9-2]
DR Ensembl; ENST00000590208.5; ENSP00000468785.1; ENSG00000141644.18. [Q9UIS9-12]
DR Ensembl; ENST00000591416.5; ENSP00000467017.1; ENSG00000141644.18. [Q9UIS9-1]
DR Ensembl; ENST00000591535.5; ENSP00000465923.1; ENSG00000141644.18. [Q9UIS9-8]
DR GeneID; 4152; -.
DR KEGG; hsa:4152; -.
DR MANE-Select; ENST00000269468.10; ENSP00000269468.5; NM_015846.4; NP_056671.2.
DR UCSC; uc002leg.4; human. [Q9UIS9-1]
DR CTD; 4152; -.
DR DisGeNET; 4152; -.
DR GeneCards; MBD1; -.
DR HGNC; HGNC:6916; MBD1.
DR HPA; ENSG00000141644; Low tissue specificity.
DR MIM; 156535; gene.
DR neXtProt; NX_Q9UIS9; -.
DR OpenTargets; ENSG00000141644; -.
DR PharmGKB; PA30659; -.
DR VEuPathDB; HostDB:ENSG00000141644; -.
DR eggNOG; ENOG502QQE9; Eukaryota.
DR GeneTree; ENSGT00950000183005; -.
DR HOGENOM; CLU_031386_0_0_1; -.
DR InParanoid; Q9UIS9; -.
DR OMA; VGPQKSH; -.
DR OrthoDB; 1431783at2759; -.
DR PhylomeDB; Q9UIS9; -.
DR PathwayCommons; Q9UIS9; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR SignaLink; Q9UIS9; -.
DR SIGNOR; Q9UIS9; -.
DR BioGRID-ORCS; 4152; 13 hits in 1102 CRISPR screens.
DR ChiTaRS; MBD1; human.
DR EvolutionaryTrace; Q9UIS9; -.
DR GeneWiki; MBD1; -.
DR GenomeRNAi; 4152; -.
DR Pharos; Q9UIS9; Tbio.
DR PRO; PR:Q9UIS9; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9UIS9; protein.
DR Bgee; ENSG00000141644; Expressed in left testis and 205 other tissues.
DR ExpressionAtlas; Q9UIS9; baseline and differential.
DR Genevisible; Q9UIS9; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR IDEAL; IID00332; -.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR002857; Znf_CXXC.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF02008; zf-CXXC; 3.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS51058; ZF_CXXC; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..605
FT /note="Methyl-CpG-binding domain protein 1"
FT /id="PRO_0000096258"
FT DOMAIN 1..69
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338,
FT ECO:0000269|PubMed:10581239, ECO:0000269|PubMed:11371345,
FT ECO:0000269|Ref.36"
FT ZN_FING 169..216
FT /note="CXXC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:26354109"
FT ZN_FING 217..263
FT /note="CXXC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 330..378
FT /note="CXXC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034"
FT REGION 80..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..592
FT /note="Transcriptional repression domain (TRD)"
FT /evidence="ECO:0000269|PubMed:14555760"
FT MOTIF 84..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 80..95
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9Q"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 499
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 173..221
FT /note="Missing (in isoform 5 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:9207790"
FT /id="VSP_011064"
FT VAR_SEQ 264
FT /note="R -> RHLAHRLRRRHQRCQRRTPLAVAPPT (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042812"
FT VAR_SEQ 304..326
FT /note="Missing (in isoform 2 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10454587, ECO:0000303|Ref.5"
FT /id="VSP_011065"
FT VAR_SEQ 326..382
FT /note="LQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQC
FT LQFAM -> L (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_054736"
FT VAR_SEQ 327..382
FT /note="Missing (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10454587,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011066"
FT VAR_SEQ 327
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_054737"
FT VAR_SEQ 483..528
FT /note="Missing (in isoform 2, isoform 4, isoform 6, isoform
FT 8 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10454587, ECO:0000303|Ref.5"
FT /id="VSP_011068"
FT VAR_SEQ 573..596
FT /note="ITEIFSLGGTRFRDTAVWLPRSKD -> EPTTQPQYSGNFDNDLYEIYLIDI
FT (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_011069"
FT VAR_SEQ 593..605
FT /note="RSKDLKKPGARKQ -> SLQGRHSGREDGCKVWETEDTVEPTSTSWNPRGWP
FT GTHVSLSPPPASMMWVSCRRSWCPSSQS (in isoform 2 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:10454587"
FT /id="VSP_011070"
FT VAR_SEQ 594..605
FT /note="SKDLKKPGARKQ -> YYHLALDWKCNCGYHLCCRSVLVP (in isoform
FT 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_054738"
FT VAR_SEQ 594..605
FT /note="SKDLKKPGARKQ -> AGTREGKMDVKCGRPRTQWSPRARAGTHEDGLEPMS
FT VSHHLQLR (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_054739"
FT VAR_SEQ 597..605
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_011071"
FT VARIANT 401
FT /note="P -> A (in dbSNP:rs125555)"
FT /evidence="ECO:0000269|PubMed:10441743"
FT /id="VAR_019513"
FT MUTAGEN 22
FT /note="R->A,K: Abolishes binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 30
FT /note="R->A: Strongly reduces binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 30
FT /note="R->K: No loss of binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:11371345"
FT MUTAGEN 32
FT /note="D->A: Strongly reduces binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 34
FT /note="Y->A,F: Strongly reduces binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 44
FT /note="R->A,K: Abolishes binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 45
FT /note="S->A: Reduces binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 46
FT /note="K->A: Strongly reduces binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:11371345"
FT MUTAGEN 52
FT /note="Y->A: No loss of binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:10581239,
FT ECO:0000269|PubMed:11371345"
FT MUTAGEN 64
FT /note="F->A: Disrupts tertiary structure and abolishes DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:10581239"
FT MUTAGEN 65
FT /note="K->A: Strongly reduces binding to methylated DNA."
FT /evidence="ECO:0000269|PubMed:11371345"
FT MUTAGEN 576
FT /note="I->R: Abolishes interaction with ATF7IP and
FT subsequent transcription repression activity."
FT /evidence="ECO:0000269|PubMed:15691849"
FT CONFLICT 239
FT /note="H -> R (in Ref. 5; ABP02056)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="T -> M (in Ref. 5; ABP02056)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..349
FT /note="MD -> NG (in Ref. 1; CAA71735 and 3; AAD51442/
FT AAD51443)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="L -> M (in Ref. 1; CAA71735)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1IG4"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6D1T"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6D1T"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:6D1T"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6D1T"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1D9N"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6D1T"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1IG4"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:6D1T"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4D4W"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:4D4W"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4D4W"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5W9Q"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:5W9Q"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5W9Q"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:5W9Q"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5W9Q"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5W9Q"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:5W9Q"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5W9Q"
FT CONFLICT Q9UIS9-7:327
FT /note="K -> Q (in Ref. 3; AAD51444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 66607 MW; 665732782CC6A32A CRC64;
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT RYLGPACDLT
LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV GPQSGEVRKE APRDETKADT
DTAPASFPAP GCCENCGISF SGDGTQRQRL KTLCKDCRAQ RIAFNREQRM FKRVGCGECA
ACQVTEDCGA CSTCLLQLPH DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC
PICLRPPRPG LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC GRCDFCCDKP
KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP PPYRRRKRPS SARRHHLGPT
LKPTLATRTA QPDHTQAPTK QEAGGGFVLP PPGTDLVFLR EGASSPVQVP GPVAASTEAL
LQEAQCSGLS WVVALPQVKQ EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE
PPDPEEDKEE NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPRSKDLKKP
GARKQ
