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Database: UniProt
Entry: Q9UBC3
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Original site: Q9UBC3 
ID   DNM3B_HUMAN             Reviewed;         853 AA.
AC   Q9UBC3; A2A2E2; B4DSM8; B4DSU1; E1P5M6; E1P5M7; E7EN63; E9PBF2; Q9UBD4;
AC   Q9UJQ5; Q9UKA6; Q9UNE5; Q9Y5R9; Q9Y5S0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 199.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 3B;
DE            Short=Dnmt3b;
DE            EC=2.1.1.37;
DE   AltName: Full=DNA methyltransferase HsaIIIB;
DE            Short=DNA MTase HsaIIIB;
DE            Short=M.HsaIIIB;
GN   Name=DNMT3B;
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] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Fetal testis, and Small intestine;
RX   PubMed=10433969; DOI=10.1016/s0378-1119(99)00252-8;
RA   Xie S., Wang Z., Okano M., Nogami M., Li Y., He W.-W., Okumura K., Li E.;
RT   "Cloning, expression and chromosome locations of the human DNMT3 gene
RT   family.";
RL   Gene 236:87-95(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND VARIANTS ICF1 SER-663; GLY-726;
RP   GLY-817 AND MET-818.
RC   TISSUE=Testis;
RX   PubMed=10647011; DOI=10.1038/46052;
RA   Xu G.-L., Bestor T.H., Bourc'his D., Hsieh C.-L., Tommerup N., Bugge M.,
RA   Hulten M., Qu X., Russo J.J., Viegas-Pequignot E.;
RT   "Chromosome instability and immunodeficiency syndrome caused by mutations
RT   in a DNA methyltransferase gene.";
RL   Nature 402:187-191(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ni J., Pradhan S., Roberts R.J.;
RT   "Cloning, expression and characterization of human DNMT3 genes.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 636-853 (ISOFORMS 1; 4 AND 5).
RC   TISSUE=Testis;
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   [8]
RP   INTERACTION WITH UBL1 AND UBE2I9, SUMOYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=11735126; DOI=10.1006/bbrc.2001.6057;
RA   Kang E.S., Park C.W., Chung J.H.;
RT   "Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9
RT   through its N-terminal region and is subject to modification by SUMO-1.";
RL   Biochem. Biophys. Res. Commun. 289:862-868(2001).
RN   [9]
RP   INTERACTION WITH DNMT1 AND DNMT3A, 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   [10]
RP   INTERACTION WITH SETDB1.
RX   PubMed=16682412; DOI=10.1074/jbc.m513249200;
RA   Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.;
RT   "The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A
RT   interact directly and localize to promoters silenced in cancer cells.";
RL   J. Biol. Chem. 281:19489-19500(2006).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
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   [12]
RP   ERRATUM.
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   [13]
RP   FUNCTION, AND INTERACTION WITH ZHX1.
RX   PubMed=17303076; DOI=10.1016/j.bbrc.2007.01.187;
RA   Kim S.H., Park J., Choi M.C., Kim H.P., Park J.H., Jung Y., Lee J.H.,
RA   Oh D.Y., Im S.A., Bang Y.J., Kim T.Y.;
RT   "Zinc-fingers and homeoboxes 1 (ZHX1) binds DNA methyltransferase (DNMT) 3B
RT   to enhance DNMT3B-mediated transcriptional repression.";
RL   Biochem. Biophys. Res. Commun. 355:318-323(2007).
RN   [14]
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   [15]
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   [16]
RP   FUNCTION.
RX   PubMed=18567530; DOI=10.1016/j.biocel.2008.04.018;
RA   Kim S.-H., Park J., Choi M.-C., Park J.-H., Kim H.-P., Lee J.-H., Oh D.-Y.,
RA   Im S.-A., Bang Y.-J., Kim T.-Y.;
RT   "DNA methyltransferase 3B acts as a co-repressor of the human polycomb
RT   protein hPc2 to repress fibroblast growth factor receptor 3
RT   transcription.";
RL   Int. J. Biochem. Cell Biol. 40:2462-2471(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP   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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; THR-96; SER-100; SER-110;
RP   SER-136; SER-195; SER-202 AND SER-209, AND IDENTIFICATION BY MASS
RP   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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-209, AND
RP   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   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-617, 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   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 206-355.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the PWWP domain of human DNA (cytosine-5-)-
RT   methyltransferase 3 beta.";
RL   Submitted (MAR-2009) to the PDB data bank.
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 380-509.
RX   PubMed=21720545; DOI=10.1371/journal.pone.0018919;
RA   Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
RA   Qiu W., Wang Y., Min J.;
RT   "Structural and histone binding ability characterizations of human PWWP
RT   domains.";
RL   PLoS ONE 6:E18919-E18919(2011).
RN   [23]
RP   VARIANTS ICF1 THR-603 AND SER-THR-PRO-806 INS.
RX   PubMed=10555141; DOI=10.1016/s0092-8674(00)81656-6;
RA   Okano M., Bell D.W., Haber D.A., Li E.;
RT   "DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo
RT   methylation and mammalian development.";
RL   Cell 99:247-257(1999).
RN   [24]
RP   VARIANTS ICF1 THR-603; GLY-726 AND SER-THR-PRO-806 INS.
RX   PubMed=10588719; DOI=10.1073/pnas.96.25.14412;
RA   Hansen R.S., Wijmenga C., Luo P., Stanek A.M., Canfield T.K.,
RA   Weemaes C.M.R., Gartler S.M.;
RT   "The DNMT3B DNA methyltransferase gene is mutated in the ICF
RT   immunodeficiency syndrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14412-14417(1999).
RN   [25]
RP   VARIANTS ICF1 VAL-585; THR-603; ALA-606; GLY-699; GLY-726; PRO-766; ARG-814
RP   AND MET-818.
RX   PubMed=11102980;
RX   DOI=10.1002/1098-1004(200012)16:6<509::aid-humu8>3.0.co;2-v;
RA   Wijmenga C., Hansen R.S., Gimelli G., Bjoerck E.J., Davies E.G.,
RA   Valentine D., Belohradsky B.H., van Dongen J.J., Smeets D.F.C.M.,
RA   van den Heuvel L.P.W.J., Luyten J.A.F.M., Strengman E., Weemaes C.M.R.,
RA   Pearson P.L.;
RT   "Genetic variation in ICF syndrome: evidence for genetic heterogeneity.";
RL   Hum. Mutat. 16:509-517(2000).
RN   [26]
RP   VARIANTS ICF1 PRO-270; VAL-585; THR-603; ALA-606; SER-663; PRO-664;
RP   GLY-699; GLY-726; PRO-766; ARG-814; GLY-817; MET-818 AND GLN-840.
RX   PubMed=15580563; DOI=10.1002/humu.20113;
RA   Jiang Y.L., Rigolet M., Bourc'his D., Nigon F., Bokesoy I., Fryns J.-P.,
RA   Hulten M., Jonveaux P., Maraschio P., Megarbane A., Moncla A.,
RA   Viegas-Pequignot E.;
RT   "DNMT3B mutations and DNA methylation defect define two types of ICF
RT   syndrome.";
RL   Hum. Mutat. 25:56-63(2005).
RN   [27]
RP   VARIANT ICF1 MET-836.
RX   PubMed=21120685; DOI=10.1007/s10875-010-9488-0;
RA   Kaya N., Al-Muhsen S., Al-Saud B., Al-Bakheet A., Colak D., Al-Ghonaium A.,
RA   Al-Dhekri H., Al-Mousa H., Arnaout R., Al-Owain M., Iqbal M.;
RT   "ICF syndrome in Saudi Arabia: immunological, cytogenetic and molecular
RT   analysis.";
RL   J. Clin. Immunol. 31:245-252(2011).
RN   [28]
RP   VARIANTS FSHD2 ARG-527 AND LEU-691, AND FUNCTION.
RX   PubMed=27153398; DOI=10.1016/j.ajhg.2016.03.013;
RA   van den Boogaard M.L., Lemmers R.J., Balog J., Wohlgemuth M., Auranen M.,
RA   Mitsuhashi S., van der Vliet P.J., Straasheijm K.R., van den Akker R.F.,
RA   Kriek M., Laurense-Bik M.E., Raz V., van Ostaijen-Ten Dam M.M.,
RA   Hansson K.B., van der Kooi E.L., Kiuru-Enari S., Udd B., van Tol M.J.,
RA   Nishino I., Tawil R., Tapscott S.J., van Engelen B.G., van der Maarel S.M.;
RT   "Mutations in DNMT3B modify epigenetic repression of the D4Z4 repeat and
RT   the penetrance of facioscapulohumeral dystrophy.";
RL   Am. J. Hum. Genet. 98:1020-1029(2016).
RN   [29]
RP   VARIANT ICF1 THR-585.
RX   PubMed=27734333; DOI=10.1007/s10875-016-0340-z;
RA   Rechavi E., Lev A., Eyal E., Barel O., Kol N., Barhom S.F.,
RA   Pode-Shakked B., Anikster Y., Somech R., Simon A.J.;
RT   "A novel mutation in a critical region for the methyl donor binding in
RT   DNMT3B causes immunodeficiency, centromeric instability, and facial
RT   anomalies syndrome (ICF).";
RL   J. Clin. Immunol. 36:801-809(2016).
CC   -!- FUNCTION: Required for genome-wide de novo methylation and is essential
CC       for the establishment of DNA methylation patterns during development.
CC       DNA methylation is coordinated with methylation of histones. May
CC       preferentially methylates nucleosomal DNA within the nucleosome core
CC       region. May function as transcriptional co-repressor by associating
CC       with CBX4 and independently of DNA methylation. Seems to be involved in
CC       gene silencing (By similarity). In association with DNMT1 and via the
CC       recruitment of CTCFL/BORIS, involved in activation of BAG1 gene
CC       expression by modulating dimethylation of promoter histone H3 at H3K4
CC       and H3K9. Isoforms 4 and 5 are probably not functional due to the
CC       deletion of two conserved methyltransferase motifs. Function as
CC       transcriptional corepressor by associating with ZHX1. Required for DUX4
CC       silencing in somatic cells (PubMed:27153398). {ECO:0000250,
CC       ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:17303076,
CC       ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18567530,
CC       ECO:0000269|PubMed:27153398}.
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   -!- ACTIVITY REGULATION: Activated by binding to the regulatory factor
CC       DNMT3L. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BAZ2A/TIP5, SUV39H1 and CBX4. Interacts with
CC       UHRF1 (By similarity). Interacts with DNMT1 and DNMT3A, SETDB1, UBL1,
CC       UBE2I9 and ZHX1. Interacts with the PRC2/EED-EZH2 complex.
CC       {ECO:0000250, ECO:0000269|PubMed:11735126, ECO:0000269|PubMed:12145218,
CC       ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:16682412,
CC       ECO:0000269|PubMed:17303076}.
CC   -!- INTERACTION:
CC       O75530:EED; NbExp=4; IntAct=EBI-80125, EBI-923794;
CC       Q96KQ7:EHMT2; NbExp=2; IntAct=EBI-80125, EBI-744366;
CC       Q15910:EZH2; NbExp=14; IntAct=EBI-80125, EBI-530054;
CC       Q9QR71:LANA1 (xeno); NbExp=2; IntAct=EBI-80125, EBI-15602554;
CC       P63165:SUMO1; NbExp=4; IntAct=EBI-80125, EBI-80140;
CC       P63279:UBE2I; NbExp=3; IntAct=EBI-80125, EBI-80168;
CC       Q96T88:UHRF1; NbExp=7; IntAct=EBI-80125, EBI-1548946;
CC       Q9UKY1:ZHX1; NbExp=6; IntAct=EBI-6083193, EBI-347767;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11735126,
CC       ECO:0000269|PubMed:12145218}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1;
CC         IsoId=Q9UBC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UBC3-2; Sequence=VSP_005637;
CC       Name=3;
CC         IsoId=Q9UBC3-3; Sequence=VSP_005637, VSP_005638;
CC       Name=4;
CC         IsoId=Q9UBC3-4; Sequence=VSP_005637, VSP_005639, VSP_005640;
CC       Name=5;
CC         IsoId=Q9UBC3-5; Sequence=VSP_005637, VSP_005641;
CC       Name=6;
CC         IsoId=Q9UBC3-6; Sequence=VSP_005636, VSP_005637;
CC       Name=7;
CC         IsoId=Q9UBC3-7; Sequence=VSP_045874, VSP_005637, VSP_045876;
CC       Name=8;
CC         IsoId=Q9UBC3-8; Sequence=VSP_045875, VSP_005637, VSP_045876;
CC   -!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal liver, heart,
CC       kidney, placenta, and at lower levels in spleen, colon, brain, liver,
CC       small intestine, lung, peripheral blood mononuclear cells, and skeletal
CC       muscle. Isoform 1 is expressed in all tissues except brain, skeletal
CC       muscle and PBMC, 3 is ubiquitous, 4 is expressed in all tissues except
CC       brain, skeletal muscle, lung and prostate and 5 is detectable only in
CC       testis and at very low level in brain and prostate.
CC   -!- DOMAIN: The PWWP domain is essential for targeting to pericentric
CC       heterochromatin.
CC   -!- PTM: Sumoylated. {ECO:0000269|PubMed:11735126}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC   -!- DISEASE: Immunodeficiency-centromeric instability-facial anomalies
CC       syndrome 1 (ICF1) [MIM:242860]: A rare disorder characterized by a
CC       variable immunodeficiency resulting in recurrent infections, facial
CC       anomalies, and branching of chromosomes 1, 9, and 16. Other variable
CC       symptoms include growth retardation, failure to thrive, and psychomotor
CC       retardation. Laboratory studies show limited hypomethylation of DNA in
CC       a small fraction of the genome in some, but not all, patients.
CC       {ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:10588719,
CC       ECO:0000269|PubMed:10647011, ECO:0000269|PubMed:11102980,
CC       ECO:0000269|PubMed:15580563, ECO:0000269|PubMed:21120685,
CC       ECO:0000269|PubMed:27734333}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Facioscapulohumeral muscular dystrophy 2 (FSHD2) [MIM:158901]:
CC       A degenerative muscle disease characterized by slowly progressive
CC       weakness of the muscles of the face, upper-arm, and shoulder girdle.
CC       The onset of symptoms usually occurs in the first or second decade of
CC       life. Affected individuals usually present with impairment of upper
CC       extremity elevation. This tends to be followed by facial weakness,
CC       primarily involving the orbicularis oris and orbicularis oculi muscles.
CC       {ECO:0000269|PubMed:27153398}. Note=The gene represented in this entry
CC       may act as a disease modifier. DNMT3B mutations lead to DUX4 expression
CC       in somatic tissues, including muscle cells, when an haplotype on
CC       chromosome 4 is permissive for DUX4 expression. Ectopic expression of
CC       DUX4 in skeletal muscle activates the expression of stem cell and
CC       germline genes, and, when overexpressed in somatic cells, DUX4 can
CC       ultimately lead to cell death.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   -!- WEB RESOURCE: Name=DNMT3Bbase; Note=DNMT3B mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/DNMT3Bbase/";
DR   EMBL; AF156487; AAD53062.1; -; mRNA.
DR   EMBL; AF156488; AAD53063.1; -; mRNA.
DR   EMBL; AF176228; AAF04015.1; -; mRNA.
DR   EMBL; AF331857; AAL57040.1; -; mRNA.
DR   EMBL; AK299821; BAG61690.1; -; mRNA.
DR   EMBL; AK299915; BAG61753.1; -; mRNA.
DR   EMBL; AL035071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76351.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76352.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76353.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76354.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76356.1; -; Genomic_DNA.
DR   EMBL; AF129267; AAD31432.1; -; mRNA.
DR   EMBL; AF129268; AAD31433.1; -; mRNA.
DR   EMBL; AF129269; AAD31434.1; -; mRNA.
DR   CCDS; CCDS13204.1; -. [Q9UBC3-6]
DR   CCDS; CCDS13205.1; -. [Q9UBC3-1]
DR   CCDS; CCDS13206.1; -. [Q9UBC3-2]
DR   CCDS; CCDS13207.1; -. [Q9UBC3-3]
DR   CCDS; CCDS56183.1; -. [Q9UBC3-8]
DR   CCDS; CCDS56184.1; -. [Q9UBC3-7]
DR   RefSeq; NP_001193984.1; NM_001207055.1. [Q9UBC3-8]
DR   RefSeq; NP_001193985.1; NM_001207056.1. [Q9UBC3-7]
DR   RefSeq; NP_008823.1; NM_006892.3. [Q9UBC3-1]
DR   RefSeq; NP_787044.1; NM_175848.1. [Q9UBC3-2]
DR   RefSeq; NP_787045.1; NM_175849.1. [Q9UBC3-3]
DR   RefSeq; NP_787046.1; NM_175850.2. [Q9UBC3-6]
DR   PDB; 3FLG; X-ray; 1.80 A; A=206-355.
DR   PDB; 3QKJ; X-ray; 2.04 A; A/B/C/D=206-355.
DR   PDB; 5CIU; X-ray; 2.24 A; A/B=206-355.
DR   PDB; 5NR3; X-ray; 2.30 A; A/B=206-355.
DR   PDB; 5NRR; X-ray; 1.70 A; A/B=206-355.
DR   PDB; 5NRS; X-ray; 2.30 A; A/B=206-355.
DR   PDB; 5NRV; X-ray; 2.08 A; A/D=206-355.
DR   PDB; 5NV0; X-ray; 2.40 A; A/B=206-355.
DR   PDB; 5NV2; X-ray; 2.03 A; A/B=206-355.
DR   PDB; 5NV7; X-ray; 2.57 A; A/B=206-355.
DR   PDB; 5NVO; X-ray; 2.40 A; A/B=206-355.
DR   PDBsum; 3FLG; -.
DR   PDBsum; 3QKJ; -.
DR   PDBsum; 5CIU; -.
DR   PDBsum; 5NR3; -.
DR   PDBsum; 5NRR; -.
DR   PDBsum; 5NRS; -.
DR   PDBsum; 5NRV; -.
DR   PDBsum; 5NV0; -.
DR   PDBsum; 5NV2; -.
DR   PDBsum; 5NV7; -.
DR   PDBsum; 5NVO; -.
DR   SMR; Q9UBC3; -.
DR   BioGrid; 108126; 81.
DR   CORUM; Q9UBC3; -.
DR   DIP; DIP-30000N; -.
DR   IntAct; Q9UBC3; 35.
DR   MINT; Q9UBC3; -.
DR   STRING; 9606.ENSP00000328547; -.
DR   BindingDB; Q9UBC3; -.
DR   ChEMBL; CHEMBL6095; -.
DR   DrugCentral; Q9UBC3; -.
DR   REBASE; 4120; M.HsaDnmt3B.
DR   iPTMnet; Q9UBC3; -.
DR   PhosphoSitePlus; Q9UBC3; -.
DR   BioMuta; DNMT3B; -.
DR   DMDM; 17375667; -.
DR   EPD; Q9UBC3; -.
DR   jPOST; Q9UBC3; -.
DR   MassIVE; Q9UBC3; -.
DR   MaxQB; Q9UBC3; -.
DR   PaxDb; Q9UBC3; -.
DR   PeptideAtlas; Q9UBC3; -.
DR   PRIDE; Q9UBC3; -.
DR   ProteomicsDB; 17089; -.
DR   ProteomicsDB; 19210; -.
DR   ProteomicsDB; 83935; -. [Q9UBC3-1]
DR   ProteomicsDB; 83936; -. [Q9UBC3-2]
DR   ProteomicsDB; 83937; -. [Q9UBC3-3]
DR   ProteomicsDB; 83938; -. [Q9UBC3-4]
DR   ProteomicsDB; 83939; -. [Q9UBC3-5]
DR   ProteomicsDB; 83940; -. [Q9UBC3-6]
DR   DNASU; 1789; -.
DR   Ensembl; ENST00000201963; ENSP00000201963; ENSG00000088305. [Q9UBC3-6]
DR   Ensembl; ENST00000328111; ENSP00000328547; ENSG00000088305. [Q9UBC3-1]
DR   Ensembl; ENST00000348286; ENSP00000337764; ENSG00000088305. [Q9UBC3-3]
DR   Ensembl; ENST00000353855; ENSP00000313397; ENSG00000088305. [Q9UBC3-2]
DR   Ensembl; ENST00000443239; ENSP00000403169; ENSG00000088305. [Q9UBC3-8]
DR   Ensembl; ENST00000456297; ENSP00000412305; ENSG00000088305. [Q9UBC3-7]
DR   GeneID; 1789; -.
DR   KEGG; hsa:1789; -.
DR   UCSC; uc002wyc.3; human. [Q9UBC3-1]
DR   CTD; 1789; -.
DR   DisGeNET; 1789; -.
DR   EuPathDB; HostDB:ENSG00000088305.18; -.
DR   GeneCards; DNMT3B; -.
DR   HGNC; HGNC:2979; DNMT3B.
DR   HPA; CAB069896; -.
DR   HPA; HPA001595; -.
DR   HPA; HPA001803; -.
DR   MalaCards; DNMT3B; -.
DR   MIM; 158901; phenotype.
DR   MIM; 242860; phenotype.
DR   MIM; 602900; gene.
DR   neXtProt; NX_Q9UBC3; -.
DR   OpenTargets; ENSG00000088305; -.
DR   Orphanet; 2268; ICF syndrome.
DR   PharmGKB; PA27446; -.
DR   eggNOG; ENOG410IGHW; Eukaryota.
DR   eggNOG; ENOG410XQ4Y; LUCA.
DR   GeneTree; ENSGT00940000156928; -.
DR   HOGENOM; HOG000230875; -.
DR   InParanoid; Q9UBC3; -.
DR   KO; K17399; -.
DR   OMA; IKPMLDW; -.
DR   OrthoDB; 539311at2759; -.
DR   PhylomeDB; Q9UBC3; -.
DR   TreeFam; TF329039; -.
DR   BRENDA; 2.1.1.37; 2681.
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; Q9UBC3; -.
DR   ChiTaRS; DNMT3B; human.
DR   EvolutionaryTrace; Q9UBC3; -.
DR   GeneWiki; DNMT3B; -.
DR   GenomeRNAi; 1789; -.
DR   Pharos; Q9UBC3; Tchem.
DR   PRO; PR:Q9UBC3; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9UBC3; protein.
DR   Bgee; ENSG00000088305; Expressed in 137 organ(s), highest expression level in secondary oocyte.
DR   Genevisible; Q9UBC3; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009008; F:DNA-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR   GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0006306; P:DNA methylation; TAS:UniProtKB.
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; IDA: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:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR   CDD; cd11728; ADDz_Dnmt3b; 1.
DR   InterPro; IPR025766; ADD.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR040552; DNMT3_ADD.
DR   InterPro; IPR030488; DNMT3B_ADD.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF17980; ADD_DNMT3; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51533; ADD; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Citrullination;
KW   Disease mutation; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transferase;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..853
FT                   /note="DNA (cytosine-5)-methyltransferase 3B"
FT                   /id="PRO_0000088045"
FT   DOMAIN          225..283
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   DOMAIN          423..555
FT                   /note="ADD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   DOMAIN          575..853
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ZN_FING         434..464
FT                   /note="GATA-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   ZN_FING         475..531
FT                   /note="PHD-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT   REGION          1..298
FT                   /note="Interaction with DNMT1 and DNMT3A"
FT                   /evidence="ECO:0000269|PubMed:12145218"
FT   REGION          435..527
FT                   /note="Interaction with the PRC2/EED-EZH2 complex"
FT                   /evidence="ECO:0000250"
FT   REGION          582..586
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT   REGION          627..629
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT   REGION          832..834
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT   ACT_SITE        651
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
FT   BINDING         605
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         96
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         410
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        89
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        617
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1
FT                   /note="M -> MEPSPEPPSLESM (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10647011"
FT                   /id="VSP_005636"
FT   VAR_SEQ         69..144
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045874"
FT   VAR_SEQ         103..144
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045875"
FT   VAR_SEQ         356..375
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT                   5, isoform 6, isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10325416,
FT                   ECO:0000303|PubMed:10433969, ECO:0000303|PubMed:10647011,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_005637"
FT   VAR_SEQ         744..806
FT                   /note="Missing (in isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045876"
FT   VAR_SEQ         744
FT                   /note="R -> S (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10325416"
FT                   /id="VSP_005639"
FT   VAR_SEQ         745..853
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10325416"
FT                   /id="VSP_005640"
FT   VAR_SEQ         745..807
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10433969"
FT                   /id="VSP_005638"
FT   VAR_SEQ         768..853
FT                   /note="LKKVQTITTKSNSIKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVS
FT                   NMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE -> DLWLSCALHRRVQHGPWCPPE
FT                   AAGKVLERACHPTPLRPSEGLLCM (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10325416"
FT                   /id="VSP_005641"
FT   VARIANT         54
FT                   /note="R -> P (in dbSNP:rs17123590)"
FT                   /id="VAR_033885"
FT   VARIANT         270
FT                   /note="S -> P (in ICF1; dbSNP:rs121908947)"
FT                   /evidence="ECO:0000269|PubMed:15580563"
FT                   /id="VAR_022579"
FT   VARIANT         527
FT                   /note="C -> R (in FSHD2)"
FT                   /evidence="ECO:0000269|PubMed:27153398"
FT                   /id="VAR_077527"
FT   VARIANT         585
FT                   /note="A -> T (in ICF1; dbSNP:rs750849178)"
FT                   /evidence="ECO:0000269|PubMed:27734333"
FT                   /id="VAR_077528"
FT   VARIANT         585
FT                   /note="A -> V (in ICF1)"
FT                   /evidence="ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011506"
FT   VARIANT         603
FT                   /note="A -> T (in ICF1; dbSNP:rs121908943)"
FT                   /evidence="ECO:0000269|PubMed:10555141,
FT                   ECO:0000269|PubMed:10588719, ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011499"
FT   VARIANT         606
FT                   /note="V -> A (in ICF1; dbSNP:rs867732105)"
FT                   /evidence="ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011507"
FT   VARIANT         663
FT                   /note="G -> S (in ICF1; dbSNP:rs121908942)"
FT                   /evidence="ECO:0000269|PubMed:10647011,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011500"
FT   VARIANT         664
FT                   /note="L -> P (in ICF1)"
FT                   /evidence="ECO:0000269|PubMed:15580563"
FT                   /id="VAR_022580"
FT   VARIANT         691
FT                   /note="P -> L (in FSHD2; dbSNP:rs889145646)"
FT                   /evidence="ECO:0000269|PubMed:27153398"
FT                   /id="VAR_077529"
FT   VARIANT         699
FT                   /note="V -> G (in ICF1)"
FT                   /evidence="ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011508"
FT   VARIANT         726
FT                   /note="V -> G (in ICF1; dbSNP:rs121908941)"
FT                   /evidence="ECO:0000269|PubMed:10588719,
FT                   ECO:0000269|PubMed:10647011, ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011501"
FT   VARIANT         766
FT                   /note="A -> P (in ICF1; dbSNP:rs1191203668)"
FT                   /evidence="ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011509"
FT   VARIANT         806
FT                   /note="E -> ESTP (in ICF1)"
FT                   /id="VAR_011502"
FT   VARIANT         814
FT                   /note="H -> R (in ICF1; dbSNP:rs1219696128)"
FT                   /evidence="ECO:0000269|PubMed:11102980,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011510"
FT   VARIANT         817
FT                   /note="D -> G (in ICF1; dbSNP:rs121908939)"
FT                   /evidence="ECO:0000269|PubMed:10647011,
FT                   ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011503"
FT   VARIANT         818
FT                   /note="V -> M (in ICF1; dbSNP:rs121908940)"
FT                   /evidence="ECO:0000269|PubMed:10647011,
FT                   ECO:0000269|PubMed:11102980, ECO:0000269|PubMed:15580563"
FT                   /id="VAR_011504"
FT   VARIANT         836
FT                   /note="V -> M (in ICF1; unknown pathological significance;
FT                   dbSNP:rs866792483)"
FT                   /evidence="ECO:0000269|PubMed:21120685"
FT                   /id="VAR_077530"
FT   VARIANT         840
FT                   /note="R -> Q (in ICF1; dbSNP:rs121908946)"
FT                   /evidence="ECO:0000269|PubMed:15580563"
FT                   /id="VAR_022581"
FT   CONFLICT        575
FT                   /note="I -> T (in Ref. 4; BAG61690)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        583
FT                   /note="G -> D (in Ref. 4; BAG61753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        655
FT                   /note="S -> P (in Ref. 4; BAG61690)"
FT                   /evidence="ECO:0000305"
FT   STRAND          219..222
FT                   /evidence="ECO:0000244|PDB:5CIU"
FT   STRAND          228..231
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   STRAND          239..244
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           246..248
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   STRAND          258..263
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   TURN            264..266
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   STRAND          269..273
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           274..276
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   STRAND          277..279
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           283..286
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           289..294
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           296..313
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           325..337
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   TURN            341..343
FT                   /evidence="ECO:0000244|PDB:5NRR"
FT   HELIX           344..348
FT                   /evidence="ECO:0000244|PDB:5NRR"
SQ   SEQUENCE   853 AA;  95751 MW;  F20A67CF78951532 CRC64;
     MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV
     SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS
     PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT
     PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP
     AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK
     AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPVVNKS
     KVRRAGSRKL ESRKYENKTR RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM
     ASDVANNKSS LEDGCLSCGR KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV
     CCEGRELLLC SNTSCCRCFC VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK
     DWNVRLQAFF TSDTGLEYEA PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK
     YVASEVCEES IAVGTVKHEG NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA
     RKGLYEGTGR LFFEFYHLLN YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM
     IDAIKVSAAH RARYFWGNLP GMNRPVIASK NDKLELQDCL EYNRIAKLKK VQTITTKSNS
     IKQGKNQLFP VVMNGKEDVL WCTELERIFG FPVHYTDVSN MGRGARQKLL GRSWSVPVIR
     HLFAPLKDYF ACE
//
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