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Database: UniProt/SWISS-PROT
Entry: SETB1_HUMAN
LinkDB: SETB1_HUMAN
Original site: SETB1_HUMAN 
ID   SETB1_HUMAN             Reviewed;        1291 AA.
AC   Q15047; A6NEW2; Q5SZD8; Q5SZD9; Q5SZE0; Q5SZE7; Q96GM9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   05-DEC-2018, entry version 202.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB1;
DE            EC=2.1.1.43;
DE   AltName: Full=ERG-associated protein with SET domain;
DE            Short=ESET;
DE   AltName: Full=Histone H3-K9 methyltransferase 4;
DE            Short=H3-K9-HMTase 4;
DE   AltName: Full=Lysine N-methyltransferase 1E;
DE   AltName: Full=SET domain bifurcated 1;
GN   Name=SETDB1; Synonyms=KIAA0067, KMT1E;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA   Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA   Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. II.
RT   The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT   analysis of cDNA clones from human cell line KG-1.";
RL   DNA Res. 1:223-229(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP   VARIANT SER-506.
RC   TISSUE=Muscle, and Uterus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   CHARACTERIZATION, MUTAGENESIS OF 729-CYS--CYS-731; HIS-1224; CYS-1226
RP   AND CYS-1279, AND INTERACTION WITH TRIM28.
RX   PubMed=11959841; DOI=10.1101/gad.973302;
RA   Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III;
RT   "SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific
RT   methyltransferase that contributes to HP1-mediated silencing of
RT   euchromatic genes by KRAB zinc-finger proteins.";
RL   Genes Dev. 16:919-932(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=12869583; DOI=10.1101/gad.1102803;
RA   Ayyanathan K., Lechner M.S., Bell P., Maul G.G., Schultz D.C.,
RA   Yamada Y., Tanaka K., Torigoe K., Rauscher F.J. III;
RT   "Regulated recruitment of HP1 to a euchromatic gene induces
RT   mitotically heritable, epigenetic gene silencing: a mammalian cell
RT   culture model of gene variegation.";
RL   Genes Dev. 17:1855-1869(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
RP   ATF7IP.
RX   PubMed=14536086; DOI=10.1016/j.molcel.2003.08.007;
RA   Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B.,
RA   Tempst P., Roeder R.G., Zhang Y.;
RT   "mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9
RT   of histone H3 to cause transcriptional repression.";
RL   Mol. Cell 12:475-487(2003).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH MBD1 AND CHAF1A.
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
RT   lysine 9 by SETDB1 to DNA replication and chromatin assembly.";
RL   Mol. Cell 15:595-605(2004).
RN   [9]
RP   INTERACTION WITH CBX1 AND CBX5.
RX   PubMed=15899859; DOI=10.1128/MCB.25.11.4552-4564.2005;
RA   Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J.,
RA   Carpenter A.E., Belmont A.S., van Driel R.;
RT   "In vivo HP1 targeting causes large-scale chromatin condensation and
RT   enhanced histone lysine methylation.";
RL   Mol. Cell. Biol. 25:4552-4564(2005).
RN   [10]
RP   INTERACTION WITH MBD1.
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
RT   PIAS proteins.";
RL   EMBO J. 25:5317-5328(2006).
RN   [11]
RP   INTERACTION WITH ATF7IP AND ATF7IP2.
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   [12]
RP   INTERACTION WITH DNMT3A AND DNMT3B.
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
RT   DNMT3A interact directly and localize to promoters silenced in cancer
RT   cells.";
RL   J. Biol. Chem. 281:19489-19500(2006).
RN   [13]
RP   INTERACTION WITH SUMO2.
RX   PubMed=16567619; DOI=10.1073/pnas.0601066103;
RA   Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A.,
RA   Shi Y., Shi Y., Gill G.;
RT   "NXP-2 association with SUMO-2 depends on lysines required for
RT   transcriptional repression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006).
RN   [14]
RP   EXPRESSION IN HUNTINGTON DISEASE.
RX   PubMed=17142323; DOI=10.1073/pnas.0606373103;
RA   Ryu H., Lee J., Hagerty S.W., Soh B.Y., McAlpin S.E., Cormier K.A.,
RA   Smith K.M., Ferrante R.J.;
RT   "ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in
RT   Huntington's disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19176-19181(2006).
RN   [15]
RP   FUNCTION, INTERACTION WITH CHD7; NLK1 AND PPARG, PHOSPHORYLATION AT
RP   THR-976, AND MUTAGENESIS OF THR-976.
RX   PubMed=17952062; DOI=10.1038/ncb1647;
RA   Takada I., Mihara M., Suzawa M., Ohtake F., Kobayashi S., Igarashi M.,
RA   Youn M.Y., Takeyama K., Nakamura T., Mezaki Y., Takezawa S.,
RA   Yogiashi Y., Kitagawa H., Yamada G., Takada S., Minami Y., Shibuya H.,
RA   Matsumoto K., Kato S.;
RT   "A histone lysine methyltransferase activated by non-canonical Wnt
RT   signalling suppresses PPAR-gamma transactivation.";
RL   Nat. Cell Biol. 9:1273-1285(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, AND IDENTIFICATION
RP   BY 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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [17]
RP   IDENTIFICATION IN A COMPLEX WITH REST; CDYL; WIZ; EHMT1 AND EHMT2.
RX   PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
RA   Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
RA   Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
RA   Shi Y.;
RT   "CDYL bridges REST and histone methyltransferases for gene repression
RT   and suppression of cellular transformation.";
RL   Mol. Cell 32:718-726(2008).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, AND IDENTIFICATION
RP   BY 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   [19]
RP   INTERACTION WITH MPHOSPH8.
RX   PubMed=20871592; DOI=10.1038/emboj.2010.239;
RA   Kokura K., Sun L., Bedford M.T., Fang J.;
RT   "Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing
RT   and promotes tumour cell motility and invasion.";
RL   EMBO J. 29:3673-3687(2010).
RN   [20]
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.,
RA   Buerckstuemmer T., 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   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, AND IDENTIFICATION
RP   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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025 AND SER-1066, 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   [23]
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
RT   CpG island methylator phenotype.";
RL   Elife 3:E02313-E02313(2014).
RN   [24]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [25]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1170 AND LYS-1178, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1032 AND LYS-1069, AND
RP   IDENTIFICATION BY MASS 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   [27]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1032, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [28]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1032 AND LYS-1069, AND
RP   IDENTIFICATION BY MASS 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-1032 AND LYS-1069, 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [30]
RP   FUNCTION, INTERACTION WITH ATRX, AND FORMATION OF A COMPLEX WITH ATRX;
RP   TRIM28 AND ZNF274.
RX   PubMed=27029610; DOI=10.1080/15592294.2016.1169351;
RA   Valle-Garcia D., Qadeer Z.A., McHugh D.S., Ghiraldini F.G.,
RA   Chowdhury A.H., Hasson D., Dyer M.A., Recillas-Targa F., Bernstein E.;
RT   "ATRX binds to atypical chromatin domains at the 3' exons of zinc
RT   finger genes to preserve H3K9me3 enrichment.";
RL   Epigenetics 11:398-414(2016).
RN   [31]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182; LYS-1032; LYS-1038;
RP   LYS-1069 AND LYS-1149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 196-402.
RG   Structural genomics consortium (SGC);
RT   "The crystal structure of Tudor domain of human histone-lysine N-
RT   methyltransferase SETDB1.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to
CC       methylated histones. Mainly functions in euchromatin regions,
CC       thereby playing a central role in the silencing of euchromatic
CC       genes. H3 'Lys-9' trimethylation is coordinated with DNA
CC       methylation. Probably forms a complex with MBD1 and ATF7IP that
CC       represses transcription and couples DNA methylation and histone
CC       'Lys-9' trimethylation. Its activity is dependent on MBD1 and is
CC       heritably maintained through DNA replication by being recruited by
CC       CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor
CC       recruited by KRAB zinc-finger proteins. Probably forms a
CC       corepressor complex required for activated KRAS-mediated promoter
CC       hypermethylation and transcriptional silencing of tumor suppressor
CC       genes (TSGs) or other tumor-related genes in colorectal cancer
CC       (CRC) cells (PubMed:24623306). Also required to maintain a
CC       transcriptionally repressive state of genes in undifferentiated
CC       embryonic stem cells (ESCs) (PubMed:24623306). Associates at
CC       promoter regions of tumor suppressor genes (TSGs) leading to their
CC       gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex
CC       may play a role in recruiting ATRX to the 3'-exons of zinc-finger
CC       coding genes with atypical chromatin signatures to establish or
CC       maintain/protect H3K9me3 at these transcriptionally active regions
CC       (PubMed:27029610). {ECO:0000269|PubMed:12869583,
CC       ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:15327775,
CC       ECO:0000269|PubMed:17952062, ECO:0000269|PubMed:24623306,
CC       ECO:0000269|PubMed:27029610}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00906};
CC   -!- SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ,
CC       SETB1, EHMT1 and EHMT2 (PubMed:19061646). During DNA replication,
CC       it is recruited by SETDB1 to form a S phase-specific complex that
CC       facilitates methylation of H3 'Lys-9' during replication-coupled
CC       chromatin assembly and is at least composed of the CAF-1 subunit
CC       CHAF1A, MBD1 and SETDB1 (PubMed:15327775). Probably part of a
CC       corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1
CC       (PubMed:24623306). Interacts with TRIM28/TIF1B (PubMed:11959841).
CC       Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is
CC       required to stimulate histone methyltransferase activity and
CC       facilitate the conversion of dimethylated to trimethylated H3
CC       'Lys-9' (PubMed:14536086, PubMed:15691849). Interacts with MBD1;
CC       interaction is abolished when MBD1 is sumoylated (PubMed:15327775,
CC       PubMed:17066076). Interacts with CBX1 and CBX5 (PubMed:15899859).
CC       Interacts with DNMT3A and DNMT3B (PubMed:16682412). Interacts with
CC       SUMO2. Interacts with CHD7, NLK1 and PPARG (PubMed:17952062).
CC       Interacts with MPHOSPH8 (PubMed:20871592). Interacts with ERG (By
CC       similarity). Interacts with HDAC1, HDAC2, SIN3A and SIN3B (By
CC       similarity). Interacts with ATRX. Forms a complex with ATRX,
CC       TRIM28 and ZNF274 (PubMed:27029610).
CC       {ECO:0000250|UniProtKB:O88974, ECO:0000269|PubMed:11959841,
CC       ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:15327775,
CC       ECO:0000269|PubMed:15691849, ECO:0000269|PubMed:15899859,
CC       ECO:0000269|PubMed:16567619, ECO:0000269|PubMed:16682412,
CC       ECO:0000269|PubMed:17066076, ECO:0000269|PubMed:17952062,
CC       ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:20871592,
CC       ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:27029610}.
CC   -!- INTERACTION:
CC       P31749:AKT1; NbExp=9; IntAct=EBI-79691, EBI-296087;
CC       Q9Y6K1:DNMT3A; NbExp=7; IntAct=EBI-79691, EBI-923653;
CC       Q9UIS9:MBD1; NbExp=3; IntAct=EBI-79691, EBI-867196;
CC       Q99549:MPHOSPH8; NbExp=3; IntAct=EBI-79691, EBI-2653928;
CC       Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-9090795, EBI-524753;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with
CC       non-pericentromeric regions of chromatin. Excluded from nucleoli
CC       and islands of condensed chromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q15047-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15047-2; Sequence=VSP_002217, VSP_002218;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q15047-3; Sequence=VSP_034600;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed. High expression in testis.
CC   -!- DOMAIN: The pre-SET, SET and post-SET domains are all required for
CC       methyltransferase activity. The 347-amino-acid insertion in the
CC       SET domain has no effect on the catalytic activity.
CC   -!- DOMAIN: Isoform 2 lacks all domains required for histone
CC       methyltransferase activity.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Highly up-regulated in Huntington disease patients,
CC       suggesting that participates in the altered chromatin modulation
CC       and transcription dysfunction observed in Huntington disease. Its
CC       down-regulation has salubrious effects on patients, suggesting
CC       that it may be a promising treatment in Huntington disease
CC       patients.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00906}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA06689.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; D31891; BAA06689.2; ALT_INIT; mRNA.
DR   EMBL; AL590133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53506.1; -; Genomic_DNA.
DR   EMBL; BC009362; AAH09362.1; -; mRNA.
DR   EMBL; BC028671; AAH28671.1; -; mRNA.
DR   CCDS; CCDS44217.1; -. [Q15047-1]
DR   CCDS; CCDS58026.1; -. [Q15047-2]
DR   CCDS; CCDS972.1; -. [Q15047-3]
DR   RefSeq; NP_001138887.1; NM_001145415.1. [Q15047-1]
DR   RefSeq; NP_001230420.1; NM_001243491.1. [Q15047-2]
DR   RefSeq; NP_036564.3; NM_012432.3. [Q15047-3]
DR   RefSeq; XP_016858444.1; XM_017002955.1. [Q15047-2]
DR   UniGene; Hs.643565; -.
DR   PDB; 3DLM; X-ray; 1.77 A; A=196-402.
DR   PDB; 4X3S; X-ray; 1.60 A; C/D=1165-1174.
DR   PDB; 5KCH; X-ray; 1.70 A; A=196-403.
DR   PDB; 5KCO; X-ray; 1.47 A; A=196-403.
DR   PDB; 5KE2; X-ray; 1.56 A; A=196-402.
DR   PDB; 5KE3; X-ray; 1.70 A; A=196-402.
DR   PDB; 5KH6; X-ray; 2.05 A; A=196-400.
DR   PDB; 6AU2; X-ray; 1.63 A; A=196-402.
DR   PDB; 6AU3; X-ray; 1.80 A; A=196-402.
DR   PDB; 6BHD; X-ray; 1.25 A; A=190-410.
DR   PDB; 6BHE; X-ray; 1.35 A; A=190-410.
DR   PDB; 6BHG; X-ray; 1.45 A; A=190-410.
DR   PDB; 6BHH; X-ray; 1.85 A; A=190-410.
DR   PDB; 6BHI; X-ray; 1.40 A; A=190-410.
DR   PDB; 6BPI; X-ray; 1.64 A; A=196-402.
DR   PDBsum; 3DLM; -.
DR   PDBsum; 4X3S; -.
DR   PDBsum; 5KCH; -.
DR   PDBsum; 5KCO; -.
DR   PDBsum; 5KE2; -.
DR   PDBsum; 5KE3; -.
DR   PDBsum; 5KH6; -.
DR   PDBsum; 6AU2; -.
DR   PDBsum; 6AU3; -.
DR   PDBsum; 6BHD; -.
DR   PDBsum; 6BHE; -.
DR   PDBsum; 6BHG; -.
DR   PDBsum; 6BHH; -.
DR   PDBsum; 6BHI; -.
DR   PDBsum; 6BPI; -.
DR   ProteinModelPortal; Q15047; -.
DR   SMR; Q15047; -.
DR   BioGrid; 115202; 140.
DR   CORUM; Q15047; -.
DR   DIP; DIP-31029N; -.
DR   IntAct; Q15047; 121.
DR   MINT; Q15047; -.
DR   STRING; 9606.ENSP00000271640; -.
DR   BindingDB; Q15047; -.
DR   ChEMBL; CHEMBL2321646; -.
DR   iPTMnet; Q15047; -.
DR   PhosphoSitePlus; Q15047; -.
DR   BioMuta; SETDB1; -.
DR   DMDM; 25091210; -.
DR   EPD; Q15047; -.
DR   MaxQB; Q15047; -.
DR   PaxDb; Q15047; -.
DR   PeptideAtlas; Q15047; -.
DR   PRIDE; Q15047; -.
DR   ProteomicsDB; 60397; -.
DR   ProteomicsDB; 60398; -. [Q15047-2]
DR   ProteomicsDB; 60399; -. [Q15047-3]
DR   Ensembl; ENST00000271640; ENSP00000271640; ENSG00000143379. [Q15047-1]
DR   Ensembl; ENST00000368962; ENSP00000357958; ENSG00000143379. [Q15047-2]
DR   Ensembl; ENST00000368969; ENSP00000357965; ENSG00000143379. [Q15047-3]
DR   GeneID; 9869; -.
DR   KEGG; hsa:9869; -.
DR   UCSC; uc001evu.3; human. [Q15047-1]
DR   CTD; 9869; -.
DR   DisGeNET; 9869; -.
DR   EuPathDB; HostDB:ENSG00000143379.12; -.
DR   GeneCards; SETDB1; -.
DR   HGNC; HGNC:10761; SETDB1.
DR   HPA; HPA018142; -.
DR   HPA; HPA058484; -.
DR   MIM; 604396; gene.
DR   neXtProt; NX_Q15047; -.
DR   OpenTargets; ENSG00000143379; -.
DR   PharmGKB; PA35679; -.
DR   eggNOG; KOG1141; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157471; -.
DR   HOVERGEN; HBG061013; -.
DR   InParanoid; Q15047; -.
DR   KO; K11421; -.
DR   OMA; KNMSGPM; -.
DR   OrthoDB; EOG091G014F; -.
DR   PhylomeDB; Q15047; -.
DR   TreeFam; TF106411; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   SIGNOR; Q15047; -.
DR   ChiTaRS; SETDB1; human.
DR   EvolutionaryTrace; Q15047; -.
DR   GeneWiki; SETDB1; -.
DR   GenomeRNAi; 9869; -.
DR   PRO; PR:Q15047; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000143379; Expressed in 215 organ(s), highest expression level in testis.
DR   CleanEx; HS_SETDB1; -.
DR   ExpressionAtlas; Q15047; baseline and differential.
DR   Genevisible; Q15047; HS.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0033273; P:response to vitamin; IEA:Ensembl.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR025796; Hist-Lys_N-MeTrfase_SETDB1.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF54171; SSF54171; 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51573; SAM_MT43_SUVAR39_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Coiled coil; Complete proteome; Isopeptide bond; Metal-binding;
KW   Methylation; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Zinc.
FT   CHAIN         1   1291       Histone-lysine N-methyltransferase
FT                                SETDB1.
FT                                /FTId=PRO_0000186064.
FT   DOMAIN      257    320       Tudor 1.
FT   DOMAIN      347    403       Tudor 2.
FT   DOMAIN      594    665       MBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00338}.
FT   DOMAIN      727    800       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      803   1266       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1275   1291       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      813    815       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1223   1224       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COILED       18     64       {ECO:0000255}.
FT   METAL       729    729       Zinc 1. {ECO:0000250}.
FT   METAL       729    729       Zinc 2. {ECO:0000250}.
FT   METAL       731    731       Zinc 1. {ECO:0000250}.
FT   METAL       735    735       Zinc 1. {ECO:0000250}.
FT   METAL       735    735       Zinc 3. {ECO:0000250}.
FT   METAL       741    741       Zinc 1. {ECO:0000250}.
FT   METAL       743    743       Zinc 2. {ECO:0000250}.
FT   METAL       781    781       Zinc 2. {ECO:0000250}.
FT   METAL       781    781       Zinc 3. {ECO:0000250}.
FT   METAL       785    785       Zinc 2. {ECO:0000250}.
FT   METAL       787    787       Zinc 3. {ECO:0000250}.
FT   METAL       792    792       Zinc 3. {ECO:0000250}.
FT   METAL      1226   1226       Zinc 4. {ECO:0000250}.
FT   METAL      1279   1279       Zinc 4. {ECO:0000250}.
FT   METAL      1281   1281       Zinc 4. {ECO:0000250}.
FT   METAL      1286   1286       Zinc 4. {ECO:0000250}.
FT   BINDING     851    851       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     853    853       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1220   1220       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     112    112       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O88974}.
FT   MOD_RES     117    117       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O88974}.
FT   MOD_RES     120    120       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O88974}.
FT   MOD_RES     976    976       Phosphothreonine; by NLK.
FT                                {ECO:0000305|PubMed:17952062}.
FT   MOD_RES    1025   1025       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1066   1066       Phosphoserine.
FT                                {ECO:0000244|PubMed:18220336,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1170   1170       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1170   1170       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1178   1178       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    1178   1178       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000244|PubMed:24129315}.
FT   CROSSLNK    182    182       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    182    182       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate.
FT   CROSSLNK   1032   1032       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate. {ECO:0000244|PubMed:25114211}.
FT   CROSSLNK   1032   1032       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1038   1038       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1069   1069       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1149   1149       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ     381    397       DDKRCEWIYRGSTRLEP -> VLFFSTILEAEVGGGGT
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_002217.
FT   VAR_SEQ     398   1291       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_002218.
FT   VAR_SEQ    1254   1254       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_034600.
FT   VARIANT     236    236       N -> S (in dbSNP:rs2271075).
FT                                /FTId=VAR_014284.
FT   VARIANT     506    506       P -> S (in dbSNP:rs17852587).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_031281.
FT   VARIANT     824    824       A -> G (in dbSNP:rs2691551).
FT                                /FTId=VAR_014286.
FT   VARIANT     824    824       A -> P (in dbSNP:rs2814054).
FT                                /FTId=VAR_014285.
FT   MUTAGEN     729    731       CDC->LDP: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11959841}.
FT   MUTAGEN     976    976       T->A: Abrogates interaction with CHD7,
FT                                NLK and PPARG. Reduces phosphorylation by
FT                                NLK. Reduces transcriptional repression.
FT                                {ECO:0000269|PubMed:17952062}.
FT   MUTAGEN    1224   1224       H->K: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11959841}.
FT   MUTAGEN    1226   1226       C->A: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11959841}.
FT   MUTAGEN    1279   1279       C->Y: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11959841}.
FT   STRAND      191    195       {ECO:0000244|PDB:6BHD}.
FT   STRAND      203    207       {ECO:0000244|PDB:6BHD}.
FT   STRAND      213    224       {ECO:0000244|PDB:6BHD}.
FT   STRAND      227    237       {ECO:0000244|PDB:6BHD}.
FT   STRAND      239    242       {ECO:0000244|PDB:6BHD}.
FT   HELIX       244    246       {ECO:0000244|PDB:6BHD}.
FT   STRAND      247    251       {ECO:0000244|PDB:6BHD}.
FT   HELIX       255    257       {ECO:0000244|PDB:6BHE}.
FT   STRAND      263    269       {ECO:0000244|PDB:6BHD}.
FT   STRAND      274    283       {ECO:0000244|PDB:6BHD}.
FT   TURN        287    290       {ECO:0000244|PDB:6BHD}.
FT   STRAND      293    297       {ECO:0000244|PDB:6BHD}.
FT   STRAND      302    305       {ECO:0000244|PDB:6BHD}.
FT   HELIX       307    309       {ECO:0000244|PDB:6BHD}.
FT   STRAND      310    315       {ECO:0000244|PDB:6BHD}.
FT   HELIX       320    323       {ECO:0000244|PDB:6BHD}.
FT   HELIX       327    339       {ECO:0000244|PDB:6BHD}.
FT   STRAND      353    358       {ECO:0000244|PDB:6BHD}.
FT   STRAND      361    371       {ECO:0000244|PDB:6BHD}.
FT   STRAND      374    379       {ECO:0000244|PDB:6BHD}.
FT   TURN        380    383       {ECO:0000244|PDB:6BHD}.
FT   STRAND      384    389       {ECO:0000244|PDB:6BHD}.
FT   HELIX       396    403       {ECO:0000244|PDB:6BHD}.
FT   STRAND     1167   1172       {ECO:0000244|PDB:4X3S}.
SQ   SEQUENCE   1291 AA;  143157 MW;  D8841B4C41B911C5 CRC64;
     MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK MDCVQQRKKQ
     LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY SKLGLQYRDS SSEDESSRPT
     EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL
     HKGTLSQMSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS
     LLSGNHIAYD YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG
     YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS GQLIKTEWEG
     TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASALE KKQGQLRTRP
     NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL
     AQSRKQVAKK STSFRPGSVG SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS
     ALPAPPAPPV FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL
     LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC DFLFLEMFCL
     DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT PPPQVAYSKE RIPGKGVFIN
     TGPEFLVGCD CKDGCRDKSK CACHQLTIQA TACTPGGQIN PNSGYQYKRL EECLPTGVYE
     CNKRCKCDPN MCTNRLVQHG LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD
     FADKEGLEMG DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE
     SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP DLGPPHIPVP
     PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS HSSFKTNEGG EGRAGGSRME
     AEKASTSGLG IKDEGDIKQA KKEDTDDRNK MSVVTESSRN YGYNPSPVKP EGLRRPPSKT
     SMHQSRRLMA SAQSNPDDVL TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS
     EGDDFEDKKN MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF
     YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF ASKRIRAGTE
     LTWDYNYEVG SVEGKELLCC CGAIECRGRL L
//
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