GenomeNet

Database: UniProt
Entry: O88974
LinkDB: O88974
Original site: O88974 
ID   SETB1_MOUSE             Reviewed;        1307 AA.
AC   O88974; Q6AXH8; Q78N64; Q78N65; Q80U84; Q8BTV6; Q8CIX7; Q922K1;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   10-APR-2019, entry version 161.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB1 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:22939622};
DE   AltName: Full=ERG-associated protein with SET domain;
DE            Short=ESET {ECO:0000303|PubMed:20164836};
DE   AltName: Full=SET domain bifurcated 1;
GN   Name=Setdb1 {ECO:0000312|MGI:MGI:1934229};
GN   Synonyms=Eset {ECO:0000303|PubMed:20164836}, Kiaa0067;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY,
RP   INTERACTION WITH ERG, MUTAGENESIS OF CYS-798 AND CYS-1242, AND
RP   FUNCTION.
RC   STRAIN=BDF1; TISSUE=Blood;
RX   PubMed=11791185; DOI=10.1038/sj.onc.1204998;
RA   Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H.,
RA   Hickstein D.D., Zhang Y.;
RT   "Molecular cloning of ESET, a novel histone H3-specific
RT   methyltransferase that interacts with ERG transcription factor.";
RL   Oncogene 21:148-152(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [GENOMIC
RP   DNA], ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE SPECIFICITY.
RC   STRAIN=BDF1, and C57BL/6J X DBA/2;
RX   PubMed=14522075; DOI=10.1016/S0167-4781(03)00155-6;
RA   Blackburn M.L., Chansky H.A., Zielinska-Kwiatkowska A., Matsui Y.,
RA   Yang L.;
RT   "Genomic structure and expression of the mouse ESET gene encoding an
RT   ERG-associated histone methyltransferase with a SET domain.";
RL   Biochim. Biophys. Acta 1629:8-14(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1307 (ISOFORM 4).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 4).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   INTERACTION WITH HDAC1; HDAC2; SIN3A AND SIN3B.
RX   PubMed=12398767; DOI=10.1042/BJ20020854;
RA   Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
RA   Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
RT   "An ERG (ets-related gene)-associated histone methyltransferase
RT   interacts with histone deacetylases 1/2 and transcription co-
RT   repressors mSin3A/B.";
RL   Biochem. J. 369:651-657(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-117 AND
RP   THR-120, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF CYS-1242.
RX   PubMed=20164836; DOI=10.1038/nature08858;
RA   Matsui T., Leung D., Miyashita H., Maksakova I.A., Miyachi H.,
RA   Kimura H., Tachibana M., Lorincz M.C., Shinkai Y.;
RT   "Proviral silencing in embryonic stem cells requires the histone
RT   methyltransferase ESET.";
RL   Nature 464:927-931(2010).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA   Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA   Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA   Reinberg D., Lachner M., Jenuwein T.;
RT   "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for
RT   mammalian heterochromatin integrity.";
RL   Cell 150:948-960(2012).
RN   [10]
RP   FUNCTION, INTERACTION WITH RESF1, AND SUBCELLULAR LOCATION.
RX   PubMed=29728365; DOI=10.1101/gr.227280.117;
RA   Fukuda K., Okuda A., Yusa K., Shinkai Y.;
RT   "A CRISPR knockout screen identifies SETDB1-target retroelement
RT   silencing factors in embryonic stem cells.";
RL   Genome Res. 28:846-858(2018).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 (PubMed:11791185,
CC       PubMed:22939622). H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in euchromatin regions, thereby playing a central role
CC       in the silencing of euchromatic genes. H3 'Lys-9' trimethylation
CC       is coordinated with DNA methylation. Probably forms a complex with
CC       MBD1 and ATF7IP that represses transcription and couples DNA
CC       methylation and histone 'Lys-9' trimethylation. Its activity is
CC       dependent on MBD1 and is heritably maintained through DNA
CC       replication by being recruited by CAF-1. SETDB1 is targeted to
CC       histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger
CC       proteins. Probably forms a corepressor complex required for
CC       activated KRAS-mediated promoter hypermethylation and
CC       transcriptional silencing of tumor suppressor genes (TSGs) or
CC       other tumor-related genes in colorectal cancer (CRC) cells (By
CC       similarity). Required to maintain a transcriptionally repressive
CC       state of genes in undifferentiated embryonic stem cells (ESCs) (By
CC       similarity). In ESCs, in collaboration with TRIM28, is also
CC       required for H3K9me3 and silencing of endogenous and introduced
CC       retroviruses in a DNA-methylation independent-pathway
CC       (PubMed:20164836, PubMed:29728365). Associates at promoter regions
CC       of tumor suppressor genes (TSGs) leading to their gene silencing.
CC       The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting
CC       ATRX to the 3'-exons of zinc-finger coding genes with atypical
CC       chromatin signatures to establish or maintain/protect H3K9me3 at
CC       these transcriptionally active regions (By similarity).
CC       {ECO:0000250|UniProtKB:Q15047, ECO:0000269|PubMed:11791185,
CC       ECO:0000269|PubMed:20164836, ECO:0000269|PubMed:22939622,
CC       ECO:0000269|PubMed:29728365}.
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         ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:22939622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10025;
CC         Evidence={ECO:0000269|PubMed:11791185};
CC   -!- SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ,
CC       SETDB1, EHMT1 and EHMT2. During DNA replication, it is recruited
CC       by SETDB1 to form a S phase-specific complex that facilitates
CC       methylation of H3 'Lys-9' during replication-coupled chromatin
CC       assembly and is at least composed of the CAF-1 subunit CHAF1A,
CC       MBD1 and SETDB1. Probably part of a corepressor complex containing
CC       ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with TRIM28/TIF1B.
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'. Interacts with MBD1; interaction is abolished when MBD1
CC       is sumoylated. Interacts with CBX1 and CBX5. Interacts with DNMT3A
CC       and DNMT3B. Interacts with SUMO2. Interacts with CHD7, NLK1 and
CC       PPARG. Interacts with MPHOSPH8 (By similarity). Interacts with ERG
CC       (PubMed:11791185). Interacts with HDAC1, HDAC2, SIN3A, SIN3B
CC       (PubMed:12398767). Interacts with ATRX. Forms a complex with ATRX,
CC       TRIM28 and ZNF274 (By similarity). Interacts with RESF1
CC       (PubMed:29728365). {ECO:0000250|UniProtKB:Q15047,
CC       ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:12398767,
CC       ECO:0000269|PubMed:29728365}.
CC   -!- INTERACTION:
CC       P81270:Erg; NbExp=3; IntAct=EBI-79658, EBI-79647;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29728365}.
CC       Chromosome {ECO:0000269|PubMed:29728365}. Note=Associated with
CC       non-pericentromeric regions of chromatin. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC         Comment=Experimental confirmation may be lacking for some
CC         isoforms.;
CC       Name=1;
CC         IsoId=O88974-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88974-2; Sequence=VSP_002219, VSP_002220;
CC       Name=3;
CC         IsoId=O88974-3; Sequence=VSP_002221;
CC       Name=4;
CC         IsoId=O88974-4; Sequence=VSP_024031;
CC       Name=5;
CC         IsoId=O88974-5; Sequence=VSP_024032;
CC       Name=6;
CC         IsoId=O88974-6; Sequence=VSP_024031, VSP_024032;
CC       Name=7;
CC         IsoId=O88974-7; Sequence=VSP_024033;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in
CC       liver and testis. {ECO:0000269|PubMed:14522075}.
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: 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   -!- PTM: Degraded by the proteasome, shielded by interaction with
CC       ATF7IP. {ECO:0000250|UniProtKB:Q15047}.
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}.
DR   EMBL; AF091628; AAC43039.1; -; mRNA.
DR   EMBL; AY091600; AAM13922.1; -; mRNA.
DR   EMBL; AF546078; AAN52358.1; -; mRNA.
DR   EMBL; AY226577; AAO73535.2; -; Genomic_DNA.
DR   EMBL; AY226577; AAO73536.2; -; Genomic_DNA.
DR   EMBL; BC007176; AAH07176.1; -; mRNA.
DR   EMBL; BC079537; AAH79537.1; -; mRNA.
DR   EMBL; AK122198; BAC65480.3; -; Transcribed_RNA.
DR   EMBL; AK088590; BAC40439.1; -; mRNA.
DR   CCDS; CCDS17613.1; -. [O88974-4]
DR   CCDS; CCDS50991.1; -. [O88974-1]
DR   PIR; T17453; T17453.
DR   UniGene; Mm.490259; -.
DR   ProteinModelPortal; O88974; -.
DR   SMR; O88974; -.
DR   IntAct; O88974; 9.
DR   STRING; 10090.ENSMUSP00000015841; -.
DR   iPTMnet; O88974; -.
DR   PhosphoSitePlus; O88974; -.
DR   EPD; O88974; -.
DR   MaxQB; O88974; -.
DR   PaxDb; O88974; -.
DR   PeptideAtlas; O88974; -.
DR   PRIDE; O88974; -.
DR   UCSC; uc008qjo.2; mouse. [O88974-5]
DR   MGI; MGI:1934229; Setdb1.
DR   eggNOG; KOG1141; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOVERGEN; HBG061013; -.
DR   InParanoid; O88974; -.
DR   ChiTaRS; Setdb1; mouse.
DR   PRO; PR:O88974; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060348; P:bone development; IMP:MGI.
DR   GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
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   Alternative splicing; Chromatin regulator; Chromosome; Coiled coil;
KW   Complete proteome; Isopeptide bond; Metal-binding; Methylation;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc.
FT   CHAIN         1   1307       Histone-lysine N-methyltransferase
FT                                SETDB1.
FT                                /FTId=PRO_0000186065.
FT   DOMAIN      257    320       Tudor 1.
FT   DOMAIN      347    403       Tudor 2.
FT   DOMAIN      611    682       MBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00338}.
FT   DOMAIN      744    817       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      820   1282       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1291   1307       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      830    832       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1239   1240       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COILED       30     65       {ECO:0000255}.
FT   METAL       746    746       Zinc 1. {ECO:0000250}.
FT   METAL       746    746       Zinc 2. {ECO:0000250}.
FT   METAL       748    748       Zinc 1. {ECO:0000250}.
FT   METAL       752    752       Zinc 1. {ECO:0000250}.
FT   METAL       752    752       Zinc 3. {ECO:0000250}.
FT   METAL       758    758       Zinc 1. {ECO:0000250}.
FT   METAL       760    760       Zinc 2. {ECO:0000250}.
FT   METAL       798    798       Zinc 2. {ECO:0000250}.
FT   METAL       798    798       Zinc 3. {ECO:0000250}.
FT   METAL       802    802       Zinc 2. {ECO:0000250}.
FT   METAL       804    804       Zinc 3. {ECO:0000250}.
FT   METAL       809    809       Zinc 3. {ECO:0000250}.
FT   METAL      1242   1242       Zinc 4. {ECO:0000250}.
FT   METAL      1295   1295       Zinc 4. {ECO:0000250}.
FT   METAL      1297   1297       Zinc 4. {ECO:0000250}.
FT   METAL      1302   1302       Zinc 4. {ECO:0000250}.
FT   BINDING     868    868       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     870    870       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1236   1236       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     112    112       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     117    117       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     120    120       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     993    993       Phosphothreonine; by NLK.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   MOD_RES    1042   1042       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   MOD_RES    1186   1186       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   MOD_RES    1186   1186       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   MOD_RES    1194   1194       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   MOD_RES    1194   1194       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK    182    182       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK    182    182       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK   1049   1049       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK   1049   1049       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK   1055   1055       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK   1085   1085       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   CROSSLNK   1165   1165       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q15047}.
FT   VAR_SEQ       1    807       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_002221.
FT   VAR_SEQ     474    474       D -> ES (in isoform 4 and isoform 6).
FT                                {ECO:0000303|PubMed:12693553,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024031.
FT   VAR_SEQ     482    486       SRKQV -> AQSQK (in isoform 2).
FT                                {ECO:0000303|PubMed:11791185}.
FT                                /FTId=VSP_002219.
FT   VAR_SEQ     489   1307       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11791185}.
FT                                /FTId=VSP_002220.
FT   VAR_SEQ     527   1307       Missing (in isoform 5 and isoform 6).
FT                                {ECO:0000303|PubMed:14522075}.
FT                                /FTId=VSP_024032.
FT   VAR_SEQ     756   1307       Missing (in isoform 7).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024033.
FT   MUTAGEN     798    798       C->T: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11791185}.
FT   MUTAGEN    1242   1242       C->A: Decreases endogenous retroviruses
FT                                silencing and cell growth.
FT                                {ECO:0000269|PubMed:20164836}.
FT   MUTAGEN    1242   1242       C->T: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:11791185}.
FT   CONFLICT    463    463       I -> M (in Ref. 5; BAC40439).
FT                                {ECO:0000305}.
FT   CONFLICT   1092   1092       P -> S (in Ref. 4; BAC65480).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1307 AA;  144549 MW;  326AED6371D156C2 CRC64;
     MSSLPGCMSL AAAPAAADSA EIAELQQAVV EELGISMEEL RQYIDEELEK MDCIQQRKKQ
     LAELETWVLQ KESEVAYVDR LFDDASREVT NCESLVKDFY SKLGLQYHDS SSEDEASRPT
     EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL
     HKGTLGQVSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGLGKKY KVKFDNKGKS
     LLSGNHIAYD YHPPADKLFV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG
     YASYVTQSEL YPICRPLKKT WEDIEDSSCR DFIEEYITAY PNRPMVLLKS GQLIKTEWEG
     TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASAME KKQGGQLRTR
     PNMGAVRSKG PVVQYTQDLT GTGIQFKPME PLQPIAPPAP LPIPPLSPQA ADTDLESQLA
     QSRKQVAKKS TSFRPGSVGS GHSSPTSSTL SENVSAGKLG INQTYRSPLA SVTSTPASAA
     PPVPPVPPGP PTPPGPPAPP GPLAPPAFHG MLERAPAEPS YRAPMEKLFY LPHVCSYTCL
     SRIRPMRNEQ YRGKNPLLVP LLYDFRRMTA RRRVNRKMGF HVIYKTPCGL CLRTMQEIER
     YLFETGCDFL FLEMFCLDPY VLVDRKFQPF KPFYYILDIT YGKEDVPLSC VNEIDTTPPP
     QVAYSKERIP GKGVFINTGP EFLVGCDCKD GCRDKSKCAC HQLTIQATAC TPGGQVNPNS
     GYQYKRLEEC LPTGVYECNK RCNCDPNMCT NRLVQHGLQV RLQLFKTQNK GWGIRCLDDI
     AKGSFVCIYA GKILTDDFAD KEGLEMGDEY FANLDHIESV ENFKEGYESD VPTSSDSSGV
     DMKDQEDGNS GSEDPEESND DSSDDNFCKD EDFSTSSVWR SYATRRQTRG QKENELSEMT
     SKDSRPPDLG PPHVPIPSSV SVGGCNPPSS EETPKNKVAS WLSCNSVSEG GFADSDSRSS
     FKTSEGGDGR AGGGRGEAER ASTSGLSFKD EGDNKQPKKE DPENRNKMPV VTEGSQNHGH
     NPPMKSEGLR RPASKMSVLQ SQRVVTSTQS NPDDILTLSS STESEGESGT SRKPTAGHTS
     ATAVDSDDIQ TISSGSDGDD FEDKKNLSGP TKRQVAVKST RGFALKSTHG IAIKSTNMAS
     VDKGESAPVR KNTRQFYDGE ESCYIIDAKL EGNLGRYLNH SCSPNLFVQN VFVDTHDLRF
     PWVAFFASKR IRAGTELTWD YNYEVGSVEG KELLCCCGAI ECRGRLL
//
DBGET integrated database retrieval system