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Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (ERG-associated protein with SET domain) (ESET) (SET domain bifurcated 1)

 SETB1_MOUSE             Reviewed;        1307 AA.
O88974; Q6AXH8; Q78N64; Q78N65; Q80U84; Q8BTV6; Q8CIX7; Q922K1;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
13-FEB-2019, entry version 160.
RecName: Full=Histone-lysine N-methyltransferase SETDB1 {ECO:0000305};
EC=2.1.1.43 {ECO:0000269|PubMed:11791185};
AltName: Full=ERG-associated protein with SET domain;
Short=ESET {ECO:0000303|PubMed:20164836};
AltName: Full=SET domain bifurcated 1;
Name=Setdb1 {ECO:0000312|MGI:MGI:1934229};
Synonyms=Eset {ECO:0000303|PubMed:20164836}, Kiaa0067;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY,
INTERACTION WITH ERG, MUTAGENESIS OF CYS-798 AND CYS-1242, AND
FUNCTION.
STRAIN=BDF1; TISSUE=Blood;
PubMed=11791185; DOI=10.1038/sj.onc.1204998;
Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H.,
Hickstein D.D., Zhang Y.;
"Molecular cloning of ESET, a novel histone H3-specific
methyltransferase that interacts with ERG transcription factor.";
Oncogene 21:148-152(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [GENOMIC
DNA], ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE SPECIFICITY.
STRAIN=BDF1, and C57BL/6J X DBA/2;
PubMed=14522075; DOI=10.1016/S0167-4781(03)00155-6;
Blackburn M.L., Chansky H.A., Zielinska-Kwiatkowska A., Matsui Y.,
Yang L.;
"Genomic structure and expression of the mouse ESET gene encoding an
ERG-associated histone methyltransferase with a SET domain.";
Biochim. Biophys. Acta 1629:8-14(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-1307 (ISOFORM 4).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 4).
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
INTERACTION WITH HDAC1; HDAC2; SIN3A AND SIN3B.
PubMed=12398767; DOI=10.1042/BJ20020854;
Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
"An ERG (ets-related gene)-associated histone methyltransferase
interacts with histone deacetylases 1/2 and transcription co-
repressors mSin3A/B.";
Biochem. J. 369:651-657(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-117 AND
THR-120, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, AND MUTAGENESIS OF CYS-1242.
PubMed=20164836; DOI=10.1038/nature08858;
Matsui T., Leung D., Miyashita H., Maksakova I.A., Miyachi H.,
Kimura H., Tachibana M., Lorincz M.C., Shinkai Y.;
"Proviral silencing in embryonic stem cells requires the histone
methyltransferase ESET.";
Nature 464:927-931(2010).
[9]
FUNCTION, INTERACTION WITH RESF1, AND SUBCELLULAR LOCATION.
PubMed=29728365; DOI=10.1101/gr.227280.117;
Fukuda K., Okuda A., Yusa K., Shinkai Y.;
"A CRISPR knockout screen identifies SETDB1-target retroelement
silencing factors in embryonic stem cells.";
Genome Res. 28:846-858(2018).
-!- FUNCTION: Histone methyltransferase that specifically
trimethylates 'Lys-9' of histone H3 (PubMed:11791185). H3 'Lys-9'
trimethylation represents a specific tag for epigenetic
transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or
CBX5) proteins to methylated histones. Mainly functions in
euchromatin regions, thereby playing a central role in the
silencing of euchromatic genes. H3 'Lys-9' trimethylation is
coordinated with DNA methylation. Probably forms a complex with
MBD1 and ATF7IP that represses transcription and couples DNA
methylation and histone 'Lys-9' trimethylation. Its activity is
dependent on MBD1 and is heritably maintained through DNA
replication by being recruited by CAF-1. SETDB1 is targeted to
histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger
proteins. Probably forms a corepressor complex required for
activated KRAS-mediated promoter hypermethylation and
transcriptional silencing of tumor suppressor genes (TSGs) or
other tumor-related genes in colorectal cancer (CRC) cells (By
similarity). Required to maintain a transcriptionally repressive
state of genes in undifferentiated embryonic stem cells (ESCs) (By
similarity). In ESCs, in collaboration with TRIM28, is also
required for H3K9me3 and silencing of endogenous and introduced
retroviruses in a DNA-methylation independent-pathway
(PubMed:20164836, PubMed:29728365). Associates at promoter regions
of tumor suppressor genes (TSGs) leading to their gene silencing.
The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting
ATRX to the 3'-exons of zinc-finger coding genes with atypical
chromatin signatures to establish or maintain/protect H3K9me3 at
these transcriptionally active regions (By similarity).
{ECO:0000250|UniProtKB:Q15047, ECO:0000269|PubMed:11791185,
ECO:0000269|PubMed:20164836, ECO:0000269|PubMed:29728365}.
-!- CATALYTIC ACTIVITY:
Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00906,
ECO:0000269|PubMed:11791185};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10025;
Evidence={ECO:0000269|PubMed:11791185};
-!- SUBUNIT: Part of a complex containing at least CDYL, REST, WIZ,
SETDB1, EHMT1 and EHMT2. During DNA replication, it is recruited
by SETDB1 to form a S phase-specific complex that facilitates
methylation of H3 'Lys-9' during replication-coupled chromatin
assembly and is at least composed of the CAF-1 subunit CHAF1A,
MBD1 and SETDB1. Probably part of a corepressor complex containing
ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with TRIM28/TIF1B.
Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is
required to stimulate histone methyltransferase activity and
facilitate the conversion of dimethylated to trimethylated H3
'Lys-9'. Interacts with MBD1; interaction is abolished when MBD1
is sumoylated. Interacts with CBX1 and CBX5. Interacts with DNMT3A
and DNMT3B. Interacts with SUMO2. Interacts with CHD7, NLK1 and
PPARG. Interacts with MPHOSPH8 (By similarity). Interacts with ERG
(PubMed:11791185). Interacts with HDAC1, HDAC2, SIN3A, SIN3B
(PubMed:12398767). Interacts with ATRX. Forms a complex with ATRX,
TRIM28 and ZNF274 (By similarity). Interacts with RESF1
(PubMed:29728365). {ECO:0000250|UniProtKB:Q15047,
ECO:0000269|PubMed:11791185, ECO:0000269|PubMed:12398767,
ECO:0000269|PubMed:29728365}.
-!- INTERACTION:
P81270:Erg; NbExp=3; IntAct=EBI-79658, EBI-79647;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29728365}.
Chromosome {ECO:0000269|PubMed:29728365}. Note=Associated with
non-pericentromeric regions of chromatin. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=O88974-1; Sequence=Displayed;
Name=2;
IsoId=O88974-2; Sequence=VSP_002219, VSP_002220;
Name=3;
IsoId=O88974-3; Sequence=VSP_002221;
Name=4;
IsoId=O88974-4; Sequence=VSP_024031;
Name=5;
IsoId=O88974-5; Sequence=VSP_024032;
Name=6;
IsoId=O88974-6; Sequence=VSP_024031, VSP_024032;
Name=7;
IsoId=O88974-7; Sequence=VSP_024033;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in
liver and testis. {ECO:0000269|PubMed:14522075}.
-!- DOMAIN: The pre-SET, SET and post-SET domains are all required for
methyltransferase activity. The 347-amino-acid insertion in the
SET domain has no effect on the catalytic activity.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
{ECO:0000250}.
-!- PTM: Degraded by the proteasome, shielded by interaction with
ATF7IP. {ECO:0000250|UniProtKB:Q15047}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00906}.
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EMBL; AF091628; AAC43039.1; -; mRNA.
EMBL; AY091600; AAM13922.1; -; mRNA.
EMBL; AF546078; AAN52358.1; -; mRNA.
EMBL; AY226577; AAO73535.2; -; Genomic_DNA.
EMBL; AY226577; AAO73536.2; -; Genomic_DNA.
EMBL; BC007176; AAH07176.1; -; mRNA.
EMBL; BC079537; AAH79537.1; -; mRNA.
EMBL; AK122198; BAC65480.3; -; Transcribed_RNA.
EMBL; AK088590; BAC40439.1; -; mRNA.
CCDS; CCDS17613.1; -. [O88974-4]
CCDS; CCDS50991.1; -. [O88974-1]
PIR; T17453; T17453.
UniGene; Mm.490259; -.
ProteinModelPortal; O88974; -.
SMR; O88974; -.
IntAct; O88974; 9.
STRING; 10090.ENSMUSP00000015841; -.
iPTMnet; O88974; -.
PhosphoSitePlus; O88974; -.
EPD; O88974; -.
MaxQB; O88974; -.
PaxDb; O88974; -.
PeptideAtlas; O88974; -.
PRIDE; O88974; -.
UCSC; uc008qjo.2; mouse. [O88974-5]
MGI; MGI:1934229; Setdb1.
eggNOG; KOG1141; Eukaryota.
eggNOG; COG2940; LUCA.
HOVERGEN; HBG061013; -.
InParanoid; O88974; -.
ChiTaRS; Setdb1; mouse.
PRO; PR:O88974; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:MGI.
GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; IMP:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR025796; Hist-Lys_N-MeTrfase_SETDB1.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR002999; Tudor.
Pfam; PF01429; MBD; 1.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
SMART; SM00391; MBD; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SMART; SM00333; TUDOR; 2.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS51573; SAM_MT43_SUVAR39_1; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Chromosome; Coiled coil;
Complete proteome; Isopeptide bond; Metal-binding; Methylation;
Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase; Ubl conjugation; Zinc.
CHAIN 1 1307 Histone-lysine N-methyltransferase
SETDB1.
/FTId=PRO_0000186065.
DOMAIN 257 320 Tudor 1.
DOMAIN 347 403 Tudor 2.
DOMAIN 611 682 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
DOMAIN 744 817 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 820 1282 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1291 1307 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
REGION 830 832 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1239 1240 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COILED 30 65 {ECO:0000255}.
METAL 746 746 Zinc 1. {ECO:0000250}.
METAL 746 746 Zinc 2. {ECO:0000250}.
METAL 748 748 Zinc 1. {ECO:0000250}.
METAL 752 752 Zinc 1. {ECO:0000250}.
METAL 752 752 Zinc 3. {ECO:0000250}.
METAL 758 758 Zinc 1. {ECO:0000250}.
METAL 760 760 Zinc 2. {ECO:0000250}.
METAL 798 798 Zinc 2. {ECO:0000250}.
METAL 798 798 Zinc 3. {ECO:0000250}.
METAL 802 802 Zinc 2. {ECO:0000250}.
METAL 804 804 Zinc 3. {ECO:0000250}.
METAL 809 809 Zinc 3. {ECO:0000250}.
METAL 1242 1242 Zinc 4. {ECO:0000250}.
METAL 1295 1295 Zinc 4. {ECO:0000250}.
METAL 1297 1297 Zinc 4. {ECO:0000250}.
METAL 1302 1302 Zinc 4. {ECO:0000250}.
BINDING 868 868 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 870 870 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 1236 1236 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 993 993 Phosphothreonine; by NLK.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1186 1186 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1186 1186 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1194 1194 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
MOD_RES 1194 1194 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1049 1049 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1049 1049 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1055 1055 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1085 1085 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15047}.
CROSSLNK 1165 1165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15047}.
VAR_SEQ 1 807 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_002221.
VAR_SEQ 474 474 D -> ES (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024031.
VAR_SEQ 482 486 SRKQV -> AQSQK (in isoform 2).
{ECO:0000303|PubMed:11791185}.
/FTId=VSP_002219.
VAR_SEQ 489 1307 Missing (in isoform 2).
{ECO:0000303|PubMed:11791185}.
/FTId=VSP_002220.
VAR_SEQ 527 1307 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:14522075}.
/FTId=VSP_024032.
VAR_SEQ 756 1307 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024033.
MUTAGEN 798 798 C->T: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11791185}.
MUTAGEN 1242 1242 C->A: Decreases endogenous retroviruses
silencing and cell growth.
{ECO:0000269|PubMed:20164836}.
MUTAGEN 1242 1242 C->T: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11791185}.
CONFLICT 463 463 I -> M (in Ref. 5; BAC40439).
{ECO:0000305}.
CONFLICT 1092 1092 P -> S (in Ref. 4; BAC65480).
{ECO:0000305}.
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


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1673: Naphthalene and anthracene degradation
WP1700: Selenoamino acid metabolism
WP1714: Tyrosine metabolism
WP1006: metapathway biotransformation
WP1049: G Protein Signaling Pathways
WP1124: metapathway biotransformation
WP1165: G Protein Signaling Pathways
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1581: Histidine metabolism
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation

Related Genes :
[Setdb1 Eset Kiaa0067] Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (ERG-associated protein with SET domain) (ESET) (SET domain bifurcated 1)
[SETDB1 ESET KIAA0067 KMT1E] Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (ERG-associated protein with SET domain) (ESET) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Lysine N-methyltransferase 1E) (SET domain bifurcated 1)
[setdb1] Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (SET domain bifurcated 1)
[egg CG12196] Histone-lysine N-methyltransferase eggless (EC 2.1.1.43) (SETDB1 homolog)
[setdb1b zgc:152899] Histone-lysine N-methyltransferase SETDB1-B (EC 2.1.1.43) (SET domain bifurcated 1B)
[KMT5A PRSET7 SET07 SET8 SETD8] N-lysine methyltransferase KMT5A (EC 2.1.1.-) (H4-K20-HMTase KMT5A) (Histone-lysine N-methyltransferase KMT5A) (EC 2.1.1.43) (Lysine N-methyltransferase 5A) (Lysine-specific methylase 5A) (PR/SET domain-containing protein 07) (PR-Set7) (PR/SET07) (SET domain-containing protein 8)
[SETD1A KIAA0339 KMT2F SET1 SET1A] Histone-lysine N-methyltransferase SETD1A (EC 2.1.1.43) (Lysine N-methyltransferase 2F) (SET domain-containing protein 1A) (hSET1A) (Set1/Ash2 histone methyltransferase complex subunit SET1)
[SETD2 HIF1 HYPB KIAA1732 KMT3A SET2 HSPC069] Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)
[SETD7 KIAA1717 KMT7 SET7 SET9] Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (Lysine N-methyltransferase 7) (SET domain-containing protein 7) (SET7/9)
[setdb1a si:ch211-81a5.6] Histone-lysine N-methyltransferase SETDB1-A (EC 2.1.1.43) (SET domain bifurcated 1A)
[SETDB2 C13orf4 CLLD8 KMT1F] Histone-lysine N-methyltransferase SETDB2 (EC 2.1.1.43) (Chronic lymphocytic leukemia deletion region gene 8 protein) (Lysine N-methyltransferase 1F) (SET domain bifurcated 2)
[Setd7 Kiaa1717 Set7 Set9] Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (SET domain-containing protein 7) (SET7/9)
[SUVR5 CZS SDG6 SET6 At2g23740/At2g23730/At2g23750 F27L4.8/F27L4.9/F27L4.7] Histone-lysine N-methyltransferase SUVR5 (EC 2.1.1.43) (C2H2 zinc finger-SET histone methyltransferase) (Protein C2H2 SET) (Protein SET DOMAIN GROUP 6) (Suppressor of variegation 3-9-related protein 5) (Su(var)3-9-related protein 5)
[NSD1 ARA267 KMT3B] Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.43) (Androgen receptor coactivator 267 kDa protein) (Androgen receptor-associated protein of 267 kDa) (H3-K36-HMTase) (H4-K20-HMTase) (Lysine N-methyltransferase 3B) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein)
[SUVH4 KYP SDG33 SET33 At5g13960 MAC12.7] Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Protein KRYPTONITE) (Protein SET DOMAIN GROUP 33) (Suppressor of variegation 3-9 homolog protein 4) (Su(var)3-9 homolog protein 4)
[SETD1B KIAA1076 KMT2G SET1B] Histone-lysine N-methyltransferase SETD1B (EC 2.1.1.43) (Lysine N-methyltransferase 2G) (SET domain-containing protein 1B) (hSET1B)
[ASHH2 EFS LAZ2 SDG8 SET8 At1g77300 T14N5.15] Histone-lysine N-methyltransferase ASHH2 (EC 2.1.1.43) (ASH1 homolog 2) (H3-K4-HMTase) (Histone H3-K36 methyltransferase 8) (H3-K36-HMTase 8) (Protein EARLY FLOWERING IN SHORT DAYS) (Protein LAZARUS 2) (Protein SET DOMAIN GROUP 8)
[Setd2 Kiaa1732 Kmt3a] Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2)
[SETMAR] Histone-lysine N-methyltransferase SETMAR (SET domain and mariner transposase fusion protein) (Metnase) [Includes: Histone-lysine N-methyltransferase (EC 2.1.1.43); Transposon Hsmar1 transposase (EC 3.1.-.-)]
[CLF ICU1 PIF1 PIF2 SDG1 SET1 At2g23380 F26B6.3] Histone-lysine N-methyltransferase CLF (EC 2.1.1.43) (Polycomb group protein CURLY LEAF) (Protein INCURVATA 1) (Protein SET DOMAIN GROUP 1) (Protein photoperiod insensitive flowering)
[setdb2 zgc:77298] Histone-lysine N-methyltransferase SETDB2 (EC 2.1.1.43) (SET domain bifurcated 2)
[MEA EMB173 FIS1 MEDEA SDG5 SET5 At1g02580 T14P4.11] Histone-lysine N-methyltransferase MEDEA (EC 2.1.1.43) (Maternal embryogenesis control protein) (Protein EMBRYO DEFECTIVE 173) (Protein FERTILIZATION-INDEPENDENT SEED 1) (Protein SET DOMAIN GROUP 5)
[Smyd3 Zmynd1] Histone-lysine N-methyltransferase SMYD3 (EC 2.1.1.43) (SET and MYND domain-containing protein 3) (Zinc finger MYND domain-containing protein 1)
[NSD3 WHSC1L1 DC28] Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.43) (Nuclear SET domain-containing protein 3) (Protein whistle) (WHSC1-like 1 isoform 9 with methyltransferase activity to lysine) (Wolf-Hirschhorn syndrome candidate 1-like protein 1) (WHSC1-like protein 1)
[SMYD3 ZMYND1 ZNFN3A1] Histone-lysine N-methyltransferase SMYD3 (EC 2.1.1.43) (SET and MYND domain-containing protein 3) (Zinc finger MYND domain-containing protein 1)
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[ATXR5 SDG15 SET15 At5g09790 17I14.20 MTH16.26] Histone-lysine N-methyltransferase ATXR5 (EC 2.1.1.43) (Protein SET DOMAIN GROUP 15) (Trithorax-related protein 5) (TRX-related protein 5)
[ATXR6 SDG34 SET34 At5g24330 MOP9.18] Histone-lysine N-methyltransferase ATXR6 (EC 2.1.1.43) (Protein SET DOMAIN GROUP 34) (Trithorax-related protein 6) (TRX-related protein 6)
[set9 kmt5 SPCC4B3.12] Histone-lysine N-methyltransferase set9 (EC 2.1.1.43) (Lysine N-methyltransferase 5) (SET domain protein 9)
[Setd1a] Histone-lysine N-methyltransferase SETD1A (EC 2.1.1.43) (SET domain-containing protein 1A)

Bibliography :
[28879500] In silico probing and biological evaluation of SETDB1/ESET-targeted novel compounds that reduce tri-methylated histone H3K9 (H3K9me3) level.
[11791185] Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor.
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