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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)

 ASHH2_ARATH             Reviewed;        1759 AA.
Q2LAE1; A9QA57; O80663; Q56WW4;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 1.
30-AUG-2017, entry version 96.
RecName: Full=Histone-lysine N-methyltransferase ASHH2;
EC=2.1.1.43;
AltName: Full=ASH1 homolog 2 {ECO:0000303|PubMed:19915673};
AltName: Full=H3-K4-HMTase;
AltName: Full=Histone H3-K36 methyltransferase 8;
Short=H3-K36-HMTase 8;
AltName: Full=Protein EARLY FLOWERING IN SHORT DAYS;
AltName: Full=Protein LAZARUS 2 {ECO:0000303|PubMed:20949080};
AltName: Full=Protein SET DOMAIN GROUP 8;
Name=ASHH2 {ECO:0000303|PubMed:19915673};
Synonyms=EFS, LAZ2 {ECO:0000303|PubMed:20949080}, SDG8, SET8;
OrderedLocusNames=At1g77300; ORFNames=T14N5.15;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=16299497; DOI=10.1038/ncb1329;
Zhao Z., Yu Y., Meyer D., Wu C., Shen W.-H.;
"Prevention of early flowering by expression of FLOWERING LOCUS C
requires methylation of histone H3 K36.";
Nat. Cell Biol. 7:1256-1260(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1299-1759 (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NOMENCLATURE.
PubMed=11691919; DOI=10.1093/nar/29.21.4319;
Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
"The Arabidopsis thaliana genome contains at least 29 active genes
encoding SET domain proteins that can be assigned to four
evolutionarily conserved classes.";
Nucleic Acids Res. 29:4319-4333(2001).
[6]
FUNCTION.
PubMed=10518493;
Soppe W.J.J., Bentsink L., Koornneef M.;
"The early-flowering mutant efs is involved in the autonomous
promotion pathway of Arabidopsis thaliana.";
Development 126:4763-4770(1999).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16258034; DOI=10.1105/tpc.105.034645;
Kim S.Y., He Y., Jacob Y., Noh Y.-S., Michaels S., Amasino R.;
"Establishment of the vernalization-responsive, winter-annual habit in
Arabidopsis requires a putative histone H3 methyl transferase.";
Plant Cell 17:3301-3310(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=18070919; DOI=10.1128/MCB.01607-07;
Xu L., Zhao Z., Dong A., Soubigou-Taconnat L., Renou J.P.,
Steinmetz A., Shen W.H.;
"Di- and tri- but not monomethylation on histone H3 lysine 36 marks
active transcription of genes involved in flowering time regulation
and other processes in Arabidopsis thaliana.";
Mol. Cell. Biol. 28:1348-1360(2008).
[9]
INDUCTION BY VERNALIZATION, AND TISSUE SPECIFICITY.
PubMed=19121105; DOI=10.1111/j.1365-313X.2008.03776.x;
Choi J., Hyun Y., Kang M.J., In Yun H., Yun J.Y., Lister C., Dean C.,
Amasino R.M., Noh B., Noh Y.S., Choi Y.;
"Resetting and regulation of Flowering Locus C expression during
Arabidopsis reproductive development.";
Plant J. 57:918-931(2009).
[10]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19915673; DOI=10.1371/journal.pone.0007817;
Grini P.E., Thorstensen T., Alm V., Vizcay-Barrena G., Windju S.S.,
Jorstad T.S., Wilson Z.A., Aalen R.B.;
"The ASH1 HOMOLOG 2 (ASHH2) histone H3 methyltransferase is required
for ovule and anther development in Arabidopsis.";
PLoS ONE 4:E7817-E7817(2009).
[11]
FUNCTION, AND INTERACTION WITH FRI AND SUF4.
PubMed=20711170; DOI=10.1038/emboj.2010.198;
Ko J.H., Mitina I., Tamada Y., Hyun Y., Choi Y., Amasino R.M., Noh B.,
Noh Y.S.;
"Growth habit determination by the balance of histone methylation
activities in Arabidopsis.";
EMBO J. 29:3208-3215(2010).
[12]
FUNCTION.
PubMed=20949080; DOI=10.1371/journal.ppat.1001137;
Palma K., Thorgrimsen S., Malinovsky F.G., Fiil B.K., Nielsen H.B.,
Brodersen P., Hofius D., Petersen M., Mundy J.;
"Autoimmunity in Arabidopsis acd11 is mediated by epigenetic
regulation of an immune receptor.";
PLoS Pathog. 6:E1001137-E1001137(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH THE FRI-C
COMPLEX AND SWC6.
PubMed=21282526; DOI=10.1105/tpc.110.075911;
Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
"The FRIGIDA complex activates transcription of FLC, a strong
flowering repressor in Arabidopsis, by recruiting chromatin
modification factors.";
Plant Cell 23:289-303(2011).
[14]
FUNCTION, INTERACTION WITH BZR2/BES1 AND IWS1, SUBCELLULAR LOCATION,
AND DISRUPTION PHENOTYPE.
PubMed=24838002; DOI=10.1093/mp/ssu056;
Wang X., Chen J., Xie Z., Liu S., Nolan T., Ye H., Zhang M., Guo H.,
Schnable P.S., Li Z., Yin Y.;
"Histone lysine methyltransferase SDG8 is involved in brassinosteroid-
regulated gene expression in Arabidopsis thaliana.";
Mol. Plant 7:1303-1315(2014).
[15]
STRUCTURE BY NMR OF 849-937 IN COMPLEX WITH ZINC AND METHYLATED H3K4
PEPTIDE, AND MUTAGENESIS OF TRP-865; TRP-874; TRP-891; GLN-908 AND
GLU-909.
PubMed=21522130; DOI=10.1038/emboj.2011.108;
Hoppmann V., Thorstensen T., Kristiansen P.E., Veiseth S.V.,
Rahman M.A., Finne K., Aalen R.B., Aasland R.;
"The CW domain, a new histone recognition module in chromatin
proteins.";
EMBO J. 30:1939-1952(2011).
-!- FUNCTION: Histone methyltransferase involved in di and tri-
methylation of 'Lys-36' of histone H3 (H3K36me2 and H3K36me3).
Binds to H3 already mono- or di-methylated on 'Lys-4'(H3K4me1 or
H3K4me2), but not to H3K4me3. H3K4me and H3K36me represent
specific tags for epigenetic transcriptional activation. Regulates
positively FLC transcription to prevent early flowering
transition. Required for flowering transition in response to
vernalization and for the maintenance of FLC expression in late
embryos, but dispensable for the initial reactivation in early
embryos during reprogramming. Seems also to modulate several
traits including floral organ size, root size and dormancy.
Promotes apical dominance (PubMed:16299497, PubMed:10518493,
PubMed:16258034, PubMed:18070919, PubMed:19915673,
PubMed:20711170). Directly involved in the tri-methylation of
'Lys-36' of histone H3 (H3K36me3) at LAZ5 chromatin to maintain a
transcriptionally active state of LAZ5, a TIR-NB-LRR protein
involved in innate immunity (PubMed:20949080). Required for
brassinosteroid (BR)-induced gene expression and histone H3
trimethylation on 'Lys-36' (H3K36me3) in BR-regulated genes
(PubMed:24838002). {ECO:0000269|PubMed:10518493,
ECO:0000269|PubMed:16258034, ECO:0000269|PubMed:16299497,
ECO:0000269|PubMed:18070919, ECO:0000269|PubMed:19915673,
ECO:0000269|PubMed:20711170, ECO:0000269|PubMed:20949080,
ECO:0000269|PubMed:24838002}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Interacts with FRI and SUF4, two components of the
transcription activator complex FRI-C, and with SWC6, a component
of the SWR1 chromatin-remodeling complex (PubMed:20711170,
PubMed:21282526, PubMed:21522130). Interacts with BZR2/BES1 and
IWS1 (PubMed:24838002). {ECO:0000269|PubMed:20711170,
ECO:0000269|PubMed:21282526, ECO:0000269|PubMed:21522130,
ECO:0000269|PubMed:24838002}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18070919,
ECO:0000269|PubMed:24838002}. Chromosome, centromere
{ECO:0000305|PubMed:18070919}. Note=Associates with centromeric
constitutive heterochromatin. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q2LAE1-1; Sequence=Displayed;
Name=2;
IsoId=Q2LAE1-2; Sequence=VSP_018133;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in young
tissues, including shoot and root apex. Expressed in ovules,
tapetum layer and microspores. {ECO:0000269|PubMed:16258034,
ECO:0000269|PubMed:16299497, ECO:0000269|PubMed:19121105,
ECO:0000269|PubMed:19915673}.
-!- INDUCTION: Not regulated by vernalization.
{ECO:0000269|PubMed:19121105}.
-!- DISRUPTION PHENOTYPE: Early flowering. Pleiotropic developmental
effects including dwarf and bushy phenotype, reduced seed setting
and defects in ovule and embryo sac development (PubMed:18070919,
PubMed:19915673, PubMed:24838002). Altered responses to
brassinosteroid (BR) (PubMed:24838002).
{ECO:0000269|PubMed:18070919, ECO:0000269|PubMed:19915673,
ECO:0000269|PubMed:24838002}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAC34358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAD94318.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; DQ340869; ABC69038.1; -; mRNA.
EMBL; EU014690; ABV68921.1; -; mRNA.
EMBL; AC004260; AAC34358.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE35960.1; -; Genomic_DNA.
EMBL; AK221916; BAD94318.1; ALT_INIT; mRNA.
PIR; T00458; T00458.
RefSeq; NP_177854.6; NM_106379.9. [Q2LAE1-2]
UniGene; At.34505; -.
PDB; 2L7P; NMR; -; A=849-937.
PDBsum; 2L7P; -.
ProteinModelPortal; Q2LAE1; -.
SMR; Q2LAE1; -.
BioGrid; 29285; 15.
IntAct; Q2LAE1; 2.
MINT; MINT-8049764; -.
STRING; 3702.AT1G77300.1; -.
iPTMnet; Q2LAE1; -.
PaxDb; Q2LAE1; -.
PRIDE; Q2LAE1; -.
EnsemblPlants; AT1G77300.1; AT1G77300.1; AT1G77300. [Q2LAE1-2]
GeneID; 844066; -.
Gramene; AT1G77300.1; AT1G77300.1; AT1G77300.
KEGG; ath:AT1G77300; -.
Araport; AT1G77300; -.
TAIR; locus:2196000; AT1G77300.
eggNOG; KOG4442; Eukaryota.
eggNOG; COG2940; LUCA.
HOGENOM; HOG000029212; -.
InParanoid; Q2LAE1; -.
OMA; KNESHEG; -.
OrthoDB; EOG0936006B; -.
PhylomeDB; Q2LAE1; -.
PRO; PR:Q2LAE1; -.
Proteomes; UP000006548; Chromosome 1.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:TAIR.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048653; P:anther development; IMP:TAIR.
GO; GO:0016116; P:carotenoid metabolic process; IMP:TAIR.
GO; GO:0009553; P:embryo sac development; IMP:TAIR.
GO; GO:0010452; P:histone H3-K36 methylation; IDA:TAIR.
GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
GO; GO:0048481; P:plant ovule development; IMP:TAIR.
GO; GO:0009555; P:pollen development; IMP:TAIR.
GO; GO:0031062; P:positive regulation of histone methylation; IDA:TAIR.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
GO; GO:0010363; P:regulation of plant-type hypersensitive response; IMP:TAIR.
GO; GO:0043067; P:regulation of programmed cell death; IGI:TAIR.
GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
InterPro; IPR006560; AWS_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR011124; Znf_CW.
Pfam; PF00856; SET; 1.
Pfam; PF07496; zf-CW; 1.
SMART; SM00570; AWS; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS51050; ZF_CW; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Centromere; Chromatin regulator;
Chromosome; Complete proteome; Metal-binding; Methyltransferase;
Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase;
Zinc; Zinc-finger.
CHAIN 1 1759 Histone-lysine N-methyltransferase ASHH2.
/FTId=PRO_0000233371.
DOMAIN 974 1024 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 1026 1143 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1151 1167 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
ZN_FING 859 912 CW-type. {ECO:0000255|PROSITE-
ProRule:PRU00454}.
COMPBIAS 1400 1405 Poly-Leu.
METAL 868 868 Zinc. {ECO:0000269|PubMed:21522130}.
METAL 871 871 Zinc. {ECO:0000269|PubMed:21522130}.
METAL 893 893 Zinc. {ECO:0000269|PubMed:21522130}.
METAL 904 904 Zinc. {ECO:0000269|PubMed:21522130}.
BINDING 1142 1142 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
VAR_SEQ 1447 1447 G -> GLQMLHNIMKQYRGDFKRIPIIRKLLKVLEYLATRK
ILALEHIIRRP (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_018133.
MUTAGEN 865 865 W->A: Loss of histone tail binding.
{ECO:0000269|PubMed:21522130}.
MUTAGEN 874 874 W->A: Loss of histone tail binding.
{ECO:0000269|PubMed:21522130}.
MUTAGEN 891 891 W->A: Loss of histone tail binding.
{ECO:0000269|PubMed:21522130}.
MUTAGEN 908 908 Q->A: Loss of histone tail binding.
{ECO:0000269|PubMed:21522130}.
MUTAGEN 909 909 E->A: Loss of histone tail binding.
{ECO:0000269|PubMed:21522130}.
CONFLICT 1426 1426 I -> T (in Ref. 4; BAD94318).
{ECO:0000305}.
STRAND 860 867 {ECO:0000244|PDB:2L7P}.
TURN 869 871 {ECO:0000244|PDB:2L7P}.
STRAND 874 877 {ECO:0000244|PDB:2L7P}.
HELIX 879 882 {ECO:0000244|PDB:2L7P}.
HELIX 893 895 {ECO:0000244|PDB:2L7P}.
STRAND 899 901 {ECO:0000244|PDB:2L7P}.
HELIX 912 919 {ECO:0000244|PDB:2L7P}.
SEQUENCE 1759 AA; 193228 MW; 5616BE25ECEF2155 CRC64;
MDCKENGVGD ASGCNIDANS LASNLAMNTN EDFYEKLSSR GQNLDSVSSL EIPQTASSVN
HTIEGQRKCF TEIEQMGYGN SNSQEDAGNT DDDLYVCYNA DDTQEQGVVS GELEQSQELI
CDTDLLVNCN KLDDGKESQD TNVSLVSIFS GSMQEKEAPQ AKEDEGYGGT TLPIGGSGID
TESTFVNDAP EQFESLETTK HIKPDEVESD GISYRFDDGG KEGRNGPSSD LDTGSSDDIS
LSQSFSFPDS LLDSSVFGCS ATESYLEDAI DIEGNGTIVV SPSLAITEML NNDDGGLCSH
DLNKITVTET INPDLKLVRE DRLDTDLSVM NEKMLKNHVG DSSSESAVAA LSMNNGMAAD
LRAENFSQSS PIDEKTLDME ANSPITDSSL IWNFPLNFGS GGIEVCNPEN AVEPLRIVDD
NGRIGGEVAS ASGSDFCEAG MSSSRRKARD GKQCKVVQTK TSARHLRKSS RKKQSERDIE
SIFKCSKQKR SSLLKTSRSS EWGLPSKTTE IFLQSNNIPY DGPPHHEPQR SQGNLNNGEH
NRSSHNGNVE GSNRNIQASS GSCLRLKVKF GKSGGQNPLN ITVSKVSGNS LPGNGIVKAG
TCLELPGSAH FGEDKMQTVE TKEDLVEKSN PVEKVSYLQS SDSMRDKKYN QDAGGLCRKV
GGDVLDDDPH LSSIRMVEEC ERATGTQSLD AETSPDSEVI NSVPDSIVNI EHKEGLHHGF
FSTPEDVVKK NRVLEKEDEL RASKSPSENG SHLIPNAKKA KHPKSKSNGT KKGKSKFSES
AKDGRKNESH EGVEQRKSLN TSMGRDDSDY PEVGRIESHK TTGALLDADI GKTSATYGTI
SSDVTHGEMV VDVTIEDSYS TESAWVRCDD CFKWRRIPAS VVGSIDESSR WICMNNSDKR
FADCSKSQEM SNEEINEELG IGQDEADAYD CDAAKRGKEK EQKSKRLTGK QKACFKAIKT
NQFLHRNRKS QTIDEIMVCH CKPSPDGRLG CGEECLNRML NIECLQGTCP AGDLCSNQQF
QKRKYVKFER FQSGKKGYGL RLLEDVREGQ FLIEYVGEVL DMQSYETRQK EYAFKGQKHF
YFMTLNGNEV IDAGAKGNLG RFINHSCEPN CRTEKWMVNG EICVGIFSMQ DLKKGQELTF
DYNYVRVFGA AAKKCYCGSS HCRGYIGGDP LNGDVIIQSD SDEEYPELVI LDDDESGEGI
LGATSRTFTD DADEQMPQSF EKVNGYKDLA PDNTQTQSSV SVKLPEREIP PPLLQPTEVL
KELSSGISIT AVQQEVPAEK KTKSTSPTSS SLSRMSPGGT NSDKTTKHGS GEDKKILPRP
RPRMKTSRSS ESSKRDKGGI YPGVNKAQVI PVNKLQQQPI KSKGSEKVSP SIETFEGKLN
ELLDAVGGIS KRRDSAKGYL KLLLLTAASR GTDEEGIYSN RDLSMILDAL LKTKSKSVLV
DIINKNGPFA GMESFKDSVL SFTEHDDYTV HNIARSFRDR WIPKHFRKPW RINREERSES
MRSPINRRFR ASQEPRYDHQ SPRPAEPAAS VTSSKAATPE TASVSEGYSE PNSGLPETNG
RKRKSRWDQP SKTKEQRIMT ILSQQTDETN GNQDVQDDLP PGFSSPCTDV PDAITAQPQQ
KFLSRLPVSY GIPLSIVHQF GSPGKEDPTT WSVAPGMPFY PFPPLPPVSH GEFFAKRNVR
ACSSSMGNLT YSNEILPATP VTDSTAPTRK RELFSSDIGT TYFRQQKQSV PPWLRNNGGE
KTANSPIPGN LTLEKKLNS


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EIAAB12653 EHMT1,Euchromatic histone-lysine N-methyltransferase 1,EUHMTASE1,Eu-HMTase1,G9a-like protein 1,GLP,GLP,GLP1,H3-K9-HMTase 5,Histone H3-K9 methyltransferase 5,Histone-lysine N-methyltransferase EHMT1,Ho
EIAAB37977 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Homo sapiens,Human,KMT5A,Lysine N-methyltransferase 5A,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PRSET7
EIAAB37976 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Kiaa1717,Mouse,Mus musculus,SET domain-containing protein 7,Set7,SET7_9,Set9,Setd7
18-003-42222 Histone-lysine N-methyltransferase. H3 lysine-9 specific 1 - EC 2.1.1.43; Histone H3-K9 methyltransferase 1; H3-K9-HMTase 1; Suppressor of variegation 3-9 homolog 1; Su(var)3-9 homolog 1 Polyclonal 0.1 mg Protein A
EIAAB37978 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Mouse,Mus musculus,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,Se
EIAAB37979 Bos taurus,Bovine,H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,SET
EIAAB27930 Androgen receptor coactivator 267 kDa protein,Androgen receptor-associated protein of 267 kDa,ARA267,H3-K36-HMTase,H4-K20-HMTase,Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 speci
EIAAB12655 BAT8,C6orf30,EHMT2,Euchromatic histone-lysine N-methyltransferase 2,G9A,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Homo sap
EIAAB12654 Bat8,Ehmt2,Euchromatic histone-lysine N-methyltransferase 2,G9a,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Mouse,Mus muscul
EIAAB40613 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Mouse,Mus musculus,Position-effect variegation 3-9 homolog,Su(var)3-9 homolog 1,Suppressor of variegation 3-
EIAAB40617 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Mouse,Mus musculus,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 homolog 2,Suv39h2
10-002-38056 Set7_9 Histone methyltransferase - EC 2.1.1.43; Histone H3-K4 methyltransferase; H3-K4-HMTase; SET domain-containing protein 7; Set9; SET7_9 N_A 1 mg
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
EIAAB12652 Ehmt1,Euchromatic histone-lysine N-methyltransferase 1,Euhmtase1,Eu-HMTase1,G9a-like protein 1,GLP,Glp,GLP1,Histone-lysine N-methyltransferase EHMT1,Kmt1d,Lysine N-methyltransferase 1D,Mouse,Mus muscu
20-002-35013 SET7_9 (anti-human SET7_9. clone s4E5) - EC 2.1.1.43; Histone H3-K4 methyltransferase; H3-K4-HMTase; SET domain-containing protein 7; Set9; SET7_9 Monoclonal 0.1 ml
18-272-195678 SETDB1 - Rabbit polyclonal to SETDB1; EC 2.1.1.43; SET domain bifurcated 1; ERG-associated protein with SET domain; ESET; Histone H3-K9 methyltransferase 4; H3-K9-HMTase 4 Polyclonal 0.05 mg
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
EIAAB37958 C13orf4,Chronic lymphocytic leukemia deletion region gene 8 protein,CLLD8,Histone-lysine N-methyltransferase SETDB2,Homo sapiens,Human,KMT1F,Lysine N-methyltransferase 1F,SET domain bifurcated 2,SETDB


 

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