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Histone-lysine N-methyltransferase, H3 lysine-9 specific (EC 2.1.1.43) (Cryptic loci regulator 4) (Histone H3-K9 methyltransferase) (H3-K9-HMTase) (Lysine N-methyltransferase 1)

 CLR4_SCHPO              Reviewed;         490 AA.
O60016; O74565;
08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
08-DEC-2000, sequence version 2.
13-FEB-2019, entry version 180.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific;
EC=2.1.1.43;
AltName: Full=Cryptic loci regulator 4;
AltName: Full=Histone H3-K9 methyltransferase;
Short=H3-K9-HMTase;
AltName: Full=Lysine N-methyltransferase 1;
Name=clr4; Synonyms=kmt1; ORFNames=SPBC428.08c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9620780; DOI=10.1038/566;
Ivanova A.V., Bonaduce M.J., Ivanov S.V., Klar A.J.S.;
"The chromo and SET domains of the Clr4 protein are essential for
silencing in fission yeast.";
Nat. Genet. 19:192-195(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SP813;
Lord P.;
Thesis (1998), University of Edinburgh, United Kingdom.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[4]
PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE RIK1-ASSOCIATED E3
UBIQUITIN LIGASE COMPLEX, AND FUNCTION.
PubMed=16024659; DOI=10.1101/gad.1328005;
Horn P.J., Bastie J.-N., Peterson C.L.;
"A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential
for heterochromatin formation.";
Genes Dev. 19:1705-1714(2005).
[5]
PROTEIN SEQUENCE OF 64-85; 127-150; 190-205; 371-406; 429-455 AND
486-490, AND INTERACTION WITH CUL4.
PubMed=16127433; DOI=10.1038/ncb1300;
Jia S., Kobayashi R., Grewal S.I.S.;
"Ubiquitin ligase component Cul4 associates with Clr4 histone
methyltransferase to assemble heterochromatin.";
Nat. Cell Biol. 7:1007-1013(2005).
[6]
FUNCTION.
PubMed=8138176;
Ekwall K., Ruusala T.;
"Mutations in rik1, clr2, clr3 and clr4 genes asymmetrically derepress
the silent mating-type loci in fission yeast.";
Genetics 136:53-64(1994).
[7]
ENZYME ACTIVITY, AND MUTAGENESIS OF TRP-31; TRP-41; ARG-320; GLY-378
AND GLY-486.
PubMed=11283354; DOI=10.1126/science.1060118;
Nakayama J., Rice J.C., Strahl B.D., Allis C.D., Grewal S.I.S.;
"Role of histone H3 lysine 9 methylation in epigenetic control of
heterochromatin assembly.";
Science 292:110-113(2001).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[9]
STRUCTURE BY NMR OF 2-69.
PubMed=11273706; DOI=10.1006/jmbi.2001.4515;
Horita D.A., Ivanova A.V., Altieri A.S., Klar A.J., Byrd R.A.;
"Solution structure, domain features, and structural implications of
mutants of the chromo domain from the fission yeast histone
methyltransferase Clr4.";
J. Mol. Biol. 307:861-870(2001).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 192-490 IN COMPLEX WITH ZINC
IONS.
PubMed=12389037; DOI=10.1038/nsb860;
Min J., Zhang X., Cheng X., Grewal S.I.S., Xu R.M.;
"Structure of the SET domain histone lysine methyltransferase Clr4.";
Nat. Struct. Biol. 9:828-832(2002).
-!- FUNCTION: Histone methyltransferase. Catalytic component of the
rik1-associated E3 ubiquitin ligase complex that shows ubiquitin
ligase activity and is required for histone H3K9 methylation.
H3K9me represents a specific tag for epigenetic transcriptional
repression by recruiting swi6/HP1 to methylated histones which
leads to transcriptional silencing within centromeric
heterochromatin, telomeric regions and at the silent mating-type
loci. {ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:8138176}.
-!- 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:0000269|PubMed:11283354};
-!- SUBUNIT: Component of the rik1-associated E3 ubiquitin ligase
complex composed of at least clr4, cul4, pip1, raf1 and raf2.
Interacts directly with cul4. {ECO:0000269|PubMed:12389037,
ECO:0000269|PubMed:16024659, ECO:0000269|PubMed:16127433}.
-!- INTERACTION:
O14122:cul4; NbExp=3; IntAct=EBI-354657, EBI-904890;
Q10426:rik1; NbExp=3; IntAct=EBI-354657, EBI-1111936;
O94276:SPBP8B7.28c; NbExp=2; IntAct=EBI-354657, EBI-2651917;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
Cytoplasm, cytoskeleton, microtubule organizing center, spindle
pole body {ECO:0000269|PubMed:16823372}. Chromosome
{ECO:0000305|PubMed:16823372}.
-!- 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.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
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EMBL; AF061854; AAC18302.1; -; Genomic_DNA.
EMBL; AJ007840; CAA07709.1; -; Genomic_DNA.
EMBL; CU329671; CAA22283.1; -; Genomic_DNA.
PIR; T43700; T43700.
PIR; T43745; T43745.
RefSeq; NP_595186.1; NM_001021094.2.
PDB; 1G6Z; NMR; -; A=2-69.
PDB; 1MVH; X-ray; 2.30 A; A=192-490.
PDB; 1MVX; X-ray; 3.00 A; A=192-490.
PDB; 6BOX; X-ray; 2.41 A; A/B=192-490.
PDB; 6BP4; X-ray; 2.77 A; A/B=192-490.
PDBsum; 1G6Z; -.
PDBsum; 1MVH; -.
PDBsum; 1MVX; -.
PDBsum; 6BOX; -.
PDBsum; 6BP4; -.
ProteinModelPortal; O60016; -.
SMR; O60016; -.
BioGrid; 277343; 299.
DIP; DIP-32588N; -.
IntAct; O60016; 8.
MINT; O60016; -.
STRING; 4896.SPBC428.08c.1; -.
iPTMnet; O60016; -.
MaxQB; O60016; -.
PaxDb; O60016; -.
PRIDE; O60016; -.
EnsemblFungi; SPBC428.08c.1; SPBC428.08c.1:pep; SPBC428.08c.
GeneID; 2540825; -.
KEGG; spo:SPBC428.08c; -.
EuPathDB; FungiDB:SPBC428.08c; -.
PomBase; SPBC428.08c; clr4.
InParanoid; O60016; -.
KO; K11419; -.
OMA; NCRGWLF; -.
PhylomeDB; O60016; -.
Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
Reactome; R-SPO-427359; SIRT1 negatively regulates rRNA expression.
EvolutionaryTrace; O60016; -.
PRO; PR:O60016; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0034507; C:chromosome, centromeric outer repeat region; IEA:GOC.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0043494; C:CLRC ubiquitin ligase complex; IDA:PomBase.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0031934; C:mating-type region heterochromatin; NAS:PomBase.
GO; GO:0031618; C:nuclear pericentric heterochromatin; TAS:PomBase.
GO; GO:1990707; C:nuclear subtelomeric heterochromatin; NAS:PomBase.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:PomBase.
GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
GO; GO:0003727; F:single-stranded RNA binding; IDA:PomBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0034613; P:cellular protein localization; IMP:PomBase.
GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
GO; GO:0030702; P:chromatin silencing at centromere; IMP:PomBase.
GO; GO:0000183; P:chromatin silencing at rDNA; IMP:PomBase.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:PomBase.
GO; GO:0006348; P:chromatin silencing at telomere; TAS:PomBase.
GO; GO:0007535; P:donor selection; IMP:PomBase.
GO; GO:1902368; P:heterochromatin maintenance involved in chromatin silencing at centromere outer repeat region; IGI:PomBase.
GO; GO:0045141; P:meiotic telomere clustering; IMP:PomBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
CDD; cd00024; CHROMO; 1.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR023779; Chromodomain_CS.
InterPro; IPR011381; Histone_H3-K9_MeTrfase.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF00385; Chromo; 1.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
PIRSF; PIRSF009343; SUV39_SET; 1.
SMART; SM00298; CHROMO; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Metal-binding;
Methyltransferase; Nucleus; Reference proteome;
S-adenosyl-L-methionine; Transferase; Zinc.
CHAIN 1 490 Histone-lysine N-methyltransferase, H3
lysine-9 specific.
/FTId=PRO_0000186063.
DOMAIN 8 69 Chromo. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 258 325 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 328 452 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 473 489 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
REGION 338 340 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 409 410 S-adenosyl-L-methionine binding.
{ECO:0000250}.
METAL 260 260 Zinc 1.
METAL 260 260 Zinc 2.
METAL 262 262 Zinc 1.
METAL 268 268 Zinc 1.
METAL 268 268 Zinc 3.
METAL 276 276 Zinc 1.
METAL 278 278 Zinc 2.
METAL 307 307 Zinc 2.
METAL 307 307 Zinc 3.
METAL 311 311 Zinc 2.
METAL 313 313 Zinc 3.
METAL 317 317 Zinc 3.
METAL 412 412 Zinc 4. {ECO:0000250}.
METAL 477 477 Zinc 4. {ECO:0000250}.
METAL 479 479 Zinc 4. {ECO:0000250}.
METAL 484 484 Zinc 4. {ECO:0000250}.
BINDING 381 381 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 406 406 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MUTAGEN 31 31 W->G: Weak effect on methyltransferase
activity. {ECO:0000269|PubMed:11283354}.
MUTAGEN 41 41 W->G: Weak effect on methyltransferase
activity. {ECO:0000269|PubMed:11283354}.
MUTAGEN 320 320 R->H: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11283354}.
MUTAGEN 378 378 G->S: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11283354}.
MUTAGEN 486 486 G->D: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:11283354}.
CONFLICT 19 19 D -> G (in Ref. 1; AAC18302).
{ECO:0000305}.
CONFLICT 142 142 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 437 437 A -> G (in Ref. 1; AAC18302).
{ECO:0000305}.
STRAND 14 17 {ECO:0000244|PDB:1G6Z}.
STRAND 26 29 {ECO:0000244|PDB:1G6Z}.
TURN 32 35 {ECO:0000244|PDB:1G6Z}.
STRAND 40 42 {ECO:0000244|PDB:1G6Z}.
HELIX 44 47 {ECO:0000244|PDB:1G6Z}.
HELIX 51 61 {ECO:0000244|PDB:1G6Z}.
TURN 62 65 {ECO:0000244|PDB:1G6Z}.
HELIX 196 214 {ECO:0000244|PDB:1MVH}.
STRAND 216 219 {ECO:0000244|PDB:1MVH}.
STRAND 221 224 {ECO:0000244|PDB:1MVH}.
STRAND 226 228 {ECO:0000244|PDB:6BOX}.
STRAND 237 239 {ECO:0000244|PDB:1MVH}.
HELIX 254 256 {ECO:0000244|PDB:1MVH}.
STRAND 265 268 {ECO:0000244|PDB:1MVH}.
TURN 273 275 {ECO:0000244|PDB:1MVH}.
STRAND 277 279 {ECO:0000244|PDB:1MVH}.
STRAND 294 296 {ECO:0000244|PDB:1MVH}.
STRAND 302 305 {ECO:0000244|PDB:1MVH}.
STRAND 309 313 {ECO:0000244|PDB:6BOX}.
HELIX 322 324 {ECO:0000244|PDB:1MVH}.
STRAND 330 334 {ECO:0000244|PDB:1MVH}.
STRAND 336 346 {ECO:0000244|PDB:1MVH}.
STRAND 353 356 {ECO:0000244|PDB:1MVH}.
STRAND 360 363 {ECO:0000244|PDB:1MVH}.
HELIX 364 371 {ECO:0000244|PDB:1MVH}.
STRAND 382 385 {ECO:0000244|PDB:1MVH}.
STRAND 390 392 {ECO:0000244|PDB:1MVH}.
STRAND 394 397 {ECO:0000244|PDB:1MVH}.
STRAND 399 402 {ECO:0000244|PDB:1MVH}.
HELIX 404 407 {ECO:0000244|PDB:1MVH}.
STRAND 415 423 {ECO:0000244|PDB:1MVH}.
STRAND 432 439 {ECO:0000244|PDB:1MVH}.
TURN 452 454 {ECO:0000244|PDB:6BOX}.
STRAND 455 458 {ECO:0000244|PDB:1MVH}.
HELIX 470 472 {ECO:0000244|PDB:6BP4}.
SEQUENCE 490 AA; 55918 MW; 53C3EC87BCBA51FF CRC64;
MSPKQEEYEV ERIVDEKLDR NGAVKLYRIR WLNYSSRSDT WEPPENLSGC SAVLAEWKRR
KRRLKGSNSD SDSPHHASNP HPNSRQKHQH QTSKSVPRSQ RFSRELNVKK ENKKVFSSQT
TKRQSRKQST ALTTNDTSII LDDSLHTNSK KLGKTRNEVK EESQKRELVS NSIKEATSPK
TSSILTKPRN PSKLDSYTHL SFYEKRELFR KKLREIEGPE VTLVNEVDDE PCPSLDFQFI
SQYRLTQGVI PPDPNFQSGC NCSSLGGCDL NNPSRCECLD DLDEPTHFAY DAQGRVRADT
GAVIYECNSF CSCSMECPNR VVQRGRTLPL EIFKTKEKGW GVRSLRFAPA GTFITCYLGE
VITSAEAAKR DKNYDDDGIT YLFDLDMFDD ASEYTVDAQN YGDVSRFFNH SCSPNIAIYS
AVRNHGFRTI YDLAFFAIKD IQPLEELTFD YAGAKDFSPV QSQKSQQNRI SKLRRQCKCG
SANCRGWLFG


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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
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
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
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

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1006: metapathway biotransformation
WP1124: metapathway biotransformation
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1581: Histidine metabolism
WP1669: Lysine biosynthesis
WP1673: Naphthalene and anthracene degradation
WP1700: Selenoamino acid metabolism
WP1714: Tyrosine metabolism
WP533: Lysine Biosynthesis
WP702: metapathway biotransformation
WP889: metapathway biotransformation
WP2361: Gastric cancer network 1
WP2366: Butyrate-induced histone acetylation
WP2369: Histone modifications
WP300: Histone modifications
WP1689: Porphyrin and chlorophyll metabolism

Related Genes :
[EHMT1 EUHMTASE1 GLP KIAA1876 KMT1D] Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Histone H3-K9 methyltransferase 5) (H3-K9-HMTase 5) (Lysine N-methyltransferase 1D)
[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)
[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)
[EHMT2 BAT8 C6orf30 G9A KMT1C NG36] Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Lysine N-methyltransferase 1C) (Protein G9a)
[Ehmt2 Bat8 G9a Ng36] Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein G9a)
[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)
[SUV39H1 KMT1A SUV39H] Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Lysine N-methyltransferase 1A) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
[Suv39h1 Suv39h] Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
[SUV39H2 KMT1B] Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Lysine N-methyltransferase 1B) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2)
[Suv39h2] Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2)
[HIST1H3A H3FA; HIST1H3B H3FL; HIST1H3C H3FC; HIST1H3D H3FB; HIST1H3E H3FD; HIST1H3F H3FI; HIST1H3G H3FH; HIST1H3H H3FK; HIST1H3I H3FF; HIST1H3J H3FJ] Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l)
[Hist1h3b H3-53 H3.2 H3b; Hist1h3c H3-143; Hist1h3d H3-B; Hist1h3e H3-F; Hist1h3f H3.2-221 H3f; Hist2h3b H3.2-616; Hist2h3c1 H3.2-615 Hist2h3ca1; Hist2h3c2 H3.2-614 Hist2h3ca2] Histone H3.2
[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)
[Hist1h3a H3a; Hist1h3g H3.1-221 H3g; Hist1h3h H3.1-291 H3h; Hist1h3i H3.1-I H3i] Histone H3.1
[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)
[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)
[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)
[HIST2H3A; HIST2H3C H3F2 H3FM; HIST2H3D] Histone H3.2 (Histone H3/m) (Histone H3/o)
[H3f3a H3.3a; H3f3b H3.3b] Histone H3.3
[HTR2 At1g09200 T12M4.9; HTR3 At3g27360 K1G2.8; HTR13 At5g10390 F12B17_260; HTR9 At5g10400 F12B17_250; HTR1 At5g65360 MNA5.9] Histone H3.2 (Histone H3.1)
[H3-I; H3-II; H3-III; H3-IV; H3-V; H3-VI; H3-VII; H3-VIII] Histone H3.2 (Histone H3 class I)
[H3F3A H3.3A H3F3 PP781; H3F3B H3.3B] Histone H3.3
[HHT1 TTHERM_00570560; HHT2 TTHERM_00189180] Histone H3 (H3S) (Histone H3-I/H3-II) (Major histone H3) [Cleaved into: H3F]
[HTR4 At4g40030 T5J17.200; HTR5 At4g40040 T5J17.210; HTR8 At5g10980 T30N20_250 T5K6.6] Histone H3.3 (Histone H3.2)
[HIST3H3 H3FT] Histone H3.1t (H3/t) (H3t) (H3/g)
[H3-1.1 ALH3-1.1; H3.1] Histone H3.2 (Histone H3.1) (Major histone H3)
[H3F3C] Histone H3.3C (Histone H3.5)
[] Histone H3.3 (Histone H3.2) (Minor histone H3)
[Ehmt1 Euhmtase1 Glp Kmt1d] Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Lysine N-methyltransferase 1D)
[HHT1 YBR010W YBR0201; HHT2 SIN2 YNL031C N2749] Histone H3

Bibliography :