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Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.43) (Disrupter of telomere silencing protein 1) (Histone H3-K79 methyltransferase) (H3-K79-HMTase) (Lysine N-methyltransferase 4)

 DOT1_YEAST              Reviewed;         582 AA.
Q04089; D6VT67;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 166.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
EC=2.1.1.43;
AltName: Full=Disrupter of telomere silencing protein 1;
AltName: Full=Histone H3-K79 methyltransferase;
Short=H3-K79-HMTase;
AltName: Full=Lysine N-methyltransferase 4;
Name=DOT1; Synonyms=KMT4, PCH1; OrderedLocusNames=YDR440W;
ORFNames=D9461.26;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=9755194;
Singer M.S., Kahana A., Wolf A.J., Meisinger L.L., Peterson S.E.,
Goggin C., Mahowald M., Gottschling D.E.;
"Identification of high-copy disruptors of telomeric silencing in
Saccharomyces cerevisiae.";
Genetics 150:613-632(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11029058; DOI=10.1091/mbc.11.10.3601;
San-Segundo P.A., Roeder G.S.;
"Role for the silencing protein Dot1 in meiotic checkpoint control.";
Mol. Biol. Cell 11:3601-3615(2000).
[5]
ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-401.
PubMed=12086673; DOI=10.1016/S0092-8674(02)00759-6;
van Leeuwen F., Gafken P.R., Gottschling D.E.;
"Dot1p modulates silencing in yeast by methylation of the nucleosome
core.";
Cell 109:745-756(2002).
[6]
ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-399 AND 401-GLY--GLY-403.
PubMed=12080090; DOI=10.1101/gad.1001502;
Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y.,
Struhl K.;
"Lysine methylation within the globular domain of histone H3 by Dot1
is important for telomeric silencing and Sir protein association.";
Genes Dev. 16:1518-1527(2002).
[7]
FUNCTION.
PubMed=12097318; DOI=10.1074/jbc.C200366200;
Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
"Disruptor of telomeric silencing-1 is a chromatin-specific histone H3
methyltransferase.";
J. Biol. Chem. 277:30421-30424(2002).
[8]
ENZYME REGULATION.
PubMed=12167634; DOI=10.1074/jbc.C200433200;
Ng H.H., Xu R.-M., Zhang Y., Struhl K.;
"Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-
mediated methylation of histone H3 lysine 79.";
J. Biol. Chem. 277:34655-34657(2002).
[9]
FUNCTION.
PubMed=12152067; DOI=10.1038/nature00970;
Briggs S.D., Xiao T., Sun Z.-W., Caldwell J.A., Shabanowitz J.,
Hunt D.F., Allis C.D., Strahl B.D.;
"Gene silencing: trans-histone regulatory pathway in chromatin.";
Nature 418:498-498(2002).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
FUNCTION.
PubMed=12574507; DOI=10.1073/pnas.0437846100;
Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.;
"Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast
and mammalian cells: a potential mechanism for position-effect
variegation.";
Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003).
[12]
FUNCTION.
PubMed=15632126; DOI=10.1074/jbc.M414453200;
Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.;
"The DNA damage checkpoint response requires histone H2B
ubiquitination by Rad6-Bre1 and H3 methylation by Dot1.";
J. Biol. Chem. 280:9879-9886(2005).
[13]
FUNCTION.
PubMed=16166626; DOI=10.1128/MCB.25.19.8430-8443.2005;
Wysocki R., Javaheri A., Allard S., Sha F., Cote J., Kron S.J.;
"Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA
damage checkpoint functions of Rad9.";
Mol. Cell. Biol. 25:8430-8443(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[16]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 158-582 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, DNA-BINDING, AND MUTAGENESIS
OF ASP-301; TYR-350; TYR-372; GLU-374; GLU-422; TRP-543 AND TYR-550.
PubMed=15292170; DOI=10.1074/jbc.M405902200;
Sawada K., Yang Z., Horton J.R., Collins R.E., Zhang X., Cheng X.;
"Structure of the conserved core of the yeast Dot1p, a nucleosomal
histone H3 lysine 79 methyltransferase.";
J. Biol. Chem. 279:43296-43306(2004).
-!- FUNCTION: Histone methyltransferase that specifically methylates
histone H3 to form H3K79me. This methylation is required for
telomere silencing and for the pachytene checkpoint during the
meiotic cell cycle by allowing the recruitment of RAD9 to double
strand breaks. Nucleosomes are preferred as substrate compared to
free histones. Can bind to DNA (in vitro).
{ECO:0000269|PubMed:11029058, ECO:0000269|PubMed:12097318,
ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12574507,
ECO:0000269|PubMed:15292170, ECO:0000269|PubMed:15632126,
ECO:0000269|PubMed:16166626, ECO:0000269|PubMed:9755194}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00902,
ECO:0000269|PubMed:12080090, ECO:0000269|PubMed:12086673,
ECO:0000269|PubMed:15292170}.
-!- ENZYME REGULATION: Ubiquitination of histone H2B by the RAD6/UBC2-
BRE1 complex to form H2BK123ub1 is required for efficient DOT1
methyltransferase activity on histone H3. Interaction with DNA is
required for optimal histone methyltransferase activity.
{ECO:0000269|PubMed:12167634, ECO:0000269|PubMed:15292170}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8 to 9. {ECO:0000269|PubMed:15292170};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11029058}.
-!- MISCELLANEOUS: In contrast to other lysine histone
methyltransferases, it does not contain a SET domain, suggesting
the existence of another mechanism for methylation of lysine
residues of histones.
-!- MISCELLANEOUS: Present with 2160 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. DOT1 family. {ECO:0000255|PROSITE-
ProRule:PRU00902}.
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EMBL; U33007; AAB64868.1; -; Genomic_DNA.
EMBL; BK006938; DAA12277.1; -; Genomic_DNA.
PIR; S69720; S69720.
RefSeq; NP_010728.1; NM_001180748.1.
PDB; 1M0R; Model; -; A=392-511.
PDB; 1U2Z; X-ray; 2.20 A; A/B/C=158-582.
PDBsum; 1M0R; -.
PDBsum; 1U2Z; -.
ProteinModelPortal; Q04089; -.
SMR; Q04089; -.
BioGrid; 32496; 293.
DIP; DIP-2560N; -.
IntAct; Q04089; 4.
MINT; Q04089; -.
STRING; 4932.YDR440W; -.
iPTMnet; Q04089; -.
MaxQB; Q04089; -.
PaxDb; Q04089; -.
PRIDE; Q04089; -.
EnsemblFungi; YDR440W; YDR440W; YDR440W.
GeneID; 852050; -.
KEGG; sce:YDR440W; -.
EuPathDB; FungiDB:YDR440W; -.
SGD; S000002848; DOT1.
GeneTree; ENSGT00390000013515; -.
HOGENOM; HOG000112251; -.
InParanoid; Q04089; -.
KO; K11427; -.
OMA; YISTVME; -.
OrthoDB; EOG092C18VU; -.
BioCyc; YEAST:G3O-29974-MONOMER; -.
Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
EvolutionaryTrace; Q04089; -.
PRO; PR:Q04089; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0099115; C:chromosome, subtelomeric region; IEA:GOC.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IDA:SGD.
GO; GO:0031493; F:nucleosomal histone binding; IDA:SGD.
GO; GO:0099114; P:chromatin silencing at subtelomere; IMP:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0000077; P:DNA damage checkpoint; IMP:SGD.
GO; GO:0044783; P:G1 DNA damage checkpoint; IMP:SGD.
GO; GO:0070911; P:global genome nucleotide-excision repair; IMP:SGD.
GO; GO:0034729; P:histone H3-K79 methylation; IDA:SGD.
GO; GO:0031573; P:intra-S DNA damage checkpoint; IMP:SGD.
GO; GO:0051598; P:meiotic recombination checkpoint; IGI:SGD.
GO; GO:0031452; P:negative regulation of heterochromatin assembly; IMP:SGD.
GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
GO; GO:0006301; P:postreplication repair; IGI:SGD.
GO; GO:0000725; P:recombinational repair; IMP:SGD.
GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR021162; Dot1.
InterPro; IPR025789; DOT1_dom.
InterPro; IPR030445; H3-K79_meTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR21451; PTHR21451; 2.
Pfam; PF08123; DOT1; 1.
PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51569; DOT1; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Complete proteome; DNA-binding;
Methyltransferase; Nucleus; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase.
CHAIN 1 582 Histone-lysine N-methyltransferase, H3
lysine-79 specific.
/FTId=PRO_0000186091.
DOMAIN 254 568 DOT1. {ECO:0000255|PROSITE-
ProRule:PRU00902}.
REGION 158 172 Required for interaction with nucleosomes
and DNA.
REGION 372 375 S-adenosyl-L-methionine binding.
REGION 395 404 S-adenosyl-L-methionine binding.
REGION 459 460 S-adenosyl-L-methionine binding.
COMPBIAS 106 169 Lys-rich.
BINDING 422 422 S-adenosyl-L-methionine.
MUTAGEN 301 301 D->A,N: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:15292170}.
MUTAGEN 350 350 Y->F: Reduces methyltransferase activity.
{ECO:0000269|PubMed:15292170}.
MUTAGEN 372 372 Y->F: Reduces methyltransferase activity.
{ECO:0000269|PubMed:15292170}.
MUTAGEN 374 374 E->A,Q: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:15292170}.
MUTAGEN 399 399 G->R: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:12080090}.
MUTAGEN 401 403 Missing: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:12080090}.
MUTAGEN 401 401 G->A,R: Abolishes silencing function.
{ECO:0000269|PubMed:12086673}.
MUTAGEN 422 422 E->A: Abolishes S-adenosyl-L-methionine
binding and methyltransferase activity.
{ECO:0000269|PubMed:15292170}.
MUTAGEN 422 422 E->D: No effect.
{ECO:0000269|PubMed:15292170}.
MUTAGEN 543 543 W->A: Abolishes methyltransferase
activity, but not S-adenosyl-L-methionine
binding. {ECO:0000269|PubMed:15292170}.
MUTAGEN 550 550 Y->A: Abolishes methyltransferase
activity, but not S-adenosyl-L-methionine
binding. {ECO:0000269|PubMed:15292170}.
MUTAGEN 550 550 Y->F: No effect.
{ECO:0000269|PubMed:15292170}.
STRAND 178 180 {ECO:0000244|PDB:1U2Z}.
STRAND 186 188 {ECO:0000244|PDB:1U2Z}.
HELIX 196 201 {ECO:0000244|PDB:1U2Z}.
HELIX 212 214 {ECO:0000244|PDB:1U2Z}.
STRAND 236 240 {ECO:0000244|PDB:1U2Z}.
STRAND 248 252 {ECO:0000244|PDB:1U2Z}.
STRAND 255 257 {ECO:0000244|PDB:1U2Z}.
STRAND 260 262 {ECO:0000244|PDB:1U2Z}.
HELIX 264 277 {ECO:0000244|PDB:1U2Z}.
HELIX 284 291 {ECO:0000244|PDB:1U2Z}.
HELIX 293 301 {ECO:0000244|PDB:1U2Z}.
HELIX 305 319 {ECO:0000244|PDB:1U2Z}.
HELIX 324 331 {ECO:0000244|PDB:1U2Z}.
STRAND 336 338 {ECO:0000244|PDB:1U2Z}.
HELIX 340 353 {ECO:0000244|PDB:1U2Z}.
HELIX 355 361 {ECO:0000244|PDB:1U2Z}.
HELIX 368 370 {ECO:0000244|PDB:1U2Z}.
HELIX 377 386 {ECO:0000244|PDB:1U2Z}.
STRAND 394 399 {ECO:0000244|PDB:1U2Z}.
HELIX 404 413 {ECO:0000244|PDB:1U2Z}.
STRAND 416 422 {ECO:0000244|PDB:1U2Z}.
HELIX 425 444 {ECO:0000244|PDB:1U2Z}.
STRAND 452 458 {ECO:0000244|PDB:1U2Z}.
HELIX 464 469 {ECO:0000244|PDB:1U2Z}.
HELIX 470 472 {ECO:0000244|PDB:1U2Z}.
STRAND 474 478 {ECO:0000244|PDB:1U2Z}.
HELIX 485 495 {ECO:0000244|PDB:1U2Z}.
STRAND 503 508 {ECO:0000244|PDB:1U2Z}.
STRAND 519 521 {ECO:0000244|PDB:1U2Z}.
HELIX 525 528 {ECO:0000244|PDB:1U2Z}.
STRAND 529 535 {ECO:0000244|PDB:1U2Z}.
STRAND 544 546 {ECO:0000244|PDB:1U2Z}.
STRAND 549 555 {ECO:0000244|PDB:1U2Z}.
HELIX 561 563 {ECO:0000244|PDB:1U2Z}.
SEQUENCE 582 AA; 66201 MW; 05CAA6A8F8CBAB9A CRC64;
MGGQESISNN NSDSFIMSSP NLDSQESSIS PIDEKKGTDM QTKSLSSYSK GTLLSKQVQN
LLEEANKYDP IYGSSLPRGF LRDRNTKGKD NGLVPLVEKV IPPIHKKTNN RNTRKKSSTT
TKKDVKKPKA AKVKGKNGRT NHKHTPISKQ EIDTAREKKP LKKGRANKKN DRDSPSSTFV
DWNGPCLRLQ YPLFDIEYLR SHEIYSGTPI QSISLRTNSP QPTSLTSDND TSSVTTAKLQ
SILFSNYMEE YKVDFKRSTA IYNPMSEIGK LIEYSCLVFL PSPYAEQLKE TILPDLNASF
DNSDTKGFVN AINLYNKMIR EIPRQRIIDH LETIDKIPRS FIHDFLHIVY TRSIHPQANK
LKHYKAFSNY VYGELLPNFL SDVYQQCQLK KGDTFMDLGS GVGNCVVQAA LECGCALSFG
CEIMDDASDL TILQYEELKK RCKLYGMRLN NVEFSLKKSF VDNNRVAELI PQCDVILVNN
FLFDEDLNKK VEKILQTAKV GCKIISLKSL RSLTYQINFY NVENIFNRLK VQRYDLKEDS
VSWTHSGGEY YISTVMEDVD ESLFSPAARG RRNRGTPVKY TR


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CSB-EL016100MO Mouse Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit SpeciesMouse 96T
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
CSB-EL016100MO Mouse Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit 96T
CSB-EL016100HU Human Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific(NSD1) ELISA kit 96T
NSD1_MOUSE Mouse ELISA Kit FOR Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific 96T
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


 

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