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Identification
NameHistone-lysine N-methyltransferase, H3 lysine-36 specific
Synonyms
  • Lysine N-methyltransferase 3
  • SET domain-containing protein 2
Gene NameSET2
Enzyme Class
Biological Properties
General FunctionInvolved in histone-lysine N-methyltransferase activity
Specific FunctionHistone methyltransferase that methylates histone H3 to form H3K36me. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent
Cellular LocationNucleus. Chromosome (Probable)
SMPDB PathwaysNot Available
KEGG Pathways
Lysine degradationec00310 Map00310
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00438S-Adenosyl-L-methionineShow
GO Classification
Component
non-membrane-bounded organelle
intracellular non-membrane-bounded organelle
chromosome
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
Function
transferase activity, transferring one-carbon groups
protein-lysine N-methyltransferase activity
methyltransferase activity
histone-lysine N-methyltransferase activity
binding
protein binding
catalytic activity
transferase activity
protein methyltransferase activity
Process
biological regulation
regulation of biological process
regulation of metabolic process
regulation of macromolecule metabolic process
regulation of gene expression
regulation of transcription
regulation of transcription, DNA-dependent
Gene Properties
Chromosome Locationchromosome 10
LocusYJL168C
Gene Sequence>2202 bp ATGTCGAAGAACCAAAGTGTGAGTGCGTCGGAAGATGAAAAAGAAATACTGAATAACAAC GCTGAGGGCCATAAACCTCAAAGGCTTTTTGATCAAGAGCCTGATCTCACAGAGGAAGCA TTGACCAAATTTGAAAACTTGGATGACTGTATATATGCGAACAAGAGGATCGGAACATTT AAGAATAATGATTTCATGGAATGTGACTGTTATGAAGAATTCTCAGATGGCGTCAACCAT GCCTGTGACGAGGATTCTGACTGTATCAATAGACTTACGTTGATAGAATGTGTCAACGAT TTGTGTTCATCTTGTGGTAATGATTGTCAAAATCAGAGATTTCAAAAGAAGCAGTACGCT CCGATAGCCATATTTAAAACAAAGCATAAAGGTTATGGCGTAAGAGCCGAACAGGACATA GAAGCCAACCAGTTCATTTACGAGTACAAAGGTGAGGTGATCGAGGAGATGGAATTTAGA GATAGGTTAATAGACTATGACCAACGTCATTTCAAGCATTTTTATTTTATGATGTTACAG AACGGAGAATTCATTGACGCCACAATAAAGGGTTCGTTGGCCAGATTTTGCAATCACTCT TGCAGCCCCAATGCATATGTTAATAAATGGGTTGTTAAGGATAAGCTACGCATGGGAATA TTTGCTCAAAGAAAAATTTTAAAAGGTGAGGAAATCACTTTTGATTATAATGTGGATCGT TATGGTGCTCAAGCTCAGAAATGCTACTGTGAGGAGCCAAATTGTATTGGGTTTCTCGGT GGTAAGACTCAAACAGATGCGGCATCTTTATTGCCCCAGAACATCGCTGATGCCTTGGGA GTGACTGTTTCCATGGAGAAAAAATGGCTAAAGTTAAAGAAATTAAGCGGTGAGCCAATA ATAAAGAATGAAAACGAGAACATAAATATTGAATTTCTTCAATCATTGGAAGTCCAACCT ATCGACAGCCCAGTGGATGTGACGAAGATCATGAGTGTATTACTACAGCAAGATAATAAG ATAATTGCATCCAAACTCTTGAAGAGACTTTTTACTATCGATGATGACTCTCTTCGTCAT CAGGCTATCAAACTACACGGTTACACCTGTTTTAGCAAAATGCTTAAATTGTTTATCACG GAACAACCTCAGGTAGATGGAAAAGGAAACGAGACTGAAGAAGATGATATAAAGTTTATA AAGGGAATTTTAGATTTTTTGTTGGAATTACCAAAGACAACTCGAAACGGTATTGAGTCG TCACAAATTGATAATGTAGTAAAAACTCTCCCTGCAAAGTTTCCATTTTTAAAGCCAAAC TGCGATGAGTTATTGGAGAAATGGTCGAAATTTGAAACATATAAAAGGATAACGAAGAAA GACATAAACGTCGCAGCCAGCAAAATGATAGATTTGAGAAGGGTGAGATTACCTCCAGGC TGGGAGATCATTCACGAAAACGGTCGCCCATTGTATTATAATGCAGAACAGAAAACGAAA CTACACTATCCACCTTCGGGATCATCTAAGGTCTTTAGTTCAAGGTCAAATACACAAGTA AATTCTCCGAGTAGCAGTGGAATACCAAAAACGCCTGGCGCTTTAGACTCTAAGAAACAT AAGCTGAGTGACGAAGAATATGAGAGGAAGAAACAAAAAAGACTGGAATACGAAAGAATT GCGCTAGAAAGAGCCAAACAAGAAGAATTGGAAAGCCTGAAGCAAAAGCTAAAGCTTGAG AATGAAAGAAAAAGCGTTTTGGAGGATATTATAGCGGAGTTCAACAAACAGAAGGAGTTA CAAAAGGAAGAGTCCAAAAAACTAGTGGAAGCAAAAGAGGCTAAGCGGTTGAAAAGAAAA ACGGTCTCCCAGTCCCAAAGACTAGAGCACAACTGGAATAAATTCTTTGCATCTTTTGTA CCCAACTTAATAAAAAAAAACCCACAAAGTAAACAATTTGATCATGAAAACATTAAACAA TGTGCTAAAGACATCGTGAAAATCCTAACTACAAAGGAACTTAAAAAAGATTCTTCAAGA GCGCCGCCTGATGACTTAACCAAAGGAAAAAGGCATAAAGTTAAAGAATTCATAAATTCA TACATGGATAAGATTATCCTCAAGAAGAAGCAAAAAAAGGCGTTGGGATTATCATCAGCA TCAACAAGGATGTCTTCTCCTCCACCTTCAACATCATCATAA
Protein Properties
Pfam Domain Function
Protein Residues733
Protein Molecular Weight84538.79688
Protein Theoretical pI8.67
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Histone-lysine N-methyltransferase, H3 lysine-36 specific MSKNQSVSASEDEKEILNNNAEGHKPQRLFDQEPDLTEEALTKFENLDDCIYANKRIGTF KNNDFMECDCYEEFSDGVNHACDEDSDCINRLTLIECVNDLCSSCGNDCQNQRFQKKQYA PIAIFKTKHKGYGVRAEQDIEANQFIYEYKGEVIEEMEFRDRLIDYDQRHFKHFYFMMLQ NGEFIDATIKGSLARFCNHSCSPNAYVNKWVVKDKLRMGIFAQRKILKGEEITFDYNVDR YGAQAQKCYCEEPNCIGFLGGKTQTDAASLLPQNIADALGVTVSMEKKWLKLKKLSGEPI IKNENENINIEFLQSLEVQPIDSPVDVTKIMSVLLQQDNKIIASKLLKRLFTIDDDSLRH QAIKLHGYTCFSKMLKLFITEQPQVDGKGNETEEDDIKFIKGILDFLLELPKTTRNGIES SQIDNVVKTLPAKFPFLKPNCDELLEKWSKFETYKRITKKDINVAASKMIDLRRVRLPPG WEIIHENGRPLYYNAEQKTKLHYPPSGSSKVFSSRSNTQVNSPSSSGIPKTPGALDSKKH KLSDEEYERKKQKRLEYERIALERAKQEELESLKQKLKLENERKSVLEDIIAEFNKQKEL QKEESKKLVEAKEAKRLKRKTVSQSQRLEHNWNKFFASFVPNLIKKNPQSKQFDHENIKQ CAKDIVKILTTKELKKDSSRAPPDDLTKGKRHKVKEFINSYMDKIILKKKQKKALGLSSA STRMSSPPPSTSS
References
External Links
ResourceLink
Saccharomyces Genome Database SET2
Uniprot IDP46995
Uniprot NameSET2_YEAST
GenBank Gene IDZ49444
Genebank Protein ID1008361
General Reference
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Li, J., Moazed, D., Gygi, S. P. (2002). "Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation." J Biol Chem 277:49383-49388.12381723
  • Strahl, B. D., Grant, P. A., Briggs, S. D., Sun, Z. W., Bone, J. R., Caldwell, J. A., Mollah, S., Cook, R. G., Shabanowitz, J., Hunt, D. F., Allis, C. D. (2002). "Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression." Mol Cell Biol 22:1298-1306.11839797
  • Xiao, T., Hall, H., Kizer, K. O., Shibata, Y., Hall, M. C., Borchers, C. H., Strahl, B. D. (2003). "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast." Genes Dev 17:654-663.12629047
  • Li, B., Howe, L., Anderson, S., Yates, J. R. 3rd, Workman, J. L. (2003). "The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II." J Biol Chem 278:8897-8903.12511561
  • Krogan, N. J., Kim, M., Tong, A., Golshani, A., Cagney, G., Canadien, V., Richards, D. P., Beattie, B. K., Emili, A., Boone, C., Shilatifard, A., Buratowski, S., Greenblatt, J. (2003). "Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II." Mol Cell Biol 23:4207-4218.12773564
  • Landry, J., Sutton, A., Hesman, T., Min, J., Xu, R. M., Johnston, M., Sternglanz, R. (2003). "Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae." Mol Cell Biol 23:5972-5978.12917322
  • Schaft, D., Roguev, A., Kotovic, K. M., Shevchenko, A., Sarov, M., Shevchenko, A., Neugebauer, K. M., Stewart, A. F. (2003). "The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation." Nucleic Acids Res 31:2475-2482.12736296
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Kizer, K. O., Phatnani, H. P., Shibata, Y., Hall, H., Greenleaf, A. L., Strahl, B. D. (2005). "A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation." Mol Cell Biol 25:3305-3316.15798214
  • Rao, B., Shibata, Y., Strahl, B. D., Lieb, J. D. (2005). "Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide." Mol Cell Biol 25:9447-9459.16227595
  • Tripic, T., Edmondson, D. G., Davie, J. K., Strahl, B. D., Dent, S. Y. (2006). "The Set2 methyltransferase associates with Ssn6 yet Tup1-Ssn6 repression is independent of histone methylation." Biochem Biophys Res Commun 339:905-914.16329992
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Macias, M. J., Gervais, V., Civera, C., Oschkinat, H. (2000). "Structural analysis of WW domains and design of a WW prototype." Nat Struct Biol 7:375-379.10802733
  • Vojnic, E., Simon, B., Strahl, B. D., Sattler, M., Cramer, P. (2006). "Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription." J Biol Chem 281:13-15.16286474