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P46995

- SET2_YEAST

UniProt

P46995 - SET2_YEAST

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Protein

Histone-lysine N-methyltransferase, H3 lysine-36 specific

Gene

SET2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Histone 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.7 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

GO - Molecular functioni

  1. histone methyltransferase activity Source: SGD
  2. histone methyltransferase activity (H3-K36 specific) Source: SGD

GO - Biological processi

  1. ascospore formation Source: SGD
  2. DNA-templated transcription, elongation Source: SGD
  3. DNA-templated transcription, termination Source: SGD
  4. histone deacetylation Source: SGD
  5. histone methylation Source: SGD
  6. negative regulation of antisense RNA transcription Source: SGD
  7. negative regulation of histone H3-K14 acetylation Source: SGD
  8. negative regulation of histone H3-K9 acetylation Source: SGD
  9. negative regulation of reciprocal meiotic recombination Source: SGD
  10. positive regulation of histone acetylation Source: SGD
  11. regulation of DNA-dependent DNA replication initiation Source: SGD
  12. regulation of histone exchange Source: SGD
  13. regulation of transcription, DNA-templated Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-31606-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC:2.1.1.43)
Alternative name(s):
Lysine N-methyltransferase 3
SET domain-containing protein 2
Gene namesi
Name:SET2
Synonyms:EZL1, KMT3
Ordered Locus Names:YJL168C
ORF Names:J0520
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJL168c.
SGDiS000003704. SET2.

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. cytosol Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951R → G: Reduces dramatically histone methyltransferase activity toward nucleosomes. 1 Publication
Mutagenesisi201 – 2011C → A: Reduces dramatically histone methyltransferase activity toward nucleosomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Histone-lysine N-methyltransferase, H3 lysine-36 specificPRO_0000186087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei522 – 5221Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46995.
PaxDbiP46995.
PeptideAtlasiP46995.

Expressioni

Gene expression databases

GenevestigatoriP46995.

Interactioni

Subunit structurei

Interacts with the RNA polymerase II hyperphosphorylated CTD. Interacts with CYC8.7 Publications

Protein-protein interaction databases

BioGridi33591. 392 interactions.
DIPiDIP-2150N.
IntActiP46995. 62 interactions.
MINTiMINT-500810.
STRINGi4932.YJL168C.

Structurei

Secondary structure

1
733
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi481 – 49414Combined sources
Turni495 – 4984Combined sources
Beta strandi499 – 5035Combined sources
Helixi624 – 64522Combined sources
Turni648 – 6525Combined sources
Helixi655 – 67622Combined sources
Helixi688 – 71225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0NNMR-A479-505[»]
2C5ZNMR-A620-719[»]
ProteinModelPortaliP46995.
SMRiP46995. Positions 23-261, 479-505, 622-703.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46995.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 11856AWSPROSITE-ProRule annotationAdd
BLAST
Domaini120 – 237118SETPROSITE-ProRule annotationAdd
BLAST
Domaini244 – 26017Post-SETPROSITE-ProRule annotationAdd
BLAST
Domaini475 – 50733WWAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni619 – 718100Binding to RNA polymerase II CTDAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili548 – 63083Sequence AnalysisAdd
BLAST

Domaini

The AWS and SET domains are necessary for transcription repression.2 Publications

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.PROSITE-ProRule annotation
Contains 1 AWS domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation
Contains 1 WW domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000118855.
HOGENOMiHOG000248214.
InParanoidiP46995.
KOiK11423.
OMAiSCNPNAY.
OrthoDBiEOG7P8PH3.

Family and domain databases

InterProiIPR006560. AWS_dom.
IPR025788. Hist-Lys_N-MeTrfase_SET2_fun.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
[Graphical view]
SMARTiSM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS51568. SAM_MT43_SET2_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46995-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKNQSVSAS EDEKEILNNN AEGHKPQRLF DQEPDLTEEA LTKFENLDDC
60 70 80 90 100
IYANKRIGTF KNNDFMECDC YEEFSDGVNH ACDEDSDCIN RLTLIECVND
110 120 130 140 150
LCSSCGNDCQ NQRFQKKQYA PIAIFKTKHK GYGVRAEQDI EANQFIYEYK
160 170 180 190 200
GEVIEEMEFR DRLIDYDQRH FKHFYFMMLQ NGEFIDATIK GSLARFCNHS
210 220 230 240 250
CSPNAYVNKW VVKDKLRMGI FAQRKILKGE EITFDYNVDR YGAQAQKCYC
260 270 280 290 300
EEPNCIGFLG GKTQTDAASL LPQNIADALG VTVSMEKKWL KLKKLSGEPI
310 320 330 340 350
IKNENENINI EFLQSLEVQP IDSPVDVTKI MSVLLQQDNK IIASKLLKRL
360 370 380 390 400
FTIDDDSLRH QAIKLHGYTC FSKMLKLFIT EQPQVDGKGN ETEEDDIKFI
410 420 430 440 450
KGILDFLLEL PKTTRNGIES SQIDNVVKTL PAKFPFLKPN CDELLEKWSK
460 470 480 490 500
FETYKRITKK DINVAASKMI DLRRVRLPPG WEIIHENGRP LYYNAEQKTK
510 520 530 540 550
LHYPPSGSSK VFSSRSNTQV NSPSSSGIPK TPGALDSKKH KLSDEEYERK
560 570 580 590 600
KQKRLEYERI ALERAKQEEL ESLKQKLKLE NERKSVLEDI IAEANKQKEL
610 620 630 640 650
QKEEAKKLVE AKEAKRLKRK TVSQSQRLEH NWNKFFASFV PNLIKKNPQS
660 670 680 690 700
KQFDHENIKQ CAKDIVKILT TKELKKDSSR APPDDLTKGK RHKVKEFINS
710 720 730
YMDKIILKKK QKKALALSSA STRMSSPPPS TSS
Length:733
Mass (Da):84,461
Last modified:September 21, 2011 - v2
Checksum:i05436B181E88EFF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti594 – 5941A → F in CAA89464. (PubMed:8641269)Curated
Sequence conflicti605 – 6051A → S in CAA89464. (PubMed:8641269)Curated
Sequence conflicti716 – 7161A → G in CAA89464. (PubMed:8641269)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49444 Genomic DNA. Translation: CAA89464.1.
BK006943 Genomic DNA. Translation: DAA08635.2.
PIRiS56951.
RefSeqiNP_012367.2. NM_001181601.2.

Genome annotation databases

EnsemblFungiiYJL168C; YJL168C; YJL168C.
GeneIDi853271.
KEGGisce:YJL168C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49444 Genomic DNA. Translation: CAA89464.1 .
BK006943 Genomic DNA. Translation: DAA08635.2 .
PIRi S56951.
RefSeqi NP_012367.2. NM_001181601.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E0N NMR - A 479-505 [» ]
2C5Z NMR - A 620-719 [» ]
ProteinModelPortali P46995.
SMRi P46995. Positions 23-261, 479-505, 622-703.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33591. 392 interactions.
DIPi DIP-2150N.
IntActi P46995. 62 interactions.
MINTi MINT-500810.
STRINGi 4932.YJL168C.

Proteomic databases

MaxQBi P46995.
PaxDbi P46995.
PeptideAtlasi P46995.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJL168C ; YJL168C ; YJL168C .
GeneIDi 853271.
KEGGi sce:YJL168C.

Organism-specific databases

CYGDi YJL168c.
SGDi S000003704. SET2.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000118855.
HOGENOMi HOG000248214.
InParanoidi P46995.
KOi K11423.
OMAi SCNPNAY.
OrthoDBi EOG7P8PH3.

Enzyme and pathway databases

BioCyci YEAST:G3O-31606-MONOMER.

Miscellaneous databases

EvolutionaryTracei P46995.
NextBioi 973544.

Gene expression databases

Genevestigatori P46995.

Family and domain databases

InterProi IPR006560. AWS_dom.
IPR025788. Hist-Lys_N-MeTrfase_SET2_fun.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
[Graphical view ]
SMARTi SM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS51568. SAM_MT43_SET2_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    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., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 594; 605 AND 716.
    Strain: ATCC 204508 / S288c.
  3. "Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation."
    Li J., Moazed D., Gygi S.P.
    J. Biol. Chem. 277:49383-49388(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBP1 AND RBP2.
  4. "Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression."
    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.
    Mol. Cell. Biol. 22:1298-1306(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-195 AND CYS-201.
  5. "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast."
    Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H., Strahl B.D.
    Genes Dev. 17:654-663(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNA POLYMERASE II, FUNCTION.
  6. "The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II."
    Li B., Howe L., Anderson S., Yates J.R. III, Workman J.L.
    J. Biol. Chem. 278:8897-8903(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNA POLYMERASE II.
  7. "Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II."
    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.
    Mol. Cell. Biol. 23:4207-4218(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNA POLYMERASE II.
  8. "Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae."
    Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M., Sternglanz R.
    Mol. Cell. Biol. 23:5972-5978(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAINS.
  9. "The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation."
    Schaft D., Roguev A., Kotovic K.M., Shevchenko A., Sarov M., Shevchenko A., Neugebauer K.M., Stewart A.F.
    Nucleic Acids Res. 31:2475-2482(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNA POLYMERASE II.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation."
    Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L., Strahl B.D.
    Mol. Cell. Biol. 25:3305-3316(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH RNA POLYMERASE II CTD.
  12. "Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide."
    Rao B., Shibata Y., Strahl B.D., Lieb J.D.
    Mol. Cell. Biol. 25:9447-9459(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The Set2 methyltransferase associates with Ssn6 yet Tup1-Ssn6 repression is independent of histone methylation."
    Tripic T., Edmondson D.G., Davie J.K., Strahl B.D., Dent S.Y.R.
    Biochem. Biophys. Res. Commun. 339:905-914(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CYC8.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Structural analysis of WW domains and design of a WW prototype."
    Macias M.J., Gervais V., Civera C., Oschkinat H.
    Nat. Struct. Biol. 7:375-379(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 7-33.
  17. "Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription."
    Vojnic E., Simon B., Strahl B.D., Sattler M., Cramer P.
    J. Biol. Chem. 281:13-15(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 619-718.

Entry informationi

Entry nameiSET2_YEAST
AccessioniPrimary (citable) accession number: P46995
Secondary accession number(s): D6VW19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 21, 2011
Last modified: November 26, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 217 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3