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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: 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

Miscellaneous

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

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone].PROSITE-ProRule annotation

GO - Molecular functioni

  • histone methyltransferase activity Source: SGD
  • histone methyltransferase activity (H3-K36 specific) Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • DNA-templated transcription, elongation Source: SGD
  • DNA-templated transcription, termination Source: SGD
  • histone deacetylation Source: SGD
  • histone methylation Source: SGD
  • negative regulation of antisense RNA transcription Source: SGD
  • negative regulation of histone H3-K14 acetylation Source: SGD
  • negative regulation of histone H3-K9 acetylation Source: SGD
  • negative regulation of reciprocal meiotic recombination Source: SGD
  • positive regulation of histone acetylation Source: SGD
  • regulation of DNA-dependent DNA replication initiation Source: SGD
  • regulation of histone exchange Source: SGD
  • regulation of transcription, DNA-templated Source: SGD

Keywordsi

Molecular functionMethyltransferase, Repressor, Transferase
Biological processTranscription, Transcription regulation
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-31606-MONOMER.
ReactomeiR-SCE-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-SCE-3214841. PKMTs methylate histone lysines.
R-SCE-427359. SIRT1 negatively regulates rRNA Expression.
R-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL168C.
SGDiS000003704. SET2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi195R → G: Reduces dramatically histone methyltransferase activity toward nucleosomes. 1 Publication1
Mutagenesisi201C → A: Reduces dramatically histone methyltransferase activity toward nucleosomes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860871 – 733Histone-lysine N-methyltransferase, H3 lysine-36 specificAdd BLAST733

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineCombined sources1
Modified residuei522PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46995.
PRIDEiP46995.

PTM databases

iPTMnetiP46995.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
HHT2P618302EBI-16985,EBI-8098

Protein-protein interaction databases

BioGridi33591. 559 interactors.
DIPiDIP-2150N.
IntActiP46995. 62 interactors.
MINTiMINT-500810.
STRINGi4932.YJL168C.

Structurei

Secondary structure

1733
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi481 – 494Combined sources14
Turni495 – 498Combined sources4
Beta strandi499 – 503Combined sources5
Helixi624 – 645Combined sources22
Turni648 – 652Combined sources5
Helixi655 – 676Combined sources22
Helixi688 – 712Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E0NNMR-A479-505[»]
2C5ZNMR-A620-719[»]
ProteinModelPortaliP46995.
SMRiP46995.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46995.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 118AWSPROSITE-ProRule annotationAdd BLAST56
Domaini120 – 237SETPROSITE-ProRule annotationAdd BLAST118
Domaini244 – 260Post-SETPROSITE-ProRule annotationAdd BLAST17
Domaini475 – 507WWAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni619 – 718Binding to RNA polymerase II CTDAdd BLAST100

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili548 – 630Sequence analysisAdd BLAST83

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00780000121845.
HOGENOMiHOG000248214.
InParanoidiP46995.
KOiK11423.
OMAiYVDKWVV.
OrthoDBiEOG092C3T9B.

Family and domain databases

InterProiView protein in InterPro
IPR006560. AWS_dom.
IPR025788. Hist-Lys_N-MeTrfase_SET2_fun.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
IPR036020. WW_dom_sf.
PfamiView protein in Pfam
PF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
SMARTiView protein in SMART
SM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiView protein in PROSITE
PS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS51568. SAM_MT43_SET2_1. 1 hit.
PS50280. SET. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti594A → F in CAA89464 (PubMed:8641269).Curated1
Sequence conflicti605A → S in CAA89464 (PubMed:8641269).Curated1
Sequence conflicti716A → G in CAA89464 (PubMed:8641269).Curated1

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.

Similar proteinsi

Entry informationi

Entry nameiSET2_YEAST
AccessioniPrimary (citable) accession number: P46995
Secondary accession number(s): D6VW19
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 21, 2011
Last modified: October 25, 2017
This is version 170 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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