Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P38827 (SET1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase, H3 lysine-4 specific

EC=2.1.1.43
Alternative name(s):
COMPASS component SET1
Lysine N-methyltransferase 2
SET domain-containing protein 1
Gene names
Name:SET1
Synonyms:KMT2, YTX1
Ordered Locus Names:YHR119W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1080 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.9

Subunit structure

Component of the COMPASS (Set1C) complex which consists of SET12, BRE22, SPP12, SDC11, SHG11, SWD11, SWD21, and SWD31. Interacts with MEC3. Ref.4 Ref.5 Ref.7 Ref.11

Subcellular location

Nucleus Probable. Chromosome Probable.

Miscellaneous

Present with 172 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

Contains 1 post-SET domain.

Contains 1 SET domain.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processascospore formation

Inferred from mutant phenotype PubMed 17150765. Source: SGD

chromatin silencing at rDNA

Traceable author statement PubMed 15340082. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype Ref.3. Source: SGD

chromatin silencing at telomere

Inferred from mutant phenotype Ref.11Ref.9Ref.3Ref.4. Source: SGD

histone H3-K4 methylation

Inferred from direct assay Ref.5Ref.11Ref.9. Source: SGD

peptidyl-lysine dimethylation

Inferred from mutant phenotype PubMed 16143104. Source: SGD

positive regulation of histone acetylation

Inferred from genetic interaction PubMed 19822662. Source: SGD

regulation of transcription from RNA polymerase II promoter in response to stress

Inferred from mutant phenotype PubMed 16959218. Source: SGD

telomere maintenance

Inferred from mutant phenotype Ref.5Ref.3. Source: SGD

   Cellular_componentSet1C/COMPASS complex

Inferred from physical interaction Ref.7Ref.5Ref.11. Source: SGD

chromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from direct assay PubMed 16787775. Source: SGD

histone methyltransferase activity

Inferred from sequence or structural similarity Ref.15. Source: SGD

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.5PubMed 16429126PubMed 18083099PubMed 19713935PubMed 21179020Ref.4. Source: IntAct

protein-lysine N-methyltransferase activity

Inferred from mutant phenotype PubMed 16143104. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10801080Histone-lysine N-methyltransferase, H3 lysine-4 specific
PRO_0000186086

Regions

Domain938 – 1055118SET
Domain1064 – 108017Post-SET

Amino acid modifications

Modified residue6251Phosphoserine Ref.17 Ref.18
Modified residue8751Phosphothreonine Ref.18

Secondary structure

.................... 1080
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38827 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B7FA5D60F71063FD

FASTA1,080123,912
        10         20         30         40         50         60 
MSNYYRRAHA SSGSYRQPQE QPQYSRSGHY QYSNGHSHQQ YSSQYNQRRR YNHNDGTRRR 

        70         80         90        100        110        120 
YNDDRPHSSN NASTRQYYAT NNSQSGPYVN KKSDISSRRG MSQSRYSNSN VHNTLASSSG 

       130        140        150        160        170        180 
SLPTESALLL QQRPPSVLRY NTDNLKSKFH YFDPIKGEFF NKDKMLSWKA TDKEFSETGY 

       190        200        210        220        230        240 
YVVKELQDGQ FKFKIKHRHP EIKASDPRNE NGIMTSGKVA THRKCRNSLI LLPRISYDRY 

       250        260        270        280        290        300 
SLGPPPSCEI VVYPAQDSTT TNIQDISIKN YFKKYGEISH FEAFNDPNSA LPLHVYLIKY 

       310        320        330        340        350        360 
ASSDGKINDA AKAAFSAVRK HESSGCFIMG FKFEVILNKH SILNNIISKF VEINVKKLQK 

       370        380        390        400        410        420 
LQENLKKAKE KEAENEKAKE LQGKDITLPK EPKVDTLSHS SGSEKRIPYD LLGVVNNRPV 

       430        440        450        460        470        480 
LHVSKIFVAK HRFCVEDFKY KLRGYRCAKF IDHPTGIYII FNDIAHAQTC SNAESGNLTI 

       490        500        510        520        530        540 
MSRSRRIPIL IKFHLILPRF QNRTRFNKSS SSSNSTNVPI KYESKEEFIE ATAKQILKDL 

       550        560        570        580        590        600 
EKTLHVDIKK RLIGPTVFDA LDHANFPELL AKRELKEKEK RQQIASKIAE DELKRKEEAK 

       610        620        630        640        650        660 
RDFDLFGLYG GYAKSNKRNL KRHNSLALDH TSLKRKKLSN GIKPMAHLLN EETDSKETTP 

       670        680        690        700        710        720 
LNDEGITRVS KEHDEEDENM TSSSSEEEEE EAPDKKFKSE SEPTTPESDH LHGIKPLVPD 

       730        740        750        760        770        780 
QNGSSDVLDA SSMYKPTATE IPEPVYPPEE YDLKYSQTLS SMDLQNAIKD EEDMLILKQL 

       790        800        810        820        830        840 
LSTYTPTVTP ETSAALEYKI WQSRRKVLEE EKASDWQIEL NGTLFDSELQ PGSSFKAEGF 

       850        860        870        880        890        900 
RKIADKLKIN YLPHRRRVHQ PLNTVNIHNE RNEYTPELCQ REESSNKEPS DSVPQEVSSS 

       910        920        930        940        950        960 
RDNRASNRRF QQDIEAQKAA IGTESELLSL NQLNKRKKPV MFARSAIHNW GLYALDSIAA 

       970        980        990       1000       1010       1020 
KEMIIEYVGE RIRQPVAEMR EKRYLKNGIG SSYLFRVDEN TVIDATKKGG IARFINHCCD 

      1030       1040       1050       1060       1070       1080 
PNCTAKIIKV GGRRRIVIYA LRDIAASEEL TYDYKFEREK DDEERLPCLC GAPNCKGFLN 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"SET1, a yeast member of the Trithorax family, functions in transcriptional silencing and diverse cellular processes."
Nislow C., Ray E., Pillus L.
Mol. Biol. Cell 8:2421-2436(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Interaction between Set1p and checkpoint protein Mec3p in DNA repair and telomere functions."
Corda Y., Schramke V., Longhese M.P., Smokvina T., Paciotti V., Brevet V., Gilson E., Geli V.
Nat. Genet. 21:204-208(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEC3.
[5]"The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4."
Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M., Aasland R., Stewart A.F.
EMBO J. 20:7137-7148(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET1 COMPLEX, FUNCTION OF THE SET1 COMPLEX.
[6]"Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae."
Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y.R., Winston F., Allis C.D.
Genes Dev. 15:3286-3295(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"COMPASS: a complex of proteins associated with a trithorax-related SET domain protein."
Miller T., Krogan N.J., Dover J., Erdjument-Bromage H., Tempst P., Johnston M., Greenblatt J.F., Shilatifard A.
Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism."
Bryk M., Briggs S.D., Strahl B.D., Curcio M.J., Allis C.D., Winston F.
Curr. Biol. 12:165-170(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression."
Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J., Johnston M., Shilatifard A.
J. Biol. Chem. 277:10753-10755(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, FUNCTION.
[10]"Active genes are tri-methylated at K4 of histone H3."
Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J., Bernstein B.E., Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.
Nature 419:407-411(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3."
Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.
Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET1 COMPLEX, FUNCTION OF THE SET1 COMPLEX.
[12]"Methylation of histone H3 Lys 4 in coding regions of active genes."
Bernstein B.E., Humphrey E.L., Erlich R.L., Schneider R., Bouman P., Liu J.S., Kouzarides T., Schreiber S.L.
Proc. Natl. Acad. Sci. U.S.A. 99:8695-8700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Methylation of histone H3 K4 mediates association of the Isw1p ATPase with chromatin."
Santos-Rosa H., Schneider R., Bernstein B.E., Karabetsou N., Morillon A., Weise C., Schreiber S.L., Mellor J., Kouzarides T.
Mol. Cell 12:1325-1332(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]"Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression."
Boa S., Coert C., Patterton H.-G.
Yeast 20:827-835(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription."
Morillon A., Karabetsou N., Nair A., Mellor J.
Mol. Cell 18:723-734(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE COMPASS COMPLEX.
[17]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[18]"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-625 AND THR-875, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00059 Genomic DNA. Translation: AAB68867.1.
BK006934 Genomic DNA. Translation: DAA06813.1.
PIRS48961.
RefSeqNP_011987.1. NM_001179249.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J8AX-ray3.00A247-375[»]
ProteinModelPortalP38827.
SMRP38827. Positions 247-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36552. 132 interactions.
DIPDIP-4616N.
IntActP38827. 30 interactions.
MINTMINT-552558.
STRING4932.YHR119W.

Proteomic databases

MaxQBP38827.
PaxDbP38827.
PRIDEP38827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR119W; YHR119W; YHR119W.
GeneID856519.
KEGGsce:YHR119W.

Organism-specific databases

CYGDYHR119w.
SGDS000001161. SET1.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00740000115089.
HOGENOMHOG000066111.
KOK11422.
OMAERLPCLC.
OrthoDBEOG7P8PH3.

Enzyme and pathway databases

BioCycYEAST:G3O-31161-MONOMER.

Gene expression databases

GenevestigatorP38827.

Family and domain databases

InterProIPR024657. COMPASS_Set1_N-SET.
IPR017111. Hist_H3-K4_MeTrfase_1_fun.
IPR003616. Post-SET_dom.
IPR024636. SET_assoc.
IPR001214. SET_dom.
[Graphical view]
PfamPF11764. N-SET. 1 hit.
PF00856. SET. 1 hit.
PF11767. SET_assoc. 1 hit.
[Graphical view]
PIRSFPIRSF037104. Histone_H3-K4_mtfrase_Set1_fun. 1 hit.
SMARTSM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50868. POST_SET. 1 hit.
PS51572. SAM_MT43_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38827.
NextBio982275.
PROP38827.

Entry information

Entry nameSET1_YEAST
AccessionPrimary (citable) accession number: P38827
Secondary accession number(s): D3DL69
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references