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

Q9Y7R4 (SET1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Set1 complex component set1
Short name=Set1C component set1
Spset1
Gene names
Name:set1
Synonyms:kmt2
ORF Names:SPCC306.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length920 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of the Set1 complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3. Methylation promotes maintenance of active chromatin states at euchromatic chromosomal domains and is present throughout the cell cycle. Plays a role in telomere maintenance and DNA repair in an ATM kinase rad3-dependent pathway. Required for efficient telomeric and centromeric silencing. Ref.2 Ref.3 Ref.4

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.4

Subunit structure

Component of the Set1 complex composed of ash2, sdc1, set1, shg1, spp1, swd1, swd2 and swd3. Ref.3 Ref.5

Subcellular location

Nucleus Probable. Chromosome Probable.

Domain

A construct containing set1 C-terminal fragment of 692-920 is able to form H3K4me. Ref.4

Sequence similarities

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

Contains 1 post-SET domain.

Contains 1 RRM (RNA recognition motif) domain.

Contains 1 SET domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

lid2Q9HDV42EBI-2106005,EBI-2105919

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 920920Histone-lysine N-methyltransferase, H3 lysine-4 specific
PRO_0000186085

Regions

Domain94 – 17986RRM
Domain781 – 898118SET
Domain904 – 92017Post-SET
Compositional bias469 – 4746Poly-Arg

Sequences

Sequence LengthMass (Da)Tools
Q9Y7R4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: C4AD7E6C3ECFF8BC

FASTA920105,038
        10         20         30         40         50         60 
MDFNTSTRSK SQPVQRNNYK VLYDPELGIK ENLGRKIIYR FNGVSKPPLV VRDPRLKNPI 

        70         80         90        100        110        120 
YARGIPKSGR PFLKSLQTIN YDYNENSLGP EPPTQVFVSN ISPLVTSEQL RYHFKSFGEV 

       130        140        150        160        170        180 
FDLDLKLNPY TGTSLGLCCI SFDKRSSISV AAHSAKIAVQ QANGLRFSGK PLSVVLDRDG 

       190        200        210        220        230        240 
SLCEEAFKKA LNAVEKQFQE ETLQKQRFER EDESSRQKLS AAMNEDIPPW RQPSKNSQTL 

       250        260        270        280        290        300 
SNGDLQHSKV QNVDQKSGFL TSSETDVPKN INDYIYLLID DRFVPPDRVY YTDIKHHFRK 

       310        320        330        340        350        360 
FLYEKIYMNK DGFYITFNNY REASNCYRAL DRTYVQNCRI KLKFHDIPSR TKEDGKKSAV 

       370        380        390        400        410        420 
RRVVLPPEEA YAEATSVVLR DLEAALLRDV KSKIIGPAIF KYLHSMPKPS VKEELQENLL 

       430        440        450        460        470        480 
VSSTSVPDVP LKIESTVGKL PSLPKFKKRV DSSKMNLSAG SKTKSKLQRR RRRRHEARPL 

       490        500        510        520        530        540 
HYQLNQMYNS SASEAESDQE LLLSSGDERV ERGKIGSIKS VKSDEATPVF SDTSDENDKF 

       550        560        570        580        590        600 
HRFRTKSKIS KKKYEKMEVD YTSSSETESD ASILSPSAAI PKSGSAIKDE LISPKKEIDE 

       610        620        630        640        650        660 
VLALAPKWRI NEFDETGSVY YGALPYNYPE DDVLLDLDGL QYLVKNDEDY SYLQEALKDE 

       670        680        690        700        710        720 
PLMDINDPNF WAYERKSCKF KNGDVKYGDT AILPEPKGYF RSNTSGSAKS EGYYIIPTTE 

       730        740        750        760        770        780 
KSLYLPLRNR STIDTISHST SRITSRMNRV NNRRLAAGVE KSQLPAEADL LRFNALKARK 

       790        800        810        820        830        840 
KQLHFGPSRI HTLGLFAMEN IDKNDMVIEY IGEIIRQRVA DNREKNYVRE GIGDSYLFRI 

       850        860        870        880        890        900 
DEDVIVDATK KGNIARFINH SCAPNCIARI IRVEGKRKIV IYADRDIMHG EELTYDYKFP 

       910        920 
EEADKIPCLC GAPTCRGYLN 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast."
Noma K., Grewal S.I.S.
Proc. Natl. Acad. Sci. U.S.A. 99:16438-16445(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation in budding and fission yeasts."
Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A., Stewart A.F.
J. Biol. Chem. 278:8487-8493(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX.
[4]"The fission yeast spSet1p is a histone H3-K4 methyltransferase that functions in telomere maintenance and DNA repair in an ATM kinase Rad3-dependent pathway."
Kanoh J., Francesconi S., Collura A., Schramke V., Ishikawa F., Baldacci G., Geli V.
J. Mol. Biol. 326:1081-1094(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]"A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe."
Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F., Shevchenko A.
Mol. Cell. Proteomics 3:125-132(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAB41652.1.
PIRT41282.
RefSeqNP_587812.1. NM_001022805.2.

3D structure databases

ProteinModelPortalQ9Y7R4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275345. 358 interactions.
IntActQ9Y7R4. 1 interaction.
MINTMINT-4718299.
STRING4896.SPCC306.04c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC306.04c.1; SPCC306.04c.1:pep; SPCC306.04c.
GeneID2538762.
KEGGspo:SPCC306.04c.

Organism-specific databases

PomBaseSPCC306.04c.

Phylogenomic databases

eggNOGCOG2940.
KOK11422.
OMACGAPGCK.
OrthoDBEOG7P8PH3.
PhylomeDBQ9Y7R4.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR024657. COMPASS_Set1_N-SET.
IPR017111. Hist_H3-K4_MeTrfase_1_fun.
IPR015722. Histone-lysine_MeTfrase.
IPR012677. Nucleotide-bd_a/b_plait.
IPR003616. Post-SET_dom.
IPR000504. RRM_dom.
IPR024636. SET_assoc.
IPR001214. SET_dom.
[Graphical view]
PANTHERPTHR22884:SF10. PTHR22884:SF10. 1 hit.
PfamPF11764. N-SET. 1 hit.
PF00076. RRM_1. 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.
SM00360. RRM. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50868. POST_SET. 1 hit.
PS50102. RRM. 1 hit.
PS51572. SAM_MT43_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20799946.
PROQ9Y7R4.

Entry information

Entry nameSET1_SCHPO
AccessionPrimary (citable) accession number: Q9Y7R4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names