Q9Y7R4 (SET1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	920 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Contains 1 post-SET domain. Contains 1 RRM (RNA recognition motif) domain. Contains 1 SET domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from genetic interaction Ref.4. Source: PomBase DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin remodeling Inferred from sequence or structural similarity. Source: PomBase telomere maintenance Inferred from mutant phenotype Ref.4. Source: PomBase
Cellular_component	Set1C/COMPASS complex Inferred from direct assay Ref.3. Source: PomBase cytoplasm Inferred from direct assay PubMed 16823372. Source: PomBase nuclear chromatin Non-traceable author statement. Source: PomBase
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone methyltransferase activity (H3-K4 specific) Traceable author statement Ref.2. Source: PomBase nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
lid2	Q9HDV4	2	EBI-2106005,EBI-2105919

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 920	920	Histone-lysine N-methyltransferase, H3 lysine-4 specific		PRO_0000186085
Regions
	Domain	94 – 179	86	RRM
	Domain	780 – 902	123	SET
	Domain	904 – 920	17	Post-SET
	Compositional bias	469 – 474	6	Poly-Arg

Sequences

	Sequence		Length	Mass (Da)
	Q9Y7R4 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C4AD7E6C3ECFF8BC	FASTA	920	105,038
	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

References

	« Hide 'large scale' referencesShow '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. , 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 AND COMPOSITION OF 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: COMPOSITION OF THE SET1 COMPLEX.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAB41652.1.
PIR	T41282.
RefSeq	NP_587812.1. NM_001022805.2.
3D structure databases
ProteinModelPortal	Q9Y7R4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y7R4. 1 interaction.
STRING	4896.SPCC306.04c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC306.04c.1; SPCC306.04c.1:pep; SPCC306.04c.
GeneID	2538762.
KEGG	spo:SPCC306.04c.
Organism-specific databases
PomBase	SPCC306.04c.
Phylogenomic databases
eggNOG	COG2940.
KO	K11422.
OMA	TIDTISH.
OrthoDB	EOG4ZW8K8.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR024657. 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]
PANTHER	PTHR22884:SF10. PTHR22884:SF10. 1 hit.
Pfam	PF11764. N-SET. 1 hit. PF00076. RRM_1. 1 hit. PF00856. SET. 1 hit. PF11767. SET_assoc. 1 hit. [Graphical view]
PIRSF	PIRSF037104. Histone_H3-K4_mtfrase_Set1_fun. 1 hit.
SMART	SM00508. PostSET. 1 hit. SM00360. RRM. 1 hit. SM00317. SET. 1 hit. [Graphical view]
PROSITE	PS50868. POST_SET. 1 hit. PS50102. RRM. 1 hit. PS50280. SET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20799946.

Entry information

Entry name

SET1_SCHPO

Accession

Primary (citable) accession number: Q9Y7R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program