P31380 (FUN30_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent helicase FUN30
EC=3.6.4.12

Gene names

Name:	FUN30
Ordered Locus Names:	YAL019W
ORF Names:	YAL001

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1131 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Homodimer. Ref.11
Subcellular location	Nucleus. Chromosome. Note: Recruited to double-strand breaks (DSBs) sites of DNA damage. Ref.12 Ref.13
Disruption phenotype	Impaired ability to repair double-strand breaks (DSBs). Ref.13
Miscellaneous	Present with 6800 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Caution	Was initially reported to contain a CUE domain (Ref.10). However, no CUE domain is predicted by prediction tools and the CUE-like region does not show no affinity for ubiquitinated histones (Ref.11).

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from mutant phenotype Ref.11. Source: SGD DNA double-strand break processing Inferred from mutant phenotype Ref.13Ref.14. Source: SGD chromatin silencing at rDNA Inferred from mutant phenotype Ref.10. Source: SGD chromatin silencing at silent mating-type cassette Inferred from mutant phenotype Ref.10. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype Ref.10. Source: SGD heterochromatin assembly involved in chromatin silencing Inferred from mutant phenotype PubMed 21388962. Source: SGD heterochromatin maintenance involved in chromatin silencing Inferred from mutant phenotype PubMed 21388962. Source: SGD
Cellular_component	chromosome, centromeric region Inferred from direct assay Ref.15. Source: SGD mating-type region heterochromatin Inferred from physical interaction Ref.10. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD nucleus Inferred from direct assay PubMed 14562095PubMed 22842922. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay Ref.11. Source: SGD DNA-dependent ATPase activity Inferred from direct assay Ref.11. Source: SGD chromatin binding Inferred from direct assay Ref.11. Source: SGD helicase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1131	1131	ATP-dependent helicase FUN30		PRO_0000074384
Regions
	Domain	584 – 752	169	Helicase ATP-binding
	Domain	953 – 1108	156	Helicase C-terminal
	Nucleotide binding	597 – 604	8	ATP Probable
	Region	76 – 111	36	CUE-like region
	Motif	703 – 706	4	DEGH box
Amino acid modifications
	Modified residue	26	1	Phosphoserine Ref.8 Ref.9
	Modified residue	27	1	Phosphoserine Ref.9
	Modified residue	28	1	Phosphoserine Ref.7 Ref.8 Ref.9
	Modified residue	33	1	Phosphothreonine Ref.9
	Modified residue	34	1	Phosphoserine Ref.7 Ref.9
	Modified residue	88	1	Phosphothreonine Ref.9
	Modified residue	96	1	Phosphoserine Ref.9
	Modified residue	98	1	Phosphoserine Ref.9
	Modified residue	131	1	Phosphothreonine Ref.9
	Modified residue	226	1	Phosphoserine Ref.9
	Modified residue	232	1	Phosphoserine Ref.9
	Modified residue	369	1	Phosphoserine Ref.9
	Modified residue	383	1	Phosphoserine Ref.9
	Modified residue	451	1	Phosphoserine Ref.7 Ref.9
Experimental info
	Mutagenesis	603	1	K → R: Abolishes both the silencing function and the ability to promote DNA end resection of double-strand breaks (DSBs). Ref.14

Sequences

	Sequence		Length	Mass (Da)
	P31380 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 7E61B9ABB3A42ED2	FASTA	1,131	128,507
	10 20 30 40 50 60 MSGSHSNDED DVVQVPETSS PTKVASSSPL KPTSPTVPDA SVASLRSRFT FKPSDPSEGA 70 80 90 100 110 120 HTSKPLPSGS PEVALVNLAR EFPDFSQTLV QAVFKSNSFN LQSARERLTR LRQQRQNWTW 130 140 150 160 170 180 NKNASPKKSE TPPPVKKSLP LANTGRLSSI HGNINNKSSK ITVAKQKTSI FDRYSNVINQ 190 200 210 220 230 240 KQYTFELPTN LNIDSEALSK LPVNYNKKRR LVRADQHPIG KSYESSATQL GSAREKLLAN 250 260 270 280 290 300 RKYGRHANDN DEEEEESMMT DDDDASGDDY TESTPQINLD EQVLQFINDS DIVDLSDLSD 310 320 330 340 350 360 TTMHKAQLIA SHRPYSSLNA FVNTNFNDKD TEENASNKRK RRAAASANES ERLLDKITQS 370 380 390 400 410 420 IRGYNAIESV IKKCSSYGDL VTSQMKKWGV QVEGDNSELD LMNLGEDDDD DNDDGNNDNN 430 440 450 460 470 480 NSNNNNTAGA DATSKEKEDT KAVVEGFDET SAEPTPAPAP APVERETKRI RNTTKPKVVE 490 500 510 520 530 540 DEDDDVDLEA IDDELPQSEH EDDDYEEEDE DYNDEEEDVE YDDGDDDDDD DDEFVATRKN 550 560 570 580 590 600 THVISTTSRN GRKPIVKFFK GKPRLLSPEI SLKDYQQTGI NWLNLLYQNK MSCILADDMG 610 620 630 640 650 660 LGKTCQVISF FAYLKQINEP GPHLVVVPSS TLENWLREFQ KFAPALKIEP YYGSLQEREE 670 680 690 700 710 720 LRDILERNAG KYDVIVTTYN LAAGNKYDVS FLKNRNFNVV VYDEGHMLKN STSERFAKLM 730 740 750 760 770 780 KIRANFRLLL TGTPLQNNLK ELMSLLEFIM PNLFISKKES FDAIFKQRAK TTDDNKNHNP 790 800 810 820 830 840 LLAQEAITRA KTMMKPFILR RRKDQVLKHL PPKHTHIQYC ELNAIQKKIY DKEIQIVLEH 850 860 870 880 890 900 KRMIKDGELP KDAKEKSKLQ SSSSKNLIMA LRKASLHPLL FRNIYNDKII TKMSDAILDE 910 920 930 940 950 960 PAYAENGNKE YIKEDMSYMT DFELHKLCCN FPNTLSKYQL HNDEWMQSGK IDALKKLLKT 970 980 990 1000 1010 1020 IIVDKQEKVL IFSLFTQVLD ILEMVLSTLD YKFLRLDGST QVNDRQLLID KFYEDKDIPI 1030 1040 1050 1060 1070 1080 FILSTKAGGF GINLVCANNV IIFDQSFNPH DDRQAADRAH RVGQTKEVNI TTLITKDSIE 1090 1100 1110 1120 1130 EKIHQLAKNK LALDSYISED KKSQDVLESK VSDMLEDIIY DENSKPKGTK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a Saccharomyces cerevisiae homolog of the SNF2 transcriptional regulator in the DNA sequence of an 8.6 kb region in the LTE1-CYS1 interval on the left arm of chromosome I." Clark M.W., Zhong W.-W., Keng T., Storms R.K., Barton A.B., Kaback D.B., Bussey H. Yeast 8:133-145(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes." Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H. Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: analysis of the genes in the FUN38-MAK16-SPO7 region." Barton A.B., Kaback D.B. J. Bacteriol. 176:1872-1880(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"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].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34 AND SER-451, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-28, MASS SPECTROMETRY.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-28; THR-33; SER-34; THR-88; SER-96; SER-98; THR-131; SER-226; SER-232; SER-369; SER-383 AND SER-451, MASS SPECTROMETRY.
[10]	"The SNF2-family member Fun30 promotes gene silencing in heterochromatic loci." Neves-Costa A., Will W.R., Vetter A.T., Miller J.R., Varga-Weisz P. PLoS ONE 4:E8111-E8111(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"The Snf2 homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme." Awad S., Ryan D., Prochasson P., Owen-Hughes T., Hassan A.H. J. Biol. Chem. 285:9477-9484(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[12]	"The Saccharomyces cerevisiae chromatin remodeler Fun30 regulates DNA end-resection and checkpoint deactivation." Eapen V.V., Sugawara N., Tsabar M., Wu W.H., Haber J.E. Mol. Cell. Biol. 32:4727-4740(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"The Fun30 nucleosome remodeller promotes resection of DNA double-strand break ends." Chen X., Cui D., Papusha A., Zhang X., Chu C.D., Tang J., Chen K., Pan X., Ira G. Nature 489:576-580(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[14]	"The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end resection." Costelloe T., Louge R., Tomimatsu N., Mukherjee B., Martini E., Khadaroo B., Dubois K., Wiegant W.W., Thierry A., Burma S., van Attikum H., Llorente B. Nature 489:581-584(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-603.
[15]	"SWI/SNF-Like chromatin remodeling factor Fun30 supports point centromere function in S. cerevisiae." Durand-Dubief M., Will W.R., Petrini E., Theodorou D., Harris R.R., Crawford M.R., Paszkiewicz K., Krueger F., Correra R.M., Vetter A.T., Miller J.R., Kent N.A., Varga-Weisz P. PLoS Genet. 8:E1002974-E1002974(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L05146 Genomic DNA. Translation: AAC04938.1. BK006935 Genomic DNA. Translation: DAA06969.1.
PIR	S22266.
RefSeq	NP_009383.1. NM_001178164.1.
3D structure databases
ProteinModelPortal	P31380.
SMR	P31380. Positions 538-1099.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2541N.
IntAct	P31380. 10 interactions.
MINT	MINT-425278.
STRING	4932.YAL019W.
Proteomic databases
PaxDb	P31380.
PeptideAtlas	P31380.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAL019W; YAL019W; YAL019W.
GeneID	851214.
KEGG	sce:YAL019W.
Organism-specific databases
CYGD	YAL019w.
SGD	S000000017. FUN30.
Phylogenomic databases
eggNOG	COG0553.
GeneTree	ENSGT00630000089890.
HOGENOM	HOG000195581.
KO	K14439.
OMA	KIEPYYG.
OrthoDB	EOG4BCHW4.
Gene expression databases
Genevestigator	P31380.
GermOnline	YAL019W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. [Graphical view]
Pfam	PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968097.

Entry information

Entry name

FUN30_YEAST

Accession

Primary (citable) accession number: P31380
Secondary accession number(s): D6VPJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program