Q06337 (EAF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromatin modification-related protein EAF1

Alternative name(s):
ESA1-associated factor 1
Vacuolar import and degradation protein 21

Gene names

Name:	EAF1
Synonyms:	VID21
Ordered Locus Names:	YDR359C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	982 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Ref.4 Ref.6
Subunit structure	Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the EAF1 family. Contains 1 HSA domain. Contains 1 Myb-like domain.
Sequence caution	The sequence AAB64794.1 differs from that shown. Reason: Frameshift at position 942.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: SGD cellular protein complex assembly Inferred from mutant phenotype. Source: SGD chromatin modification Inferred from physical interaction. Source: SGD regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Inferred from physical interaction Ref.7Ref.5. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.6. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESA1	Q08649	7	EBI-35867,EBI-6648
SWC4	P53201	4	EBI-35867,EBI-23061
YAF9	P53930	2	EBI-35867,EBI-28841

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 982	982	Chromatin modification-related protein EAF1		PRO_0000065825
Regions
	Domain	346 – 425	80	HSA
	Domain	642 – 704	63	Myb-like
	Compositional bias	825 – 942	118	Gln-rich
Amino acid modifications
	Modified residue	94	1	Phosphothreonine Ref.8
	Modified residue	591	1	Phosphoserine Ref.8
	Modified residue	613	1	Phosphoserine Ref.8
	Modified residue	841	1	Phosphoserine Ref.8
	Modified residue	951	1	Phosphoserine Ref.8
	Modified residue	971	1	Phosphothreonine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q06337 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 75F0C9594EF4ED8D	FASTA	982	112,502
	10 20 30 40 50 60 MSSRPSSAVP NSASLSEDQS SDRSKFPKAD DLIDERDRKL TELYCVSRLN QLLELTDENK 70 80 90 100 110 120 LRKEIDAFLK KNDIRRGIRF DEASLPKLLH TAATPITKKK LKDVNLINVP NQRLSDSKMS 130 140 150 160 170 180 RELPENSENV SVKSESHFVP SHDNSIRENM MDSLRPAEKT GGMWNKRPLE STMGGEEERH 190 200 210 220 230 240 EKRQKMQSQS LESSNNSEMA SLPISPRPPV PNALAHYTYY ENIEYPPADP TEVQPAVKFK 250 260 270 280 290 300 DPLIKNIMAK EIDTSDHYNE NNVDALETVF LLMNDYIPSK IPQALPLAEL KYMSQTLPLI 310 320 330 340 350 360 NLIPRAHKAL TTNIINNALN EARITVVGSR IEELRRLGLW SLRQPKRFID PWKQHNTHQN 370 380 390 400 410 420 ILLEEAKWMQ ADFKEGHKYK VAICTAMAQA IKDYWTYGEI CCVKRKTLLP GKENKLSDDG 430 440 450 460 470 480 RISEKSGRPS DTSRNDSDIS IAGKDDIGII ANVDDITEKE SAAANDNDEN GKNEAGAKSD 490 500 510 520 530 540 FDFADGLLSQ EGAHDQIISS IDTKLLLKKP SSSSEVVLIQ HEVAASSALI ETEESKKELA 550 560 570 580 590 600 PPFKLSIFVD ELNTFEKTLI QDLPLYNGIN EERPKKDDSL PFIPISKSVV SLDDNGFYKL 610 620 630 640 650 660 LERQLIDEEP SISQLSKRRG MFYGNRRNHY LRPPAVPSLR YLQNRTPTIW LSEDDQELVK 670 680 690 700 710 720 NINTYGYNWE LISAHMTHRL TYSYLSNIER RTPWQCFERF VQLNERFNFS DLKGPRAHSA 730 740 750 760 770 780 QQWLIEAHKF QQRQNRRISP LGVNTESIQR GHRRLRWASM FEAIRKCMKK RENTPRPNPT 790 800 810 820 830 840 QPRKPLDCKN MKVPTPAEMS LLKAQRDEAL RRDIQLRRTV KNRLQQRQQQ SQQAHSSRAQ 850 860 870 880 890 900 SPIPSNGKSS SNLARNGQAS APRPNQKQYT EQDIIESYSR KLLEQKPDIG PEMALKAAKN 910 920 930 940 950 960 YYRTLREQQQ QLKQHQIQQQ RQQLQEESSH VQQLQQLQPG SQAPPPKSSP SQSSLSNISN 970 980 INSAPRIKSP TPQEILQRFQ KQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Auger A., Galarneau L., Cote J. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 200060 / W303 and ATCC 201388 / BY4741.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Genes required for ionizing radiation resistance in yeast." Bennett C.B., Lewis L.K., Karthikeyan G., Lobachev K.S., Jin Y.H., Sterling J.F., Snipe J.R., Resnick M.A. Nat. Genet. 29:426-434(2001) [PubMed: 11726929] [Abstract] Cited for: FUNCTION.
[5]	"The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres." Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R. Mol. Cell. Biol. 24:9424-9436(2004) [PubMed: 15485911] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[6]	"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin." Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J. PLoS Biol. 2:587-599(2004) [PubMed: 15045029] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[7]	"Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4." Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F. Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed: 15353583] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[8]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94; SER-591; SER-613; SER-841; SER-951 AND THR-971, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY464182 Genomic DNA. Translation: AAR27935.1. AY464183 Genomic DNA. Translation: AAR27936.1. U28372 Genomic DNA. Translation: AAB64794.1. Frameshift. BK006938 Genomic DNA. Translation: DAA12198.1.
PIR	S61155.
RefSeq	NP_010646.2. NM_001180667.1.
3D structure databases
ProteinModelPortal	Q06337.
SMR	Q06337. Positions 648-703.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6330N.
IntAct	Q06337. 25 interactions.
MINT	MINT-600777.
STRING	Q06337.
Proteomic databases
PeptideAtlas	Q06337.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR359C; YDR359C; YDR359C.
GeneID	851962.
KEGG	sce:YDR359C.
NMPDR	fig|4932.3.peg.1413.
Organism-specific databases
CYGD	YDR359c.
SGD	S000002767. VID21.
Phylogenomic databases
eggNOG	fuNOG08073.
GeneTree	EFGT00050000000179.
HOGENOM	HBG203264.
OMA	NRRNHYL.
OrthoDB	EOG4G1QR0.
Gene expression databases
ArrayExpress	Q06337.
Genevestigator	Q06337.
GermOnline	YDR359C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013999. HAS_subgr. IPR014012. Helicase/SANT-assoc_DNA-bd. IPR009057. Homeodomain-like. IPR012287. Homeodomain-rel. IPR006562. HSA. IPR017877. MYB-like. IPR001005. SANT_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
KO	K11397.
Pfam	PF07529. HSA. 1 hit. [Graphical view]
SMART	SM00573. HSA. 1 hit. SM00717. SANT. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit.
PROSITE	PS51204. HSA. 1 hit. PS50090. MYB_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970071.

Entry information

Entry name

EAF1_YEAST

Accession

Primary (citable) accession number: Q06337
Secondary accession number(s): D6VSY8, Q6S6F6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	December 14, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program