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Q9Y0I1 (EAF3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NuA4 complex subunit EAF3 homolog
Alternative name(s):
Protein MRG15
Gene names
Name:MRG15
ORF Names:CG6363
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, this complex acetylates phosphorylated H2AV in nucleosomes and exchanges it with unmodified H2AV. Ref.5

Subunit structure

Component of the Tip60 chromatin-remodeling complex which contains the catalytic subunit Tip60 and the subunits Domino, Tra1, Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP, Gas41 and YL-1. Ref.5

Subcellular location

Nucleus Probable.

Sequence similarities

Contains 1 MRG domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424NuA4 complex subunit EAF3 homolog
PRO_0000088771

Regions

Domain252 – 424173MRG

Amino acid modifications

Modified residue1191Phosphoserine Ref.6
Modified residue1751Phosphothreonine Ref.6
Modified residue1831Phosphothreonine Ref.6
Modified residue1961Phosphothreonine Ref.6
Modified residue1971Phosphothreonine Ref.6
Modified residue2111Phosphoserine Ref.6
Modified residue2351Phosphothreonine Ref.6

Secondary structure

.................. 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y0I1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B0E1F615252D8EDD

FASTA42447,194
        10         20         30         40         50         60 
MGEVKPAKVE NYSTGTDANT LFVDGERVLC FHGPLIYEAK VLKTKPDATP VEYYIHYAGW 

        70         80         90        100        110        120 
SKNWDEWVPE NRVLKYNDDN VKRRQELARQ CGERSKKDNK KGSAKAKKME QMRNESRAST 

       130        140        150        160        170        180 
PSKDSNTSQS TASSTPTTSA GPGSKSEAGS TGTTTTNSTA NSTTSRAHRK STQSTPSTAR 

       190        200        210        220        230        240 
PGTPSDKKED PAAAETTEEE GPVAPKKKRM SEQRPSLTGS DVAEKPLPPT TTPSTPTTEP 

       250        260        270        280        290        300 
APCVESEEAY AAKVEVKIKI PDELKHYLTD DWYAVVREHK LLELPAKVTV QQISEQYLAH 

       310        320        330        340        350        360 
KKSVKSTSAS KEVAINDVLD GIVEYFNVML GSQLLYKFER TQYADVMQKH PDTPLSELYG 

       370        380        390        400        410        420 
SFHLLRLFVR LGSMLSYSAL DQQSMQNLLT HVQDFLKFLV KNSSIFFSMS NFINVDPEYV 


RNAQ 

« Hide

References

« Hide 'large scale' references
[1]"Conservation of the MORF4 related gene family: identification of a new chromo domain subfamily and novel protein motif."
Bertram M.J., Pereira-Smith O.M.
Gene 266:111-121(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions."
Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L., Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.
Science 306:2084-2087(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TIP60 COMPLEX, FUNCTION.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; THR-175; THR-183; THR-196; THR-197; SER-211 AND THR-235, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152245 mRNA. Translation: AAD38047.1.
AE014297 Genomic DNA. Translation: AAF55161.1.
AY051679 mRNA. Translation: AAK93103.1.
RefSeqNP_650442.1. NM_142185.2.
UniGeneDm.3453.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LRQNMR-A11-94[»]
ProteinModelPortalQ9Y0I1.
SMRQ9Y0I1. Positions 11-94, 256-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66914. 32 interactions.
DIPDIP-20132N.
IntActQ9Y0I1. 2 interactions.
MINTMINT-838509.

Proteomic databases

PaxDbQ9Y0I1.
PRIDEQ9Y0I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083125; FBpp0082579; FBgn0027378.
GeneID41850.
KEGGdme:Dmel_CG6363.
UCSCCG6363-RA. d. melanogaster.

Organism-specific databases

CTD84045.
FlyBaseFBgn0027378. MRG15.

Phylogenomic databases

eggNOGNOG238705.
GeneTreeENSGT00530000063018.
InParanoidQ9Y0I1.
KOK11339.
OrthoDBEOG7ZPNK7.
PhylomeDBQ9Y0I1.

Gene expression databases

BgeeQ9Y0I1.

Family and domain databases

InterProIPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERPTHR10880. PTHR10880. 1 hit.
PfamPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 2 hits.
PROSITEPS51640. MRG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi41850.
NextBio825893.
PROQ9Y0I1.

Entry information

Entry nameEAF3_DROME
AccessionPrimary (citable) accession number: Q9Y0I1
Secondary accession number(s): Q9VF99
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase