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Q9Y0I1

- EAF3_DROME

UniProt

Q9Y0I1 - EAF3_DROME

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Protein

NuA4 complex subunit EAF3 homolog

Gene

MRG15

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. methylated histone binding Source: FlyBase

GO - Biological processi

  1. chromatin silencing Source: FlyBase
  2. chromosome organization Source: FlyBase
  3. chromosome separation Source: FlyBase
  4. DNA repair Source: UniProtKB-KW
  5. histone acetylation Source: UniProtKB
  6. histone exchange Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
NuA4 complex subunit EAF3 homolog
Alternative name(s):
Protein MRG15
Gene namesi
Name:MRG15
ORF Names:CG6363
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0027378. MRG15.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. histone acetyltransferase complex Source: FlyBase
  2. NuA4 histone acetyltransferase complex Source: UniProtKB
  3. nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424NuA4 complex subunit EAF3 homologPRO_0000088771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191Phosphoserine1 Publication
Modified residuei175 – 1751Phosphothreonine1 Publication
Modified residuei183 – 1831Phosphothreonine1 Publication
Modified residuei196 – 1961Phosphothreonine1 Publication
Modified residuei197 – 1971Phosphothreonine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Modified residuei235 – 2351Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Y0I1.
PRIDEiQ9Y0I1.

Expressioni

Gene expression databases

BgeeiQ9Y0I1.

Interactioni

Subunit structurei

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-1.1 Publication

Protein-protein interaction databases

BioGridi66914. 32 interactions.
DIPiDIP-20132N.
IntActiQ9Y0I1. 2 interactions.
MINTiMINT-838509.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213
Beta strandi27 – 315
Beta strandi33 – 4412
Beta strandi47 – 504
Beta strandi52 – 576
Helixi62 – 643
Beta strandi66 – 694
Helixi70 – 723
Helixi78 – 9114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LRQNMR-A11-94[»]
ProteinModelPortaliQ9Y0I1.
SMRiQ9Y0I1. Positions 11-94, 256-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini252 – 424173MRGPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MRG domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG238705.
GeneTreeiENSGT00530000063018.
InParanoidiQ9Y0I1.
KOiK11339.
OrthoDBiEOG7ZPNK7.
PhylomeDBiQ9Y0I1.

Family and domain databases

InterProiIPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERiPTHR10880. PTHR10880. 1 hit.
PfamiPF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS51640. MRG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y0I1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGEVKPAKVE NYSTGTDANT LFVDGERVLC FHGPLIYEAK VLKTKPDATP
60 70 80 90 100
VEYYIHYAGW SKNWDEWVPE NRVLKYNDDN VKRRQELARQ CGERSKKDNK
110 120 130 140 150
KGSAKAKKME QMRNESRAST PSKDSNTSQS TASSTPTTSA GPGSKSEAGS
160 170 180 190 200
TGTTTTNSTA NSTTSRAHRK STQSTPSTAR PGTPSDKKED PAAAETTEEE
210 220 230 240 250
GPVAPKKKRM SEQRPSLTGS DVAEKPLPPT TTPSTPTTEP APCVESEEAY
260 270 280 290 300
AAKVEVKIKI PDELKHYLTD DWYAVVREHK LLELPAKVTV QQISEQYLAH
310 320 330 340 350
KKSVKSTSAS KEVAINDVLD GIVEYFNVML GSQLLYKFER TQYADVMQKH
360 370 380 390 400
PDTPLSELYG SFHLLRLFVR LGSMLSYSAL DQQSMQNLLT HVQDFLKFLV
410 420
KNSSIFFSMS NFINVDPEYV RNAQ
Length:424
Mass (Da):47,194
Last modified:November 1, 1999 - v1
Checksum:iB0E1F615252D8EDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF152245 mRNA. Translation: AAD38047.1.
AE014297 Genomic DNA. Translation: AAF55161.1.
AY051679 mRNA. Translation: AAK93103.1.
RefSeqiNP_650442.1. NM_142185.2.
UniGeneiDm.3453.

Genome annotation databases

EnsemblMetazoaiFBtr0083125; FBpp0082579; FBgn0027378.
GeneIDi41850.
KEGGidme:Dmel_CG6363.
UCSCiCG6363-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF152245 mRNA. Translation: AAD38047.1 .
AE014297 Genomic DNA. Translation: AAF55161.1 .
AY051679 mRNA. Translation: AAK93103.1 .
RefSeqi NP_650442.1. NM_142185.2.
UniGenei Dm.3453.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LRQ NMR - A 11-94 [» ]
ProteinModelPortali Q9Y0I1.
SMRi Q9Y0I1. Positions 11-94, 256-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66914. 32 interactions.
DIPi DIP-20132N.
IntActi Q9Y0I1. 2 interactions.
MINTi MINT-838509.

Proteomic databases

PaxDbi Q9Y0I1.
PRIDEi Q9Y0I1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0083125 ; FBpp0082579 ; FBgn0027378 .
GeneIDi 41850.
KEGGi dme:Dmel_CG6363.
UCSCi CG6363-RA. d. melanogaster.

Organism-specific databases

CTDi 84045.
FlyBasei FBgn0027378. MRG15.

Phylogenomic databases

eggNOGi NOG238705.
GeneTreei ENSGT00530000063018.
InParanoidi Q9Y0I1.
KOi K11339.
OrthoDBi EOG7ZPNK7.
PhylomeDBi Q9Y0I1.

Miscellaneous databases

GenomeRNAii 41850.
NextBioi 825893.
PROi Q9Y0I1.

Gene expression databases

Bgeei Q9Y0I1.

Family and domain databases

InterProi IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR008676. MRG.
IPR026541. MRG_dom.
IPR025995. Tudor-knot.
[Graphical view ]
PANTHERi PTHR10880. PTHR10880. 1 hit.
Pfami PF05712. MRG. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 2 hits.
PROSITEi PS51640. MRG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiEAF3_DROME
AccessioniPrimary (citable) accession number: Q9Y0I1
Secondary accession number(s): Q9VF99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3