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Protein

Histone acetyltransferase Tip60

Gene

Tip60

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

Functioni

Catalytic subunit of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, acetylates phosphorylated histone H2AV in nucleosomes on 'Lys-4' and exchanges it with unmodified H2AV.1 Publication

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei431Proton donor/acceptorBy similarity1
Binding sitei435Acetyl-CoABy similarity1
Binding sitei444Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri288 – 313C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

  • histone acetyltransferase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to DNA damage stimulus Source: FlyBase
  • histone acetylation Source: UniProtKB
  • histone exchange Source: UniProtKB
  • histone H4 acetylation Source: FlyBase
  • negative regulation of neuron apoptotic process Source: FlyBase
  • nervous system development Source: FlyBase
  • regulation of gene expression Source: FlyBase
  • regulation of synaptic plasticity Source: FlyBase
  • regulation of terminal button organization Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionAcyltransferase, Chromatin regulator, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-201722. Formation of the beta-catenin:TCF transactivating complex.
R-DME-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-DME-5693548. Sensing of DNA Double Strand Breaks.
R-DME-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-DME-5693571. Nonhomologous End-Joining (NHEJ).
R-DME-5693607. Processing of DNA double-strand break ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase Tip60 (EC:2.3.1.481 Publication)
Gene namesi
Name:Tip60
ORF Names:CG6121
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0026080. Tip60.

Subcellular locationi

GO - Cellular componenti

  • histone acetyltransferase complex Source: FlyBase
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nucleus Source: FlyBase
  • polytene chromosome interband Source: FlyBase

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515831 – 541Histone acetyltransferase Tip60Add BLAST541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei355N6-acetyllysine; by autocatalysisBy similarity1

Post-translational modificationi

Autoacetylation at Lys-355 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ960X4.
PRIDEiQ960X4.

Expressioni

Gene expression databases

BgeeiFBgn0026080.
GenevisibleiQ960X4. DM.

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

BioGridi57879. 5 interactors.
IntActiQ960X4. 4 interactors.
MINTiMINT-785367.
STRINGi7227.FBpp0070636.

Structurei

3D structure databases

ProteinModelPortaliQ960X4.
SMRiQ960X4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini255 – 533MYST-type HATPROSITE-ProRule annotationAdd BLAST279

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni398 – 400Acetyl-CoA bindingBy similarity3
Regioni405 – 411Acetyl-CoA bindingBy similarity7

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri288 – 313C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
InParanoidiQ960X4.
KOiK11304.
OMAiITHADVM.
OrthoDBiEOG091G0B73.
PhylomeDBiQ960X4.

Family and domain databases

InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
PfamiView protein in Pfam
PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
SMARTiView protein in SMART
SM00298. CHROMO. 1 hit.
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51726. MYST_HAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Q960X4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKINHKYEFD DDVASICEST AALTEGCRLP VRMHKTDDWP LAEIVSIKEL
60 70 80 90 100
DGRRQFYVHY VDFNKRLDEW VNEEDLYTRK VQFPRRDGSQ TGTSTGVTTP
110 120 130 140 150
QRHHSLAGSV SRPTSPQHPG SGALAAIPQT PTGASGSVPP PAGIPNSVAP
160 170 180 190 200
PGTPSSGGEL VNGNNLAAAL QKRINRKRKN HGGSAHGHHS LTSQQQQSHP
210 220 230 240 250
HPTTPQTPTA TPVHVTGDGL ISGAANDDGD GSQDGKTPTP RQSGSMVTHQ
260 270 280 290 300
DDVVTRMKNV EMIELGRHRI KPWYFSPYPQ ELCQMPCIYI CEFCLKYRKS
310 320 330 340 350
RKCLERHLSK CNLRHPPGNE IYRKHTISFF EIDGRKNKVY AQNLCLLAKL
360 370 380 390 400
FLDHKTLYYD TDPFLFYVMT EFDSRGFHIV GYFSKEKEST EDYNVACILT
410 420 430 440 450
MPPYQRKGYG KLLIEFSYEL SKFEGKTGSP EKPLSDLGLL SYRSYWAQTI
460 470 480 490 500
LEIFISQNPS TDGEKPTITI NDICECTSIK KEDVISTLQN LNLINYYKGQ
510 520 530 540
YIVCINRVII EQHRRAMDKR KIRIDSKCLH WTPKDWSKRS K
Length:541
Mass (Da):61,234
Last modified:December 1, 2001 - v1
Checksum:iF48A3415B708A97C
GO

Sequence cautioni

The sequence CAA21829 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF45923.3.
AL033125 Genomic DNA. Translation: CAA21829.1. Sequence problems.
AY051795 mRNA. Translation: AAK93219.1.
RefSeqiNP_001259234.1. NM_001272305.1.
NP_572151.1. NM_131923.4.
UniGeneiDm.75.

Genome annotation databases

EnsemblMetazoaiFBtr0070668; FBpp0070636; FBgn0026080.
FBtr0333186; FBpp0305388; FBgn0026080.
GeneIDi31362.
KEGGidme:Dmel_CG6121.

Similar proteinsi

Entry informationi

Entry nameiTIP60_DROME
AccessioniPrimary (citable) accession number: Q960X4
Secondary accession number(s): O97425
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: December 1, 2001
Last modified: August 30, 2017
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families