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Q960X4 (TIP60_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase Tip60
EC=2.3.1.48
Gene names
Name:Tip60
ORF Names:CG6121
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

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.

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Sequence caution

The sequence CAA21829.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Histone acetyltransferase Tip60
PRO_0000051583

Regions

Region405 – 4117Acetyl-CoA binding By similarity

Sites

Active site3971Nucleophile By similarity
Binding site4001Acetyl-CoA By similarity
Binding site4351Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q960X4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F48A3415B708A97C

FASTA54161,234
        10         20         30         40         50         60 
MKINHKYEFD DDVASICEST AALTEGCRLP VRMHKTDDWP LAEIVSIKEL DGRRQFYVHY 

        70         80         90        100        110        120 
VDFNKRLDEW VNEEDLYTRK VQFPRRDGSQ TGTSTGVTTP QRHHSLAGSV SRPTSPQHPG 

       130        140        150        160        170        180 
SGALAAIPQT PTGASGSVPP PAGIPNSVAP PGTPSSGGEL VNGNNLAAAL QKRINRKRKN 

       190        200        210        220        230        240 
HGGSAHGHHS LTSQQQQSHP HPTTPQTPTA TPVHVTGDGL ISGAANDDGD GSQDGKTPTP 

       250        260        270        280        290        300 
RQSGSMVTHQ DDVVTRMKNV EMIELGRHRI KPWYFSPYPQ ELCQMPCIYI CEFCLKYRKS 

       310        320        330        340        350        360 
RKCLERHLSK CNLRHPPGNE IYRKHTISFF EIDGRKNKVY AQNLCLLAKL FLDHKTLYYD 

       370        380        390        400        410        420 
TDPFLFYVMT EFDSRGFHIV GYFSKEKEST EDYNVACILT MPPYQRKGYG KLLIEFSYEL 

       430        440        450        460        470        480 
SKFEGKTGSP EKPLSDLGLL SYRSYWAQTI LEIFISQNPS TDGEKPTITI NDICECTSIK 

       490        500        510        520        530        540 
KEDVISTLQN LNLINYYKGQ YIVCINRVII EQHRRAMDKR KIRIDSKCLH WTPKDWSKRS 


K

« Hide

References

« Hide 'large scale' references
[1]"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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[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: 12537569] [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: 15528408] [Abstract]
Cited for: IDENTIFICATION IN THE TIP60 COMPLEX, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014298 Genomic DNA. Translation: AAF45923.3.
AL033125 Genomic DNA. Translation: CAA21829.1. Sequence problems.
AY051795 mRNA. Translation: AAK93219.1.
RefSeqNP_572151.1. NM_131923.3.
UniGeneDm.75.

3D structure databases

ProteinModelPortalQ960X4.
SMRQ960X4. Positions 18-92, 258-533.
ModBaseSearch...

Protein-protein interaction databases

IntActQ960X4. 4 interactions.
MINTMINT-785367.
STRINGQ960X4.

Proteomic databases

PRIDEQ960X4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070668; FBpp0070636; FBgn0026080.
GeneID31362.
KEGGdme:Dmel_CG6121.
NMPDRfig|7227.3.peg.16445.

Organism-specific databases

CTD31362.
FlyBaseFBgn0026080. Tip60.

Phylogenomic databases

eggNOGinNOG07801.
GeneTreeEMGT00050000000694.
InParanoidQ960X4.
OMACMCTRDE.
OrthoDBEOG4TQJR4.
PhylomeDBQ960X4.

Gene expression databases

BgeeQ960X4.
GermOnlineCG6121. Drosophila melanogaster.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KOK11304.
PfamPF01853. MOZ_SAS. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF54160. Chromodomain-like. 1 hit.
ProtoNetSearch...

Other

NextBio773249.

Entry information

Entry nameTIP60_DROME
AccessionPrimary (citable) accession number: Q960X4
Secondary accession number(s): O97425
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents