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Histone acetyltransferase Tip60 (EC 2.3.1.48)

 TIP60_DROME             Reviewed;         541 AA.
Q960X4; O97425;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Histone acetyltransferase Tip60;
EC=2.3.1.48 {ECO:0000269|PubMed:15528408};
Name=Tip60; ORFNames=CG6121;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
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., 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.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
IDENTIFICATION IN THE TIP60 COMPLEX, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15528408; DOI=10.1126/science.1103455;
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.;
"Acetylation by Tip60 is required for selective histone variant
exchange at DNA lesions.";
Science 306:2084-2087(2004).
-!- 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.
{ECO:0000269|PubMed:15528408}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:15528408}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:15528408}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- PTM: Autoacetylation at Lys-355 is required for proper function.
{ECO:0000250|UniProtKB:Q9H7Z6}.
-!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA21829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE014298; AAF45923.3; -; Genomic_DNA.
EMBL; AL033125; CAA21829.1; ALT_SEQ; Genomic_DNA.
EMBL; AY051795; AAK93219.1; -; mRNA.
RefSeq; NP_001259234.1; NM_001272305.1.
RefSeq; NP_572151.1; NM_131923.4.
UniGene; Dm.75; -.
ProteinModelPortal; Q960X4; -.
SMR; Q960X4; -.
BioGrid; 57879; 21.
IntAct; Q960X4; 4.
MINT; MINT-785367; -.
STRING; 7227.FBpp0070636; -.
PaxDb; Q960X4; -.
PRIDE; Q960X4; -.
EnsemblMetazoa; FBtr0070668; FBpp0070636; FBgn0026080.
EnsemblMetazoa; FBtr0333186; FBpp0305388; FBgn0026080.
GeneID; 31362; -.
KEGG; dme:Dmel_CG6121; -.
CTD; 31362; -.
FlyBase; FBgn0026080; Tip60.
eggNOG; KOG2747; Eukaryota.
eggNOG; COG5027; LUCA.
GeneTree; ENSGT00550000074503; -.
InParanoid; Q960X4; -.
KO; K11304; -.
OMA; ITHADVM; -.
OrthoDB; EOG091G0B73; -.
PhylomeDB; Q960X4; -.
Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-DME-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-DME-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
GenomeRNAi; 31362; -.
PRO; PR:Q960X4; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0026080; -.
Genevisible; Q960X4; DM.
GO; GO:0000123; C:histone acetyltransferase complex; IPI:FlyBase.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IMP:FlyBase.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:FlyBase.
GO; GO:0007399; P:nervous system development; IMP:FlyBase.
GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
GO; GO:0048167; P:regulation of synaptic plasticity; IDA:FlyBase.
GO; GO:2000331; P:regulation of terminal button organization; IDA:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR016197; Chromodomain-like.
InterPro; IPR002717; HAT_MYST-type.
InterPro; IPR025995; Tudor-knot.
Pfam; PF01853; MOZ_SAS; 1.
Pfam; PF11717; Tudor-knot; 1.
SMART; SM00298; CHROMO; 1.
SUPFAM; SSF54160; SSF54160; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51726; MYST_HAT; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Chromatin regulator; Complete proteome;
Metal-binding; Nucleus; Reference proteome; Transcription;
Transcription regulation; Transferase; Zinc; Zinc-finger.
CHAIN 1 541 Histone acetyltransferase Tip60.
/FTId=PRO_0000051583.
DOMAIN 255 533 MYST-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
ZN_FING 288 313 C2HC MYST-type. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
REGION 398 400 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q9H7Z6}.
REGION 405 411 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q9H7Z6}.
ACT_SITE 431 431 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q9H7Z6}.
BINDING 435 435 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q9H7Z6}.
BINDING 444 444 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q9H7Z6}.
MOD_RES 355 355 N6-acetyllysine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9H7Z6}.
SEQUENCE 541 AA; 61234 MW; F48A3415B708A97C CRC64;
MKINHKYEFD DDVASICEST AALTEGCRLP VRMHKTDDWP LAEIVSIKEL DGRRQFYVHY
VDFNKRLDEW VNEEDLYTRK VQFPRRDGSQ TGTSTGVTTP QRHHSLAGSV SRPTSPQHPG
SGALAAIPQT PTGASGSVPP PAGIPNSVAP PGTPSSGGEL VNGNNLAAAL QKRINRKRKN
HGGSAHGHHS LTSQQQQSHP HPTTPQTPTA TPVHVTGDGL ISGAANDDGD GSQDGKTPTP
RQSGSMVTHQ DDVVTRMKNV EMIELGRHRI KPWYFSPYPQ ELCQMPCIYI CEFCLKYRKS
RKCLERHLSK CNLRHPPGNE IYRKHTISFF EIDGRKNKVY AQNLCLLAKL FLDHKTLYYD
TDPFLFYVMT EFDSRGFHIV GYFSKEKEST EDYNVACILT MPPYQRKGYG KLLIEFSYEL
SKFEGKTGSP EKPLSDLGLL SYRSYWAQTI LEIFISQNPS TDGEKPTITI NDICECTSIK
KEDVISTLQN LNLINYYKGQ YIVCINRVII EQHRRAMDKR KIRIDSKCLH WTPKDWSKRS
K


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