{{Short description|Protein-coding gene in the species Homo sapiens}} {{cs1 config|name-list-style=vanc}} {{Infobox_gene}} '''Histone acetyltransferase KAT5''' is an enzyme that in humans is encoded by the ''KAT5'' gene.<ref name="pmid8607265">{{cite journal | vauthors = Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G | title = Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator | journal = Virology | volume = 216 | issue = 2 | pages = 357–66 | date = Feb 1996 | pmid = 8607265 | doi = 10.1006/viro.1996.0071 | doi-access = free }}</ref><ref name="entrez">{{cite web| title = Entrez Gene: HTATIP HIV-1 Tat interacting protein, 60kDa| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=10524| access-date = 2024-04-27| archive-date = 2024-04-27| archive-url = https://web.archive.org/web/20240427165110/https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=10524| url-status = live}}</ref> It is also commonly identified as TIP60.
The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction. Alternative splicing of this gene results in multiple transcript variants.<ref name="entrez" />
== Structure == The structure of KAT5 includes an acetyl CoA binding domain and a zinc finger in the MYST domain, and a CHROMO domain.<ref name="hdl.handle.net">{{Cite journal|title = HTATIP (HIV-1 Tat interacting protein, 60kDa)|hdl=2042/38522|journal = Atlas of Genetics and Cytogenetics in Oncology and Haematology|issue=3|doi= 10.4267/2042/38522|year=2011|last1=Mattera|first1=L|doi-broken-date=12 July 2025 |doi-access=free}}</ref> Excess acetyl CoA is necessary for acetylation of histones. The zinc finger domain has been shown to aid in the acetylation process as well.<ref>{{cite journal | vauthors = Kim MY, Ann EJ, Kim JY, Mo JS, Park JH, Kim SY, Seo MS, Park HS | title = Tip60 histone acetyltransferase acts as a negative regulator of Notch1 signaling by means of acetylation | journal = Molecular and Cellular Biology | volume = 27 | issue = 18 | pages = 6506–19 | date = Sep 2007 | pmid = 17636029 | doi = 10.1128/MCB.01515-06 | pmc=2099611}}</ref> The CHROMO domain aids in KAT5 ability to bind chromatin, which is important for DNA repair.<ref>{{cite journal | vauthors = Koonin EV, Zhou S, Lucchesi JC | title = The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcription regulators to chromatin | journal = Nucleic Acids Research | volume = 23 | issue = 21 | pages = 4229–33 | date = Nov 1995 | pmid = 7501439 | pmc = 307373 | doi = 10.1093/nar/23.21.4229 }}</ref>
== Function ==
KAT5 enzyme is known for acetylating histones in the nucleosome, which alters binding with DNA. Acetylation neutralizes the positive charge on histones, decreasing binding affinity of negatively charged DNA.<ref>{{Cite book|title = Molecular Biology Web Book|last = Lee|first = Frank|publisher = Web Books Publishing|chapter = Gene Transcription: Histone Acetylation, DNA Methylation and Epigenetics|chapter-url = http://www.web-books.com/MoBio/Free/Ch4G.htm|access-date = 2015-05-06|archive-date = 2015-05-04|archive-url = https://web.archive.org/web/20150504040813/http://www.web-books.com/MoBio/Free/Ch4G.htm|url-status = dead}}</ref> This in turn decreases steric hindrance of DNA and increases interaction of transcription factors and other proteins. Three key functions of KAT5 are its ability to regulate transcription, DNA repair, and apoptosis.
=== Transcription === Transcription factors such as E2F proteins and c-Myc can regulate the expression of proteins, particularly those involved with the cell cycle.<ref name="Broeck 320–325">{{cite journal | vauthors = Van Den Broeck A, Nissou D, Brambilla E, Eymin B, Gazzeri S | title = Activation of a Tip60/E2F1/ERCC1 network in human lung adenocarcinoma cells exposed to cisplatin | journal = Carcinogenesis | volume = 33 | issue = 2 | pages = 320–5 | date = Feb 2012 | pmid = 22159227 | doi = 10.1093/carcin/bgr292 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Patel JH, Du Y, Ard PG, Phillips C, Carella B, Chen CJ, Rakowski C, Chatterjee C, Lieberman PM, Lane WS, Blobel GA, McMahon SB | title = The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60 | journal = Molecular and Cellular Biology | volume = 24 | issue = 24 | pages = 10826–34 | date = Dec 2004 | pmid = 15572685 | doi = 10.1128/MCB.24.24.10826-10834.2004 | pmc=533976}}</ref> KAT5 acetylates histones on genes of these transcription factors, which promote their activity.
=== DNA repair === KAT5 is an important enzyme for repairing DNA and returning cellular function to normal through its regulation of ataxia telangiectasia mutant (ATM) protein kinase.<ref>{{cite journal | vauthors = Sun Y, Jiang X, Chen S, Fernandes N, Price BD | title = A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 37 | pages = 13182–7 | date = Sep 2005 | pmid = 16141325 | doi = 10.1073/pnas.0504211102 | pmc=1197271| bibcode = 2005PNAS..10213182S | doi-access = free }}</ref> ATM protein kinase phosphorylates and therefore activates proteins involved in DNA repair. However, to be functional, ATM protein kinase must be acetylated by the KAT5 protein. Lack of KAT5 suppresses ATM protein kinase activity and reduces the ability of a cell to correct its DNA.
KAT5 also works later in the DNA repair process, as it serves as a cofactor for TRRAP.<ref>{{cite journal | vauthors = Murr R, Loizou JI, Yang YG, Cuenin C, Li H, Wang ZQ, Herceg Z | title = Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks | journal = Nature Cell Biology | volume = 8 | issue = 1 | pages = 91–9 | date = Jan 2006 | pmid = 16341205 | doi = 10.1038/ncb1343 | s2cid = 25051471 }}</ref> TRRAP enhances DNA remodeling by binding to chromatin near broken double stranded DNA sequences. KAT5 aids this recognition.
=== Apoptosis === P53 is well known for causing cell apoptosis after DNA damage. Acetylation of p53 by KAT5 induces this cell death.<ref name="Broeck 320–325"/> Therefore, lack of KAT5 allows cells with damaged DNA to avoid apoptosis and continue dividing.
== Regulation == KAT5 catalytic activity is regulated by the phosphorylation of its histones during the G2/M phase of the cell cycle.<ref>{{cite journal | vauthors = Lemercier C, Legube G, Caron C, Louwagie M, Garin J, Trouche D, Khochbin S | title = Tip60 acetyltransferase activity is controlled by phosphorylation | journal = The Journal of Biological Chemistry | volume = 278 | issue = 7 | pages = 4713–8 | date = Feb 2003 | pmid = 12468530 | doi = 10.1074/jbc.M211811200 | s2cid = 8276821 | url = https://hal.archives-ouvertes.fr/hal-00380484/document | doi-access = free | access-date = 2024-04-27 | archive-date = 2022-01-11 | archive-url = https://web.archive.org/web/20220111091748/https://hal.archives-ouvertes.fr/hal-00380484/document | url-status = live }}</ref> Phosphorylation of KAT5 serines 86 and 90 reduces its activity. Therefore, cancer cells with uncontrolled growth and improper G2/M checkpoints lack KAT5 regulation by cyclin dependent kinase (CDK) phosphorylation.
== Clinical relevance == KAT5 has many clinically significant implications that make it a useful target for diagnostic or therapeutic approaches. Most notably, KAT5 helps to regulate cancers, HIV, and neurodegenerative diseases.<ref name="hdl.handle.net"/>
=== Cancer === As mentioned above, KAT5 helps to repair DNA and upregualte tumor suppressors such as p53. Therefore, many cancers are marked by a reduction of KAT5 mRNA. KAT5 also is linked to metastasis and malignancy.<ref name="Chen G p60">{{cite journal | vauthors = Chen G, Cheng Y, Tang Y, Martinka M, Li G | title = Role of Tip60 in human melanoma cell migration, metastasis, and patient survival | journal = The Journal of Investigative Dermatology | volume = 132 | issue = 11 | pages = 2632–41 | date = Nov 2012 | pmid = 22673729 | doi = 10.1038/jid.2012.193 | doi-access = free }}</ref> * Colon cancer<ref>{{cite journal | vauthors = Chevillard-Briet M, Quaranta M, Grézy A, Mattera L, Courilleau C, Philippe M, Mercier P, Corpet D, Lough J, Ueda T, Fukunaga R, Trouche D, Escaffit F | title = Interplay between chromatin-modifying enzymes controls colon cancer progression through Wnt signaling | journal = Human Molecular Genetics | volume = 23 | issue = 8 | pages = 2120–31 | date = Apr 2014 | pmid = 24287617 | doi = 10.1093/hmg/ddt604 | doi-access = free }}</ref> * Lung cancer<ref name="Broeck 320–325"/> * Breast cancer<ref name = "Ravichandran_2015">{{cite journal |title = Tip60 Overexpression Exacerbates Chemotherapeutic Drug Treatment in Breast, Pancreatic, and Lung Cancer Cell Lines|last1 = Ravichandran|first1 = Priyadarshini |date = April 2015|journal = The FASEB Journal |last2 = Ginsburg|first2 = Daniel|volume = 29|pages = Supplement 725.21 | issue=S1 | doi = 10.1096/fasebj.29.1_supplement.725.21 |doi-access = free}}</ref> * Pancreatic<ref name = "Ravichandran_2015"/> * Gastric cancer<ref>{{cite journal | vauthors = Sakuraba K, Yokomizo K, Shirahata A, Goto T, Saito M, Ishibashi K, Kigawa G, Nemoto H, Hibi K | title = TIP60 as a potential marker for the malignancy of gastric cancer | journal = Anticancer Research | volume = 31 | issue = 1 | pages = 77–9 | date = Jan 2011 | pmid = 21273583 }}</ref> * Metastatic melanoma<ref name="Chen G p60"/> Studies have also shown that KAT5 augmented the ability of chemotherapy to stop tumor growth, demonstrating its potential for use in combination therapy.<ref name = "Ravichandran_2015"/>
However, KAT5 isn't always anti-cancer. It can enhance the activity of proteins for viruses that cause cancer such as human T-cell lymphotropic virus type-1 (HTLV), which may result in leukemia and lymphoma.<ref>{{cite journal | vauthors = Awasthi S, Sharma A, Wong K, Zhang J, Matlock EF, Rogers L, Motloch P, Takemoto S, Taguchi H, Cole MD, Lüscher B, Dittrich O, Tagami H, Nakatani Y, McGee M, Girard AM, Gaughan L, Robson CN, Monnat RJ, Harrod R | title = A human T-cell lymphotropic virus type 1 enhancer of Myc transforming potential stabilizes Myc-TIP60 transcriptional interactions | journal = Molecular and Cellular Biology | volume = 25 | issue = 14 | pages = 6178–98 | date = Jul 2005 | pmid = 15988028 | doi = 10.1128/MCB.25.14.6178-6198.2005 | pmc=1168837}}</ref> Additionally, KAT5 reacts with human papillomavirus (HPV), the virus responsible for cervical cancer.<ref>{{cite journal | vauthors = Hong S, Dutta A, Laimins LA | title = The acetyltransferase Tip60 is a critical regulator of the differentiation-dependent amplification of human papillomaviruses | journal = Journal of Virology | volume = 89 | issue = 8 | pages = 4668–75 | date = Apr 2015 | pmid = 25673709 | doi = 10.1128/JVI.03455-14 | pmc=4442364}}</ref>
Other proteins that KAT5 promotes may lead to cancer as well. For example, overexpressed E2F1, a transcriptional factor, is implicated in melanoma progression.<ref>{{cite journal | vauthors = Alla V, Engelmann D, Niemetz A, Pahnke J, Schmidt A, Kunz M, Emmrich S, Steder M, Koczan D, Pützer BM | title = E2F1 in melanoma progression and metastasis | journal = Journal of the National Cancer Institute | volume = 102 | issue = 2 | pages = 127–33 | date = Jan 2010 | pmid = 20026813 | doi = 10.1093/jnci/djp458 }}</ref> More research needs to be performed to clearly elucidate the overall role KAT5 has in cancer.
=== HIV ===
KAT5 binds to HIV-1 Tat transactivator and helps to promote HIV replication.<ref>{{cite journal | vauthors = Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G | title = Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator | journal = Virology | volume = 216 | issue = 2 | pages = 357–66 | date = Feb 1996 | pmid = 8607265 | doi = 10.1006/viro.1996.0071 | doi-access = free }}</ref>
=== Aging and Neurodegeneration === TIP60 regulates diverse cellular pathways including autophagy, DNA repair, neuronal survival, learning/memory, sleep/wake patterns, and protein turnover, all of which contribute to cellular homeostasis and organismal health so as to counteract aging and neurodegeneration.<ref>{{Cite journal|last1=Li|first1=Zhiquan|last2=Rasmussen|first2=Lene Juel|date=2020-10-19|title=TIP60 in Aging and Neurodegeneration|url=http://www.sciencedirect.com/science/article/pii/S1568163720303305|journal=Ageing Research Reviews|volume=64|language=en|article-number=101195|doi=10.1016/j.arr.2020.101195|pmid=33091598|s2cid=224775578|issn=1568-1637|access-date=2024-04-27|archive-date=2023-03-04|archive-url=https://web.archive.org/web/20230304223130/https://www.sciencedirect.com/science/article/pii/S1568163720303305|url-status=live|url-access=subscription}}</ref>
== Interactions ==
HTATIP has been shown to interact with: {{div col|colwidth=20em}} * Androgen receptor,<ref name = pmid11994312>{{cite journal | vauthors = Gaughan L, Logan IR, Cook S, Neal DE, Robson CN | title = Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor | journal = The Journal of Biological Chemistry | volume = 277 | issue = 29 | pages = 25904–13 | date = Jul 2002 | pmid = 11994312 | doi = 10.1074/jbc.M203423200 | s2cid = 9930504 | doi-access = free }}</ref> * BCL3,<ref name = pmid10362352>{{cite journal | vauthors = Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG, Scheidereit C, Leutz A | title = The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators | journal = Oncogene | volume = 18 | issue = 22 | pages = 3316–23 | date = Jun 1999 | pmid = 10362352 | doi = 10.1038/sj.onc.1202717 | s2cid = 2356435 | doi-access = free }}</ref> * CREB1,<ref name = pmid10720489>{{cite journal | vauthors = Gavaravarapu S, Kamine J | title = Tip60 inhibits activation of CREB protein by protein kinase A | journal = Biochemical and Biophysical Research Communications | volume = 269 | issue = 3 | pages = 758–66 | date = Mar 2000 | pmid = 10720489 | doi = 10.1006/bbrc.2000.2358 | bibcode = 2000BBRC..269..758G | doi-access = free }}</ref> * ETV6,<ref name = pmid12737628>{{cite journal | vauthors = Nordentoft I, Jørgensen P | title = The acetyltransferase 60 kDa trans-acting regulatory protein of HIV type 1-interacting protein (Tip60) interacts with the translocation E26 transforming-specific leukaemia gene (TEL) and functions as a transcriptional co-repressor | journal = The Biochemical Journal | volume = 374 | issue = Pt 1 | pages = 165–73 | date = Aug 2003 | pmid = 12737628 | pmc = 1223570 | doi = 10.1042/BJ20030087 }}</ref> * EDNRA<ref name = pmid11262386>{{cite journal | vauthors = Lee HJ, Chun M, Kandror KV | title = Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling | journal = The Journal of Biological Chemistry | volume = 276 | issue = 20 | pages = 16597–600 | date = May 2001 | pmid = 11262386 | doi = 10.1074/jbc.C000909200 | s2cid = 38498534 | doi-access = free }}</ref> * FANCD2,<ref name = pmid18263878>{{cite journal | vauthors = Hejna J, Holtorf M, Hines J, Mathewson L, Hemphill A, Al-Dhalimy M, Olson SB, Moses RE | title = Tip60 is required for DNA interstrand cross-link repair in the Fanconi anemia pathway | journal = The Journal of Biological Chemistry | volume = 283 | issue = 15 | pages = 9844–51 | date = Apr 2008 | pmid = 18263878 | pmc = 2398728 | doi = 10.1074/jbc.M709076200 | doi-access = free }}</ref> * HDAC7A,<ref name = pmid12551922>{{cite journal | vauthors = Xiao H, Chung J, Kao HY, Yang YC | title = Tip60 is a co-repressor for STAT3 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 13 | pages = 11197–204 | date = Mar 2003 | pmid = 12551922 | doi = 10.1074/jbc.M210816200 | s2cid = 6317335 | doi-access = free }}</ref> * Mdm2,<ref name = pmid11927554>{{cite journal | vauthors = Legube G, Linares LK, Lemercier C, Scheffner M, Khochbin S, Trouche D | title = Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation | journal = The EMBO Journal | volume = 21 | issue = 7 | pages = 1704–12 | date = Apr 2002 | pmid = 11927554 | pmc = 125958 | doi = 10.1093/emboj/21.7.1704 }}</ref> * Myc,<ref name = pmid12776177>{{cite journal | vauthors = Frank SR, Parisi T, Taubert S, Fernandez P, Fuchs M, Chan HM, Livingston DM, Amati B | title = MYC recruits the TIP60 histone acetyltransferase complex to chromatin | journal = EMBO Reports | volume = 4 | issue = 6 | pages = 575–80 | date = Jun 2003 | pmid = 12776177 | pmc = 1319201 | doi = 10.1038/sj.embor.embor861 }}</ref> and * PLA2G4A.<ref name = pmid11416127>{{cite journal | vauthors = Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV | title = PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production | journal = Molecular and Cellular Biology | volume = 21 | issue = 14 | pages = 4470–81 | date = Jul 2001 | pmid = 11416127 | pmc = 87107 | doi = 10.1128/MCB.21.14.4470-4481.2001 }}</ref> *PXR<ref>Bakshi, K., Ranjitha, B., Dubey, S. et al. Novel complex of HAT protein TIP60 and nuclear receptor PXR promotes cell migration and adhesion. Sci Rep 7, 3635 (2017). https://doi.org/10.1038/s41598-017-03783-w</ref>{{Div col end}}
== References == {{reflist|33em}}
== Further reading == {{refbegin|33em}} * {{cite journal | vauthors = Doyon Y, Côté J | title = The highly conserved and multifunctional NuA4 HAT complex | journal = Current Opinion in Genetics & Development | volume = 14 | issue = 2 | pages = 147–54 | date = Apr 2004 | pmid = 15196461 | doi = 10.1016/j.gde.2004.02.009 }} * {{cite journal | vauthors = Sapountzi V, Logan IR, Robson CN | title = Cellular functions of TIP60 | journal = The International Journal of Biochemistry & Cell Biology | volume = 38 | issue = 9 | pages = 1496–509 | year = 2006 | pmid = 16698308 | doi = 10.1016/j.biocel.2006.03.003 }} * {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }} * {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }} * {{cite journal | vauthors = Yamamoto T, Horikoshi M | title = Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60 | journal = The Journal of Biological Chemistry | volume = 272 | issue = 49 | pages = 30595–8 | date = Dec 1997 | pmid = 9388189 | doi = 10.1074/jbc.272.49.30595 | s2cid = 21873080 | doi-access = free }} * {{cite journal | vauthors = Kimura A, Horikoshi M | title = Tip60 acetylates six lysines of a specific class in core histones in vitro | journal = Genes to Cells | volume = 3 | issue = 12 | pages = 789–800 | date = Dec 1998 | pmid = 10096020 | doi = 10.1046/j.1365-2443.1998.00229.x | s2cid = 41070266 | doi-access = free }} * {{cite journal | vauthors = Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG, Scheidereit C, Leutz A | title = The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators | journal = Oncogene | volume = 18 | issue = 22 | pages = 3316–23 | date = Jun 1999 | pmid = 10362352 | doi = 10.1038/sj.onc.1202717 | s2cid = 2356435 | doi-access = free }} * {{cite journal | vauthors = Brady ME, Ozanne DM, Gaughan L, Waite I, Cook S, Neal DE, Robson CN | title = Tip60 is a nuclear hormone receptor coactivator | journal = The Journal of Biological Chemistry | volume = 274 | issue = 25 | pages = 17599–604 | date = Jun 1999 | pmid = 10364196 | doi = 10.1074/jbc.274.25.17599 | s2cid = 38058299 | doi-access = free }} * {{cite journal | vauthors = Creaven M, Hans F, Mutskov V, Col E, Caron C, Dimitrov S, Khochbin S | title = Control of the histone-acetyltransferase activity of Tip60 by the HIV-1 transactivator protein, Tat | journal = Biochemistry | volume = 38 | issue = 27 | pages = 8826–30 | date = Jul 1999 | pmid = 10393559 | doi = 10.1021/bi9907274 }} * {{cite journal | vauthors = Sliva D, Zhu YX, Tsai S, Kamine J, Yang YC | title = Tip60 interacts with human interleukin-9 receptor alpha-chain | journal = Biochemical and Biophysical Research Communications | volume = 263 | issue = 1 | pages = 149–55 | date = Sep 1999 | pmid = 10486269 | doi = 10.1006/bbrc.1999.1083 | bibcode = 1999BBRC..263..149S }} * {{cite journal | vauthors = Gavaravarapu S, Kamine J | title = Tip60 inhibits activation of CREB protein by protein kinase A | journal = Biochemical and Biophysical Research Communications | volume = 269 | issue = 3 | pages = 758–66 | date = Mar 2000 | pmid = 10720489 | doi = 10.1006/bbrc.2000.2358 | bibcode = 2000BBRC..269..758G | doi-access = free }} * {{cite journal | vauthors = Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG | title = Proteomic analysis of NMDA receptor-adhesion protein signaling complexes | journal = Nature Neuroscience | volume = 3 | issue = 7 | pages = 661–9 | date = Jul 2000 | pmid = 10862698 | doi = 10.1038/76615 | hdl = 1842/742 | s2cid = 14392630 | hdl-access = free }} * {{cite journal | vauthors = Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y | title = Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis | journal = Cell | volume = 102 | issue = 4 | pages = 463–73 | date = Aug 2000 | pmid = 10966108 | doi = 10.1016/S0092-8674(00)00051-9 | s2cid = 18047169 | doi-access = free }} * {{cite journal | vauthors = Ran Q, Pereira-Smith OM | title = Identification of an alternatively spliced form of the Tat interactive protein (Tip60), Tip60(beta) | journal = Gene | volume = 258 | issue = 1–2 | pages = 141–6 | date = Nov 2000 | pmid = 11111051 | doi = 10.1016/S0378-1119(00)00410-8 }} * {{cite journal | vauthors = Lee HJ, Chun M, Kandror KV | title = Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling | journal = The Journal of Biological Chemistry | volume = 276 | issue = 20 | pages = 16597–600 | date = May 2001 | pmid = 11262386 | doi = 10.1074/jbc.C000909200 | s2cid = 38498534 | doi-access = free }} * {{cite journal | vauthors = Hlubek F, Löhberg C, Meiler J, Jung A, Kirchner T, Brabletz T | title = Tip60 is a cell-type-specific transcriptional regulator | journal = Journal of Biochemistry | volume = 129 | issue = 4 | pages = 635–41 | date = Apr 2001 | pmid = 11275565 | doi = 10.1093/oxfordjournals.jbchem.a002901 }} * {{cite journal | vauthors = Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV | title = PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production | journal = Molecular and Cellular Biology | volume = 21 | issue = 14 | pages = 4470–81 | date = Jul 2001 | pmid = 11416127 | pmc = 87107 | doi = 10.1128/MCB.21.14.4470-4481.2001 }} * {{cite journal | vauthors = Cao X, Südhof TC | title = A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60 | journal = Science | volume = 293 | issue = 5527 | pages = 115–20 | date = Jul 2001 | pmid = 11441186 | doi = 10.1126/science.1058783 | s2cid = 43920642 }} * {{cite journal | vauthors = Legube G, Linares LK, Lemercier C, Scheffner M, Khochbin S, Trouche D | title = Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation | journal = The EMBO Journal | volume = 21 | issue = 7 | pages = 1704–12 | date = Apr 2002 | pmid = 11927554 | pmc = 125958 | doi = 10.1093/emboj/21.7.1704 }} {{refend}}
== External links == * {{PDBe-KB2|Q92993|Histone acetyltransferase KAT5}}
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Category:EC 2.3.1