UniProt Accession

 KAT5_HUMAN; Q92993; B4E3C7; C9JL99; O95624; Q13430; Q17RW5; Q561W3; Q6GSE8; Q9BWK7 

Genbank Protein ID

 U74667; U40989; U67734; AY214165; AK304664; AP001266; CH471076; CH471076; BC000166; BC064912; BC093032; BC143296; BC117167 

Genbank Nucleotide ID

 AAB18236.1; AAB02683.1; AAD00163.1; AAO21130.1; BAG65439.1; EAW74427.1; EAW74429.1; AAH00166.3; AAH64912.1; AAH93032.1; AAI43297.1; AAI17168.1 

Protein Name

 Histone acetyltransferase KAT5 

Protein Synonyms/Alias

 60 kDa Tat-interactive protein; Tip60; Histone acetyltransferase HTATIP; HIV-1 Tat interactive protein; Lysine acetyltransferase 5; cPLA(2)-interacting protein 

Gene Name

 KAT5 

Gene Synonyms/Alias

 HTATIP; TIP60 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
35	LAEILSVKDISGRKL	ubiquitination	[1]
52	VHYIDFNKRLDEWVT	acetylation	[2]
76	QFPKKEAKTPTKNGL	acetylation	[3, 4]
80	KEAKTPTKNGLPGSR	acetylation	[3, 4]
104	ASAQASGKTLPIPVQ	acetylation	[4]
150	NHRSTKRKVEVVSPA	acetylation	[4]
187	VAAQPGRKRKSNCLG	acetylation	[4]
189	AQPGRKRKSNCLGTD	acetylation	[3]
327	AKCFLDHKTLYYDTD	acetylation	[3, 4]
383	YQRRGYGKLLIEFSY	acetylation	[4]
430	LEILMGLKSESGERP	sumoylation	[5]
451	ISEITSIKKEDVIST	sumoylation	[5]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60.
 Wang J, Chen J.
 J Biol Chem. 2010 Apr 9;285(15):11458-64. [PMID: 20100829]
 [4] Function of the active site lysine autoacetylation in Tip60 catalysis.
 Yang C, Wu J, Zheng YG.
 PLoS One. 2012;7(3):e32886. [PMID: 22470428]
 [5] Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response.
 Cheng Z, Ke Y, Ding X, Wang F, Wang H, Wang W, Ahmed K, Liu Z, Xu Y, Aikhionbare F, Yan H, Liu J, Xue Y, Yu J, Powell M, Liang S, Wu Q, Reddy SE, Hu R, Huang H, Jin C, Yao X.
 Oncogene. 2008 Feb 7;27(7):931-41. [PMID: 17704809] 

Functional Description

 Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. 

Sequence Annotation

 ZN_FING 261 283 C2HC-type.
 REGION 377 383 Acetyl-CoA binding.
 ACT_SITE 327 327 By similarity.
 ACT_SITE 369 369 Nucleophile (By similarity).
 BINDING 372 372 Acetyl-CoA.
 BINDING 407 407 Acetyl-CoA.
 MOD_RES 52 52 N6-acetyllysine.
 MOD_RES 86 86 Phosphoserine.
 MOD_RES 90 90 Phosphoserine; by CDK1.
 MOD_RES 327 327 N6-acetyllysine; by autocatalysis (By
 CROSSLNK 430 430 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; Activator; Acyltransferase; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; Growth regulation; Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 513 AA 

Protein Sequence

Gene Ontology

 GO:0000785; C:chromatin; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
 GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
 GO:0006302; P:double-strand break repair; IMP:UniProtKB.
 GO:0016573; P:histone acetylation; IDA:UniProtKB.
 GO:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR016181; Acyl_CoA_acyltransferase.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR002717; MOZ_SAS.
 IPR025995; Tudor-knot. 

Pfam

 PF01853; MOZ_SAS
 PF11717; Tudor-knot 

SMART

 SM00298; CHROMO 

PROSITE

  

PRINTS