Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Tip60 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Tip60 a histone acetyl transferase (HAT) of the MYST family. Originally isolated as an HIV-1 TAT-interactive protein. Plays an important role in regulating chromatin remodeling, transcription and other nuclear processes by acetylating nuclear proteins. Plays a role in DNA repair and apoptosis. Three splice variants have been described.. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; EC 2.3.1.48; EC 2.3.1.-; Nucleolus; Acetyltransferase
Cellular Component: nucleoplasm; transcription factor complex; NuA4 histone acetyltransferase complex; perinuclear region of cytoplasm; nucleolus; cytosol; nucleus
Molecular Function: protein binding; histone acetyltransferase activity; androgen receptor binding; metal ion binding; transcription coactivator activity; protein complex binding
Biological Process: proteasomal ubiquitin-dependent protein catabolic process; establishment and/or maintenance of chromatin architecture; transcription, DNA-dependent; viral reproduction; positive regulation of transcription, DNA-dependent; negative regulation of transcription from RNA polymerase II promoter; negative regulation of interleukin-2 production; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; double-strand break repair; regulation of growth; androgen receptor signaling pathway; positive regulation of transcription from RNA polymerase II promoter; histone acetylation; response to ionizing radiation; negative regulation of transcription, DNA-dependent
Reference #:  Q92993 (UniProtKB)
Alt. Names/Synonyms: 60 kDa Tat-interactive protein; cPLA(2)-interacting protein; cPLA2; cPLA2 interacting protein; ESA1; Histone acetyltransferase HTATIP; Histone acetyltransferase KAT5; HIV-1 Tat interactive protein; HIV-1 Tat interactive protein, 60kDa; HTATIP; HTATIP1; K(lysine) acetyltransferase 5; K-acetyltransferase 5; KAT5; Lysine acetyltransferase 5; PLIP; Tat interacting protein, 60kDa; TIP; TIP60
Gene Symbols: KAT5
Molecular weight: 58,582 Da
Basal Isoelectric point: 8.75  Predict pI for various phosphorylation states
CST Pathways:  Crosstalk between PTMs  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Tip60

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  NURSA


Sites Implicated In
apoptosis, induced: S86‑p
transcription, altered: S86‑p, S90‑p
transcription, induced: S86‑p
acetylation: S86‑p
phosphorylation: S90‑p
protein stabilization: S86‑p, S90‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K35-ub LAEILSVkDISGRKL
1 0 Y44-p ISGRKLFyVHYIDFN
0 3 K52-ac VHYIDFNkRLDEWVT
3 16 S86-p TKNGLPGsRPGsPER
3 28 S90-p LPGsRPGsPEREVPA
0 1 K104-ac ASAQASGkTLPIPVQ
0 8 S155-p KRKVEVVsPAtPVPS
1 3 T158-p VEVVsPAtPVPSETA
0 11 S190-p QPGRKRKsNCLGtDE
0 9 T195-p RKsNCLGtDEDsQDs
0 16 S199-p CLGtDEDsQDssDGI
0 5 S202-p tDEDsQDssDGIPSA
0 5 S203-p DEDsQDssDGIPSAP
0 1 T227-p RSHDDIVtRMKNIEC
0 1 T281-p KCLQRHLtKCDLRHP
1 0 Y294-p HPPGNEIyRKGTISF
0 3 K327-ac AKCFLDHkTLYYDTD
1 0 K430-sm LEILMGLksESGERP
0 1 S431-p EILMGLksESGERPQ
1 0 K451-sm ISEITSIkKEDVIST
0 2 Y472-p INYYKGQyILTLSED
  Tip60 iso2  
K35 LAEILSVKDISGRKL
Y44 ISGRKLFYVHYIDFN
K52 VHYIDFNKRLDEWVT
S86-p TKNGLPGsRPGsPER
S90-p LPGsRPGsPEREVKR
- gap
S103 KRKVEVVSPAtPVPS
T106-p VEVVSPAtPVPSETA
S138 QPGRKRKSNCLGTDE
T143 RKSNCLGTDEDSQDS
S147 CLGTDEDSQDSSDGI
S150 TDEDSQDSSDGIPSA
S151 DEDSQDSSDGIPSAP
T175 RSHDDIVTRMKNIEC
T229 KCLQRHLTKCDLRHP
Y242 HPPGNEIYRKGTISF
K275 AKCFLDHKTLYYDTD
K378 LEILMGLKSESGERP
S379 EILMGLKSESGERPQ
K399 ISEITSIKKEDVIST
Y420 INYYKGQYILTLSED
  mouse

► Hide Isoforms
 
K35 LAEILSVKDISGRKL
Y44 ISGRKLFYVHYIDFN
K52 VHYIDFNKRLDEWVT
S86-p TKNGLPGsRPGsPER
S90-p LPGsRPGsPEREVPA
K104 ASAQASGKTLPIPVQ
S155-p KRKVEVVsPATPVPS
T158 VEVVsPATPVPSETA
S190-p QPGRKRKsNCLGtDE
T195-p RKsNCLGtDEDsQDs
S199-p CLGtDEDsQDssDGI
S202-p tDEDsQDssDGIPSA
S203-p DEDsQDssDGIPSAP
T227 RSHDDIVTRMKNIEC
T281 KCLQRHLTKCDLRHP
Y294 HPPGNEIYRKGTISF
K327 AKCFLDHKTLYYDTD
K430 LEILMGLKSESGERP
S431 EILMGLKSESGERPQ
K451 ISEITSIKKEDVIST
Y472 INYYKGQYILTLSED
  Tip60 iso2  
K35 LAEILSVKDISGRKL
Y44 ISGRKLFYVHYIDFN
K52 VHYIDFNKRLDEWVT
S86-p TKNGLPGsRPGsPER
S90-p LPGsRPGsPEREVKR
- gap
S103 KRKVEVVSPATPVPS
T106 VEVVSPATPVPSETA
S138 QPGRKRKSNCLGTDE
T143 RKSNCLGTDEDSQDS
S147 CLGTDEDSQDSSDGI
S150 TDEDSQDSSDGIPSA
S151 DEDSQDSSDGIPSAP
T175 RSHDDIVTRMKNIEC
T229 KCLQRHLTKCDLRHP
Y242 HPPGNEIYRKGTISF
K275 AKCFLDHKTLYYDTD
K378 LEILMGLKSESGERP
S379 EILMGLKSESGERPQ
K399 ISEITSIKKEDVIST
Y420 INYYKGQYILTLSED
  rat

 
K35 LAEILSVKDISGRKL
Y44 ISGRKLFYVHYIDFN
K52 VHYIDFNKRLDEWVT
S86 TKNGLPGSRPGsPER
S90-p LPGSRPGsPEREVPA
K104 ASAQASGKTLPIPVQ
S155 KRKVEVVSPATPVPS
T158 VEVVSPATPVPSETA
S190 QPGRKRKSNCLGTDE
T195 RKSNCLGTDEDSQDS
S199 CLGTDEDSQDSSDGI
S202 TDEDSQDSSDGIPSA
S203 DEDSQDSSDGIPSAP
T227 RSHDDIVTRMKNIEC
T281 KCLQRHLTKCDLRHP
Y294 HPPGNEIYRKGTISF
K327 AKCFLDHKTLYYDTD
K430 LEILMGLKSESGERP
S431 EILMGLKSESGERPQ
K451 ISEITSIKKEDVIST
Y472 INYYKGQYILTLSED
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.