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Q92993

- KAT5_HUMAN

UniProt

Q92993 - KAT5_HUMAN

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Protein

Histone acetyltransferase KAT5

Gene

KAT5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2.10 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei403 – 4031Proton donor/acceptorBy similarity
Binding sitei407 – 4071Acetyl-CoA1 Publication
Binding sitei416 – 4161Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri261 – 28323C2HC-type1 PublicationAdd
BLAST

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. histone acetyltransferase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. repressing transcription factor binding Source: BHF-UCL
  5. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. cellular response to estradiol stimulus Source: UniProt
  3. chromatin organization Source: Reactome
  4. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  5. double-strand break repair Source: UniProtKB
  6. histone acetylation Source: UniProtKB
  7. negative regulation of interleukin-2 production Source: BHF-UCL
  8. negative regulation of transcription, DNA-templated Source: BHF-UCL
  9. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProt
  12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  13. regulation of growth Source: UniProtKB-KW
  14. response to ionizing radiation Source: UniProtKB
  15. transcription, DNA-templated Source: UniProtKB-KW
  16. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Growth regulation, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
SignaLinkiQ92993.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT5 (EC:2.3.1.482 Publications)
Alternative name(s):
60 kDa Tat-interactive protein
Short name:
Tip60
Histone acetyltransferase HTATIP
Short name:
HIV-1 Tat interactive protein
Lysine acetyltransferase 5
cPLA(2)-interacting protein
Gene namesi
Name:KAT5
Synonyms:HTATIP, TIP60
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:5275. KAT5.

Subcellular locationi

Nucleus. Nucleusnucleolus. Cytoplasmperinuclear region
Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies.

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. NuA4 histone acetyltransferase complex Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. Piccolo NuA4 histone acetyltransferase complex Source: UniProtKB
  7. Swr1 complex Source: UniProtKB
  8. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced HAT activity. 1 Publication
Mutagenesisi90 – 901S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-86. Reduced HAT activity. 1 Publication
Mutagenesisi254 – 2541L → A: Does not affect phosphorylation; when associated with A-257. 1 Publication
Mutagenesisi257 – 2571L → A: Does not affect phosphorylation; when associated with A-254. 1 Publication
Mutagenesisi380 – 3801G → A: Loss of function. Does not affect phosphorylation. 1 Publication
Mutagenesisi430 – 4301K → R: Abrogates sumoylation. 1 Publication
Mutagenesisi451 – 4511K → R: Abrogates sumoylation. 1 Publication

Organism-specific databases

PharmGKBiPA162392746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Histone acetyltransferase KAT5PRO_0000051580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521N6-acetyllysine1 Publication
Modified residuei86 – 861Phosphoserine1 Publication
Modified residuei90 – 901Phosphoserine; by CDK11 Publication
Modified residuei327 – 3271N6-acetyllysine; by autocatalysis1 Publication
Cross-linki430 – 430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki451 – 451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies.1 Publication
Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. The phosphorylated form has a higher HAT activity.1 Publication
Ubiquitinated by MDM2, leading to its proteasome-dependent degradation.1 Publication
Autoacetylation at Lys-327 is required for proper function.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92993.
PaxDbiQ92993.
PRIDEiQ92993.

PTM databases

PhosphoSiteiQ92993.

Expressioni

Gene expression databases

BgeeiQ92993.
CleanExiHS_KAT5.
ExpressionAtlasiQ92993. baseline and differential.
GenevestigatoriQ92993.

Organism-specific databases

HPAiHPA016953.

Interactioni

Subunit structurei

Interacts with the cytoplasmic tail of APP and APBB1/FE65 (By similarity). Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Interacts with ATM. Interacts with JADE1. Interacts with HIV-1 Tat. Interacts with TRIM24 and TRIM68. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1. Interacts with ATF2 and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-like complex.By similarity17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN1P542533EBI-399080,EBI-930964
CBX8Q9HC522EBI-399080,EBI-712912
DLEU1O432612EBI-399080,EBI-710057
FOXP3Q9BZS1-12EBI-399080,EBI-9695448
GADD45GO952572EBI-399080,EBI-448202
KIAA1377Q9P2H02EBI-399080,EBI-473176
Myod1P100855EBI-399080,EBI-4405734From a different organism.
PTPN4P290742EBI-399080,EBI-710431
SRSF2Q011303EBI-399080,EBI-627047
TP53P046373EBI-399080,EBI-366083

Protein-protein interaction databases

BioGridi115779. 186 interactions.
DIPiDIP-5998N.
IntActiQ92993. 70 interactions.
MINTiMINT-94861.
STRINGi9606.ENSP00000340330.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154
Beta strandi28 – 347
Beta strandi37 – 393
Beta strandi43 – 475
Beta strandi56 – 583
Turni60 – 623
Helixi65 – 673
Beta strandi235 – 2373
Beta strandi240 – 2423
Helixi252 – 2543
Beta strandi260 – 2623
Turni264 – 2663
Beta strandi269 – 2713
Helixi273 – 28210
Beta strandi289 – 2968
Beta strandi299 – 3057
Turni306 – 3083
Helixi310 – 32112
Turni328 – 3314
Beta strandi336 – 34510
Beta strandi348 – 36013
Beta strandi365 – 3684
Beta strandi370 – 3723
Helixi374 – 3763
Helixi381 – 39515
Beta strandi400 – 4023
Helixi408 – 42518
Helixi441 – 4488
Helixi452 – 46110
Beta strandi469 – 4746
Helixi497 – 4993

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKONMR-A5-78[»]
2OU2X-ray2.30A227-506[»]
4QQGX-ray2.80A/B/C/D/E/F/G1-80[»]
ProteinModelPortaliQ92993.
SMRiQ92993. Positions 11-79, 230-504.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92993.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini227 – 504278MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 513146Interaction with ATF2Add
BLAST
Regioni370 – 3723Acetyl-CoA binding1 Publication
Regioni377 – 3837Acetyl-CoA binding1 Publication

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri261 – 28323C2HC-type1 PublicationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ92993.
KOiK11304.
OMAiHDDIITR.
OrthoDBiEOG7ZKS9R.
PhylomeDBiQ92993.
TreeFamiTF317619.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92993-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF
60 70 80 90 100
NKRLDEWVTH ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ
110 120 130 140 150
ASGKTLPIPV QITLRFNLPK EREAIPGGEP DQPLSSSSCL QPNHRSTKRK
160 170 180 190 200
VEVVSPATPV PSETAPASVF PQNGAARRAV AAQPGRKRKS NCLGTDEDSQ
210 220 230 240 250
DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH RLKPWYFSPY
260 270 280 290 300
PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS
310 320 330 340 350
FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH
360 370 380 390 400
IVGYFSKEKE STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG
410 420 430 440 450
TPEKPLSDLG LLSYRSYWSQ TILEILMGLK SESGERPQIT INEISEITSI
460 470 480 490 500
KKEDVISTLQ YLNLINYYKG QYILTLSEDI VDGHERAMLK RLLRIDSKCL
510
HFTPKDWSKR GKW
Length:513
Mass (Da):58,582
Last modified:May 16, 2003 - v2
Checksum:i63724F5E10B957D5
GO
Isoform 2 (identifier: Q92993-2) [UniParc]FASTAAdd to Basket

Also known as: PLIP

The sequence of this isoform differs from the canonical sequence as follows:
     96-147: Missing.

Show »
Length:461
Mass (Da):53,077
Checksum:i5A0E9324550AF246
GO
Isoform 3 (identifier: Q92993-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ

Show »
Length:546
Mass (Da):61,798
Checksum:i0CEB1A8E8C8D3E24
GO
Isoform 4 (identifier: Q92993-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
     96-147: Missing.

Note: No experimental confirmation available.

Show »
Length:494
Mass (Da):56,292
Checksum:i761BF5859BE89793
GO

Sequence cautioni

The sequence AAB02683.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3821G → R in AAB18236. (PubMed:8607265)Curated
Sequence conflicti382 – 3821G → R in AAB02683. (PubMed:8607265)Curated
Isoform 3 (identifier: Q92993-3)
Sequence conflicti32 – 321V → A no nucleotide entry (PubMed:12801643)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781P → T.
Corresponds to variant rs11541271 [ dbSNP | Ensembl ].
VAR_059456

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei4 – 41V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3 and isoform 4. 2 PublicationsVSP_009104
Alternative sequencei96 – 14752Missing in isoform 2 and isoform 4. 3 PublicationsVSP_007438Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U74667 mRNA. Translation: AAB18236.1.
U40989 mRNA. Translation: AAB02683.1. Different initiation.
U67734 mRNA. Translation: AAD00163.1.
AY214165 Genomic DNA. Translation: AAO21130.1.
AK304664 mRNA. Translation: BAG65439.1.
AP001266 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74427.1.
CH471076 Genomic DNA. Translation: EAW74429.1.
BC000166 mRNA. Translation: AAH00166.3.
BC064912 mRNA. Translation: AAH64912.1.
BC093032 mRNA. Translation: AAH93032.1.
BC143296 mRNA. Translation: AAI43297.1.
BC117167 mRNA. Translation: AAI17168.1.
CCDSiCCDS31610.1. [Q92993-1]
CCDS55771.1. [Q92993-4]
CCDS8109.1. [Q92993-2]
CCDS8110.1. [Q92993-3]
RefSeqiNP_001193762.1. NM_001206833.1. [Q92993-4]
NP_006379.2. NM_006388.3. [Q92993-1]
NP_874368.1. NM_182709.2. [Q92993-2]
NP_874369.1. NM_182710.2. [Q92993-3]
UniGeneiHs.397010.

Genome annotation databases

EnsembliENST00000341318; ENSP00000340330; ENSG00000172977. [Q92993-3]
ENST00000352980; ENSP00000344955; ENSG00000172977. [Q92993-2]
ENST00000377046; ENSP00000366245; ENSG00000172977. [Q92993-1]
ENST00000530446; ENSP00000434765; ENSG00000172977. [Q92993-4]
GeneIDi10524.
KEGGihsa:10524.
UCSCiuc001ofi.3. human. [Q92993-1]
uc001ofj.3. human. [Q92993-2]
uc001ofk.3. human. [Q92993-3]
uc010roo.2. human. [Q92993-4]

Polymorphism databases

DMDMi30923328.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U74667 mRNA. Translation: AAB18236.1 .
U40989 mRNA. Translation: AAB02683.1 . Different initiation.
U67734 mRNA. Translation: AAD00163.1 .
AY214165 Genomic DNA. Translation: AAO21130.1 .
AK304664 mRNA. Translation: BAG65439.1 .
AP001266 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74427.1 .
CH471076 Genomic DNA. Translation: EAW74429.1 .
BC000166 mRNA. Translation: AAH00166.3 .
BC064912 mRNA. Translation: AAH64912.1 .
BC093032 mRNA. Translation: AAH93032.1 .
BC143296 mRNA. Translation: AAI43297.1 .
BC117167 mRNA. Translation: AAI17168.1 .
CCDSi CCDS31610.1. [Q92993-1 ]
CCDS55771.1. [Q92993-4 ]
CCDS8109.1. [Q92993-2 ]
CCDS8110.1. [Q92993-3 ]
RefSeqi NP_001193762.1. NM_001206833.1. [Q92993-4 ]
NP_006379.2. NM_006388.3. [Q92993-1 ]
NP_874368.1. NM_182709.2. [Q92993-2 ]
NP_874369.1. NM_182710.2. [Q92993-3 ]
UniGenei Hs.397010.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EKO NMR - A 5-78 [» ]
2OU2 X-ray 2.30 A 227-506 [» ]
4QQG X-ray 2.80 A/B/C/D/E/F/G 1-80 [» ]
ProteinModelPortali Q92993.
SMRi Q92993. Positions 11-79, 230-504.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115779. 186 interactions.
DIPi DIP-5998N.
IntActi Q92993. 70 interactions.
MINTi MINT-94861.
STRINGi 9606.ENSP00000340330.

Chemistry

BindingDBi Q92993.
ChEMBLi CHEMBL5750.
GuidetoPHARMACOLOGYi 2664.

PTM databases

PhosphoSitei Q92993.

Polymorphism databases

DMDMi 30923328.

Proteomic databases

MaxQBi Q92993.
PaxDbi Q92993.
PRIDEi Q92993.

Protocols and materials databases

DNASUi 10524.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341318 ; ENSP00000340330 ; ENSG00000172977 . [Q92993-3 ]
ENST00000352980 ; ENSP00000344955 ; ENSG00000172977 . [Q92993-2 ]
ENST00000377046 ; ENSP00000366245 ; ENSG00000172977 . [Q92993-1 ]
ENST00000530446 ; ENSP00000434765 ; ENSG00000172977 . [Q92993-4 ]
GeneIDi 10524.
KEGGi hsa:10524.
UCSCi uc001ofi.3. human. [Q92993-1 ]
uc001ofj.3. human. [Q92993-2 ]
uc001ofk.3. human. [Q92993-3 ]
uc010roo.2. human. [Q92993-4 ]

Organism-specific databases

CTDi 10524.
GeneCardsi GC11P065479.
HGNCi HGNC:5275. KAT5.
HPAi HPA016953.
MIMi 601409. gene.
neXtProti NX_Q92993.
PharmGKBi PA162392746.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOGENOMi HOG000182457.
InParanoidi Q92993.
KOi K11304.
OMAi HDDIITR.
OrthoDBi EOG7ZKS9R.
PhylomeDBi Q92993.
TreeFami TF317619.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
SignaLinki Q92993.

Miscellaneous databases

EvolutionaryTracei Q92993.
GeneWikii KAT5.
GenomeRNAii 10524.
NextBioi 39922.
PROi Q92993.
SOURCEi Search...

Gene expression databases

Bgeei Q92993.
CleanExi HS_KAT5.
ExpressionAtlasi Q92993. baseline and differential.
Genevestigatori Q92993.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator."
    Kamine J., Elangovan B., Subramanian T., Coleman D., Chinnadurai G.
    Virology 216:357-366(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HIV-1 TAT.
    Tissue: Lymphoblast.
  2. "PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production."
    Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., Bonventre J.V.
    Mol. Cell. Biol. 21:4470-4481(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PLA2G4A, SUBCELLULAR LOCATION.
    Tissue: Fibroblast and Placenta.
  3. "Identification of a larger form of the histone acetyl transferase Tip60."
    Legube G., Trouche D.
    Gene 310:161-168(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cervix, Liver, Placenta and Testis.
  9. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-35; 150-177 AND 297-307, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Tip60 acetylates six lysines of a specific class in core histones in vitro."
    Kimura A., Horikoshi M.
    Genes Cells 3:789-800(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY IN VITRO.
  11. "Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
    Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
    Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling."
    Lee H.-J., Chun M., Kandror K.V.
    J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDNRA.
  13. "Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation."
    Legube G., Linares L.K., Lemercier C., Scheffner M., Khochbin S., Trouche D.
    EMBO J. 21:1704-1712(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  14. "MYC recruits the TIP60 histone acetyltransferase complex to chromatin."
    Frank S.R., Parisi T., Taubert S., Fernandez P., Fuchs M., Chan H.M., Livingston D.M., Amati B.
    EMBO Rep. 4:575-580(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN MYC-DEPENDENT TRANSCRIPTION.
  15. "Tip60 acetyltransferase activity is controlled by phosphorylation."
    Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D., Khochbin S.
    J. Biol. Chem. 278:4713-4718(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-86 AND SER-90, MUTAGENESIS OF SER-86; SER-90; LEU-254; LEU-257 AND GLY-380, CATALYTIC ACTIVITY.
  16. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HDAC7.
  17. "The highly conserved and multifunctional NuA4 HAT complex."
    Doyon Y., Cote J.
    Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON NUA4 COMPLEX.
  18. Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
  19. "von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity."
    Panchenko M.V., Zhou M.I., Cohen H.T.
    J. Biol. Chem. 279:56032-56041(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JADE1.
  20. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 COMPLEX.
  21. "E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1."
    Taubert S., Gorrini C., Frank S.R., Parisi T., Fuchs M., Chan H.M., Livingston D.M., Amati B.
    Mol. Cell. Biol. 24:4546-4556(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN E2F1-DEPENDENT TRANSCRIPTION.
  22. Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
  23. "HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses."
    Col E., Caron C., Chable-Bessia C., Legube G., Gazzeri S., Komatsu Y., Yoshida M., Benkirane M., Trouche D., Khochbin S.
    EMBO J. 24:2634-2645(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  24. "A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM."
    Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.
    Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATM, FUNCTION.
  25. "The histidine triad protein Hint1 triggers apoptosis independent of its enzymatic activity."
    Weiske J., Huber O.
    J. Biol. Chem. 281:27356-27366(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1.
  26. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
    Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
    Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  27. "The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
    Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
    Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NR1D2, SUBCELLULAR LOCATION.
  28. "TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells."
    Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., Nonomura K., Hatakeyama S.
    Cancer Res. 68:3486-3494(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM68.
  29. "Regulation of TIP60 by ATF2 modulates ATM activation."
    Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.
    J. Biol. Chem. 283:17605-17614(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF2 AND CUL3, PROTEASOMAL DEGRADATION.
  30. "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 S.E.
    , Hu R., Huang H., Jin C., Yao X.
    Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND LYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. "TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
    Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
    Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRIM24.
  33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
  36. "The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH ACETYL-COA AND ZINC IONS, ACETYLATION AT LYS-327.
  37. "Solution structure of RUH-073, a pseudo chromo domain from human cDNA."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 5-78.

Entry informationi

Entry nameiKAT5_HUMAN
AccessioniPrimary (citable) accession number: Q92993
Secondary accession number(s): B4E3C7
, C9JL99, O95624, Q13430, Q17RW5, Q561W3, Q6GSE8, Q9BWK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 16, 2003
Last modified: October 29, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3