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Protein

Histone acetyltransferase KAT5

Gene

KAT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity (PubMed:17360565).11 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei403Proton donor/acceptorBy similarity1
Binding sitei407Acetyl-CoA1 Publication1
Binding sitei416Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri260 – 285C2HC MYST-typePROSITE-ProRule annotation1 PublicationAdd BLAST26

GO - Molecular functioni

  • acetyltransferase activity Source: Reactome
  • androgen receptor binding Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • repressing transcription factor binding Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • androgen receptor signaling pathway Source: UniProtKB
  • beta-catenin-TCF complex assembly Source: Reactome
  • cellular response to estradiol stimulus Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  • DNA double-strand break processing Source: Reactome
  • DNA replication Source: Reactome
  • DNA synthesis involved in DNA repair Source: Reactome
  • double-strand break repair Source: UniProtKB
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • histone acetylation Source: UniProtKB
  • negative regulation of interleukin-2 production Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of protein acetylation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • regulation of growth Source: UniProtKB-KW
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • response to ionizing radiation Source: UniProtKB
  • strand displacement Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
  • 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

BioCyciZFISH:HS10602-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214847. HATs acetylate histones.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693548. Sensing of DNA Double Strand Breaks.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ92993.
SIGNORiQ92993.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:5275. KAT5.

Subcellular locationi

GO - Cellular componenti

  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • Piccolo NuA4 histone acetyltransferase complex Source: UniProtKB
  • Swr1 complex Source: UniProtKB
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced HAT activity. 1 Publication1
Mutagenesisi90S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-86. Reduced HAT activity. 1 Publication1
Mutagenesisi254L → A: Does not affect phosphorylation; when associated with A-257. 1 Publication1
Mutagenesisi257L → A: Does not affect phosphorylation; when associated with A-254. 1 Publication1
Mutagenesisi380G → A: Loss of function. Does not affect phosphorylation. 1 Publication1
Mutagenesisi430K → R: Abrogates sumoylation. 1 Publication1
Mutagenesisi451K → R: Abrogates sumoylation. 1 Publication1

Organism-specific databases

DisGeNETi10524.
OpenTargetsiENSG00000172977.
PharmGKBiPA162392746.

Chemistry databases

ChEMBLiCHEMBL5750.
GuidetoPHARMACOLOGYi2664.

Polymorphism and mutation databases

BioMutaiKAT5.
DMDMi30923328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515801 – 513Histone acetyltransferase KAT5Add BLAST513

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52N6-acetyllysineCombined sources1
Modified residuei86PhosphoserineCombined sources1 Publication1
Modified residuei90Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei199PhosphoserineCombined sources1
Modified residuei327N6-acetyllysine; by autocatalysis1 Publication1
Cross-linki430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

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

EPDiQ92993.
MaxQBiQ92993.
PaxDbiQ92993.
PeptideAtlasiQ92993.
PRIDEiQ92993.

PTM databases

iPTMnetiQ92993.
PhosphoSitePlusiQ92993.

Expressioni

Gene expression databases

BgeeiENSG00000172977.
CleanExiHS_KAT5.
ExpressionAtlasiQ92993. baseline and differential.
GenevisibleiQ92993. HS.

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. Interacts with FOXP3. Interacts with ZBTB49 (PubMed:25245946).By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN1P542533EBI-399080,EBI-930964
CBX8Q9HC522EBI-399080,EBI-712912
CCDC136Q96JN2-23EBI-399080,EBI-10171416
CEP126Q9P2H02EBI-399080,EBI-473176
DLEU1O432612EBI-399080,EBI-710057
FLJ13057Q53SE73EBI-399080,EBI-10172181
FOXP3Q9BZS1-12EBI-399080,EBI-9695448
GADD45GO952572EBI-399080,EBI-448202
GMCL1Q96IK54EBI-399080,EBI-2548508
GMCL1P1Q8NEA93EBI-399080,EBI-745707
GOLGA2Q083793EBI-399080,EBI-618309
HMBOX1Q6NT765EBI-399080,EBI-2549423
IKZF3Q9UKT95EBI-399080,EBI-747204
KRT40Q6A1623EBI-399080,EBI-10171697
KRTAP10-9P604113EBI-399080,EBI-10172052
LONRF1Q17RB83EBI-399080,EBI-2341787
LZTS2Q9BRK45EBI-399080,EBI-741037
MDFIQ997503EBI-399080,EBI-724076
MEOX2A4D1273EBI-399080,EBI-10172134
MTUS2Q5JR593EBI-399080,EBI-742948
Myod1P100855EBI-399080,EBI-4405734From a different organism.
NINLQ9Y2I63EBI-399080,EBI-719716
NOD2Q9HC292EBI-399080,EBI-7445625
ODC1P119263EBI-399080,EBI-1044287
PHC2Q8IXK03EBI-399080,EBI-713786
PIH1D3Q9NQM45EBI-399080,EBI-10239299
PTPN4P290742EBI-399080,EBI-710431
SOX5P357113EBI-399080,EBI-3505701
SRSF2Q011303EBI-399080,EBI-627047
SSX2IPQ9Y2D83EBI-399080,EBI-2212028
STX11O755583EBI-399080,EBI-714135
TMCC2Q7Z6C63EBI-399080,EBI-10177480
TP53P046373EBI-399080,EBI-366083
TRIM23P364063EBI-399080,EBI-740098
TRIM27P143733EBI-399080,EBI-719493
TRIM37O949723EBI-399080,EBI-741602
TUFT1Q9NNX13EBI-399080,EBI-2557363
TWIST1Q156722EBI-399080,EBI-1797287
ZBTB14O438293EBI-399080,EBI-10176632
ZBTB8AQ96BR94EBI-399080,EBI-742740
ZNF513Q8N8E23EBI-399080,EBI-10279993

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • repressing transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi115779. 223 interactors.
DIPiDIP-5998N.
IntActiQ92993. 131 interactors.
MINTiMINT-94861.
STRINGi9606.ENSP00000340330.

Chemistry databases

BindingDBiQ92993.

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi12 – 15Combined sources4
Beta strandi28 – 35Combined sources8
Beta strandi37 – 40Combined sources4
Beta strandi42 – 47Combined sources6
Helixi52 – 54Combined sources3
Beta strandi56 – 58Combined sources3
Helixi60 – 62Combined sources3
Helixi65 – 67Combined sources3
Beta strandi235 – 237Combined sources3
Beta strandi240 – 242Combined sources3
Helixi252 – 254Combined sources3
Beta strandi260 – 262Combined sources3
Turni264 – 266Combined sources3
Beta strandi269 – 271Combined sources3
Helixi273 – 282Combined sources10
Beta strandi289 – 296Combined sources8
Beta strandi299 – 305Combined sources7
Turni306 – 308Combined sources3
Helixi310 – 321Combined sources12
Turni328 – 331Combined sources4
Beta strandi336 – 345Combined sources10
Beta strandi348 – 360Combined sources13
Beta strandi365 – 368Combined sources4
Beta strandi370 – 372Combined sources3
Helixi374 – 376Combined sources3
Helixi381 – 395Combined sources15
Beta strandi400 – 402Combined sources3
Helixi408 – 425Combined sources18
Helixi441 – 448Combined sources8
Helixi452 – 461Combined sources10
Beta strandi469 – 474Combined sources6
Helixi497 – 499Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EKONMR-A5-78[»]
2OU2X-ray2.30A227-506[»]
4QQGX-ray2.80A/B/C/D/E/F/G1-80[»]
ProteinModelPortaliQ92993.
SMRiQ92993.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92993.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini227 – 504MYST-type HATPROSITE-ProRule annotationAdd BLAST278

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni368 – 513Interaction with ATF21 PublicationAdd BLAST146
Regioni370 – 372Acetyl-CoA binding1 Publication3
Regioni377 – 383Acetyl-CoA binding1 Publication7

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC MYST-type zinc finger.PROSITE-ProRule annotation
Contains 1 MYST-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri260 – 285C2HC MYST-typePROSITE-ProRule annotation1 PublicationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ92993.
KOiK11304.
OMAiLDMKKLQ.
OrthoDBiEOG091G0B73.
PhylomeDBiQ92993.
TreeFamiTF317619.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti382G → R in AAB18236 (PubMed:8607265).Curated1
Sequence conflicti382G → R in AAB02683 (PubMed:8607265).Curated1
Isoform 3 (identifier: Q92993-3)
Sequence conflicti32V → A no nucleotide entry (PubMed:12801643).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05945678P → T.Corresponds to variant rs11541271dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0091044V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3 and isoform 4. 2 Publications1
Alternative sequenceiVSP_00743896 – 147Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST52

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q92993-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EKONMR-A5-78[»]
2OU2X-ray2.30A227-506[»]
4QQGX-ray2.80A/B/C/D/E/F/G1-80[»]
ProteinModelPortaliQ92993.
SMRiQ92993.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115779. 223 interactors.
DIPiDIP-5998N.
IntActiQ92993. 131 interactors.
MINTiMINT-94861.
STRINGi9606.ENSP00000340330.

Chemistry databases

BindingDBiQ92993.
ChEMBLiCHEMBL5750.
GuidetoPHARMACOLOGYi2664.

PTM databases

iPTMnetiQ92993.
PhosphoSitePlusiQ92993.

Polymorphism and mutation databases

BioMutaiKAT5.
DMDMi30923328.

Proteomic databases

EPDiQ92993.
MaxQBiQ92993.
PaxDbiQ92993.
PeptideAtlasiQ92993.
PRIDEiQ92993.

Protocols and materials databases

DNASUi10524.
Structural Biology KnowledgebaseSearch...

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.4. human. [Q92993-1]

Organism-specific databases

CTDi10524.
DisGeNETi10524.
GeneCardsiKAT5.
HGNCiHGNC:5275. KAT5.
HPAiHPA016953.
MIMi601409. gene.
neXtProtiNX_Q92993.
OpenTargetsiENSG00000172977.
PharmGKBiPA162392746.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ92993.
KOiK11304.
OMAiLDMKKLQ.
OrthoDBiEOG091G0B73.
PhylomeDBiQ92993.
TreeFamiTF317619.

Enzyme and pathway databases

BioCyciZFISH:HS10602-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214847. HATs acetylate histones.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693548. Sensing of DNA Double Strand Breaks.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ92993.
SIGNORiQ92993.

Miscellaneous databases

ChiTaRSiKAT5. human.
EvolutionaryTraceiQ92993.
GeneWikiiKAT5.
GenomeRNAii10524.
PROiQ92993.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172977.
CleanExiHS_KAT5.
ExpressionAtlasiQ92993. baseline and differential.
GenevisibleiQ92993. HS.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.