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Protein

Histone acetyltransferase KAT6A

Gene

KAT6A

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

Functioni

Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML.6 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei680Proton donor/acceptorBy similarity1
Binding sitei684Acetyl-CoA1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri206 – 265PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri259 – 313PHD-type 2PROSITE-ProRule annotationAdd BLAST55
Zinc fingeri537 – 562C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

  • acetyltransferase activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular senescence Source: UniProtKB
  • DNA packaging Source: ProtInc
  • histone acetylation Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • myeloid cell differentiation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nucleosome assembly Source: InterPro
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein acetylation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS01435-MONOMER.
ReactomeiR-HSA-3214847. HATs acetylate histones.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
SIGNORiQ92794.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6A (EC:2.3.1.482 Publications)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
Short name:
MYST-3
Monocytic leukemia zinc finger protein
Runt-related transcription factor-binding protein 2
Zinc finger protein 220
Gene namesi
Name:KAT6A
Synonyms:MOZ, MYST3, RUNXBP2, ZNF220
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:13013. KAT6A.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: HPA
  • MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleosome Source: InterPro
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP (PubMed:8782817). Translocation t(8;22)(p11;q13) with EP300 (PubMed:10824998). KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription (PubMed:11742995). Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation (PubMed:12676584).

A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.

Mental retardation, autosomal dominant 32 (MRD32)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD32 patients manifest intellectual disability, dysmorphic facial features, delayed psychomotor development, and lack of speech.
See also OMIM:616268

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi543C → G: Abrogates HAT activity. 1 Publication1
Mutagenesisi545K → A: Reduced affinity for DNA. 1 Publication1
Mutagenesisi657G → E: Abrogates HAT activity. 1 Publication1
Mutagenesisi727I → E: Slightly reduced affinity for DNA. 1 Publication1
Mutagenesisi732H → D: Reduced affinity for DNA. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei813 – 814Breakpoint for translocation to form KAT6A-ASXL22
Sitei1117 – 1118Breakpoint for translocation to form KAT6A-EP300 and KAT6A-NCOA22
Sitei1546 – 1547Breakpoint for translocation to form KAT6A-CREBBP2

Keywords - Diseasei

Mental retardation, Proto-oncogene

Organism-specific databases

DisGeNETi7994.
MalaCardsiKAT6A.
MIMi616268. phenotype.
OpenTargetsiENSG00000083168.
Orphaneti370026. Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
PharmGKBiPA37592.

Polymorphism and mutation databases

BioMutaiKAT6A.
DMDMi215274095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515721 – 2004Histone acetyltransferase KAT6AAdd BLAST2004

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172N6-acetyllysineBy similarity1
Modified residuei350N6-acetyllysineCombined sources1
Modified residuei355N6-acetyllysineCombined sources1
Modified residuei369Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei420PhosphoserineCombined sources1
Modified residuei473PhosphoserineCombined sources1
Modified residuei604N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei787PhosphoserineBy similarity1
Modified residuei812PhosphoserineCombined sources1
Modified residuei815N6-acetyllysineBy similarity1
Modified residuei899PhosphotyrosineBy similarity1
Modified residuei941PhosphoserineCombined sources1
Modified residuei954PhosphoserineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei1007N6-acetyllysineCombined sources1
Modified residuei1089PhosphoserineCombined sources1
Modified residuei1090PhosphoserineCombined sources1
Modified residuei1113PhosphoserineCombined sources1

Post-translational modificationi

Autoacetylation at Lys-604 is required for proper function (By similarity). Autoacetylated.By similarity1 Publication
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92794.
MaxQBiQ92794.
PaxDbiQ92794.
PeptideAtlasiQ92794.
PRIDEiQ92794.

PTM databases

iPTMnetiQ92794.
PhosphoSitePlusiQ92794.

Expressioni

Gene expression databases

BgeeiENSG00000083168.
CleanExiHS_MYST3.
ExpressionAtlasiQ92794. baseline and differential.
GenevisibleiQ92794. HS.

Organism-specific databases

HPAiCAB017023.
HPA049811.
HPA053523.

Interactioni

Subunit structurei

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML (isoform PML-4) and this interaction positively regulates its acetylation activity towards p53/TP53.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KMT2AQ0316410EBI-948013,EBI-2638616
WDR5P619644EBI-948013,EBI-540834

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113703. 42 interactors.
IntActiQ92794. 21 interactors.
STRINGi9606.ENSP00000265713.

Structurei

Secondary structure

12004
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi195 – 198Combined sources4
Beta strandi207 – 209Combined sources3
Turni210 – 212Combined sources3
Turni231 – 233Combined sources3
Helixi239 – 242Combined sources4
Helixi246 – 253Combined sources8
Turni260 – 262Combined sources3
Turni266 – 268Combined sources3
Helixi275 – 277Combined sources3
Beta strandi278 – 280Combined sources3
Turni282 – 284Combined sources3
Beta strandi287 – 289Combined sources3
Helixi290 – 292Combined sources3
Beta strandi293 – 295Combined sources3
Turni308 – 310Combined sources3
Beta strandi511 – 514Combined sources4
Beta strandi517 – 520Combined sources4
Helixi529 – 532Combined sources4
Beta strandi535 – 539Combined sources5
Turni541 – 543Combined sources3
Beta strandi546 – 549Combined sources4
Helixi550 – 559Combined sources10
Beta strandi566 – 573Combined sources8
Beta strandi576 – 582Combined sources7
Turni583 – 585Combined sources3
Helixi587 – 598Combined sources12
Beta strandi613 – 622Combined sources10
Beta strandi625 – 637Combined sources13
Beta strandi642 – 649Combined sources8
Helixi651 – 653Combined sources3
Beta strandi655 – 657Combined sources3
Helixi658 – 672Combined sources15
Beta strandi677 – 679Combined sources3
Helixi685 – 705Combined sources21
Helixi713 – 720Combined sources8
Helixi724 – 733Combined sources10
Helixi750 – 759Combined sources10
Helixi771 – 773Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M36NMR-A533-563[»]
2LN0NMR-A204-313[»]
2OZUX-ray2.30A497-780[»]
2RC4X-ray3.00A501-784[»]
3V43X-ray1.47A204-313[»]
4LJNX-ray3.00A194-323[»]
4LK9X-ray1.60A194-323[»]
4LKAX-ray1.61A194-323[»]
4LLBX-ray2.50A/B194-323[»]
ProteinModelPortaliQ92794.
SMRiQ92794.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 171H15PROSITE-ProRule annotationAdd BLAST77
Domaini504 – 778MYST-type HATPROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 144Required for activation of RUNX1-1Add BLAST144
Regioni52 – 166Required for nuclear localizationAdd BLAST115
Regioni144 – 664Interaction with PML1 PublicationAdd BLAST521
Regioni312 – 664Interaction with RUNX1-1Add BLAST353
Regioni488 – 778CatalyticAdd BLAST291
Regioni507 – 810Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity1 PublicationAdd BLAST304
Regioni645 – 649Acetyl-CoA binding1 Publication5
Regioni654 – 660Acetyl-CoA binding1 Publication7
Regioni1517 – 1741Interaction with PML1 PublicationAdd BLAST225
Regioni1517 – 1642Interaction with RUNX1-2Add BLAST126
Regioni1913 – 1948Required for activation of RUNX1-2Add BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi371 – 379Poly-Ser9
Compositional biasi788 – 801Poly-GluAdd BLAST14
Compositional biasi989 – 995Poly-Glu7
Compositional biasi1019 – 1026Poly-Arg8
Compositional biasi1069 – 1078Poly-Glu10
Compositional biasi1147 – 1150Poly-Lys4
Compositional biasi1221 – 1242Glu-richAdd BLAST22
Compositional biasi1267 – 1302Glu-richAdd BLAST36
Compositional biasi1411 – 1414Poly-Glu4
Compositional biasi1593 – 1597Poly-Ser5
Compositional biasi1643 – 1704Gln/Pro-richAdd BLAST62
Compositional biasi1897 – 1977Met-richAdd BLAST81

Domaini

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.1 Publication

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC MYST-type zinc finger.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 1 MYST-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri206 – 265PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri259 – 313PHD-type 2PROSITE-ProRule annotationAdd BLAST55
Zinc fingeri537 – 562C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ92794.
KOiK11305.
OMAiEGAYQDC.
OrthoDBiEOG091G00D2.
PhylomeDBiQ92794.
TreeFamiTF106483.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. HAT_MYST-type.
IPR005818. Histone_H1/H5_H15.
IPR031280. KAT6A.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10615:SF26. PTHR10615:SF26. 3 hits.
PfamiPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ
60 70 80 90 100
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQNVDWN
110 120 130 140 150
KLIKRAVEGL AESGGSTLKS IERFLKGQKD VSALFGGSAA SGFHQQLRLA
160 170 180 190 200
IKRAIGHGRL LKDGPLYRLN TKATNVDGKE SCESLSCLPP VSLLPHEKDK
210 220 230 240 250
PVAEPIPICS FCLGTKEQNR EKKPEELISC ADCGNSGHPS CLKFSPELTV
260 270 280 290 300
RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
310 320 330 340 350
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YTNPIGRPKN RLKKQNTVSK
360 370 380 390 400
GPFSKVRTGP GRGRKRKITL SSQSASSSSE EGYLERIDGL DFCRDSNVSL
410 420 430 440 450
KFNKKTKGLI DGLTKFFTPS PDGRKARGEV VDYSEQYRIR KRGNRKSSTS
460 470 480 490 500
DWPTDNQDGW DGKQENEERL FGSQEIMTEK DMELFRDIQE QALQKVGVTG
510 520 530 540 550
PPDPQVRCPS VIEFGKYEIH TWYSSPYPQE YSRLPKLYLC EFCLKYMKSR
560 570 580 590 600
TILQQHMKKC GWFHPPANEI YRKNNISVFE VDGNVSTIYC QNLCLLAKLF
610 620 630 640 650
LDHKTLYYDV EPFLFYVLTQ NDVKGCHLVG YFSKEKHCQQ KYNVSCIMIL
660 670 680 690 700
PQYQRKGYGR FLIDFSYLLS KREGQAGSPE KPLSDLGRLS YMAYWKSVIL
710 720 730 740 750
ECLYHQNDKQ ISIKKLSKLT GICPQDITST LHHLRMLDFR SDQFVIIRRE
760 770 780 790 800
KLIQDHMAKL QLNLRPVDVD PECLRWTPVI VSNSVVSEEE EEEAEEGENE
810 820 830 840 850
EPQCQERELE ISVGKSVSHE NKEQDSYSVE SEKKPEVMAP VSSTRLSKQV
860 870 880 890 900
LPHDSLPANS QPSRRGRWGR KNRKTQERFG DKDSKLLLEE TSSAPQEQYG
910 920 930 940 950
ECGEKSEATQ EQYTESEEQL VASEEQPSQD GKPDLPKRRL SEGVEPWRGQ
960 970 980 990 1000
LKKSPEALKC RLTEGSERLP RRYSEGDRAV LRGFSESSEE EEEPESPRSS
1010 1020 1030 1040 1050
SPPILTKPTL KRKKPFLHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE
1060 1070 1080 1090 1100
DSDSERPMPR LEPTFEIDEE EEEEDENELF PREYFRRLSS QDVLRCQSSS
1110 1120 1130 1140 1150
KRKSKDEEED EESDDADDTP ILKPVSLLRK RDVKNSPLEP DTSTPLKKKK
1160 1170 1180 1190 1200
GWPKGKSRKP IHWKKRPGRK PGFKLSREIM PVSTQACVIE PIVSIPKAGR
1210 1220 1230 1240 1250
KPKIQESEET VEPKEDMPLP EERKEEEEMQ AEAEEAEEGE EEDAASSEVP
1260 1270 1280 1290 1300
AASPADSSNS PETETKEPEV EEEEEKPRVS EEQRQSEEEQ QELEEPEPEE
1310 1320 1330 1340 1350
EEDAAAETAQ NDDHDADDED DGHLESTKKK ELEEQPTRED VKEEPGVQES
1360 1370 1380 1390 1400
FLDANMQKSR EKIKDKEETE LDSEEEQPSH DTSVVSEQMA GSEDDHEEDS
1410 1420 1430 1440 1450
HTKEELIELK EEEEIPHSEL DLETVQAVQS LTQEESSEHE GAYQDCEETL
1460 1470 1480 1490 1500
AACQTLQSYT QADEDPQMSM VEDCHASEHN SPISSVQSHP SQSVRSVSSP
1510 1520 1530 1540 1550
NVPALESGYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF
1560 1570 1580 1590 1600
SDLGSIESTT ENYENPSSYD STMGGSICGN SSSQSSCSYG GLSSSSSLTQ
1610 1620 1630 1640 1650
SSCVVTQQMA SMGSSCSMMQ QSSVQPAANC SIKSPQSCVV ERPPSNQQQQ
1660 1670 1680 1690 1700
PPPPPPQQPQ PPPPQPQPAP QPPPPQQQPQ QQPQPQPQQP PPPPPPQQQP
1710 1720 1730 1740 1750
PLSQCSMNNS FTPAPMIMEI PESGSTGNIS IYERIPGDFG AGSYSQPSAT
1760 1770 1780 1790 1800
FSLAKLQQLT NTIMDPHAMP YSHSPAVTSY ATSVSLSNTG LAQLAPSHPL
1810 1820 1830 1840 1850
AGTPQAQATM TPPPNLASTT MNLTSPLLQC NMSATNIGIP HTQRLQGQMP
1860 1870 1880 1890 1900
VKGHISIRSK SAPLPSAAAH QQQLYGRSPS AVAMQAGPRA LAVQRGMNMG
1910 1920 1930 1940 1950
VNLMPTPAYN VNSMNMNTLN AMNSYRMTQP MMNSSYHSNP AYMNQTAQYP
1960 1970 1980 1990 2000
MQMQMGMMGS QAYTQQPMQP NPHGNMMYTG PSHHSYMNAA GVPKQSLNGP

YMRR
Length:2,004
Mass (Da):225,028
Last modified:November 25, 2008 - v2
Checksum:i78357EFAC4698A5F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti401K → R in AAC50662 (PubMed:8782817).Curated1
Sequence conflicti401K → R in BAD00088 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_047548134L → S.Corresponds to variant rs3824276dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47742 mRNA. Translation: AAC50662.1.
AC090571 Genomic DNA. No translation available.
AB084281 mRNA. Translation: BAD00088.1. Different termination.
CCDSiCCDS6124.1.
RefSeqiNP_006757.2. NM_006766.4.
XP_016869352.1. XM_017013863.1.
XP_016869353.1. XM_017013864.1.
UniGeneiHs.491577.

Genome annotation databases

EnsembliENST00000265713; ENSP00000265713; ENSG00000083168.
ENST00000396930; ENSP00000380136; ENSG00000083168.
ENST00000406337; ENSP00000385888; ENSG00000083168.
GeneIDi7994.
KEGGihsa:7994.
UCSCiuc003xon.4. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47742 mRNA. Translation: AAC50662.1.
AC090571 Genomic DNA. No translation available.
AB084281 mRNA. Translation: BAD00088.1. Different termination.
CCDSiCCDS6124.1.
RefSeqiNP_006757.2. NM_006766.4.
XP_016869352.1. XM_017013863.1.
XP_016869353.1. XM_017013864.1.
UniGeneiHs.491577.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M36NMR-A533-563[»]
2LN0NMR-A204-313[»]
2OZUX-ray2.30A497-780[»]
2RC4X-ray3.00A501-784[»]
3V43X-ray1.47A204-313[»]
4LJNX-ray3.00A194-323[»]
4LK9X-ray1.60A194-323[»]
4LKAX-ray1.61A194-323[»]
4LLBX-ray2.50A/B194-323[»]
ProteinModelPortaliQ92794.
SMRiQ92794.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113703. 42 interactors.
IntActiQ92794. 21 interactors.
STRINGi9606.ENSP00000265713.

PTM databases

iPTMnetiQ92794.
PhosphoSitePlusiQ92794.

Polymorphism and mutation databases

BioMutaiKAT6A.
DMDMi215274095.

Proteomic databases

EPDiQ92794.
MaxQBiQ92794.
PaxDbiQ92794.
PeptideAtlasiQ92794.
PRIDEiQ92794.

Protocols and materials databases

DNASUi7994.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265713; ENSP00000265713; ENSG00000083168.
ENST00000396930; ENSP00000380136; ENSG00000083168.
ENST00000406337; ENSP00000385888; ENSG00000083168.
GeneIDi7994.
KEGGihsa:7994.
UCSCiuc003xon.4. human.

Organism-specific databases

CTDi7994.
DisGeNETi7994.
GeneCardsiKAT6A.
HGNCiHGNC:13013. KAT6A.
HPAiCAB017023.
HPA049811.
HPA053523.
MalaCardsiKAT6A.
MIMi601408. gene.
616268. phenotype.
neXtProtiNX_Q92794.
OpenTargetsiENSG00000083168.
Orphaneti370026. Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
PharmGKBiPA37592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ92794.
KOiK11305.
OMAiEGAYQDC.
OrthoDBiEOG091G00D2.
PhylomeDBiQ92794.
TreeFamiTF106483.

Enzyme and pathway databases

BioCyciZFISH:HS01435-MONOMER.
ReactomeiR-HSA-3214847. HATs acetylate histones.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
SIGNORiQ92794.

Miscellaneous databases

ChiTaRSiKAT6A. human.
EvolutionaryTraceiQ92794.
GeneWikiiMYST3.
GenomeRNAii7994.
PROiQ92794.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000083168.
CleanExiHS_MYST3.
ExpressionAtlasiQ92794. baseline and differential.
GenevisibleiQ92794. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. HAT_MYST-type.
IPR005818. Histone_H1/H5_H15.
IPR031280. KAT6A.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10615:SF26. PTHR10615:SF26. 3 hits.
PfamiPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAT6A_HUMAN
AccessioniPrimary (citable) accession number: Q92794
Secondary accession number(s): Q76L81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 25, 2008
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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.