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Q92794

- KAT6A_HUMAN

UniProt

Q92794 - KAT6A_HUMAN

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Protein

Histone acetyltransferase KAT6A

Gene

KAT6A

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei680 – 6801Proton donor/acceptorBy similarity
Binding sitei684 – 6841Acetyl-CoA1 Publication
Sitei813 – 8142Breakpoint for translocation to form KAT6A-ASXL2
Sitei1117 – 11182Breakpoint for translocation to form KAT6A-EP300 and KAT6A-NCOA2
Sitei1546 – 15472Breakpoint for translocation to form KAT6A-CREBBP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri206 – 26560PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri259 – 31355PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri538 – 56023C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. chromatin binding Source: Ensembl
  3. DNA binding Source: UniProtKB
  4. histone acetyltransferase activity Source: UniProtKB
  5. transcription coactivator activity Source: UniProtKB
  6. transcription factor binding Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. aorta morphogenesis Source: Ensembl
  2. cellular senescence Source: UniProtKB
  3. chromatin organization Source: Reactome
  4. DNA packaging Source: ProtInc
  5. embryonic hemopoiesis Source: Ensembl
  6. face morphogenesis Source: Ensembl
  7. heart morphogenesis Source: Ensembl
  8. histone acetylation Source: UniProtKB
  9. histone H3 acetylation Source: UniProtKB
  10. myeloid cell differentiation Source: UniProtKB
  11. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  12. negative regulation of transcription, DNA-templated Source: UniProtKB
  13. nucleosome assembly Source: InterPro
  14. positive regulation of transcription, DNA-templated Source: UniProtKB
  15. protein acetylation Source: UniProtKB
  16. somatic stem cell maintenance Source: Ensembl
  17. 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

ReactomeiREACT_172610. HATs acetylate histones.

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
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:13013. KAT6A.

Subcellular locationi

Nucleus. Nucleusnucleolus. Nucleusnucleoplasm. NucleusPML body
Note: Recruited into PML body after DNA damage.

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleosome Source: InterPro
  5. nucleus Source: UniProtKB
  6. 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; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv8(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.
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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi543 – 5431C → G: Abrogates HAT activity. 1 Publication
Mutagenesisi545 – 5451K → A: Reduced affinity for DNA. 1 Publication
Mutagenesisi657 – 6571G → E: Abrogates HAT activity. 1 Publication
Mutagenesisi727 – 7271I → E: Slightly reduced affinity for DNA. 1 Publication
Mutagenesisi732 – 7321H → D: Reduced affinity for DNA. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti370026. Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
PharmGKBiPA37592.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20042004Histone acetyltransferase KAT6APRO_0000051572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721N6-acetyllysineBy similarity
Modified residuei350 – 3501N6-acetyllysine2 Publications
Modified residuei355 – 3551N6-acetyllysine2 Publications
Modified residuei369 – 3691Phosphothreonine; by PKB/AKT11 Publication
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei604 – 6041N6-acetyllysine; by autocatalysis1 Publication
Modified residuei815 – 8151N6-acetyllysineBy similarity
Modified residuei899 – 8991PhosphotyrosineBy similarity
Modified residuei1007 – 10071N6-acetyllysine2 Publications
Modified residuei1113 – 11131Phosphoserine3 Publications

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/TP53.6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92794.
PaxDbiQ92794.
PRIDEiQ92794.

PTM databases

PhosphoSiteiQ92794.

Expressioni

Gene expression databases

BgeeiQ92794.
CleanExiHS_MYST3.
ExpressionAtlasiQ92794. baseline and differential.
GenevestigatoriQ92794.

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

Protein-protein interaction databases

BioGridi113703. 31 interactions.
IntActiQ92794. 6 interactions.
STRINGi9606.ENSP00000265713.

Structurei

Secondary structure

1
2004
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi195 – 1984Combined sources
Beta strandi207 – 2093Combined sources
Turni210 – 2123Combined sources
Turni231 – 2333Combined sources
Helixi239 – 2424Combined sources
Helixi246 – 2538Combined sources
Turni260 – 2623Combined sources
Turni266 – 2683Combined sources
Helixi275 – 2773Combined sources
Beta strandi278 – 2803Combined sources
Turni282 – 2843Combined sources
Beta strandi287 – 2893Combined sources
Helixi290 – 2923Combined sources
Beta strandi293 – 2953Combined sources
Turni308 – 3103Combined sources
Beta strandi511 – 5144Combined sources
Beta strandi517 – 5204Combined sources
Helixi529 – 5324Combined sources
Beta strandi535 – 5395Combined sources
Turni541 – 5433Combined sources
Beta strandi546 – 5494Combined sources
Helixi550 – 55910Combined sources
Beta strandi566 – 5738Combined sources
Beta strandi576 – 5827Combined sources
Turni583 – 5853Combined sources
Helixi587 – 59812Combined sources
Beta strandi613 – 62210Combined sources
Beta strandi625 – 63713Combined sources
Beta strandi642 – 6498Combined sources
Helixi651 – 6533Combined sources
Beta strandi655 – 6573Combined sources
Helixi658 – 67215Combined sources
Beta strandi677 – 6793Combined sources
Helixi685 – 70521Combined sources
Helixi713 – 7208Combined sources
Helixi724 – 73310Combined sources
Helixi750 – 75910Combined sources
Helixi771 – 7733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 204-313, 507-779.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 17177H15PROSITE-ProRule annotationAdd
BLAST
Domaini504 – 778275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 144144Required for activation of RUNX1-1Add
BLAST
Regioni52 – 166115Required for nuclear localizationAdd
BLAST
Regioni144 – 664521Interaction with PMLAdd
BLAST
Regioni312 – 664353Interaction with RUNX1-1Add
BLAST
Regioni488 – 778291CatalyticAdd
BLAST
Regioni507 – 810304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activityAdd
BLAST
Regioni645 – 6495Acetyl-CoA binding1 Publication
Regioni654 – 6607Acetyl-CoA binding1 Publication
Regioni1517 – 1741225Interaction with PMLAdd
BLAST
Regioni1517 – 1642126Interaction with RUNX1-2Add
BLAST
Regioni1913 – 194836Required for activation of RUNX1-2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi371 – 3799Poly-Ser
Compositional biasi788 – 80114Poly-GluAdd
BLAST
Compositional biasi989 – 9957Poly-Glu
Compositional biasi1019 – 10268Poly-Arg
Compositional biasi1069 – 107810Poly-Glu
Compositional biasi1147 – 11504Poly-Lys
Compositional biasi1221 – 124222Glu-richAdd
BLAST
Compositional biasi1267 – 130236Glu-richAdd
BLAST
Compositional biasi1411 – 14144Poly-Glu
Compositional biasi1593 – 15975Poly-Ser
Compositional biasi1643 – 170462Gln/Pro-richAdd
BLAST
Compositional biasi1897 – 197781Met-richAdd
BLAST

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-type zinc finger.Curated
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri206 – 26560PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri259 – 31355PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri538 – 56023C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ92794.
KOiK11305.
OMAiGAYQDCE.
OrthoDBiEOG7WHH8N.
PhylomeDBiQ92794.
TreeFamiTF106483.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF55729. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011K → R in AAC50662. (PubMed:8782817)Curated
Sequence conflicti401 – 4011K → R in BAD00088. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1341L → S.
Corresponds to variant rs3824276 [ dbSNP | Ensembl ].
VAR_047548

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_001092882.1. NM_001099412.1.
NP_001092883.1. NM_001099413.1.
NP_006757.2. NM_006766.3.
UniGeneiHs.491577.

Genome annotation databases

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

Polymorphism databases

DMDMi215274095.

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.
CCDSi CCDS6124.1.
RefSeqi NP_001092882.1. NM_001099412.1.
NP_001092883.1. NM_001099413.1.
NP_006757.2. NM_006766.3.
UniGenei Hs.491577.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M36 NMR - A 533-563 [» ]
2LN0 NMR - A 204-313 [» ]
2OZU X-ray 2.30 A 497-780 [» ]
2RC4 X-ray 3.00 A 501-784 [» ]
3V43 X-ray 1.47 A 204-313 [» ]
4LJN X-ray 3.00 A 194-323 [» ]
4LK9 X-ray 1.60 A 194-323 [» ]
4LKA X-ray 1.61 A 194-323 [» ]
4LLB X-ray 2.50 A/B 194-323 [» ]
ProteinModelPortali Q92794.
SMRi Q92794. Positions 204-313, 507-779.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113703. 31 interactions.
IntActi Q92794. 6 interactions.
STRINGi 9606.ENSP00000265713.

PTM databases

PhosphoSitei Q92794.

Polymorphism databases

DMDMi 215274095.

Proteomic databases

MaxQBi Q92794.
PaxDbi Q92794.
PRIDEi Q92794.

Protocols and materials databases

DNASUi 7994.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265713 ; ENSP00000265713 ; ENSG00000083168 .
ENST00000396930 ; ENSP00000380136 ; ENSG00000083168 .
ENST00000406337 ; ENSP00000385888 ; ENSG00000083168 .
GeneIDi 7994.
KEGGi hsa:7994.
UCSCi uc003xon.4. human.

Organism-specific databases

CTDi 7994.
GeneCardsi GC08M041786.
HGNCi HGNC:13013. KAT6A.
HPAi CAB017023.
HPA049811.
HPA053523.
MIMi 601408. gene.
neXtProti NX_Q92794.
Orphaneti 370026. Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
PharmGKBi PA37592.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOGENOMi HOG000234365.
HOVERGENi HBG052563.
InParanoidi Q92794.
KOi K11305.
OMAi GAYQDCE.
OrthoDBi EOG7WHH8N.
PhylomeDBi Q92794.
TreeFami TF106483.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi KAT6A. human.
EvolutionaryTracei Q92794.
GeneWikii MYST3.
GenomeRNAii 7994.
NextBioi 30540.
PROi Q92794.
SOURCEi Search...

Gene expression databases

Bgeei Q92794.
CleanExi HS_MYST3.
ExpressionAtlasi Q92794. baseline and differential.
Genevestigatori Q92794.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEi PS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein."
    Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G., Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M., Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.
    Nat. Genet. 14:33-41(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH CREBBP.
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "MOZ is fused to a novel Polycomb group gene in a therapy-related myelodysplastic syndrome with t(2;8)(p23;p11.2)."
    Hosoda F., Kitabayashi I., Kakazu N., Fukushima M., Aikawa Y., Abe T., Hibi S., Yagi T., Ohki M.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-813, CHROMOSOMAL TRANSLOCATION WITH ASXL2.
    Tissue: Bone marrow.
  4. "A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia."
    Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.
    Blood 91:3127-3133(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1089-1117, CHROMOSOMAL TRANSLOCATION WITH NCOA2.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1111-1128, CHROMOSOMAL TRANSLOCATION WITH EP300.
  6. "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein."
    Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.
    EMBO J. 20:7184-7196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUNX1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACETYLATION, CHROMOSOMAL TRANSLOCATION WITH CREBBP, FUNCTION.
  7. "The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase."
    Champagne N., Pelletier N., Yang X.-J.
    Oncogene 20:404-409(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, DOMAIN.
  8. "MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
    Pelletier N., Champagne N., Stifani S., Yang X.-J.
    Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUNX2, FUNCTION.
  9. "MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP."
    Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S., Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.
    Cancer Cell 3:259-271(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH NCOA2, MUTAGENESIS OF CYS-543 AND GLY-657.
  10. "Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ."
    Bristow C.A.P., Shore P.
    Nucleic Acids Res. 31:2735-2744(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function."
    Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D., Bellodi C., Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S., Heery D.M.
    Mol. Cell. Biol. 25:988-1002(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, CHROMOSOMAL TRANSLOCATION WITH NCOA2.
  12. "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, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-350; LYS-355 AND LYS-1007, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-1113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "MOZ increases p53 acetylation and premature senescence through its complex formation with PML."
    Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I., Prives C.
    Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PML AND TP53, PHOSPHORYLATION AT THR-369.
  20. "Solution structure of a CCCCCHC zinc finger from MOZ."
    Kwan A.H.Y., Gell D.A., Liew C.K., Mackay J.P.
    Submitted (JUN-2002) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 531-563.
  21. "The human monocytic leukemia zinc finger histone acetyltransferase domain contains DNA-binding activity implicated in chromatin targeting."
    Holbert M.A., Sikorski T., Carten J., Snowflack D., Hodawadekar S., Marmorstein R.
    J. Biol. Chem. 282:36603-36613(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-784 IN COMPLEXES WITH ACETYL-COA; HISTONE H3 AND HISTONE H4 AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING, MUTAGENESIS OF LYS-545; ILE-727 AND HIS-732.
  22. "The crystal structure of human MYST histone acetyltransferase 3 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 497-780 IN COMPLEX WITH ACETYL-COA, ACETYLATION AT LYS-604.

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 26, 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, 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

External Data

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