Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q92794

- KAT6A_HUMAN

UniProt

Q92794 - KAT6A_HUMAN

Protein

Histone acetyltransferase KAT6A

Gene

KAT6A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei604 – 6041By similarity
    Active sitei646 – 6461NucleophileBy similarity
    Binding sitei684 – 6841Acetyl-CoA
    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. protein binding Source: UniProtKB
    6. transcription coactivator activity Source: UniProtKB
    7. transcription factor binding Source: UniProtKB
    8. 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

    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:2.3.1.48)
    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

    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 autocatalysisBy similarity
    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 similarity
    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

    ArrayExpressiQ92794.
    BgeeiQ92794.
    CleanExiHS_MYST3.
    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. 30 interactions.
    IntActiQ92794. 6 interactions.
    STRINGi9606.ENSP00000265713.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 binding
    Regioni654 – 6607Acetyl-CoA binding
    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.
    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

    MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ     50
    LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQNVDWN 100
    KLIKRAVEGL AESGGSTLKS IERFLKGQKD VSALFGGSAA SGFHQQLRLA 150
    IKRAIGHGRL LKDGPLYRLN TKATNVDGKE SCESLSCLPP VSLLPHEKDK 200
    PVAEPIPICS FCLGTKEQNR EKKPEELISC ADCGNSGHPS CLKFSPELTV 250
    RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 300
    PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YTNPIGRPKN RLKKQNTVSK 350
    GPFSKVRTGP GRGRKRKITL SSQSASSSSE EGYLERIDGL DFCRDSNVSL 400
    KFNKKTKGLI DGLTKFFTPS PDGRKARGEV VDYSEQYRIR KRGNRKSSTS 450
    DWPTDNQDGW DGKQENEERL FGSQEIMTEK DMELFRDIQE QALQKVGVTG 500
    PPDPQVRCPS VIEFGKYEIH TWYSSPYPQE YSRLPKLYLC EFCLKYMKSR 550
    TILQQHMKKC GWFHPPANEI YRKNNISVFE VDGNVSTIYC QNLCLLAKLF 600
    LDHKTLYYDV EPFLFYVLTQ NDVKGCHLVG YFSKEKHCQQ KYNVSCIMIL 650
    PQYQRKGYGR FLIDFSYLLS KREGQAGSPE KPLSDLGRLS YMAYWKSVIL 700
    ECLYHQNDKQ ISIKKLSKLT GICPQDITST LHHLRMLDFR SDQFVIIRRE 750
    KLIQDHMAKL QLNLRPVDVD PECLRWTPVI VSNSVVSEEE EEEAEEGENE 800
    EPQCQERELE ISVGKSVSHE NKEQDSYSVE SEKKPEVMAP VSSTRLSKQV 850
    LPHDSLPANS QPSRRGRWGR KNRKTQERFG DKDSKLLLEE TSSAPQEQYG 900
    ECGEKSEATQ EQYTESEEQL VASEEQPSQD GKPDLPKRRL SEGVEPWRGQ 950
    LKKSPEALKC RLTEGSERLP RRYSEGDRAV LRGFSESSEE EEEPESPRSS 1000
    SPPILTKPTL KRKKPFLHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE 1050
    DSDSERPMPR LEPTFEIDEE EEEEDENELF PREYFRRLSS QDVLRCQSSS 1100
    KRKSKDEEED EESDDADDTP ILKPVSLLRK RDVKNSPLEP DTSTPLKKKK 1150
    GWPKGKSRKP IHWKKRPGRK PGFKLSREIM PVSTQACVIE PIVSIPKAGR 1200
    KPKIQESEET VEPKEDMPLP EERKEEEEMQ AEAEEAEEGE EEDAASSEVP 1250
    AASPADSSNS PETETKEPEV EEEEEKPRVS EEQRQSEEEQ QELEEPEPEE 1300
    EEDAAAETAQ NDDHDADDED DGHLESTKKK ELEEQPTRED VKEEPGVQES 1350
    FLDANMQKSR EKIKDKEETE LDSEEEQPSH DTSVVSEQMA GSEDDHEEDS 1400
    HTKEELIELK EEEEIPHSEL DLETVQAVQS LTQEESSEHE GAYQDCEETL 1450
    AACQTLQSYT QADEDPQMSM VEDCHASEHN SPISSVQSHP SQSVRSVSSP 1500
    NVPALESGYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF 1550
    SDLGSIESTT ENYENPSSYD STMGGSICGN SSSQSSCSYG GLSSSSSLTQ 1600
    SSCVVTQQMA SMGSSCSMMQ QSSVQPAANC SIKSPQSCVV ERPPSNQQQQ 1650
    PPPPPPQQPQ PPPPQPQPAP QPPPPQQQPQ QQPQPQPQQP PPPPPPQQQP 1700
    PLSQCSMNNS FTPAPMIMEI PESGSTGNIS IYERIPGDFG AGSYSQPSAT 1750
    FSLAKLQQLT NTIMDPHAMP YSHSPAVTSY ATSVSLSNTG LAQLAPSHPL 1800
    AGTPQAQATM TPPPNLASTT MNLTSPLLQC NMSATNIGIP HTQRLQGQMP 1850
    VKGHISIRSK SAPLPSAAAH QQQLYGRSPS AVAMQAGPRA LAVQRGMNMG 1900
    VNLMPTPAYN VNSMNMNTLN AMNSYRMTQP MMNSSYHSNP AYMNQTAQYP 1950
    MQMQMGMMGS QAYTQQPMQP NPHGNMMYTG PSHHSYMNAA GVPKQSLNGP 2000
    YMRR 2004
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 30 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.
    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

    ArrayExpressi Q92794.
    Bgeei Q92794.
    CleanExi HS_MYST3.
    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

    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, ENZYME 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: ENZYME 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 COENZYME A; 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 ACETYLCOENZYME A.

    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: October 1, 2014
    This is version 157 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

    Dasty 3