Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone acetyltransferase KAT6A

Gene

Kat6a

Organism
Mus musculus (Mouse)
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 (By similarity). Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML (By similarity).By similarity1 Publication

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei679Proton donor/acceptorBy similarity1
Binding sitei683Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri206 – 265PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri262 – 313PHD-type 2PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri536 – 561C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

GO - Biological processi

  • aorta morphogenesis Source: MGI
  • cellular senescence Source: UniProtKB
  • embryonic hemopoiesis Source: MGI
  • face morphogenesis Source: MGI
  • heart morphogenesis Source: MGI
  • histone acetylation Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • myeloid cell differentiation Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nucleosome assembly Source: InterPro
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein acetylation Source: UniProtKB
  • somatic stem cell population maintenance Source: MGI
  • 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

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6A (EC:2.3.1.48By similarity)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
Short name:
MYST-3
Monocytic leukemia zinc finger homolog
Monocytic leukemia zinc finger protein
Gene namesi
Name:Kat6a
Synonyms:Moz, Myst3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2442415. Kat6a.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Nucleusnucleolus By similarity
  • Nucleusnucleoplasm By similarity
  • NucleusPML body By similarity

  • Note: Recruited into PML body after DNA damage.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515731 – 2003Histone acetyltransferase KAT6AAdd BLAST2003

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172N6-acetyllysineCombined sources1
Modified residuei350N6-acetyllysineBy similarity1
Modified residuei355N6-acetyllysineBy similarity1
Modified residuei369Phosphothreonine; by PKB/AKT1By similarity1
Modified residuei419PhosphoserineBy similarity1
Modified residuei472PhosphoserineBy similarity1
Modified residuei603N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei786PhosphoserineCombined sources1
Modified residuei813N6-acetyllysineCombined sources1
Modified residuei816N6-acetyllysineCombined sources1
Modified residuei901PhosphotyrosineBy similarity1
Modified residuei941PhosphoserineBy similarity1
Modified residuei954PhosphoserineBy similarity1
Modified residuei1007N6-acetyllysineBy similarity1
Modified residuei1090PhosphoserineBy similarity1
Modified residuei1091PhosphoserineBy similarity1
Modified residuei1115PhosphoserineBy similarity1

Post-translational modificationi

Autoacetylated. Autoacetylation at Lys-603 is required for proper function.By similarity
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BZ21.
MaxQBiQ8BZ21.
PaxDbiQ8BZ21.
PRIDEiQ8BZ21.

PTM databases

iPTMnetiQ8BZ21.
PhosphoSitePlusiQ8BZ21.

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 (By similarity). Interacts with RUNX2 (By similarity). Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with p53/TP53 (By similarity). Interacts with PML and this interaction positively regulates its acetylation activity towards p53/TP53 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8BZ21. 1 interactor.
STRINGi10090.ENSMUSP00000038181.

Structurei

3D structure databases

ProteinModelPortaliQ8BZ21.
SMRiQ8BZ21.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 171H15PROSITE-ProRule annotationAdd BLAST77
Domaini503 – 777MYST-type HATPROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 144Required for activation of RUNX1-1By similarityAdd BLAST144
Regioni52 – 166Required for nuclear localizationBy similarityAdd BLAST115
Regioni144 – 663Interaction with PMLBy similarityAdd BLAST520
Regioni312 – 663Interaction with RUNX1-1By similarityAdd BLAST352
Regioni487 – 777CatalyticBy similarityAdd BLAST291
Regioni506 – 809Mediates interaction with BRPF1, required for histone H3 acetyltransferase activityBy similarityAdd BLAST304
Regioni644 – 648Acetyl-CoA bindingBy similarity5
Regioni653 – 659Acetyl-CoA bindingBy similarity7
Regioni1511 – 1740Interaction with PMLBy similarityAdd BLAST230
Regioni1511 – 1636Interaction with RUNX1-2By similarityAdd BLAST126
Regioni1912 – 1947Required for activation of RUNX1-2By similarityAdd BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi989 – 995Poly-Glu7
Compositional biasi1019 – 1026Poly-Arg8
Compositional biasi1066 – 1079Poly-GluAdd BLAST14
Compositional biasi1107 – 1114Poly-Glu8
Compositional biasi1149 – 1176Lys-richAdd BLAST28
Compositional biasi1232 – 1238Poly-Glu7
Compositional biasi1405 – 1408Poly-Glu4
Compositional biasi1471 – 1591Ser-richAdd BLAST121
Compositional biasi1601 – 1703Gln-richAdd BLAST103
Compositional biasi1896 – 1976Met-richAdd BLAST81

Domaini

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.By similarity

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 fingeri262 – 313PHD-type 2PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri536 – 561C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BZ21.
PhylomeDBiQ8BZ21.

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.

Q8BZ21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ
60 70 80 90 100
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN
110 120 130 140 150
KLLKRAFEGL AETGGSTLKS IERFLKSQKD VSAACGGSAA PGFHQQLRLA
160 170 180 190 200
IKRAVGHGRL LKDGPLYRLN TKAASAEGKE GCESLSCLPP VSLLPHEKDK
210 220 230 240 250
PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS CLKFSPELTV
260 270 280 290 300
RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
310 320 330 340 350
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK
360 370 380 390 400
GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK
410 420 430 440 450
FNKKTKGLID GLTKFFTPSP DGRKARGEVV DYSEQYRIRK KGNRKSSTSD
460 470 480 490 500
WPTDNQDGWE SKQENEERLF GSQEIMTERD MELFRDIQEQ ALQKVGVTGP
510 520 530 540 550
PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE FCLKYMKSRT
560 570 580 590 600
ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL
610 620 630 640 650
DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP
660 670 680 690 700
QYQRKGYGRF LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE
710 720 730 740 750
CLYHQNDKQI SIKKLSKLTG VCPQDITSTL HHLRMLDFRS DQFVIIRREK
760 770 780 790 800
LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV SNSVVSEDED EEADEGEKEE
810 820 830 840 850
PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK ELASSSRLSK
860 870 880 890 900
QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ
910 920 930 940 950
YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ
960 970 980 990 1000
LKKSPETLKC RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN
1010 1020 1030 1040 1050
SPPILTKPTL KRKKPILHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE
1060 1070 1080 1090 1100
DSDSERPMPR LEPTFEMEEE EEEEEEESEL FPRGYFHCLS SQDILRCQSS
1110 1120 1130 1140 1150
SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL EPDTSTPMKK
1160 1170 1180 1190 1200
KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG
1210 1220 1230 1240 1250
RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP
1260 1270 1280 1290 1300
LDSSNSPEAE PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT
1310 1320 1330 1340 1350
EANQNEDHDA DDEDEGHLDS LKTKEPEEQP AREDDKEEPG IQGSFLAANM
1360 1370 1380 1390 1400
QDSRENTKDK DEAEPDSEED QPSHEASVVS ETMPGSEEDH EEDSNTKEEL
1410 1420 1430 1440 1450
IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC EETLAACQTL
1460 1470 1480 1490 1500
QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE
1510 1520 1530 1540 1550
SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI
1560 1570 1580 1590 1600
ESTTENYENP SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT
1610 1620 1630 1640 1650
QQMANMGNSC SMLQQNTVQP AANCNIKSPQ TCVVERPPSN QQPPPPPPPP
1660 1670 1680 1690 1700
PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ QQPPPPQQQP QPPPPQQQPP
1710 1720 1730 1740 1750
LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA GSYSQPSATF
1760 1770 1780 1790 1800
SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA
1810 1820 1830 1840 1850
GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV
1860 1870 1880 1890 1900
KGHISIRSKS APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV
1910 1920 1930 1940 1950
NLMPTPAYNV NSMNMNTLNA MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM
1960 1970 1980 1990 2000
QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP SHHSYMNAAG VPKQSLNGPY

MRR
Length:2,003
Mass (Da):224,919
Last modified:July 5, 2005 - v2
Checksum:i93D0D687A1621B31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC115361 Genomic DNA. No translation available.
AK028058 mRNA. Translation: BAC25728.1.
AK036885 mRNA. Translation: BAC29621.1.
AK039615 mRNA. Translation: BAC30401.1.
AK054322 mRNA. Translation: BAC35729.1.
CCDSiCCDS40294.1.
UniGeneiMm.182776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC115361 Genomic DNA. No translation available.
AK028058 mRNA. Translation: BAC25728.1.
AK036885 mRNA. Translation: BAC29621.1.
AK039615 mRNA. Translation: BAC30401.1.
AK054322 mRNA. Translation: BAC35729.1.
CCDSiCCDS40294.1.
UniGeneiMm.182776.

3D structure databases

ProteinModelPortaliQ8BZ21.
SMRiQ8BZ21.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BZ21. 1 interactor.
STRINGi10090.ENSMUSP00000038181.

PTM databases

iPTMnetiQ8BZ21.
PhosphoSitePlusiQ8BZ21.

Proteomic databases

EPDiQ8BZ21.
MaxQBiQ8BZ21.
PaxDbiQ8BZ21.
PRIDEiQ8BZ21.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:2442415. Kat6a.

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BZ21.
PhylomeDBiQ8BZ21.

Miscellaneous databases

ChiTaRSiKat6a. mouse.
PROiQ8BZ21.
SOURCEiSearch...

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_MOUSE
AccessioniPrimary (citable) accession number: Q8BZ21
Secondary accession number(s): Q8BW52, Q8BYH1, Q8C1F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.