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Q8BZ21 (KAT6A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 homolog
Monocytic leukemia zinc finger protein
Gene names
Name:Kat6a
Synonyms:Moz, Myst3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2003 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

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

Subunit structure

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. Ref.3

Subcellular location

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

Domain

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

Post-translational modification

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.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Contains 2 PHD-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Repressor
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaorta morphogenesis

Inferred from mutant phenotype PubMed 22921202. Source: MGI

cellular senescence

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic hemopoiesis

Inferred from mutant phenotype PubMed 16702405. Source: MGI

face morphogenesis

Inferred from mutant phenotype PubMed 22921202. Source: MGI

heart morphogenesis

Inferred from mutant phenotype PubMed 22921202. Source: MGI

histone H3 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 22921202. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 16651658PubMed 16702405. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMOZ/MORF histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

PML body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleosome

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from genetic interaction PubMed 22921202. Source: MGI

histone acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20032003Histone acetyltransferase KAT6A
PRO_0000051573

Regions

Domain95 – 17177H15
Zinc finger206 – 26560PHD-type 1
Zinc finger262 – 31352PHD-type 2
Zinc finger537 – 55923C2HC-type
Region1 – 144144Required for activation of RUNX1-1 By similarity
Region52 – 166115Required for nuclear localization By similarity
Region144 – 663520Interaction with PML By similarity
Region312 – 663352Interaction with RUNX1-1 By similarity
Region487 – 777291Catalytic By similarity
Region506 – 809304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity By similarity
Region644 – 6485Acetyl-CoA binding By similarity
Region653 – 6597Acetyl-CoA binding By similarity
Region1511 – 1740230Interaction with PML By similarity
Region1511 – 1636126Interaction with RUNX1-2 By similarity
Region1912 – 194736Required for activation of RUNX1-2 By similarity
Compositional bias989 – 9957Poly-Glu
Compositional bias1019 – 10268Poly-Arg
Compositional bias1066 – 107914Poly-Glu
Compositional bias1107 – 11148Poly-Glu
Compositional bias1149 – 117628Lys-rich
Compositional bias1232 – 12387Poly-Glu
Compositional bias1405 – 14084Poly-Glu
Compositional bias1471 – 1591121Ser-rich
Compositional bias1601 – 1703103Gln-rich
Compositional bias1896 – 197681Met-rich

Sites

Active site6031 By similarity
Active site6451Nucleophile By similarity
Binding site6831Acetyl-CoA By similarity

Amino acid modifications

Modified residue1721N6-acetyllysine Ref.5
Modified residue3501N6-acetyllysine By similarity
Modified residue3551N6-acetyllysine By similarity
Modified residue3691Phosphothreonine; by PKB/AKT1 By similarity
Modified residue4721Phosphoserine By similarity
Modified residue6031N6-acetyllysine; by autocatalysis By similarity
Modified residue8131N6-acetyllysine Ref.5
Modified residue8161N6-acetyllysine Ref.5
Modified residue9011Phosphotyrosine By similarity
Modified residue10071N6-acetyllysine By similarity
Modified residue11151Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BZ21 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 93D0D687A1621B31

FASTA2,003224,919
        10         20         30         40         50         60 
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ LELSVKDGTI 

        70         80         90        100        110        120 
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN KLLKRAFEGL AETGGSTLKS 

       130        140        150        160        170        180 
IERFLKSQKD VSAACGGSAA PGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAASAEGKE 

       190        200        210        220        230        240 
GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS 

       250        260        270        280        290        300 
CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 

       310        320        330        340        350        360 
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK GPFSKVRTGP 

       370        380        390        400        410        420 
GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK FNKKTKGLID GLTKFFTPSP 

       430        440        450        460        470        480 
DGRKARGEVV DYSEQYRIRK KGNRKSSTSD WPTDNQDGWE SKQENEERLF GSQEIMTERD 

       490        500        510        520        530        540 
MELFRDIQEQ ALQKVGVTGP PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE 

       550        560        570        580        590        600 
FCLKYMKSRT ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL 

       610        620        630        640        650        660 
DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP QYQRKGYGRF 

       670        680        690        700        710        720 
LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE CLYHQNDKQI SIKKLSKLTG 

       730        740        750        760        770        780 
VCPQDITSTL HHLRMLDFRS DQFVIIRREK LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV 

       790        800        810        820        830        840 
SNSVVSEDED EEADEGEKEE PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK 

       850        860        870        880        890        900 
ELASSSRLSK QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ 

       910        920        930        940        950        960 
YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ LKKSPETLKC 

       970        980        990       1000       1010       1020 
RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN SPPILTKPTL KRKKPILHRR 

      1030       1040       1050       1060       1070       1080 
RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEMEEE EEEEEEESEL 

      1090       1100       1110       1120       1130       1140 
FPRGYFHCLS SQDILRCQSS SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL 

      1150       1160       1170       1180       1190       1200 
EPDTSTPMKK KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG 

      1210       1220       1230       1240       1250       1260 
RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP LDSSNSPEAE 

      1270       1280       1290       1300       1310       1320 
PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT EANQNEDHDA DDEDEGHLDS 

      1330       1340       1350       1360       1370       1380 
LKTKEPEEQP AREDDKEEPG IQGSFLAANM QDSRENTKDK DEAEPDSEED QPSHEASVVS 

      1390       1400       1410       1420       1430       1440 
ETMPGSEEDH EEDSNTKEEL IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC 

      1450       1460       1470       1480       1490       1500 
EETLAACQTL QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE 

      1510       1520       1530       1540       1550       1560 
SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI ESTTENYENP 

      1570       1580       1590       1600       1610       1620 
SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT QQMANMGNSC SMLQQNTVQP 

      1630       1640       1650       1660       1670       1680 
AANCNIKSPQ TCVVERPPSN QQPPPPPPPP PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ 

      1690       1700       1710       1720       1730       1740 
QQPPPPQQQP QPPPPQQQPP LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA 

      1750       1760       1770       1780       1790       1800 
GSYSQPSATF SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA 

      1810       1820       1830       1840       1850       1860 
GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV KGHISIRSKS 

      1870       1880       1890       1900       1910       1920 
APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV NLMPTPAYNV NSMNMNTLNA 

      1930       1940       1950       1960       1970       1980 
MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP 

      1990       2000 
SHHSYMNAAG VPKQSLNGPY MRR 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1010.
Strain: C57BL/6J.
Tissue: Cerebellum, Ovary, Spinal cord and Vagina.
[3]"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, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-813 AND LYS-816, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
UniGeneMm.182776.

3D structure databases

ProteinModelPortalQ8BZ21.
SMRQ8BZ21. Positions 98-163, 194-315, 506-778.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BZ21.

Proteomic databases

PRIDEQ8BZ21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:2442415. Kat6a.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000234365.
HOVERGENHBG052563.
InParanoidQ8BZ21.
PhylomeDBQ8BZ21.

Gene expression databases

GenevestigatorQ8BZ21.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProIPR016181. 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]
PfamPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT6A. mouse.
PROQ8BZ21.
SOURCESearch...

Entry information

Entry nameKAT6A_MOUSE
AccessionPrimary (citable) accession number: Q8BZ21
Secondary accession number(s): Q8BW52, Q8BYH1, Q8C1F3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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