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Q8BZ21

- KAT6A_MOUSE

UniProt

Q8BZ21 - KAT6A_MOUSE

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Protein
Histone acetyltransferase KAT6A
Gene
Kat6a, Moz, Myst3
Organism
Mus musculus (Mouse)
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 By similarity. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML By similarity.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei603 – 6031 By similarity
Active sitei645 – 6451Nucleophile By similarity
Binding sitei683 – 6831Acetyl-CoA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri206 – 26560PHD-type 1
Add
BLAST
Zinc fingeri262 – 31352PHD-type 2
Add
BLAST
Zinc fingeri537 – 55923C2HC-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. acetyltransferase activity Source: UniProtKB
  3. chromatin binding Source: MGI
  4. histone acetyltransferase activity Source: UniProtKB
  5. protein binding Source: MGI
  6. transcription factor binding Source: UniProtKB
  7. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. aorta morphogenesis Source: MGI
  2. cellular senescence Source: UniProtKB
  3. embryonic hemopoiesis Source: MGI
  4. face morphogenesis Source: MGI
  5. heart morphogenesis Source: MGI
  6. histone H3 acetylation Source: UniProtKB
  7. histone acetylation Source: UniProtKB
  8. myeloid cell differentiation Source: UniProtKB
  9. negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. nucleosome assembly Source: InterPro
  12. positive regulation of transcription, DNA-templated Source: UniProtKB
  13. protein acetylation Source: UniProtKB
  14. somatic stem cell maintenance Source: MGI
  15. 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:2.3.1.48)
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 namesi
Name:Kat6a
Synonyms:Moz, Myst3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2442415. Kat6a.

Subcellular locationi

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

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. PML body Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleosome Source: InterPro
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20032003Histone acetyltransferase KAT6A
PRO_0000051573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei350 – 3501N6-acetyllysine By similarity
Modified residuei355 – 3551N6-acetyllysine By similarity
Modified residuei369 – 3691Phosphothreonine; by PKB/AKT1 By similarity
Modified residuei472 – 4721Phosphoserine By similarity
Modified residuei603 – 6031N6-acetyllysine; by autocatalysis By similarity
Modified residuei813 – 8131N6-acetyllysine1 Publication
Modified residuei816 – 8161N6-acetyllysine1 Publication
Modified residuei901 – 9011Phosphotyrosine By similarity
Modified residuei1007 – 10071N6-acetyllysine By similarity
Modified residuei1115 – 11151Phosphoserine By similarity

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

PRIDEiQ8BZ21.

PTM databases

PhosphoSiteiQ8BZ21.

Expressioni

Gene expression databases

GenevestigatoriQ8BZ21.

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.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8BZ21.
SMRiQ8BZ21. Positions 194-315, 506-778.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 17177H15
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 144144Required for activation of RUNX1-1 By similarity
Add
BLAST
Regioni52 – 166115Required for nuclear localization By similarity
Add
BLAST
Regioni144 – 663520Interaction with PML By similarity
Add
BLAST
Regioni312 – 663352Interaction with RUNX1-1 By similarity
Add
BLAST
Regioni487 – 777291Catalytic By similarity
Add
BLAST
Regioni506 – 809304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity By similarity
Add
BLAST
Regioni644 – 6485Acetyl-CoA binding By similarity
Regioni653 – 6597Acetyl-CoA binding By similarity
Regioni1511 – 1740230Interaction with PML By similarity
Add
BLAST
Regioni1511 – 1636126Interaction with RUNX1-2 By similarity
Add
BLAST
Regioni1912 – 194736Required for activation of RUNX1-2 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi989 – 9957Poly-Glu
Compositional biasi1019 – 10268Poly-Arg
Compositional biasi1066 – 107914Poly-Glu
Add
BLAST
Compositional biasi1107 – 11148Poly-Glu
Compositional biasi1149 – 117628Lys-rich
Add
BLAST
Compositional biasi1232 – 12387Poly-Glu
Compositional biasi1405 – 14084Poly-Glu
Compositional biasi1471 – 1591121Ser-rich
Add
BLAST
Compositional biasi1601 – 1703103Gln-rich
Add
BLAST
Compositional biasi1896 – 197681Met-rich
Add
BLAST

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.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BZ21.
PhylomeDBiQ8BZ21.

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.
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

MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ     50
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN 100
KLLKRAFEGL AETGGSTLKS IERFLKSQKD VSAACGGSAA PGFHQQLRLA 150
IKRAVGHGRL LKDGPLYRLN TKAASAEGKE GCESLSCLPP VSLLPHEKDK 200
PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS CLKFSPELTV 250
RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 300
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK 350
GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK 400
FNKKTKGLID GLTKFFTPSP DGRKARGEVV DYSEQYRIRK KGNRKSSTSD 450
WPTDNQDGWE SKQENEERLF GSQEIMTERD MELFRDIQEQ ALQKVGVTGP 500
PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE FCLKYMKSRT 550
ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL 600
DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP 650
QYQRKGYGRF LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE 700
CLYHQNDKQI SIKKLSKLTG VCPQDITSTL HHLRMLDFRS DQFVIIRREK 750
LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV SNSVVSEDED EEADEGEKEE 800
PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK ELASSSRLSK 850
QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ 900
YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ 950
LKKSPETLKC RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN 1000
SPPILTKPTL KRKKPILHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE 1050
DSDSERPMPR LEPTFEMEEE EEEEEEESEL FPRGYFHCLS SQDILRCQSS 1100
SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL EPDTSTPMKK 1150
KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG 1200
RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP 1250
LDSSNSPEAE PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT 1300
EANQNEDHDA DDEDEGHLDS LKTKEPEEQP AREDDKEEPG IQGSFLAANM 1350
QDSRENTKDK DEAEPDSEED QPSHEASVVS ETMPGSEEDH EEDSNTKEEL 1400
IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC EETLAACQTL 1450
QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE 1500
SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI 1550
ESTTENYENP SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT 1600
QQMANMGNSC SMLQQNTVQP AANCNIKSPQ TCVVERPPSN QQPPPPPPPP 1650
PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ QQPPPPQQQP QPPPPQQQPP 1700
LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA GSYSQPSATF 1750
SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA 1800
GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV 1850
KGHISIRSKS APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV 1900
NLMPTPAYNV NSMNMNTLNA MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM 1950
QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP SHHSYMNAAG VPKQSLNGPY 2000
MRR 2003
Length:2,003
Mass (Da):224,919
Last modified:July 5, 2005 - v2
Checksum:i93D0D687A1621B31
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS40294.1.
UniGenei Mm.182776.

3D structure databases

ProteinModelPortali Q8BZ21.
SMRi Q8BZ21. Positions 194-315, 506-778.
ModBasei Search...

PTM databases

PhosphoSitei Q8BZ21.

Proteomic databases

PRIDEi Q8BZ21.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:2442415. Kat6a.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000234365.
HOVERGENi HBG052563.
InParanoidi Q8BZ21.
PhylomeDBi Q8BZ21.

Miscellaneous databases

ChiTaRSi KAT6A. mouse.
PROi Q8BZ21.
SOURCEi Search...

Gene expression databases

Genevestigatori Q8BZ21.

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.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

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: July 9, 2014
This is version 107 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

External Data

Dasty 3

Similar proteinsi