Q8BZ21 (KAT6A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Kat6a
Synonyms:	Moz, Myst3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2003 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › nucleolus By similarity. Nucleus › nucleoplasm By similarity. Nucleus › PML 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Repressor Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aorta 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 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-dependent Inferred from sequence or structural similarity. Source: UniProtKB nucleosome assembly Inferred from electronic annotation. Source: InterPro positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB somatic stem cell maintenance Inferred from mutant phenotype PubMed 16651658PubMed 16702405. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MOZ/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
Molecular_function	DNA binding 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2003	2003	Histone acetyltransferase KAT6A		PRO_0000051573
Regions
	Domain	95 – 171	77	H15
	Zinc finger	206 – 265	60	PHD-type 1
	Zinc finger	262 – 313	52	PHD-type 2
	Zinc finger	537 – 559	23	C2HC-type
	Region	1 – 144	144	Required for activation of RUNX1-1 By similarity
	Region	52 – 166	115	Required for nuclear localization By similarity
	Region	144 – 663	520	Interaction with PML By similarity
	Region	312 – 663	352	Interaction with RUNX1-1 By similarity
	Region	487 – 777	291	Catalytic By similarity
	Region	506 – 809	304	Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity By similarity
	Region	644 – 648	5	Acetyl-CoA binding By similarity
	Region	653 – 659	7	Acetyl-CoA binding By similarity
	Region	1511 – 1740	230	Interaction with PML By similarity
	Region	1511 – 1636	126	Interaction with RUNX1-2 By similarity
	Region	1912 – 1947	36	Required for activation of RUNX1-2 By similarity
	Compositional bias	989 – 995	7	Poly-Glu
	Compositional bias	1019 – 1026	8	Poly-Arg
	Compositional bias	1066 – 1079	14	Poly-Glu
	Compositional bias	1107 – 1114	8	Poly-Glu
	Compositional bias	1149 – 1176	28	Lys-rich
	Compositional bias	1232 – 1238	7	Poly-Glu
	Compositional bias	1405 – 1408	4	Poly-Glu
	Compositional bias	1471 – 1591	121	Ser-rich
	Compositional bias	1601 – 1703	103	Gln-rich
	Compositional bias	1896 – 1976	81	Met-rich
Sites
	Active site	603	1	By similarity
	Active site	645	1	Nucleophile By similarity
	Binding site	683	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	350	1	N6-acetyllysine By similarity
	Modified residue	355	1	N6-acetyllysine By similarity
	Modified residue	369	1	Phosphothreonine; by PKB/AKT1 By similarity
	Modified residue	472	1	Phosphoserine By similarity
	Modified residue	603	1	N6-acetyllysine; by autocatalysis By similarity
	Modified residue	1007	1	N6-acetyllysine By similarity
	Modified residue	1115	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8BZ21 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 93D0D687A1621B31	FASTA	2,003	224,919
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1115, MASS SPECTROMETRY. Tissue: Melanoma.
+	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.
IPI	IPI00380122.
UniGene	Mm.182776.
3D structure databases
ProteinModelPortal	Q8BZ21.
SMR	Q8BZ21. Positions 204-313, 506-778.
ModBase	Search...
PTM databases
PhosphoSite	Q8BZ21.
Proteomic databases
PRIDE	Q8BZ21.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:2442415. Kat6a.
Phylogenomic databases
eggNOG	COG5027.
HOGENOM	HOG000234365.
HOVERGEN	HBG052563.
InParanoid	Q8BZ21.
OrthoDB	EOG48KR9D.
Gene expression databases
Genevestigator	Q8BZ21.
GermOnline	ENSMUSG00000031540. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 2 hits. 3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR005818. Histone_H1/H5. IPR002717. MOZ_SAS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF01853. MOZ_SAS. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00526. H15. 1 hit. SM00249. PHD. 2 hits. SM00184. RING. 2 hits. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	PS51504. H15. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KAT6A. mouse.
SOURCE	Search...

Entry information

Entry name

KAT6A_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program