Q9D1P2 (KAT8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT8
EC=2.3.1.48

Alternative name(s):
Lysine acetyltransferase 8
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1
Short name=MYST-1

Gene names

Name:	Kat8
Synonyms:	Mof, Myst1

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	458 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex By similarity.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with the chromodomain of MORF4L1/MRG15. Interacts with ATM through the chromodomain By similarity.
Subcellular location	Nucleus. Chromosome By similarity.
Post-translational modification	Autoacetylation at Lys-274 is required for proper function By similarity.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger. Contains 1 chromo domain.
Sequence caution	The sequence BAC25539.1 differs from that shown. Reason: Frameshift at position 236.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H4-K16 acetylation Inferred from sequence or structural similarity. Source: UniProtKB histone H4-K5 acetylation Inferred from sequence or structural similarity. Source: UniProtKB histone H4-K8 acetylation Inferred from sequence or structural similarity. Source: UniProtKB myeloid cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1 complex Inferred from sequence or structural similarity. Source: UniProtKB MSL complex Inferred from sequence or structural similarity. Source: UniProtKB kinetochore Inferred from direct assay PubMed 14519686. Source: MGI
Molecular_function	acetyltransferase activity Inferred from direct assay PubMed 19578370. Source: UniProtKB histone acetyltransferase activity (H4-K16 specific) Inferred from electronic annotation. Source: Compara histone acetyltransferase activity (H4-K5 specific) Inferred from electronic annotation. Source: Compara histone acetyltransferase activity (H4-K8 specific) Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9D1P2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9D1P2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     155-194: TYAEMDPTTA...GNYEIDAWYF → VLAPPFSGPS...LFTYEKILSL
     195-458: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 458

458

Histone acetyltransferase KAT8

PRO_0000051567

Regions

Domain

69 – 123

55

Chromo

Zinc finger

208 – 230

23

C2HC-type

Region

174 – 458

285

Sufficient for interaction with KANSL1 By similarity

Region

324 – 330

7

Acetyl-CoA binding By similarity

Sites

Active site

274

1

By similarity

Active site

316

1

Nucleophile By similarity

Binding site

319

1

Acetyl-CoA By similarity

Binding site

354

1

Acetyl-CoA By similarity

Amino acid modifications

Modified residue

37

1

Phosphoserine Ref.3

Modified residue

42

1

Phosphoserine Ref.3

Modified residue

113

1

N6-acetyllysine By similarity

Modified residue

274

1

N6-acetyllysine; by autocatalysis By similarity

Natural variations

Alternative sequence

155 – 194

40

TYAEM…DAWYF → VLAPPFSGPSQQSHSNSHVK AGSMPGFFSRLFTYEKILSL in isoform 2.

VSP_014580

Alternative sequence

195 – 458

264

Missing in isoform 2.

VSP_014581

Experimental info

Sequence conflict

385

1

L → F in AAH36284. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

458

Helix Strand Turn

Details...

Beta strand

59 – 65

7

Turn

66 – 68

3

Beta strand

69 – 81

13

Turn

82 – 85

4

Beta strand

86 – 92

7

Turn

94 – 96

3

Beta strand

102 – 104

3

Turn

106 – 108

3

Turn

112 – 114

3

Beta strand

115 – 117

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: FA25E0C8D7E46CEC	FASTA	458	52,574
	10 20 30 40 50 60 MAAQGATAAV AATTSGTVGE GEPGPGENAA VEGPARSPGR VSPPTPARGE PEVTVEIGET 70 80 90 100 110 120 YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ 130 140 150 160 170 180 KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD 190 200 210 220 230 240 KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKFE KSYRFHLGQC QWRQPPGKEI 250 260 270 280 290 300 YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG 310 320 330 340 350 360 YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS 370 380 390 400 410 420 YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK 430 440 450 LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH KQVKLSKK
	Isoform 2 [UniParc]. Checksum: 36334369729A61C2	FASTA	194	21,398
	10 20 30 40 50 60 MAAQGATAAV AATTSGTVGE GEPGPGENAA VEGPARSPGR VSPPTPARGE PEVTVEIGET 70 80 90 100 110 120 YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ 130 140 150 160 170 180 KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKVLAPPF SGPSQQSHSN SHVKAGSMPG 190 FFSRLFTYEK ILSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Amnion, Embryo, Head and Thymus.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Liver.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-42, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Solution structure of the Tudor domain from mouse hypothetical protein homologous to histone acetyltransferase." RIKEN structural genomics initiative (RSGI) Submitted (MAY-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 50-169 (ISOFORM 1).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK003264 mRNA. Translation: BAB22680.1.
AK018002 mRNA. Translation: BAC25539.1. Frameshift.
AK029350 mRNA. Translation: BAC26411.1.
AK146710 mRNA. Translation: BAE27376.1.
BC036284 mRNA. Translation: AAH36284.1.

IPI

IPI00457585.
IPI00461946.

RefSeq

NP_080646.1. NM_026370.1.

UniGene

Mm.425492.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WGS	NMR	-	A	50-169	[»]

ProteinModelPortal

Q9D1P2.

SMR

Q9D1P2. Positions 47-169, 178-448.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9D1P2. 15 interactions.

PTM databases

PhosphoSite

Q9D1P2.

Proteomic databases

PaxDb

Q9D1P2.

PRIDE

Q9D1P2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000033070; ENSMUSP00000033070; ENSMUSG00000030801.

GeneID

67773.

KEGG

mmu:67773.

UCSC

uc009jxg.1. mouse.
uc009jxh.1. mouse.

Organism-specific databases

CTD

84148.

MGI

MGI:1915023. Kat8.

Phylogenomic databases

eggNOG

COG5027.

GeneTree

ENSGT00550000074503.

HOGENOM

HOG000182457.

HOVERGEN

HBG053268.

InParanoid

Q9D1P2.

KO

K11308.

OMA

DGRDHKI.

OrthoDB

EOG4933HQ.

Gene expression databases

Bgee

Q9D1P2.

CleanEx

MM_MYST1.

Genevestigator

Q9D1P2.

GermOnline

ENSMUSG00000030801. Mus musculus.

Family and domain databases

Gene3D

3.40.630.30. 1 hit.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]

Pfam

PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS00598. CHROMO_1. False negative.
PS50013. CHROMO_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9D1P2.

NextBio

325529.

SOURCE

Search...

Entry information

Entry name

KAT8_MOUSE

Accession

Primary (citable) accession number: Q9D1P2
Secondary accession number(s): Q3UIY0 , Q8BJ69, Q8BJ76, Q8CI73

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program