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Q9D1P2 (KAT8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts with KANSL1; the interaction is direct. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, 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. Interacts with MSL1; the interaction is direct. Ref.3

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 processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone 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: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

MSL complex

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

kinetochore

Inferred from direct assay PubMed 14519686. Source: MGI

   Molecular_functionacetyltransferase activity

Inferred from direct assay PubMed 19578370. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 19578370. Source: UniProtKB

histone acetyltransferase activity (H4-K16 specific)

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity (H4-K5 specific)

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity (H4-K8 specific)

Inferred from electronic annotation. Source: Ensembl

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 458457Histone acetyltransferase KAT8
PRO_0000051567

Regions

Domain69 – 12355Chromo
Zinc finger208 – 23023C2HC-type
Region174 – 458285Sufficient for interaction with KANSL1 By similarity
Region324 – 3307Acetyl-CoA binding By similarity

Sites

Active site2741 By similarity
Active site3501Proton donor/acceptor By similarity
Binding site3191Acetyl-CoA By similarity
Binding site3541Acetyl-CoA By similarity
Binding site3631Acetyl-CoA By similarity
Binding site4321Acetyl-CoA By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1131N6-acetyllysine By similarity
Modified residue2741N6-acetyllysine; by autocatalysis By similarity

Natural variations

Alternative sequence155 – 19440TYAEM…DAWYF → VLAPPFSGPSQQSHSNSHVK AGSMPGFFSRLFTYEKILSL in isoform 2.
VSP_014580
Alternative sequence195 – 458264Missing in isoform 2.
VSP_014581

Experimental info

Sequence conflict3851L → F in AAH36284. Ref.2

Secondary structure

................ 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: FA25E0C8D7E46CEC

FASTA45852,574
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 36334369729A61C2
Show »

FASTA19421,398

References

« Hide '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. 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] (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]"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MSL1.
[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.
CCDSCCDS21885.1. [Q9D1P2-1]
RefSeqNP_080646.1. NM_026370.1. [Q9D1P2-1]
UniGeneMm.425492.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGSNMR-A50-169[»]
ProteinModelPortalQ9D1P2.
SMRQ9D1P2. Positions 47-169, 178-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212433. 21 interactions.
IntActQ9D1P2. 16 interactions.

PTM databases

PhosphoSiteQ9D1P2.

Proteomic databases

PaxDbQ9D1P2.
PRIDEQ9D1P2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033070; ENSMUSP00000033070; ENSMUSG00000030801. [Q9D1P2-1]
GeneID67773.
KEGGmmu:67773.
UCSCuc009jxg.1. mouse. [Q9D1P2-2]
uc009jxh.1. mouse. [Q9D1P2-1]

Organism-specific databases

CTD84148.
MGIMGI:1915023. Kat8.

Phylogenomic databases

eggNOGCOG5027.
GeneTreeENSGT00550000074503.
HOGENOMHOG000182457.
HOVERGENHBG053268.
InParanoidQ9D1P2.
KOK11308.
OMADGRDHKI.
OrthoDBEOG7WHH8N.
PhylomeDBQ9D1P2.
TreeFamTF317619.

Gene expression databases

BgeeQ9D1P2.
CleanExMM_MYST1.
GenevestigatorQ9D1P2.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9D1P2.
NextBio325529.
PROQ9D1P2.
SOURCESearch...

Entry information

Entry nameKAT8_MOUSE
AccessionPrimary (citable) accession number: Q9D1P2
Secondary accession number(s): Q3UIY0 expand/collapse secondary AC list , Q8BJ69, Q8BJ76, Q8CI73
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 114 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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