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Protein

Histone acetyltransferase KAT8

Gene

KAT8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Can also acetylate TP53/p53 at 'Lys-120'.6 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei350Proton donor/acceptor2 PublicationsCurated1
Binding sitei354Acetyl-CoA2 Publications1
Binding sitei363Acetyl-CoA2 Publications1
Binding sitei432Acetyl-CoA2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri207 – 232C2HC MYST-typePROSITE-ProRule annotation1 PublicationAdd BLAST26

GO - Molecular functioni

  • acetyltransferase activity Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • histone acetylation Source: UniProtKB
  • histone H4-K16 acetylation Source: UniProtKB
  • histone H4-K5 acetylation Source: UniProtKB
  • histone H4-K8 acetylation Source: UniProtKB
  • myeloid cell differentiation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of autophagy Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS02515-MONOMER.
BRENDAi2.3.1.48. 2681.
ReactomeiR-HSA-3214847. HATs acetylate histones.
SIGNORiQ9H7Z6.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT8 (EC:2.3.1.484 Publications)
Alternative name(s):
Lysine acetyltransferase 8
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1
Short name:
MYST-1
Short name:
hMOF
Gene namesi
Name:KAT8
Synonyms:MOF, MYST1
ORF Names:PP7073
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:17933. KAT8.

Subcellular locationi

GO - Cellular componenti

  • histone acetyltransferase complex Source: UniProtKB
  • kinetochore Source: Ensembl
  • MLL1 complex Source: UniProtKB
  • MSL complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi274K → A: Abolishes histone acetyltransferase activity. 1 Publication1
Mutagenesisi274K → R: Abolishes histone acetyltransferase activity. 1 Publication1
Mutagenesisi316C → S: Strongly reduces histone acetyltransferase activity. 1 Publication1
Mutagenesisi350E → Q: Abolishes histone acetyltransferase activity. 1 Publication1

Organism-specific databases

DisGeNETi84148.
OpenTargetsiENSG00000103510.
PharmGKBiPA38476.

Chemistry databases

ChEMBLiCHEMBL1932912.
GuidetoPHARMACOLOGYi2668.

Polymorphism and mutation databases

BioMutaiKAT8.
DMDMi68565938.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000515662 – 458Histone acetyltransferase KAT8Add BLAST457

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei37PhosphoserineBy similarity1
Modified residuei42PhosphoserineBy similarity1
Modified residuei113N6-acetyllysineCombined sources1
Modified residuei274N6-acetyllysine; by autocatalysis5 Publications1
Modified residuei348PhosphoserineCombined sources1

Post-translational modificationi

Autoacetylation at Lys-274 is required for binding histone H4 with high affinity and for proper function.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H7Z6.
MaxQBiQ9H7Z6.
PaxDbiQ9H7Z6.
PeptideAtlasiQ9H7Z6.
PRIDEiQ9H7Z6.

PTM databases

iPTMnetiQ9H7Z6.
PhosphoSitePlusiQ9H7Z6.

Expressioni

Gene expression databases

BgeeiENSG00000103510.
CleanExiHS_MYST1.
ExpressionAtlasiQ9H7Z6. baseline and differential.
GenevisibleiQ9H7Z6. HS.

Organism-specific databases

HPAiHPA066324.

Interactioni

Subunit structurei

Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Interacts with MSL1; the interaction is direct. 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. Interacts with KANSL1; the interaction is direct.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HHF2P023092EBI-896414,EBI-8113From a different organism.
KMT2AQ031643EBI-896414,EBI-591370
RNF2Q994962EBI-896414,EBI-722416
TP53P046372EBI-896414,EBI-366083

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123914. 41 interactors.
IntActiQ9H7Z6. 13 interactors.
MINTiMINT-1897597.
STRINGi9606.ENSP00000406037.

Chemistry databases

BindingDBiQ9H7Z6.

Structurei

Secondary structure

1458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi181 – 184Combined sources4
Beta strandi187 – 190Combined sources4
Helixi199 – 203Combined sources5
Beta strandi207 – 209Combined sources3
Turni211 – 213Combined sources3
Beta strandi216 – 218Combined sources3
Helixi220 – 229Combined sources10
Beta strandi236 – 243Combined sources8
Beta strandi246 – 252Combined sources7
Turni253 – 255Combined sources3
Helixi257 – 268Combined sources12
Helixi274 – 277Combined sources4
Beta strandi283 – 292Combined sources10
Beta strandi295 – 305Combined sources11
Beta strandi312 – 315Combined sources4
Beta strandi317 – 319Combined sources3
Helixi321 – 323Combined sources3
Beta strandi325 – 327Combined sources3
Helixi328 – 342Combined sources15
Beta strandi347 – 349Combined sources3
Helixi355 – 372Combined sources18
Helixi383 – 389Combined sources7
Helixi393 – 402Combined sources10
Beta strandi406 – 409Combined sources4
Beta strandi412 – 415Combined sources4
Helixi419 – 427Combined sources9
Turni429 – 431Combined sources3
Helixi440 – 442Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GIVX-ray1.94A174-449[»]
2PQ8X-ray1.45A174-449[»]
2Y0MX-ray2.70A174-458[»]
3QAHX-ray2.10A174-449[»]
3TOAX-ray3.00A177-458[»]
3TOBX-ray2.70A177-458[»]
4DNCX-ray2.05A/B170-458[»]
5J8CX-ray2.17A177-458[»]
5J8FX-ray2.60A177-458[»]
ProteinModelPortaliQ9H7Z6.
SMRiQ9H7Z6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H7Z6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini69 – 123ChromoAdd BLAST55
Domaini174 – 447MYST-type HATPROSITE-ProRule annotationAdd BLAST274

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni174 – 458Sufficient for interaction with KANSL1Add BLAST285
Regioni317 – 319Acetyl-CoA binding2 Publications3
Regioni324 – 330Acetyl-CoA binding2 Publications7

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC MYST-type zinc finger.PROSITE-ProRule annotation
Contains 1 chromo domain.Curated
Contains 1 MYST-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri207 – 232C2HC MYST-typePROSITE-ProRule annotation1 PublicationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOVERGENiHBG053268.
InParanoidiQ9H7Z6.
KOiK11308.
OMAiMCLKWAP.
OrthoDBiEOG091G0B73.
PhylomeDBiQ9H7Z6.
TreeFamiTF317619.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H7Z6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE
60 70 80 90 100
PEVTVEIGET YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL
110 120 130 140 150
DEWVDKNRLA LTKTVKDAVQ KNSEKYLSEL AEQPERKITR NQKRKHDEIN
160 170 180 190 200
HVQKTYAEMD PTTAALEKEH EAITKVKYVD KIHIGNYEID AWYFSPFPED
210 220 230 240 250
YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI YRKSNISVYE
260 270 280 290 300
VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG
310 320 330 340 350
YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE
360 370 380 390 400
KPLSDLGKLS YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL
410 420 430 440 450
QSLNMVKYWK GQHVICVTPK LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH

KQVKLSKK
Length:458
Mass (Da):52,403
Last modified:July 5, 2005 - v2
Checksum:i66C474BE5B90E8E3
GO
Isoform 2 (identifier: Q9H7Z6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-458: VDSVCLKWAPPKHKQVKLSKK → GGWGAAVCRGRWGSVSIWTGRSQGLLIAVT

Show »
Length:467
Mass (Da):53,085
Checksum:i69AA4F8800E687E0
GO

Sequence cautioni

The sequence AAL55762 differs from that shown. Probable cloning artifact.Curated
The sequence AAL56648 differs from that shown. Reason: Frameshift at positions 23, 26 and 52.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti222S → T in AAL55762 (PubMed:15498874).Curated1
Sequence conflicti249Y → H in BAB14827 (PubMed:14702039).Curated1
Sequence conflicti372I → N in BAB14827 (PubMed:14702039).Curated1
Isoform 2 (identifier: Q9H7Z6-2)
Sequence conflicti454I → M in AAH37773 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_014579438 – 458VDSVC…KLSKK → GGWGAAVCRGRWGSVSIWTG RSQGLLIAVT in isoform 2. 2 PublicationsAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021872 mRNA. Translation: BAB13924.1.
AK024102 mRNA. Translation: BAB14827.1.
AK291106 mRNA. Translation: BAF83795.1.
AC009088 Genomic DNA. No translation available.
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52157.1.
CH471192 Genomic DNA. Translation: EAW52158.1.
BC037773 mRNA. Translation: AAH37773.1.
AF217501 mRNA. Translation: AAL56648.1. Frameshift.
AF260665 mRNA. Translation: AAF72665.2.
AF289578 mRNA. Translation: AAL55762.1. Sequence problems.
AL050395 mRNA. Translation: CAH56416.1.
CCDSiCCDS10706.1. [Q9H7Z6-1]
CCDS45468.1. [Q9H7Z6-2]
RefSeqiNP_115564.2. NM_032188.2. [Q9H7Z6-1]
NP_892003.2. NM_182958.2. [Q9H7Z6-2]
UniGeneiHs.533803.

Genome annotation databases

EnsembliENST00000219797; ENSP00000219797; ENSG00000103510. [Q9H7Z6-1]
ENST00000448516; ENSP00000406037; ENSG00000103510. [Q9H7Z6-2]
ENST00000543774; ENSP00000456933; ENSG00000103510. [Q9H7Z6-1]
GeneIDi84148.
KEGGihsa:84148.
UCSCiuc002eax.4. human. [Q9H7Z6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021872 mRNA. Translation: BAB13924.1.
AK024102 mRNA. Translation: BAB14827.1.
AK291106 mRNA. Translation: BAF83795.1.
AC009088 Genomic DNA. No translation available.
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52157.1.
CH471192 Genomic DNA. Translation: EAW52158.1.
BC037773 mRNA. Translation: AAH37773.1.
AF217501 mRNA. Translation: AAL56648.1. Frameshift.
AF260665 mRNA. Translation: AAF72665.2.
AF289578 mRNA. Translation: AAL55762.1. Sequence problems.
AL050395 mRNA. Translation: CAH56416.1.
CCDSiCCDS10706.1. [Q9H7Z6-1]
CCDS45468.1. [Q9H7Z6-2]
RefSeqiNP_115564.2. NM_032188.2. [Q9H7Z6-1]
NP_892003.2. NM_182958.2. [Q9H7Z6-2]
UniGeneiHs.533803.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GIVX-ray1.94A174-449[»]
2PQ8X-ray1.45A174-449[»]
2Y0MX-ray2.70A174-458[»]
3QAHX-ray2.10A174-449[»]
3TOAX-ray3.00A177-458[»]
3TOBX-ray2.70A177-458[»]
4DNCX-ray2.05A/B170-458[»]
5J8CX-ray2.17A177-458[»]
5J8FX-ray2.60A177-458[»]
ProteinModelPortaliQ9H7Z6.
SMRiQ9H7Z6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123914. 41 interactors.
IntActiQ9H7Z6. 13 interactors.
MINTiMINT-1897597.
STRINGi9606.ENSP00000406037.

Chemistry databases

BindingDBiQ9H7Z6.
ChEMBLiCHEMBL1932912.
GuidetoPHARMACOLOGYi2668.

PTM databases

iPTMnetiQ9H7Z6.
PhosphoSitePlusiQ9H7Z6.

Polymorphism and mutation databases

BioMutaiKAT8.
DMDMi68565938.

Proteomic databases

EPDiQ9H7Z6.
MaxQBiQ9H7Z6.
PaxDbiQ9H7Z6.
PeptideAtlasiQ9H7Z6.
PRIDEiQ9H7Z6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219797; ENSP00000219797; ENSG00000103510. [Q9H7Z6-1]
ENST00000448516; ENSP00000406037; ENSG00000103510. [Q9H7Z6-2]
ENST00000543774; ENSP00000456933; ENSG00000103510. [Q9H7Z6-1]
GeneIDi84148.
KEGGihsa:84148.
UCSCiuc002eax.4. human. [Q9H7Z6-1]

Organism-specific databases

CTDi84148.
DisGeNETi84148.
GeneCardsiKAT8.
HGNCiHGNC:17933. KAT8.
HPAiHPA066324.
MIMi609912. gene.
neXtProtiNX_Q9H7Z6.
OpenTargetsiENSG00000103510.
PharmGKBiPA38476.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOVERGENiHBG053268.
InParanoidiQ9H7Z6.
KOiK11308.
OMAiMCLKWAP.
OrthoDBiEOG091G0B73.
PhylomeDBiQ9H7Z6.
TreeFamiTF317619.

Enzyme and pathway databases

BioCyciZFISH:HS02515-MONOMER.
BRENDAi2.3.1.48. 2681.
ReactomeiR-HSA-3214847. HATs acetylate histones.
SIGNORiQ9H7Z6.

Miscellaneous databases

ChiTaRSiKAT8. human.
EvolutionaryTraceiQ9H7Z6.
GeneWikiiMYST1.
GenomeRNAii84148.
PROiQ9H7Z6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103510.
CleanExiHS_MYST1.
ExpressionAtlasiQ9H7Z6. baseline and differential.
GenevisibleiQ9H7Z6. HS.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAT8_HUMAN
AccessioniPrimary (citable) accession number: Q9H7Z6
Secondary accession number(s): A8K4Z1
, G5E9P2, Q659G0, Q7LC17, Q8IY59, Q8WYB4, Q8WZ14, Q9HAC5, Q9NR35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: November 2, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.