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Protein

Histone acetyltransferase KAT6B

Gene

Kat6b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (By similarity). Involved in cerebral cortex development.By similarity1 Publication

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei709Proton donor/acceptorBy similarity1
Binding sitei713Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri214 – 273PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri270 – 321PHD-type 2PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri566 – 591C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6B (EC:2.3.1.481 Publication)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name:
MYST-4
Protein querkopf
Gene namesi
Name:Kat6b
Synonyms:Myst4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1858746. Kat6b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice have a low body weight, craniofacial abnormalities, and defects in cortex development. Mice carrying a gene trap insertion in the gene, produces approximately 5% of the normal amount of mRNA. The hypomorphic mutant displays a number of defects that mirror SBBYSS syndrome, although the phenotype is milder. Mice are of normal size at birth but fail to thrive and have brain developmental defects as well as craniofacial defects. Observed abnormalities include short and narrow palpebral fissures, low set ears, and malocclusion. Similar to individuals with SBBYSS, mice carrying the gene trap insertion have long, slender feet and disproportionally long first digits.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515771 – 1872Histone acetyltransferase KAT6BAdd BLAST1872

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei356PhosphoserineBy similarity1
Cross-linki491Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei633N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei856N6-acetyllysineCombined sources1
Modified residuei860N6-acetyllysineCombined sources1
Modified residuei862N6-acetyllysineBy similarity1
Modified residuei866PhosphoserineBy similarity1

Post-translational modificationi

Autoacetylation at Lys-633 is required for proper function.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8BRB7.
PRIDEiQ8BRB7.

PTM databases

iPTMnetiQ8BRB7.
PhosphoSitePlusiQ8BRB7.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Developmental stagei

Strongly expressed in the ventricular zone of the developing cerebral cortex.1 Publication

Gene expression databases

BgeeiENSMUSG00000021767.
ExpressionAtlasiQ8BRB7. baseline and differential.
GenevisibleiQ8BRB7. MM.

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. Interacts with RUNX1 and RUNX2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207589. 1 interactor.
STRINGi10090.ENSMUSP00000066693.

Structurei

3D structure databases

ProteinModelPortaliQ8BRB7.
SMRiQ8BRB7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini104 – 177H15PROSITE-ProRule annotationAdd BLAST74
Domaini533 – 807MYST-type HATPROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni362 – 535Negatively regulates HAT activityBy similarityAdd BLAST174
Regioni536 – 826CatalyticBy similarityAdd BLAST291
Regioni570 – 826Interaction with BRPF1By similarityAdd BLAST257
Regioni674 – 678Acetyl-CoA bindingBy similarity5
Regioni683 – 689Acetyl-CoA bindingBy similarity7
Regioni1359 – 1872Interaction with RUNX1 and RUNX2By similarityAdd BLAST514

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi888 – 896Poly-Glu9
Compositional biasi899 – 908Poly-Glu10
Compositional biasi1008 – 1013Poly-Glu6
Compositional biasi1154 – 1175Poly-GluAdd BLAST22
Compositional biasi1209 – 1217Poly-Glu9
Compositional biasi1393 – 1562Ser-richAdd BLAST170
Compositional biasi1760 – 1860Met-richAdd BLAST101

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.Curated
Contains 1 C2HC MYST-type zinc finger.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 1 MYST-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri214 – 273PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri270 – 321PHD-type 2PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri566 – 591C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BRB7.
KOiK11306.
OMAiFTPPMQL.
OrthoDBiEOG091G00D2.
TreeFamiTF106483.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. HAT_MYST-type.
IPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8BRB7-1) [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
MVKLANPLYT EWILEAVQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ
60 70 80 90 100
LELSVQDGSV LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK PTKGSKGPPC
110 120 130 140 150
NDLRNVDWNK LLKRAIEGLE EPNGSSLKNI EKYLRSQSDL TGTTNHPAFQ
160 170 180 190 200
QRLRLGAKRA VNNGRLLKEG PQYRVNSGSS DGKGAPQYPS AFPSSLPPVS
210 220 230 240 250
LLPHEKDQPR ADPIPICSFC LGTKESNREK KPEELLSCAD CGSSGHPSCL
260 270 280 290 300
KFCPELTANV KALRWQCIEC KTCSACRVQG KNADNMLFCD SCDRGFHMEC
310 320 330 340 350
CDPPLSRMPK GMWICQVCRP KKKGRKLLHE KAAQIKRRYA KPIGRPKNKL
360 370 380 390 400
KQRLLSVTSD EGSMSAFTGR GSPGRGQKTK VSTTPSSGHA ASGKHSSSRL
410 420 430 440 450
AVTDPTRPGA TTKTTTSSTY ISASTLKVNK KTKGLIDGLT KFFTPSPDGR
460 470 480 490 500
RSRGEIIDFS KHYRPRKKVS QKQSCTSHVL ATDTDIKISI KQESADVSLV
510 520 530 540 550
GNKELVTEED LDVFKQAQEL SWEKIECESG VEDCGRYPSV IEFGKYEIQT
560 570 580 590 600
WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG WFHPPANEIY
610 620 630 640 650
RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN
660 670 680 690 700
DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR
710 720 730 740 750
REGQAGSPEK PLSDLGRLSY LAYWKSVILE YLYRHHERHI SIKAISRATG
760 770 780 790 800
MCPHDIATTL QHLHMIDRRD GRFVIIRREK LILGHMEKLK NCSRPNELDP
810 820 830 840 850
ESLRWTPMLI SNAVVSEEER EAEKEAERLM EQASCWEKEE QEILSSRVSS
860 870 880 890 900
RQSSAKVQSK NKYLHSPERR PVAGERGQLL ELSKESSEEE EEEEEEDDEE
910 920 930 940 950
EEEEEEEESI QTSPPRLTKP QSVSIKRKRP FVVKKKRGRK RRRINSSVTT
960 970 980 990 1000
ETISETTEVL NEPFDNSDEE RPMPQLEPTC EIPVEEGGRK PVLRKAFPHQ
1010 1020 1030 1040 1050
PGKKRQTEEE EGEDNHFFKT AALCRKDVDD DAEHLKEGSK DNPEPLKCRQ
1060 1070 1080 1090 1100
VWPKGAKRGL SKWKQSKERK TGFKLNLYTP PETPMEPEDQ VTIEEQKELS
1110 1120 1130 1140 1150
EDKGSPVGME REVTETVDAL LPQEGSRREE TGIPVSPHKS PGGKVDEEDL
1160 1170 1180 1190 1200
IRGEEEGEEE GEEEGEREEQ EEEEEVTTEK DLDGAKSKEN PEPEISMEKE
1210 1220 1230 1240 1250
DPVHLGDHEE DEDEEEEPSH NEDHDADDED DGHMEAANME RGDLPRETFK
1260 1270 1280 1290 1300
DALEGQEAFL DLSIQPSHSN PEVLMNCGVD LTMSCNSEPK ELAGDTGTAP
1310 1320 1330 1340 1350
ESDAEPPEEQ TQKQDQKNSD GVDAELEEGG PAAVEIDSET AQAVQSLTQE
1360 1370 1380 1390 1400
NREHDDTFPD CAETQEACRS LQNYTHTDQS PQIATTLDEC QQSDHSSPVS
1410 1420 1430 1440 1450
SVHSHPGQSV RSVNSPSVPA LENSYAQISP DQTAITVPPL QNMETSPMMD
1460 1470 1480 1490 1500
VPSVSDHSQQ VVDSGFSDLG SIESTTENYE NPSSYDSTMG GSICGNGSSQ
1510 1520 1530 1540 1550
NSCSYSSLTS SNLTQNSCAV TQQMSNISGS CSMLQQTSIS SPPTCSVKSP
1560 1570 1580 1590 1600
QGCVVERPPS SSQQLAQCSM AANFTPPMQL ADIPETSNAN IGLYERMGQS
1610 1620 1630 1640 1650
DFGAGHYPQP SATFSLAKLQ QLTNTLIDHS LPYSHSAAVT SYANSASLST
1660 1670 1680 1690 1700
PLSNTGLVQL SQSPHSVPGG PQAQATMTPP PNLTPPPMNL PPPLLQRNMA
1710 1720 1730 1740 1750
ASNIGISHSQ RLQTQIASKG HVSMRTKAAS LSPAAATHQS QIYGRSQTVA
1760 1770 1780 1790 1800
MQGPARTLTM QRGMNMSVNL MPAPAYNVNS VNMNMNTLNA MNGYSMSQPM
1810 1820 1830 1840 1850
MNSGYHSNHG YMNQTPQYPM QMQMGMMGSQ PYAQQPMQTP PHANMMYTAP
1860 1870
GHHGYMNTGM SKQSLNGSYM RR
Length:1,872
Mass (Da):208,526
Last modified:July 27, 2011 - v3
Checksum:i2807D9D473EE22C7
GO
Isoform 2 (identifier: Q8BRB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     374-482: Missing.

Show »
Length:1,763
Mass (Da):196,867
Checksum:i667EEDB2F43FF958
GO

Sequence cautioni

The sequence BAC33305 differs from that shown. Probable intron retention.Curated
The sequence BAC34930 differs from that shown. Probable intron retention.Curated
The sequence BAC38771 differs from that shown. Probable intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1033E → Q in AAF26744 (PubMed:10821753).Curated1
Sequence conflicti1418V → I in AAF26744 (PubMed:10821753).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_014592374 – 482Missing in isoform 2. 1 PublicationAdd BLAST109

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222800 mRNA. Translation: AAF26744.1.
AK045188 mRNA. Translation: BAC32253.2.
AK048336 mRNA. Translation: BAC33305.1. Sequence problems.
AK052307 mRNA. Translation: BAC34930.1. Sequence problems.
AK083123 mRNA. Translation: BAC38771.1. Sequence problems.
AC115122 Genomic DNA. No translation available.
AC148978 Genomic DNA. No translation available.
AY294423 Genomic DNA. Translation: AAQ01512.1.
CCDSiCCDS59615.1. [Q8BRB7-2]
RefSeqiNP_059507.2. NM_017479.3. [Q8BRB7-2]
XP_006519331.1. XM_006519268.3. [Q8BRB7-1]
XP_017171572.1. XM_017316083.1. [Q8BRB7-2]
UniGeneiMm.248967.

Genome annotation databases

EnsembliENSMUST00000069648; ENSMUSP00000066693; ENSMUSG00000021767. [Q8BRB7-1]
ENSMUST00000182405; ENSMUSP00000138377; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182855; ENSMUSP00000138511; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182964; ENSMUSP00000138421; ENSMUSG00000021767. [Q8BRB7-1]
GeneIDi54169.
KEGGimmu:54169.
UCSCiuc007slg.2. mouse. [Q8BRB7-2]
uc007slk.1. mouse. [Q8BRB7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222800 mRNA. Translation: AAF26744.1.
AK045188 mRNA. Translation: BAC32253.2.
AK048336 mRNA. Translation: BAC33305.1. Sequence problems.
AK052307 mRNA. Translation: BAC34930.1. Sequence problems.
AK083123 mRNA. Translation: BAC38771.1. Sequence problems.
AC115122 Genomic DNA. No translation available.
AC148978 Genomic DNA. No translation available.
AY294423 Genomic DNA. Translation: AAQ01512.1.
CCDSiCCDS59615.1. [Q8BRB7-2]
RefSeqiNP_059507.2. NM_017479.3. [Q8BRB7-2]
XP_006519331.1. XM_006519268.3. [Q8BRB7-1]
XP_017171572.1. XM_017316083.1. [Q8BRB7-2]
UniGeneiMm.248967.

3D structure databases

ProteinModelPortaliQ8BRB7.
SMRiQ8BRB7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207589. 1 interactor.
STRINGi10090.ENSMUSP00000066693.

PTM databases

iPTMnetiQ8BRB7.
PhosphoSitePlusiQ8BRB7.

Proteomic databases

PaxDbiQ8BRB7.
PRIDEiQ8BRB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069648; ENSMUSP00000066693; ENSMUSG00000021767. [Q8BRB7-1]
ENSMUST00000182405; ENSMUSP00000138377; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182855; ENSMUSP00000138511; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182964; ENSMUSP00000138421; ENSMUSG00000021767. [Q8BRB7-1]
GeneIDi54169.
KEGGimmu:54169.
UCSCiuc007slg.2. mouse. [Q8BRB7-2]
uc007slk.1. mouse. [Q8BRB7-1]

Organism-specific databases

CTDi23522.
MGIiMGI:1858746. Kat6b.

Phylogenomic databases

eggNOGiKOG2747. Eukaryota.
COG5027. LUCA.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BRB7.
KOiK11306.
OMAiFTPPMQL.
OrthoDBiEOG091G00D2.
TreeFamiTF106483.

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.

Miscellaneous databases

PROiQ8BRB7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021767.
ExpressionAtlasiQ8BRB7. baseline and differential.
GenevisibleiQ8BRB7. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. HAT_MYST-type.
IPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAT6B_MOUSE
AccessioniPrimary (citable) accession number: Q8BRB7
Secondary accession number(s): E9QK86
, Q7TNW5, Q8BG35, Q8C441, Q9JKX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 126 of the entry and version 3 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

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.