Q8BRB7 · KAT6B_MOUSE
- ProteinHistone acetyltransferase KAT6B
- GeneKat6b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1872 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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
Involved in cerebral cortex development
Catalytic activity
- acetyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-acetyl-L-lysyl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase KAT6B
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8BRB7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
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.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 142 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000051577 | 1-1872 | Histone acetyltransferase KAT6B | |||
Sequence: MVKLANPLYTEWILEAVQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKPTKGSKGPPCNDLRNVDWNKLLKRAIEGLEEPNGSSLKNIEKYLRSQSDLTGTTNHPAFQQRLRLGAKRAVNNGRLLKEGPQYRVNSGSSDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTANVKALRWQCIECKTCSACRVQGKNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMSAFTGRGSPGRGQKTKVSTTPSSGHAASGKHSSSRLAVTDPTRPGATTKTTTSSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATDTDIKISIKQESADVSLVGNKELVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYRHHERHISIKAISRATGMCPHDIATTLQHLHMIDRRDGRFVIIRREKLILGHMEKLKNCSRPNELDPESLRWTPMLISNAVVSEEEREAEKEAERLMEQASCWEKEEQEILSSRVSSRQSSAKVQSKNKYLHSPERRPVAGERGQLLELSKESSEEEEEEEEEDDEEEEEEEEEESIQTSPPRLTKPQSVSIKRKRPFVVKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIPVEEGGRKPVLRKAFPHQPGKKRQTEEEEGEDNHFFKTAALCRKDVDDDAEHLKEGSKDNPEPLKCRQVWPKGAKRGLSKWKQSKERKTGFKLNLYTPPETPMEPEDQVTIEEQKELSEDKGSPVGMEREVTETVDALLPQEGSRREETGIPVSPHKSPGGKVDEEDLIRGEEEGEEEGEEEGEREEQEEEEEVTTEKDLDGAKSKENPEPEISMEKEDPVHLGDHEEDEDEEEEPSHNEDHDADDEDDGHMEAANMERGDLPRETFKDALEGQEAFLDLSIQPSHSNPEVLMNCGVDLTMSCNSEPKELAGDTGTAPESDAEPPEEQTQKQDQKNSDGVDAELEEGGPAAVEIDSETAQAVQSLTQENREHDDTFPDCAETQEACRSLQNYTHTDQSPQIATTLDECQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQTAITVPPLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSSLTSSNLTQNSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLADIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHVSMRTKAASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGSQPYAQQPMQTPPHANMMYTAPGHHGYMNTGMSKQSLNGSYMRR | ||||||
Modified residue | 356 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 491 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 633 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | ||||||
Modified residue | 856 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 860 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 862 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 866 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autoacetylation at Lys-633 is required for proper function.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Developmental stage
Strongly expressed in the ventricular zone of the developing cerebral cortex.
Gene expression databases
Interaction
Subunit
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.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-77 | SAMD1-like winged helix (WH) | ||||
Sequence: MVKLANPLYTEWILEAVQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNP | ||||||
Region | 70-103 | Disordered | ||||
Sequence: SYKDPDNPGRFSSVKPGTFPKPTKGSKGPPCNDL | ||||||
Domain | 104-177 | H15 | ||||
Sequence: RNVDWNKLLKRAIEGLEEPNGSSLKNIEKYLRSQSDLTGTTNHPAFQQRLRLGAKRAVNNGRLLKEGPQYRVNS | ||||||
Region | 168-207 | Disordered | ||||
Sequence: KEGPQYRVNSGSSDGKGAPQYPSAFPSSLPPVSLLPHEKD | ||||||
Zinc finger | 214-273 | PHD-type 1 | ||||
Sequence: IPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTANVKALRWQCIECKTC | ||||||
Zinc finger | 270-321 | PHD-type 2 | ||||
Sequence: CKTCSACRVQGKNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPK | ||||||
Region | 361-417 | Disordered | ||||
Sequence: EGSMSAFTGRGSPGRGQKTKVSTTPSSGHAASGKHSSSRLAVTDPTRPGATTKTTTS | ||||||
Region | 362-535 | Negatively regulates HAT activity | ||||
Sequence: GSMSAFTGRGSPGRGQKTKVSTTPSSGHAASGKHSSSRLAVTDPTRPGATTKTTTSSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATDTDIKISIKQESADVSLVGNKELVTEEDLDVFKQAQELSWEKIECESGVEDCG | ||||||
Domain | 533-807 | MYST-type HAT | ||||
Sequence: DCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYRHHERHISIKAISRATGMCPHDIATTLQHLHMIDRRDGRFVIIRREKLILGHMEKLKNCSRPNELDPESLRWTP | ||||||
Region | 536-826 | Catalytic | ||||
Sequence: RYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYRHHERHISIKAISRATGMCPHDIATTLQHLHMIDRRDGRFVIIRREKLILGHMEKLKNCSRPNELDPESLRWTPMLISNAVVSEEEREAEKEA | ||||||
Zinc finger | 566-591 | C2HC MYST-type | ||||
Sequence: LYLCEFCLKYMKSKNILLRHSKKCGW | ||||||
Region | 570-826 | Interaction with BRPF1 | ||||
Sequence: EFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYRHHERHISIKAISRATGMCPHDIATTLQHLHMIDRRDGRFVIIRREKLILGHMEKLKNCSRPNELDPESLRWTPMLISNAVVSEEEREAEKEA | ||||||
Compositional bias | 846-861 | Polar residues | ||||
Sequence: SRVSSRQSSAKVQSKN | ||||||
Region | 846-1018 | Disordered | ||||
Sequence: SRVSSRQSSAKVQSKNKYLHSPERRPVAGERGQLLELSKESSEEEEEEEEEDDEEEEEEEEEESIQTSPPRLTKPQSVSIKRKRPFVVKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIPVEEGGRKPVLRKAFPHQPGKKRQTEEEEGEDNHFF | ||||||
Compositional bias | 885-909 | Acidic residues | ||||
Sequence: ESSEEEEEEEEEDDEEEEEEEEEES | ||||||
Compositional bias | 928-943 | Basic residues | ||||
Sequence: KRPFVVKKKRGRKRRR | ||||||
Compositional bias | 947-961 | Polar residues | ||||
Sequence: SVTTETISETTEVLN | ||||||
Compositional bias | 1001-1018 | Basic and acidic residues | ||||
Sequence: PGKKRQTEEEEGEDNHFF | ||||||
Region | 1031-1252 | Disordered | ||||
Sequence: DAEHLKEGSKDNPEPLKCRQVWPKGAKRGLSKWKQSKERKTGFKLNLYTPPETPMEPEDQVTIEEQKELSEDKGSPVGMEREVTETVDALLPQEGSRREETGIPVSPHKSPGGKVDEEDLIRGEEEGEEEGEEEGEREEQEEEEEVTTEKDLDGAKSKENPEPEISMEKEDPVHLGDHEEDEDEEEEPSHNEDHDADDEDDGHMEAANMERGDLPRETFKDA | ||||||
Compositional bias | 1090-1109 | Basic and acidic residues | ||||
Sequence: QVTIEEQKELSEDKGSPVGM | ||||||
Compositional bias | 1151-1178 | Acidic residues | ||||
Sequence: IRGEEEGEEEGEEEGEREEQEEEEEVTT | ||||||
Compositional bias | 1179-1206 | Basic and acidic residues | ||||
Sequence: EKDLDGAKSKENPEPEISMEKEDPVHLG | ||||||
Compositional bias | 1207-1233 | Acidic residues | ||||
Sequence: DHEEDEDEEEEPSHNEDHDADDEDDGH | ||||||
Compositional bias | 1234-1252 | Basic and acidic residues | ||||
Sequence: MEAANMERGDLPRETFKDA | ||||||
Region | 1283-1358 | Disordered | ||||
Sequence: MSCNSEPKELAGDTGTAPESDAEPPEEQTQKQDQKNSDGVDAELEEGGPAAVEIDSETAQAVQSLTQENREHDDTF | ||||||
Compositional bias | 1306-1324 | Basic and acidic residues | ||||
Sequence: PPEEQTQKQDQKNSDGVDA | ||||||
Region | 1359-1872 | Interaction with RUNX1 and RUNX2 | ||||
Sequence: PDCAETQEACRSLQNYTHTDQSPQIATTLDECQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQTAITVPPLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSSLTSSNLTQNSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLADIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHVSMRTKAASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGSQPYAQQPMQTPPHANMMYTAPGHHGYMNTGMSKQSLNGSYMRR | ||||||
Region | 1388-1418 | Disordered | ||||
Sequence: DECQQSDHSSPVSSVHSHPGQSVRSVNSPSV |
Domain
The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.
Sequence similarities
Belongs to the MYST (SAS/MOZ) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8BRB7-1
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.
- Name1
- Length1,872
- Mass (Da)208,526
- Last updated2011-07-27 v3
- Checksum2807D9D473EE22C7
Q8BRB7-2
- Name2
- Differences from canonical
- 374-482: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F8MQ39 | A0A5F8MQ39_MOUSE | Kat6b | 2054 | ||
S4R2Q8 | S4R2Q8_MOUSE | Kat6b | 79 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_014592 | 374-482 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 846-861 | Polar residues | ||||
Sequence: SRVSSRQSSAKVQSKN | ||||||
Compositional bias | 885-909 | Acidic residues | ||||
Sequence: ESSEEEEEEEEEDDEEEEEEEEEES | ||||||
Compositional bias | 928-943 | Basic residues | ||||
Sequence: KRPFVVKKKRGRKRRR | ||||||
Compositional bias | 947-961 | Polar residues | ||||
Sequence: SVTTETISETTEVLN | ||||||
Compositional bias | 1001-1018 | Basic and acidic residues | ||||
Sequence: PGKKRQTEEEEGEDNHFF | ||||||
Sequence conflict | 1033 | in Ref. 1; AAF26744 | ||||
Sequence: E → Q | ||||||
Compositional bias | 1090-1109 | Basic and acidic residues | ||||
Sequence: QVTIEEQKELSEDKGSPVGM | ||||||
Compositional bias | 1151-1178 | Acidic residues | ||||
Sequence: IRGEEEGEEEGEEEGEREEQEEEEEVTT | ||||||
Compositional bias | 1179-1206 | Basic and acidic residues | ||||
Sequence: EKDLDGAKSKENPEPEISMEKEDPVHLG | ||||||
Compositional bias | 1207-1233 | Acidic residues | ||||
Sequence: DHEEDEDEEEEPSHNEDHDADDEDDGH | ||||||
Compositional bias | 1234-1252 | Basic and acidic residues | ||||
Sequence: MEAANMERGDLPRETFKDA | ||||||
Compositional bias | 1306-1324 | Basic and acidic residues | ||||
Sequence: PPEEQTQKQDQKNSDGVDA | ||||||
Sequence conflict | 1418 | in Ref. 1; AAF26744 | ||||
Sequence: V → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF222800 EMBL· GenBank· DDBJ | AAF26744.1 EMBL· GenBank· DDBJ | mRNA | ||
AK045188 EMBL· GenBank· DDBJ | BAC32253.2 EMBL· GenBank· DDBJ | mRNA | ||
AK048336 EMBL· GenBank· DDBJ | BAC33305.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK052307 EMBL· GenBank· DDBJ | BAC34930.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK083123 EMBL· GenBank· DDBJ | BAC38771.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AC115122 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC148978 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AY294423 EMBL· GenBank· DDBJ | AAQ01512.1 EMBL· GenBank· DDBJ | Genomic DNA |