A2BIL7 · BAZ1B_DANRE
- ProteinTyrosine-protein kinase BAZ1B
- Genebaz1b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1536 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes.
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | WICH complex | |
Molecular Function | ATP binding | |
Molecular Function | histone binding | |
Molecular Function | histone H2AXY142 kinase activity | |
Molecular Function | histone kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | non-membrane spanning protein tyrosine kinase activity | |
Biological Process | chromatin remodeling | |
Biological Process | DNA damage response | |
Biological Process | post-translational protein modification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein kinase BAZ1B
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionA2BIL7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase (By similarity).
Localizes to sites of DNA damage (By similarity).
Localizes to sites of DNA damage (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000378188 | 1-1536 | Tyrosine-protein kinase BAZ1B | |||
Sequence: MAPLLGRKPYPLVKPLSEPPGPGEEVYTIEHTKEAFRNKEEYEARLRRYGERIWTCKSTGSSQLTHKEAWEEEQEVTELLQEEYPVWFEKPVLEIVHHNTVPLDKLVDQVWVEILTKYAVGEKCDLMVGNDKTLSVEVVKIHPLENPPEENAEKKMEGACDSPSSDKENASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMKEEKKKWVMPKFLPHKYDVKLVNEDKVISDVPADNLFRTERPPNKEIMRYFIRHYALRLGSGESAPWVVEDELVKKFSLPSKFSDFLLDPHKFLAENPSTKRKSLSSPEGKPRKRLKNVETGTGGEGAKGDKKKNKDSQNIPLSPTIWSHMQVKKVNGSPLKMKNSGTSKKSDEENVLGTPKSSKKQGDKKSSDPKRRRKSGLNKTPNSQRLSKKEDKSLGGAKKPRMKQMTLLDLAKSPAAAGSPKKQRRSSTTGSAKLGKPFPPMALHLLRFYKENKGKEDKKTTLSSLLSKAAKALSPEDRSRLPEELKELVQKRWELLEQKRRWALMSEEEKQSVLKQKRQEVKQKLREKAKERREKEMQVRREMSRRYEDQELEGKNLPAFRLFDMPEGLPNTIFGDVAMVVEFLHCYSGLLMPDDQYPITSIALLEALAGEKAGFLYLNRVLVVLLQTLLQDELAEGYSELDMPLSEIPLTMHSVSELVRLCLRPSDAHEEESARGSDDWQSGADFDDMVSSEFLEKLETAEVFELDPQEKVSLLLALCHRILMTYSVEDHVEAVHQKSAEMWKERVATLKEANDRKRAEKQKRKEQMETKTDGDVLIKAEKKKESTVKKETPKVLPKEEPEPEDMISTVKSRRLMSIQAKKEKEEQERLNKVRMEKEAEEERIRRQKAATEKAFQDAVTKAKLVLRRTPLGTDRNHNRYWLFSDVVPGLYIEKGWVHESIDYSFTLPPEEEPVLTEEEEEEEEVKKEEETEDGEKEDEGSIISASNDISQQGAPSHESSIETTVPKQGQNLWFVCDTPKDFDELLESLHPQGVRESELKIRLQINYQEILHSIHLTKKGNPGLKTCDGHQELLKFLRSDIIEVASRLQKGGLGYLEDTSEFEEFEERVKTLEKLPEFGECVIALQESVIKKFLQGFMAPKQKKKKKTGGEESTTAEEVDDQKKLAEEARVATAVEKWKTAVREAQTFSRMHVLLGMLDACIKWDMSAENARCKVCRRKGEDDKLILCDECNKAFHLFCLRPALYRIPAGEWLCPACQPTIARRSSRGRNYKEDSEEEEDSEEEDEEESEEEDSEEEHRNTGHSLRSRKKVKTSSKSKMQKKPAKPASRSASKTDTNPSKTSPKSSAKPKSRAAPSSPVDIDELVRQSSKPPSRKKDVELQKCEEILQKIMKFRHSWPFREPVSAEEAEDYQDVITSPMDLTTMQGKFKSSEYHSASDFIEDMKLIFSNAEEYNQPSSNVLTCMSRTEEAFVELLQKSLPGVSYLRRRTRKRAATPSDNSDDDDDDEEEDERSKKQKNGKQGKKASSKRKVEHSRTEKYQTKQK | ||||||
Modified residue | 1349 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with smarca5/snf2h; the interaction is direct and forms the WICH complex. Component of the B-WICH complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-130 | WAC | ||||
Sequence: EVYTIEHTKEAFRNKEEYEARLRRYGERIWTCKSTGSSQLTHKEAWEEEQEVTELLQEEYPVWFEKPVLEIVHHNTVPLDKLVDQVWVEILTKYAVGEKCDLMVGN | ||||||
Compositional bias | 144-162 | Basic and acidic residues | ||||
Sequence: LENPPEENAEKKMEGACDS | ||||||
Region | 144-207 | Disordered | ||||
Sequence: LENPPEENAEKKMEGACDSPSSDKENASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMK | ||||||
Compositional bias | 170-207 | Basic and acidic residues | ||||
Sequence: ASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMK | ||||||
Region | 304-470 | Disordered | ||||
Sequence: PSTKRKSLSSPEGKPRKRLKNVETGTGGEGAKGDKKKNKDSQNIPLSPTIWSHMQVKKVNGSPLKMKNSGTSKKSDEENVLGTPKSSKKQGDKKSSDPKRRRKSGLNKTPNSQRLSKKEDKSLGGAKKPRMKQMTLLDLAKSPAAAGSPKKQRRSSTTGSAKLGKPF | ||||||
Compositional bias | 312-344 | Basic and acidic residues | ||||
Sequence: SSPEGKPRKRLKNVETGTGGEGAKGDKKKNKDS | ||||||
Compositional bias | 345-372 | Polar residues | ||||
Sequence: QNIPLSPTIWSHMQVKKVNGSPLKMKNS | ||||||
Compositional bias | 373-407 | Basic and acidic residues | ||||
Sequence: GTSKKSDEENVLGTPKSSKKQGDKKSSDPKRRRKS | ||||||
Compositional bias | 416-430 | Basic and acidic residues | ||||
Sequence: QRLSKKEDKSLGGAK | ||||||
Coiled coil | 515-583 | |||||
Sequence: EELKELVQKRWELLEQKRRWALMSEEEKQSVLKQKRQEVKQKLREKAKERREKEMQVRREMSRRYEDQE | ||||||
Region | 557-579 | Disordered | ||||
Sequence: LREKAKERREKEMQVRREMSRRY | ||||||
Domain | 603-667 | DDT | ||||
Sequence: NTIFGDVAMVVEFLHCYSGLLMPDDQYPITSIALLEALAGEKAGFLYLNRVLVVLLQTLLQDELA | ||||||
Coiled coil | 768-803 | |||||
Sequence: HQKSAEMWKERVATLKEANDRKRAEKQKRKEQMETK | ||||||
Region | 785-839 | Disordered | ||||
Sequence: ANDRKRAEKQKRKEQMETKTDGDVLIKAEKKKESTVKKETPKVLPKEEPEPEDMI | ||||||
Coiled coil | 850-890 | |||||
Sequence: IQAKKEKEEQERLNKVRMEKEAEEERIRRQKAATEKAFQDA | ||||||
Region | 940-973 | Disordered | ||||
Sequence: PPEEEPVLTEEEEEEEEVKKEEETEDGEKEDEGS | ||||||
Compositional bias | 944-969 | Acidic residues | ||||
Sequence: EPVLTEEEEEEEEVKKEEETEDGEKE | ||||||
Zinc finger | 1202-1252 | PHD-type | ||||
Sequence: NARCKVCRRKGEDDKLILCDECNKAFHLFCLRPALYRIPAGEWLCPACQPT | ||||||
Region | 1256-1371 | Disordered | ||||
Sequence: RSSRGRNYKEDSEEEEDSEEEDEEESEEEDSEEEHRNTGHSLRSRKKVKTSSKSKMQKKPAKPASRSASKTDTNPSKTSPKSSAKPKSRAAPSSPVDIDELVRQSSKPPSRKKDVE | ||||||
Coiled coil | 1261-1293 | |||||
Sequence: RNYKEDSEEEEDSEEEDEEESEEEDSEEEHRNT | ||||||
Compositional bias | 1267-1287 | Acidic residues | ||||
Sequence: SEEEEDSEEEDEEESEEEDSE | ||||||
Compositional bias | 1296-1315 | Basic residues | ||||
Sequence: SLRSRKKVKTSSKSKMQKKP | ||||||
Compositional bias | 1319-1344 | Polar residues | ||||
Sequence: ASRSASKTDTNPSKTSPKSSAKPKSR | ||||||
Domain | 1383-1453 | Bromo | ||||
Sequence: MKFRHSWPFREPVSAEEAEDYQDVITSPMDLTTMQGKFKSSEYHSASDFIEDMKLIFSNAEEYNQPSSNVL | ||||||
Region | 1477-1536 | Disordered | ||||
Sequence: LRRRTRKRAATPSDNSDDDDDDEEEDERSKKQKNGKQGKKASSKRKVEHSRTEKYQTKQK | ||||||
Compositional bias | 1522-1536 | Basic and acidic residues | ||||
Sequence: KVEHSRTEKYQTKQK |
Domain
The bromo domain mediates the specific interaction with acetylated histones.
Sequence similarities
Belongs to the WAL family. BAZ1B subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,536
- Mass (Da)176,213
- Last updated2009-06-16 v2
- Checksum2493AB082E67F6B2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M1P9M0 | A0A8M1P9M0_DANRE | baz1b | 1807 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 144-162 | Basic and acidic residues | ||||
Sequence: LENPPEENAEKKMEGACDS | ||||||
Compositional bias | 170-207 | Basic and acidic residues | ||||
Sequence: ASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMK | ||||||
Compositional bias | 312-344 | Basic and acidic residues | ||||
Sequence: SSPEGKPRKRLKNVETGTGGEGAKGDKKKNKDS | ||||||
Compositional bias | 345-372 | Polar residues | ||||
Sequence: QNIPLSPTIWSHMQVKKVNGSPLKMKNS | ||||||
Compositional bias | 373-407 | Basic and acidic residues | ||||
Sequence: GTSKKSDEENVLGTPKSSKKQGDKKSSDPKRRRKS | ||||||
Compositional bias | 416-430 | Basic and acidic residues | ||||
Sequence: QRLSKKEDKSLGGAK | ||||||
Compositional bias | 944-969 | Acidic residues | ||||
Sequence: EPVLTEEEEEEEEVKKEEETEDGEKE | ||||||
Compositional bias | 1267-1287 | Acidic residues | ||||
Sequence: SEEEEDSEEEDEEESEEEDSE | ||||||
Compositional bias | 1296-1315 | Basic residues | ||||
Sequence: SLRSRKKVKTSSKSKMQKKP | ||||||
Compositional bias | 1319-1344 | Polar residues | ||||
Sequence: ASRSASKTDTNPSKTSPKSSAKPKSR | ||||||
Compositional bias | 1522-1536 | Basic and acidic residues | ||||
Sequence: KVEHSRTEKYQTKQK |
Keywords
- Technical term