Tyrosine-protein kinase BAZ1B - Danio rerio (Zebrafish)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase BAZ1B
EC=2.7.10.2

Alternative name(s):
Bromodomain adjacent to zinc finger domain protein 1B
Williams syndrome transcription factor homolog

Gene names

Name:	baz1b
Synonyms:	wstf
ORF Names:	ch211-203b8.1

Organism

Danio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	1536 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR). In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Manganese By similarity.
Subunit structure	Interacts with smarca5/ snf2h; the interaction is direct and forms the WICH complex. Component of the B-WICH complex. Component of the WINAC complex By similarity.
Subcellular location	Nucleus By similarity. Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase By similarity.
Domain	The bromo domain mediates the specific interaction with acetylated histones By similarity.
Sequence similarities	Belongs to the WAL family. BAZ1B subfamily. Contains 1 bromo domain. Contains 1 DDT domain. Contains 1 PHD-type zinc finger. Contains 1 WAC domain.
Sequence caution	The sequence CAM13000.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	DNA damage Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain Coiled coil Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB histone acetyl-lysine binding Inferred from sequence or structural similarity. Source: UniProtKB histone kinase activity Inferred from sequence or structural similarity. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1536

1536

Tyrosine-protein kinase BAZ1B

PRO_0000378188

Regions

Domain

25 – 130

106

WAC

Domain

603 – 667

65

DDT

Domain

1383 – 1453

71

Bromo

Zinc finger

1202 – 1252

51

PHD-type

Coiled coil

515 – 583

69

Potential

Coiled coil

768 – 803

36

Potential

Coiled coil

850 – 890

41

Potential

Coiled coil

1261 – 1293

33

Potential

Amino acid modifications

Modified residue

1349

1

Phosphoserine Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

A2BIL7 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 2493AB082E67F6B2
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FASTA

1,536

176,213

        10         20         30         40         50         60 
MAPLLGRKPY PLVKPLSEPP GPGEEVYTIE HTKEAFRNKE EYEARLRRYG ERIWTCKSTG 

        70         80         90        100        110        120 
SSQLTHKEAW EEEQEVTELL QEEYPVWFEK PVLEIVHHNT VPLDKLVDQV WVEILTKYAV 

       130        140        150        160        170        180 
GEKCDLMVGN DKTLSVEVVK IHPLENPPEE NAEKKMEGAC DSPSSDKENA SQENLKKEPQ 

       190        200        210        220        230        240 
SKEEESRRES LSDRARRSPR KLPTTMKEEK KKWVMPKFLP HKYDVKLVNE DKVISDVPAD 

       250        260        270        280        290        300 
NLFRTERPPN KEIMRYFIRH YALRLGSGES APWVVEDELV KKFSLPSKFS DFLLDPHKFL 

       310        320        330        340        350        360 
AENPSTKRKS LSSPEGKPRK RLKNVETGTG GEGAKGDKKK NKDSQNIPLS PTIWSHMQVK 

       370        380        390        400        410        420 
KVNGSPLKMK NSGTSKKSDE ENVLGTPKSS KKQGDKKSSD PKRRRKSGLN KTPNSQRLSK 

       430        440        450        460        470        480 
KEDKSLGGAK KPRMKQMTLL DLAKSPAAAG SPKKQRRSST TGSAKLGKPF PPMALHLLRF 

       490        500        510        520        530        540 
YKENKGKEDK KTTLSSLLSK AAKALSPEDR SRLPEELKEL VQKRWELLEQ KRRWALMSEE 

       550        560        570        580        590        600 
EKQSVLKQKR QEVKQKLREK AKERREKEMQ VRREMSRRYE DQELEGKNLP AFRLFDMPEG 

       610        620        630        640        650        660 
LPNTIFGDVA MVVEFLHCYS GLLMPDDQYP ITSIALLEAL AGEKAGFLYL NRVLVVLLQT 

       670        680        690        700        710        720 
LLQDELAEGY SELDMPLSEI PLTMHSVSEL VRLCLRPSDA HEEESARGSD DWQSGADFDD 

       730        740        750        760        770        780 
MVSSEFLEKL ETAEVFELDP QEKVSLLLAL CHRILMTYSV EDHVEAVHQK SAEMWKERVA 

       790        800        810        820        830        840 
TLKEANDRKR AEKQKRKEQM ETKTDGDVLI KAEKKKESTV KKETPKVLPK EEPEPEDMIS 

       850        860        870        880        890        900 
TVKSRRLMSI QAKKEKEEQE RLNKVRMEKE AEEERIRRQK AATEKAFQDA VTKAKLVLRR 

       910        920        930        940        950        960 
TPLGTDRNHN RYWLFSDVVP GLYIEKGWVH ESIDYSFTLP PEEEPVLTEE EEEEEEVKKE 

       970        980        990       1000       1010       1020 
EETEDGEKED EGSIISASND ISQQGAPSHE SSIETTVPKQ GQNLWFVCDT PKDFDELLES 

      1030       1040       1050       1060       1070       1080 
LHPQGVRESE LKIRLQINYQ EILHSIHLTK KGNPGLKTCD GHQELLKFLR SDIIEVASRL 

      1090       1100       1110       1120       1130       1140 
QKGGLGYLED TSEFEEFEER VKTLEKLPEF GECVIALQES VIKKFLQGFM APKQKKKKKT 

      1150       1160       1170       1180       1190       1200 
GGEESTTAEE VDDQKKLAEE ARVATAVEKW KTAVREAQTF SRMHVLLGML DACIKWDMSA 

      1210       1220       1230       1240       1250       1260 
ENARCKVCRR KGEDDKLILC DECNKAFHLF CLRPALYRIP AGEWLCPACQ PTIARRSSRG 

      1270       1280       1290       1300       1310       1320 
RNYKEDSEEE EDSEEEDEEE SEEEDSEEEH RNTGHSLRSR KKVKTSSKSK MQKKPAKPAS 

      1330       1340       1350       1360       1370       1380 
RSASKTDTNP SKTSPKSSAK PKSRAAPSSP VDIDELVRQS SKPPSRKKDV ELQKCEEILQ 

      1390       1400       1410       1420       1430       1440 
KIMKFRHSWP FREPVSAEEA EDYQDVITSP MDLTTMQGKF KSSEYHSASD FIEDMKLIFS 

      1450       1460       1470       1480       1490       1500 
NAEEYNQPSS NVLTCMSRTE EAFVELLQKS LPGVSYLRRR TRKRAATPSD NSDDDDDDEE 

      1510       1520       1530 
EDERSKKQKN GKQGKKASSK RKVEHSRTEK YQTKQK

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References

[1]	The Danio rerio sequencing project at the Sanger Institute Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tuebingen.
[2]	"Online automated in vivo zebrafish phosphoproteomics: from large-scale analysis down to a single embryo." Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J., Slijper M., Heck A.J.R. J. Proteome Res. 7:1555-1564(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950182 Genomic DNA. Translation: CAM13000.1. Sequence problems.
IPI	IPI00496386.
UniGene	Dr.105705. Dr.162164. Dr.162176. Dr.76903.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	7955.ENSDARP00000081914.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSDART00000143452; ENSDARP00000118791; ENSDARG00000061394.
Organism-specific databases
ZFIN	ZDB-GENE-010328-16. baz1b.
Phylogenomic databases
eggNOG	COG5076.
GeneTree	ENSGT00660000095335.
HOGENOM	HOG000095180.
InParanoid	A2BIL7.
OrthoDB	EOG4MKNFK.
Gene expression databases
ArrayExpress	A2BIL7.
Bgee	A2BIL7.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.30.40.10. 1 hit.
InterPro	IPR001487. Bromodomain. IPR018501. DDT_dom_superfamily. IPR013136. WSTF_Acf1_Cbp146. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00439. Bromodomain. 1 hit. PF00628. PHD. 1 hit. PF10537. WAC_Acf1_DNA_bd. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00249. PHD. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. False negative. PS50014. BROMODOMAIN_2. 1 hit. PS50827. DDT. 1 hit. PS51136. WAC. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BAZ1B_DANRE

Accession

Primary (citable) accession number: A2BIL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents