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A2BIL7 (BAZ1B_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length1536 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDNA damage
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
Coiled coil
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

histone phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP 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: UniProtKB-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15361536Tyrosine-protein kinase BAZ1B
PRO_0000378188

Regions

Domain25 – 130106WAC
Domain603 – 66765DDT
Domain1383 – 145371Bromo
Zinc finger1202 – 125251PHD-type
Coiled coil515 – 58369 Potential
Coiled coil768 – 80336 Potential
Coiled coil850 – 89041 Potential
Coiled coil1261 – 129333 Potential

Amino acid modifications

Modified residue13491Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2BIL7 [UniParc].

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

FASTA1,536176,213
        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 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950182 Genomic DNA. Translation: CAM13000.1. Sequence problems.
UniGeneDr.105705.
Dr.162164.
Dr.162176.
Dr.76903.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000081914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000095180.
InParanoidA2BIL7.
PhylomeDBA2BIL7.

Gene expression databases

BgeeA2BIL7.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR028935. WHIM3_domain.
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]
PfamPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS50014. 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]
ProtoNetSearch...

Other

PROA2BIL7.

Entry information

Entry nameBAZ1B_DANRE
AccessionPrimary (citable) accession number: A2BIL7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families