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A2BIL7

- BAZ1B_DANRE

UniProt

A2BIL7 - BAZ1B_DANRE

Protein

Tyrosine-protein kinase BAZ1B

Gene

baz1b

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

    Cofactori

    Manganese.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1202 – 125251PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. histone kinase activity Source: UniProtKB
    4. lysine-acetylated histone binding Source: UniProtKB
    5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    6. protein tyrosine kinase activity Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. histone phosphorylation Source: UniProtKB
    3. peptidyl-tyrosine phosphorylation Source: GOC
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    DNA damage, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:baz1b
    Synonyms:wstf
    ORF Names:ch211-203b8.1
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Unplaced

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation
    Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase By similarity.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15361536Tyrosine-protein kinase BAZ1BPRO_0000378188Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1349 – 13491Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Gene expression databases

    BgeeiA2BIL7.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000081914.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 130106WACPROSITE-ProRule annotationAdd
    BLAST
    Domaini603 – 66765DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini1383 – 145371BromoPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili515 – 58369Sequence AnalysisAdd
    BLAST
    Coiled coili768 – 80336Sequence AnalysisAdd
    BLAST
    Coiled coili850 – 89041Sequence AnalysisAdd
    BLAST
    Coiled coili1261 – 129333Sequence AnalysisAdd
    BLAST

    Domaini

    The bromo domain mediates the specific interaction with acetylated histones.By similarity

    Sequence similaritiesi

    Belongs to the WAL family. BAZ1B subfamily.Curated
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 DDT domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 WAC domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1202 – 125251PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000095180.
    InParanoidiA2BIL7.
    PhylomeDBiA2BIL7.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR001487. 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]
    PfamiPF00439. 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]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS50014. 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]

    Sequencei

    Sequence statusi: Complete.

    A2BIL7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPLLGRKPY PLVKPLSEPP GPGEEVYTIE HTKEAFRNKE EYEARLRRYG     50
    ERIWTCKSTG SSQLTHKEAW EEEQEVTELL QEEYPVWFEK PVLEIVHHNT 100
    VPLDKLVDQV WVEILTKYAV GEKCDLMVGN DKTLSVEVVK IHPLENPPEE 150
    NAEKKMEGAC DSPSSDKENA SQENLKKEPQ SKEEESRRES LSDRARRSPR 200
    KLPTTMKEEK KKWVMPKFLP HKYDVKLVNE DKVISDVPAD NLFRTERPPN 250
    KEIMRYFIRH YALRLGSGES APWVVEDELV KKFSLPSKFS DFLLDPHKFL 300
    AENPSTKRKS LSSPEGKPRK RLKNVETGTG GEGAKGDKKK NKDSQNIPLS 350
    PTIWSHMQVK KVNGSPLKMK NSGTSKKSDE ENVLGTPKSS KKQGDKKSSD 400
    PKRRRKSGLN KTPNSQRLSK KEDKSLGGAK KPRMKQMTLL DLAKSPAAAG 450
    SPKKQRRSST TGSAKLGKPF PPMALHLLRF YKENKGKEDK KTTLSSLLSK 500
    AAKALSPEDR SRLPEELKEL VQKRWELLEQ KRRWALMSEE EKQSVLKQKR 550
    QEVKQKLREK AKERREKEMQ VRREMSRRYE DQELEGKNLP AFRLFDMPEG 600
    LPNTIFGDVA MVVEFLHCYS GLLMPDDQYP ITSIALLEAL AGEKAGFLYL 650
    NRVLVVLLQT LLQDELAEGY SELDMPLSEI PLTMHSVSEL VRLCLRPSDA 700
    HEEESARGSD DWQSGADFDD MVSSEFLEKL ETAEVFELDP QEKVSLLLAL 750
    CHRILMTYSV EDHVEAVHQK SAEMWKERVA TLKEANDRKR AEKQKRKEQM 800
    ETKTDGDVLI KAEKKKESTV KKETPKVLPK EEPEPEDMIS TVKSRRLMSI 850
    QAKKEKEEQE RLNKVRMEKE AEEERIRRQK AATEKAFQDA VTKAKLVLRR 900
    TPLGTDRNHN RYWLFSDVVP GLYIEKGWVH ESIDYSFTLP PEEEPVLTEE 950
    EEEEEEVKKE EETEDGEKED EGSIISASND ISQQGAPSHE SSIETTVPKQ 1000
    GQNLWFVCDT PKDFDELLES LHPQGVRESE LKIRLQINYQ EILHSIHLTK 1050
    KGNPGLKTCD GHQELLKFLR SDIIEVASRL QKGGLGYLED TSEFEEFEER 1100
    VKTLEKLPEF GECVIALQES VIKKFLQGFM APKQKKKKKT GGEESTTAEE 1150
    VDDQKKLAEE ARVATAVEKW KTAVREAQTF SRMHVLLGML DACIKWDMSA 1200
    ENARCKVCRR KGEDDKLILC DECNKAFHLF CLRPALYRIP AGEWLCPACQ 1250
    PTIARRSSRG RNYKEDSEEE EDSEEEDEEE SEEEDSEEEH RNTGHSLRSR 1300
    KKVKTSSKSK MQKKPAKPAS RSASKTDTNP SKTSPKSSAK PKSRAAPSSP 1350
    VDIDELVRQS SKPPSRKKDV ELQKCEEILQ KIMKFRHSWP FREPVSAEEA 1400
    EDYQDVITSP MDLTTMQGKF KSSEYHSASD FIEDMKLIFS NAEEYNQPSS 1450
    NVLTCMSRTE EAFVELLQKS LPGVSYLRRR TRKRAATPSD NSDDDDDDEE 1500
    EDERSKKQKN GKQGKKASSK RKVEHSRTEK YQTKQK 1536
    Length:1,536
    Mass (Da):176,213
    Last modified:June 16, 2009 - v2
    Checksum:i2493AB082E67F6B2
    GO

    Sequence cautioni

    The sequence CAM13000.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX950182 Genomic DNA. Translation: CAM13000.1. Sequence problems.
    UniGeneiDr.105705.
    Dr.162164.
    Dr.162176.
    Dr.76903.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX950182 Genomic DNA. Translation: CAM13000.1 . Sequence problems.
    UniGenei Dr.105705.
    Dr.162164.
    Dr.162176.
    Dr.76903.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000081914.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000095180.
    InParanoidi A2BIL7.
    PhylomeDBi A2BIL7.

    Miscellaneous databases

    PROi A2BIL7.

    Gene expression databases

    Bgeei A2BIL7.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR001487. 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 ]
    Pfami PF00439. 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 ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiBAZ1B_DANRE
    AccessioniPrimary (citable) accession number: A2BIL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 61 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3