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A8DZJ1

- BAZ1B_XENLA

UniProt

A8DZJ1 - BAZ1B_XENLA

Protein

Tyrosine-protein kinase BAZ1B

Gene

baz1b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 43 (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 fingeri1151 – 120151PHD-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
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-866493. baz1b.

    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 – 14411441Tyrosine-protein kinase BAZ1BPRO_0000378189Add
    BLAST

    Proteomic databases

    PRIDEiA8DZJ1.

    Expressioni

    Tissue specificityi

    Highly expressed in the neural tube.1 Publication

    Developmental stagei

    Detected maternally in mature unfertilized oocytes and ubiquitously expressed until embryonic stage 16. In stage 17/18, expression becomes restricted to the closing neural tube.1 Publication

    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

    IntActiA8DZJ1. 1 interaction.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 132107WACPROSITE-ProRule annotationAdd
    BLAST
    Domaini578 – 64265DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini1321 – 139171BromoPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili513 – 55846Sequence AnalysisAdd
    BLAST
    Coiled coili813 – 86149Sequence AnalysisAdd
    BLAST
    Coiled coili1080 – 111334Sequence AnalysisAdd
    BLAST
    Coiled coili1213 – 125341Sequence 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 fingeri1151 – 120151PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Zinc-finger

    Phylogenomic databases

    KOiK11658.

    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.
    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.
    [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.

    A8DZJ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPLLGRRPF PLVKPLSEAA TGEGEEEVYM IEHSKEAFRS REEYESRLER     50
    YAERIWTCKS TGSSQLTHKE AWDEEQEVAE LLKEEFPVWY EKQVLEMVHH 100
    NTISLDKLVD QSWMEIMTKY ADGEECDFEV GPEKYLRAKI VKVHPLEKEE 150
    QASEKKSEGS CDSPSSDKEN SNKVAQDIQL KEESNRLESL SSLRESDRAR 200
    RSPRKLPTSL KKEEKKWVPP KFLPHKYDVK LLNEDKVISF VPVDSLYRSE 250
    RPPNKEILRY FIRHNALRIG TGENAPWVVE DELVKKYTLP SKFSDFLLDP 300
    HKYMTLNPSS ATKRKSLGSP DQKPAKKSKK SPLSPSSWSL ANLKKTAVNS 350
    SSSEEEMQLM IGANLNKKGS IGKKSDKKKP KNGKSQVLNG QKISAKTRSP 400
    KKGLKSPKLK QMTLLDMAKS TPKVSRAQKG GSNTPRSSSK PNKYLPPAAL 450
    HLISYYRDNK NREDRKSALS ALISKVARML SAEDRKRLPD DLQELVQKRY 500
    ELLEHRKQWA VMTEEQREEY MRKKREALKA RIKEKTRERK QKEREERLEK 550
    QKRYEDQDLT GKSLPTFKLV DTPEGLPNAL FGDVAMVIEF LSGYSDLLLP 600
    DGQYPVTAVS LMEALAAEKG GFMYLNRGLV VLLQTLLQDE IAEDYGELGM 650
    KLSEIPLTLH SASELVRLCL RKSDSPAGEN ESIEKGDEDS EGSAVYQDDE 700
    VEDEYLEKLE TSEFFELTTE EKLHILAALC HRILMTYSVQ DHVDAKQQRS 750
    GELWKERLAI LKGENDKKRA AKQKRKEQGT VKPKEEVQAA KIVKKQEKIN 800
    TQQDNDAEDM ISAVKSRRLQ AMQAKKEKEE HEKLTKERIE RETEEERSRK 850
    QKASAEKAFH EGIAKAKLVL RRSPLGTDRN HNRYWLFSDE VPGLYIEKGW 900
    VHDSINYRFS PESKQDSEQD AEESEDANSS IGCPDDSTQR EEKHAETTVP 950
    KQGQNLWFLC DTQKELDELL DSLHPQGFRE SQLKERLQNR YQDIMHSIHL 1000
    ARKQNLGLKT CDGQQELLNF LRSDIIEVAT RLQKGGLGYL DDTTEFEAKV 1050
    RTFENLKDFG ECIVFLQAAV IKKFLQGFMA PKQKKRKHQS EEAAAKAEEQ 1100
    DEEKKMAEEA KVASAVEKWK VAIRDAQTFS RMHVLLGMLD ACIKWDMSSE 1150
    NARCKVCRKK GEDDKLILCD ECNKAFHLFC LRPVLFNIPD GEWLCPACQP 1200
    ATARRSSRGR NYAEDSTQDE DEEEEEEESE EEEEEESDEE EEEQEMMGQR 1250
    LRSRKAAKGK PGRPTRRGRP PKNNTHSRVS RQRYVEDTEA DVEEMVRQSK 1300
    PTSRRQNQEF QKCEEILAKL IKYRFSWPFR EPFNADEIED YTKVVTTPMD 1350
    FQTMQSKCSC GSYQTVQEFL NDLKLVFGNT ELYYEAGSSQ LSCLEKTEQC 1400
    ARDLLGKHLP AHTYQRRHRK HQSPEPEPET ANPGRGRKQK K 1441
    Length:1,441
    Mass (Da):166,153
    Last modified:June 16, 2009 - v2
    Checksum:i9124174FDBBC09ED
    GO

    Sequence cautioni

    The sequence AAH72944.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti275 – 2751A → P in AAI26048. 1 PublicationCurated
    Sequence conflicti763 – 7631G → E in CAJ29032. (PubMed:16448863)Curated
    Sequence conflicti771 – 7711A → E in CAJ29032. (PubMed:16448863)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM084226 mRNA. Translation: CAJ29032.1.
    BC072944 mRNA. Translation: AAH72944.1. Sequence problems.
    BC126047 mRNA. Translation: AAI26048.1.
    RefSeqiNP_001136259.1. NM_001142787.1.
    UniGeneiXl.16009.

    Genome annotation databases

    GeneIDi443594.
    KEGGixla:443594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM084226 mRNA. Translation: CAJ29032.1 .
    BC072944 mRNA. Translation: AAH72944.1 . Sequence problems.
    BC126047 mRNA. Translation: AAI26048.1 .
    RefSeqi NP_001136259.1. NM_001142787.1.
    UniGenei Xl.16009.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A8DZJ1. 1 interaction.

    Proteomic databases

    PRIDEi A8DZJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 443594.
    KEGGi xla:443594.

    Organism-specific databases

    CTDi 9031.
    Xenbasei XB-GENE-866493. baz1b.

    Phylogenomic databases

    KOi K11658.

    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.
    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.
    [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. "Cloning and developmental expression of WSTF during Xenopus laevis embryogenesis."
      Cus R., Maurus D., Kuehl M.
      Gene Expr. Patterns 6:340-346(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-774.
      Tissue: Embryo and Oocyte.

    Entry informationi

    Entry nameiBAZ1B_XENLA
    AccessioniPrimary (citable) accession number: A8DZJ1
    Secondary accession number(s): A0JMY1, Q6GQ06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 43 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3