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Q9Z277

- BAZ1B_MOUSE

UniProt

Q9Z277 - BAZ1B_MOUSE

Protein

Tyrosine-protein kinase BAZ1B

Gene

Baz1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (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. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. 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), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. 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 fingeri1184 – 123451PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. histone binding Source: UniProtKB
    4. histone kinase activity Source: UniProtKB
    5. lysine-acetylated histone binding Source: UniProtKB
    6. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    7. protein binding Source: UniProtKB
    8. protein tyrosine kinase activity Source: UniProtKB
    9. vitamin D receptor activator activity Source: BHF-UCL
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP-dependent chromatin remodeling Source: Ensembl
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. chromatin assembly or disassembly Source: MGI
    4. chromatin-mediated maintenance of transcription Source: BHF-UCL
    5. chromatin remodeling Source: MGI
    6. DNA replication-dependent nucleosome disassembly Source: Ensembl
    7. double-strand break repair Source: BHF-UCL
    8. heart morphogenesis Source: BHF-UCL
    9. histone phosphorylation Source: UniProtKB
    10. positive regulation of receptor activity Source: GOC
    11. regulation of transcription, DNA-templated Source: BHF-UCL
    12. 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
    Williams-Beuren syndrome chromosomal region 9 protein homolog
    Gene namesi
    Name:Baz1b
    Synonyms:Wbscr9, Wstf
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1353499. Baz1b.

    Subcellular locationi

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

    GO - Cellular componenti

    1. condensed chromosome Source: MGI
    2. nuclear replication fork Source: Ensembl
    3. nucleus Source: MGI
    4. pericentric heterochromatin Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14791479Tyrosine-protein kinase BAZ1BPRO_0000211171Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei161 – 1611Phosphoserine1 Publication
    Modified residuei266 – 2661PhosphothreonineBy similarity
    Modified residuei330 – 3301PhosphoserineBy similarity
    Modified residuei345 – 3451PhosphoserineBy similarity
    Modified residuei361 – 3611Phosphoserine1 Publication
    Modified residuei374 – 3741PhosphoserineBy similarity
    Modified residuei706 – 7061PhosphoserineBy similarity
    Modified residuei709 – 7091PhosphoserineBy similarity
    Modified residuei717 – 7171PhosphoserineBy similarity
    Modified residuei1315 – 13151PhosphoserineBy similarity
    Modified residuei1331 – 13311N6-acetyllysine1 Publication
    Modified residuei1338 – 13381PhosphoserineBy similarity
    Modified residuei1464 – 14641Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z277.
    PaxDbiQ9Z277.
    PRIDEiQ9Z277.

    PTM databases

    PhosphoSiteiQ9Z277.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined including heart, brain, spleen, lung, skeletal muscle, kidney and testis.1 Publication

    Developmental stagei

    Expressed as early as day 7 and in equal amounts during gestation.

    Gene expression databases

    BgeeiQ9Z277.
    CleanExiMM_BAZ1B.
    GenevestigatoriQ9Z277.

    Interactioni

    Subunit structurei

    Interacts with MYO1C By similarity. Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smarca5Q91ZW32EBI-927576,EBI-927547

    Protein-protein interaction databases

    BioGridi204552. 3 interactions.
    DIPiDIP-36072N.
    IntActiQ9Z277. 2 interactions.
    MINTiMINT-4089121.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z277.
    SMRiQ9Z277. Positions 1185-1235.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 126107WACPROSITE-ProRule annotationAdd
    BLAST
    Domaini605 – 66965DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini1352 – 142271BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 345345Mediates the tyrosine-protein kinase activityBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili537 – 58751Sequence AnalysisAdd
    BLAST
    Coiled coili774 – 80936Sequence AnalysisAdd
    BLAST
    Coiled coili854 – 89037Sequence AnalysisAdd
    BLAST
    Coiled coili1257 – 128428Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi207 – 2137C motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi306 – 579274Lys-richAdd
    BLAST

    Domaini

    The N-terminal part, including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity.By similarity
    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 fingeri1184 – 123451PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    GeneTreeiENSGT00740000115051.
    HOVERGENiHBG050668.
    InParanoidiQ3USR7.
    KOiK11658.
    OMAiDEDYCPR.
    OrthoDBiEOG72G17K.
    PhylomeDBiQ9Z277.
    TreeFamiTF106397.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR018500. DDT_dom_subgr.
    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.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Z277-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW     50
    TCKSTGSSQL THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE 100
    KLVDSAWLEI MTKYAVGEEC DFEVGKEKML KVKIVKIHPL EKVDEEAVEK 150
    KSDGACDSPS SDKENSSQMA QDLQKKETVV KEDEGRRESI NDRARRSPRK 200
    LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS LIRTERPPNK 250
    EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 300
    LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP 350
    LKVKNSKNSK SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD 400
    KPLKAKGRGK GILNGQKSTG NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK 450
    MTRTPRSSGG VPRSSGKPHK HLPPAALHLI AYYKENKDKE DKKSALSCVI 500
    SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS EEQRKEYLKK 550
    KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP 600
    EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL 650
    YLNRVLVILL QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC 700
    DVQEDSEGSE TDDNKDSTPF EDNEVQDEFL EKLETSEFFE LTSEEKLRIL 750
    TALCHRILMT YSVQDHMETR QQVSAELWKE RLAVLKEEND KKRAEKQKRK 800
    EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI SAVKSRRLLS 850
    MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR 900
    RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD 950
    DDYCPRSKKA NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL 1000
    DELLSCLHPQ GIRESQLKER LEKRYQEITH SIYLARKPNL GLKSCDGNQE 1050
    LLNFLRSDLI EVATRLQKGG LGYMEGTSEF EARVISLEKL KDFGECVIAL 1100
    QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV EEAKVASALE 1150
    KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 1200
    LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST 1250
    SEGSEGDESG EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR 1300
    PGRPPGKKSH PARRSRPKDD PEVDDLVLQT KRISRRQSLE LQKCEDILHK 1350
    LVKYRFSWPF REPVTRDEAE DYYDVIEHPM DFQTIQNKCS CGNYRSVQEF 1400
    LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL PGHPYVRRKR 1450
    RKFPDRLADD EGDSDSESVG QSRGRRQKK 1479
    Length:1,479
    Mass (Da):170,651
    Last modified:June 16, 2009 - v2
    Checksum:i6EFBF3913EA93AF0
    GO
    Isoform 2 (identifier: Q9Z277-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-298: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,181
    Mass (Da):135,988
    Checksum:iA5A6A30F20BA9091
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti957 – 9571S → R in AAD08676. (PubMed:9858827)Curated
    Sequence conflicti1017 – 10171L → F in AAD08676. (PubMed:9858827)Curated
    Sequence conflicti1031 – 10344SIYL → CNYM in AAD08676. (PubMed:9858827)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 298298Missing in isoform 2. 1 PublicationVSP_037470Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF084480 mRNA. Translation: AAD08676.1.
    CH466529 Genomic DNA. Translation: EDL19376.1.
    BC141399 mRNA. Translation: AAI41400.1.
    AK017894 mRNA. Translation: BAB30992.1.
    AK037737 mRNA. Translation: BAC29862.1.
    AK137139 mRNA. Translation: BAE23247.1.
    AK140172 mRNA. Translation: BAE24264.1.
    AK141305 mRNA. Translation: BAE24643.1.
    CCDSiCCDS19736.1. [Q9Z277-1]
    PIRiT17401.
    RefSeqiNP_035844.2. NM_011714.2. [Q9Z277-1]
    UniGeneiMm.40331.

    Genome annotation databases

    EnsembliENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748. [Q9Z277-1]
    GeneIDi22385.
    KEGGimmu:22385.
    UCSCiuc008zxz.2. mouse. [Q9Z277-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF084480 mRNA. Translation: AAD08676.1 .
    CH466529 Genomic DNA. Translation: EDL19376.1 .
    BC141399 mRNA. Translation: AAI41400.1 .
    AK017894 mRNA. Translation: BAB30992.1 .
    AK037737 mRNA. Translation: BAC29862.1 .
    AK137139 mRNA. Translation: BAE23247.1 .
    AK140172 mRNA. Translation: BAE24264.1 .
    AK141305 mRNA. Translation: BAE24643.1 .
    CCDSi CCDS19736.1. [Q9Z277-1 ]
    PIRi T17401.
    RefSeqi NP_035844.2. NM_011714.2. [Q9Z277-1 ]
    UniGenei Mm.40331.

    3D structure databases

    ProteinModelPortali Q9Z277.
    SMRi Q9Z277. Positions 1185-1235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204552. 3 interactions.
    DIPi DIP-36072N.
    IntActi Q9Z277. 2 interactions.
    MINTi MINT-4089121.

    PTM databases

    PhosphoSitei Q9Z277.

    Proteomic databases

    MaxQBi Q9Z277.
    PaxDbi Q9Z277.
    PRIDEi Q9Z277.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002825 ; ENSMUSP00000002825 ; ENSMUSG00000002748 . [Q9Z277-1 ]
    GeneIDi 22385.
    KEGGi mmu:22385.
    UCSCi uc008zxz.2. mouse. [Q9Z277-1 ]

    Organism-specific databases

    CTDi 9031.
    MGIi MGI:1353499. Baz1b.

    Phylogenomic databases

    eggNOGi COG5076.
    GeneTreei ENSGT00740000115051.
    HOVERGENi HBG050668.
    InParanoidi Q3USR7.
    KOi K11658.
    OMAi DEDYCPR.
    OrthoDBi EOG72G17K.
    PhylomeDBi Q9Z277.
    TreeFami TF106397.

    Miscellaneous databases

    ChiTaRSi BAZ1B. mouse.
    NextBioi 302753.
    PROi Q9Z277.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z277.
    CleanExi MM_BAZ1B.
    Genevestigatori Q9Z277.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR018500. DDT_dom_subgr.
    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.
    SM00571. DDT. 1 hit.
    SM00249. PHD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
    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. "Identification of the WBSCR9 gene, encoding a novel transcriptional regulator, in the Williams-Beuren syndrome deletion at 7q11.23."
      Peoples R.J., Cisco M.J., Kaplan P., Francke U.
      Cytogenet. Cell Genet. 82:238-246(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-810 AND 823-1799 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-786 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina, Thymus and Urinary bladder.
    5. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
      Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
      Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription."
      Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.
      EMBO Rep. 7:525-530(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYO1C.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-1464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SMARCA5.
    10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiBAZ1B_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z277
    Secondary accession number(s): B9EJ99
    , Q3URP5, Q3USR7, Q3UVM2, Q8CAU9, Q9CU68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 118 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3