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A8DZJ1

- BAZ1B_XENLA

UniProt

A8DZJ1 - BAZ1B_XENLA

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Protein
Tyrosine-protein kinase BAZ1B
Gene
baz1b, wstf
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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.

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-type
Add
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
Complete GO annotation...

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 By similarity
Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase By similarity.

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14411441Tyrosine-protein kinase BAZ1B
PRO_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.

Protein-protein interaction databases

IntActiA8DZJ1. 1 interaction.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 132107WAC
Add
BLAST
Domaini578 – 64265DDT
Add
BLAST
Domaini1321 – 139171Bromo
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili513 – 55846 Reviewed prediction
Add
BLAST
Coiled coili813 – 86149 Reviewed prediction
Add
BLAST
Coiled coili1080 – 111334 Reviewed prediction
Add
BLAST
Coiled coili1213 – 125341 Reviewed prediction
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the WAL family. BAZ1B subfamily.
Contains 1 bromo domain.
Contains 1 DDT domain.
Contains 1 WAC domain.

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

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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.

Sequence conflict

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 42 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

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