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A8DZJ1 (BAZ1B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length1441 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Tissue specificity

Highly expressed in the neural tube. Ref.1

Developmental stage

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. Ref.1

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

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
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 – 14411441Tyrosine-protein kinase BAZ1B
PRO_0000378189

Regions

Domain26 – 132107WAC
Domain578 – 64265DDT
Domain1321 – 139171Bromo
Zinc finger1151 – 120151PHD-type
Coiled coil513 – 55846 Potential
Coiled coil813 – 86149 Potential
Coiled coil1080 – 111334 Potential
Coiled coil1213 – 125341 Potential

Experimental info

Sequence conflict2751A → P in AAI26048. Ref.2
Sequence conflict7631G → E in CAJ29032. Ref.1
Sequence conflict7711A → E in CAJ29032. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A8DZJ1 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 9124174FDBBC09ED

FASTA1,441166,153
        10         20         30         40         50         60 
MAPLLGRRPF PLVKPLSEAA TGEGEEEVYM IEHSKEAFRS REEYESRLER YAERIWTCKS 

        70         80         90        100        110        120 
TGSSQLTHKE AWDEEQEVAE LLKEEFPVWY EKQVLEMVHH NTISLDKLVD QSWMEIMTKY 

       130        140        150        160        170        180 
ADGEECDFEV GPEKYLRAKI VKVHPLEKEE QASEKKSEGS CDSPSSDKEN SNKVAQDIQL 

       190        200        210        220        230        240 
KEESNRLESL SSLRESDRAR RSPRKLPTSL KKEEKKWVPP KFLPHKYDVK LLNEDKVISF 

       250        260        270        280        290        300 
VPVDSLYRSE RPPNKEILRY FIRHNALRIG TGENAPWVVE DELVKKYTLP SKFSDFLLDP 

       310        320        330        340        350        360 
HKYMTLNPSS ATKRKSLGSP DQKPAKKSKK SPLSPSSWSL ANLKKTAVNS SSSEEEMQLM 

       370        380        390        400        410        420 
IGANLNKKGS IGKKSDKKKP KNGKSQVLNG QKISAKTRSP KKGLKSPKLK QMTLLDMAKS 

       430        440        450        460        470        480 
TPKVSRAQKG GSNTPRSSSK PNKYLPPAAL HLISYYRDNK NREDRKSALS ALISKVARML 

       490        500        510        520        530        540 
SAEDRKRLPD DLQELVQKRY ELLEHRKQWA VMTEEQREEY MRKKREALKA RIKEKTRERK 

       550        560        570        580        590        600 
QKEREERLEK QKRYEDQDLT GKSLPTFKLV DTPEGLPNAL FGDVAMVIEF LSGYSDLLLP 

       610        620        630        640        650        660 
DGQYPVTAVS LMEALAAEKG GFMYLNRGLV VLLQTLLQDE IAEDYGELGM KLSEIPLTLH 

       670        680        690        700        710        720 
SASELVRLCL RKSDSPAGEN ESIEKGDEDS EGSAVYQDDE VEDEYLEKLE TSEFFELTTE 

       730        740        750        760        770        780 
EKLHILAALC HRILMTYSVQ DHVDAKQQRS GELWKERLAI LKGENDKKRA AKQKRKEQGT 

       790        800        810        820        830        840 
VKPKEEVQAA KIVKKQEKIN TQQDNDAEDM ISAVKSRRLQ AMQAKKEKEE HEKLTKERIE 

       850        860        870        880        890        900 
RETEEERSRK QKASAEKAFH EGIAKAKLVL RRSPLGTDRN HNRYWLFSDE VPGLYIEKGW 

       910        920        930        940        950        960 
VHDSINYRFS PESKQDSEQD AEESEDANSS IGCPDDSTQR EEKHAETTVP KQGQNLWFLC 

       970        980        990       1000       1010       1020 
DTQKELDELL DSLHPQGFRE SQLKERLQNR YQDIMHSIHL ARKQNLGLKT CDGQQELLNF 

      1030       1040       1050       1060       1070       1080 
LRSDIIEVAT RLQKGGLGYL DDTTEFEAKV RTFENLKDFG ECIVFLQAAV IKKFLQGFMA 

      1090       1100       1110       1120       1130       1140 
PKQKKRKHQS EEAAAKAEEQ DEEKKMAEEA KVASAVEKWK VAIRDAQTFS RMHVLLGMLD 

      1150       1160       1170       1180       1190       1200 
ACIKWDMSSE NARCKVCRKK GEDDKLILCD ECNKAFHLFC LRPVLFNIPD GEWLCPACQP 

      1210       1220       1230       1240       1250       1260 
ATARRSSRGR NYAEDSTQDE DEEEEEEESE EEEEEESDEE EEEQEMMGQR LRSRKAAKGK 

      1270       1280       1290       1300       1310       1320 
PGRPTRRGRP PKNNTHSRVS RQRYVEDTEA DVEEMVRQSK PTSRRQNQEF QKCEEILAKL 

      1330       1340       1350       1360       1370       1380 
IKYRFSWPFR EPFNADEIED YTKVVTTPMD FQTMQSKCSC GSYQTVQEFL NDLKLVFGNT 

      1390       1400       1410       1420       1430       1440 
ELYYEAGSSQ LSCLEKTEQC ARDLLGKHLP AHTYQRRHRK HQSPEPEPET ANPGRGRKQK 


K 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM084226 mRNA. Translation: CAJ29032.1.
BC072944 mRNA. Translation: AAH72944.1. Sequence problems.
BC126047 mRNA. Translation: AAI26048.1.
RefSeqNP_001136259.1. NM_001142787.1.
UniGeneXl.16009.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA8DZJ1. 1 interaction.

Proteomic databases

PRIDEA8DZJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID443594.
KEGGxla:443594.

Organism-specific databases

CTD9031.
XenbaseXB-GENE-866493. baz1b.

Phylogenomic databases

KOK11658.

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.
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.
[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...

Entry information

Entry nameBAZ1B_XENLA
AccessionPrimary (citable) accession number: A8DZJ1
Secondary accession number(s): A0JMY1, Q6GQ06
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 41 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