Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A8DZJ1

- BAZ1B_XENLA

UniProt

A8DZJ1 - BAZ1B_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
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 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-KW
Complete GO annotation...

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

        10         20         30         40         50
MAPLLGRRPF PLVKPLSEAA TGEGEEEVYM IEHSKEAFRS REEYESRLER
60 70 80 90 100
YAERIWTCKS TGSSQLTHKE AWDEEQEVAE LLKEEFPVWY EKQVLEMVHH
110 120 130 140 150
NTISLDKLVD QSWMEIMTKY ADGEECDFEV GPEKYLRAKI VKVHPLEKEE
160 170 180 190 200
QASEKKSEGS CDSPSSDKEN SNKVAQDIQL KEESNRLESL SSLRESDRAR
210 220 230 240 250
RSPRKLPTSL KKEEKKWVPP KFLPHKYDVK LLNEDKVISF VPVDSLYRSE
260 270 280 290 300
RPPNKEILRY FIRHNALRIG TGENAPWVVE DELVKKYTLP SKFSDFLLDP
310 320 330 340 350
HKYMTLNPSS ATKRKSLGSP DQKPAKKSKK SPLSPSSWSL ANLKKTAVNS
360 370 380 390 400
SSSEEEMQLM IGANLNKKGS IGKKSDKKKP KNGKSQVLNG QKISAKTRSP
410 420 430 440 450
KKGLKSPKLK QMTLLDMAKS TPKVSRAQKG GSNTPRSSSK PNKYLPPAAL
460 470 480 490 500
HLISYYRDNK NREDRKSALS ALISKVARML SAEDRKRLPD DLQELVQKRY
510 520 530 540 550
ELLEHRKQWA VMTEEQREEY MRKKREALKA RIKEKTRERK QKEREERLEK
560 570 580 590 600
QKRYEDQDLT GKSLPTFKLV DTPEGLPNAL FGDVAMVIEF LSGYSDLLLP
610 620 630 640 650
DGQYPVTAVS LMEALAAEKG GFMYLNRGLV VLLQTLLQDE IAEDYGELGM
660 670 680 690 700
KLSEIPLTLH SASELVRLCL RKSDSPAGEN ESIEKGDEDS EGSAVYQDDE
710 720 730 740 750
VEDEYLEKLE TSEFFELTTE EKLHILAALC HRILMTYSVQ DHVDAKQQRS
760 770 780 790 800
GELWKERLAI LKGENDKKRA AKQKRKEQGT VKPKEEVQAA KIVKKQEKIN
810 820 830 840 850
TQQDNDAEDM ISAVKSRRLQ AMQAKKEKEE HEKLTKERIE RETEEERSRK
860 870 880 890 900
QKASAEKAFH EGIAKAKLVL RRSPLGTDRN HNRYWLFSDE VPGLYIEKGW
910 920 930 940 950
VHDSINYRFS PESKQDSEQD AEESEDANSS IGCPDDSTQR EEKHAETTVP
960 970 980 990 1000
KQGQNLWFLC DTQKELDELL DSLHPQGFRE SQLKERLQNR YQDIMHSIHL
1010 1020 1030 1040 1050
ARKQNLGLKT CDGQQELLNF LRSDIIEVAT RLQKGGLGYL DDTTEFEAKV
1060 1070 1080 1090 1100
RTFENLKDFG ECIVFLQAAV IKKFLQGFMA PKQKKRKHQS EEAAAKAEEQ
1110 1120 1130 1140 1150
DEEKKMAEEA KVASAVEKWK VAIRDAQTFS RMHVLLGMLD ACIKWDMSSE
1160 1170 1180 1190 1200
NARCKVCRKK GEDDKLILCD ECNKAFHLFC LRPVLFNIPD GEWLCPACQP
1210 1220 1230 1240 1250
ATARRSSRGR NYAEDSTQDE DEEEEEEESE EEEEEESDEE EEEQEMMGQR
1260 1270 1280 1290 1300
LRSRKAAKGK PGRPTRRGRP PKNNTHSRVS RQRYVEDTEA DVEEMVRQSK
1310 1320 1330 1340 1350
PTSRRQNQEF QKCEEILAKL IKYRFSWPFR EPFNADEIED YTKVVTTPMD
1360 1370 1380 1390 1400
FQTMQSKCSC GSYQTVQEFL NDLKLVFGNT ELYYEAGSSQ LSCLEKTEQC
1410 1420 1430 1440
ARDLLGKHLP AHTYQRRHRK HQSPEPEPET ANPGRGRKQK K
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

« 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: October 29, 2014
This is version 44 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