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A2BIL7

- BAZ1B_DANRE

UniProt

A2BIL7 - BAZ1B_DANRE

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Protein
Tyrosine-protein kinase BAZ1B
Gene
baz1b, wstf, ch211-203b8.1
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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 fingeri1202 – 125251PHD-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
ORF Names:ch211-203b8.1
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

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 – 15361536Tyrosine-protein kinase BAZ1B
PRO_0000378188Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1349 – 13491Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

BgeeiA2BIL7.

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

STRINGi7955.ENSDARP00000081914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 130106WAC
Add
BLAST
Domaini603 – 66765DDT
Add
BLAST
Domaini1383 – 145371Bromo
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili515 – 58369 Reviewed prediction
Add
BLAST
Coiled coili768 – 80336 Reviewed prediction
Add
BLAST
Coiled coili850 – 89041 Reviewed prediction
Add
BLAST
Coiled coili1261 – 129333 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

eggNOGiCOG5076.
HOGENOMiHOG000095180.
InParanoidiA2BIL7.
PhylomeDBiA2BIL7.

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.
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.
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.

A2BIL7-1 [UniParc]FASTAAdd to Basket

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MAPLLGRKPY PLVKPLSEPP GPGEEVYTIE HTKEAFRNKE EYEARLRRYG     50
ERIWTCKSTG SSQLTHKEAW EEEQEVTELL QEEYPVWFEK PVLEIVHHNT 100
VPLDKLVDQV WVEILTKYAV GEKCDLMVGN DKTLSVEVVK IHPLENPPEE 150
NAEKKMEGAC DSPSSDKENA SQENLKKEPQ SKEEESRRES LSDRARRSPR 200
KLPTTMKEEK KKWVMPKFLP HKYDVKLVNE DKVISDVPAD NLFRTERPPN 250
KEIMRYFIRH YALRLGSGES APWVVEDELV KKFSLPSKFS DFLLDPHKFL 300
AENPSTKRKS LSSPEGKPRK RLKNVETGTG GEGAKGDKKK NKDSQNIPLS 350
PTIWSHMQVK KVNGSPLKMK NSGTSKKSDE ENVLGTPKSS KKQGDKKSSD 400
PKRRRKSGLN KTPNSQRLSK KEDKSLGGAK KPRMKQMTLL DLAKSPAAAG 450
SPKKQRRSST TGSAKLGKPF PPMALHLLRF YKENKGKEDK KTTLSSLLSK 500
AAKALSPEDR SRLPEELKEL VQKRWELLEQ KRRWALMSEE EKQSVLKQKR 550
QEVKQKLREK AKERREKEMQ VRREMSRRYE DQELEGKNLP AFRLFDMPEG 600
LPNTIFGDVA MVVEFLHCYS GLLMPDDQYP ITSIALLEAL AGEKAGFLYL 650
NRVLVVLLQT LLQDELAEGY SELDMPLSEI PLTMHSVSEL VRLCLRPSDA 700
HEEESARGSD DWQSGADFDD MVSSEFLEKL ETAEVFELDP QEKVSLLLAL 750
CHRILMTYSV EDHVEAVHQK SAEMWKERVA TLKEANDRKR AEKQKRKEQM 800
ETKTDGDVLI KAEKKKESTV KKETPKVLPK EEPEPEDMIS TVKSRRLMSI 850
QAKKEKEEQE RLNKVRMEKE AEEERIRRQK AATEKAFQDA VTKAKLVLRR 900
TPLGTDRNHN RYWLFSDVVP GLYIEKGWVH ESIDYSFTLP PEEEPVLTEE 950
EEEEEEVKKE EETEDGEKED EGSIISASND ISQQGAPSHE SSIETTVPKQ 1000
GQNLWFVCDT PKDFDELLES LHPQGVRESE LKIRLQINYQ EILHSIHLTK 1050
KGNPGLKTCD GHQELLKFLR SDIIEVASRL QKGGLGYLED TSEFEEFEER 1100
VKTLEKLPEF GECVIALQES VIKKFLQGFM APKQKKKKKT GGEESTTAEE 1150
VDDQKKLAEE ARVATAVEKW KTAVREAQTF SRMHVLLGML DACIKWDMSA 1200
ENARCKVCRR KGEDDKLILC DECNKAFHLF CLRPALYRIP AGEWLCPACQ 1250
PTIARRSSRG RNYKEDSEEE EDSEEEDEEE SEEEDSEEEH RNTGHSLRSR 1300
KKVKTSSKSK MQKKPAKPAS RSASKTDTNP SKTSPKSSAK PKSRAAPSSP 1350
VDIDELVRQS SKPPSRKKDV ELQKCEEILQ KIMKFRHSWP FREPVSAEEA 1400
EDYQDVITSP MDLTTMQGKF KSSEYHSASD FIEDMKLIFS NAEEYNQPSS 1450
NVLTCMSRTE EAFVELLQKS LPGVSYLRRR TRKRAATPSD NSDDDDDDEE 1500
EDERSKKQKN GKQGKKASSK RKVEHSRTEK YQTKQK 1536
Length:1,536
Mass (Da):176,213
Last modified:June 16, 2009 - v2
Checksum:i2493AB082E67F6B2
GO

Sequence cautioni

The sequence CAM13000.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950182 Genomic DNA. Translation: CAM13000.1. Sequence problems.
UniGeneiDr.105705.
Dr.162164.
Dr.162176.
Dr.76903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX950182 Genomic DNA. Translation: CAM13000.1 . Sequence problems.
UniGenei Dr.105705.
Dr.162164.
Dr.162176.
Dr.76903.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000081914.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000095180.
InParanoidi A2BIL7.
PhylomeDBi A2BIL7.

Miscellaneous databases

PROi A2BIL7.

Gene expression databases

Bgeei A2BIL7.

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.
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.
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. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. "Online automated in vivo zebrafish phosphoproteomics: from large-scale analysis down to a single embryo."
    Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J., Slijper M., Heck A.J.R.
    J. Proteome Res. 7:1555-1564(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiBAZ1B_DANRE
AccessioniPrimary (citable) accession number: A2BIL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 60 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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