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A2BIL7

- BAZ1B_DANRE

UniProt

A2BIL7 - BAZ1B_DANRE

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Protein

Tyrosine-protein kinase BAZ1B

Gene

baz1b

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).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactori

Mn2+By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1202 – 125251PHD-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
ORF Names:ch211-203b8.1
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

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 – 15361536Tyrosine-protein kinase BAZ1BPRO_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).By similarity

Protein-protein interaction databases

STRINGi7955.ENSDARP00000081914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 130106WACPROSITE-ProRule annotationAdd
BLAST
Domaini603 – 66765DDTPROSITE-ProRule annotationAdd
BLAST
Domaini1383 – 145371BromoPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili515 – 58369Sequence AnalysisAdd
BLAST
Coiled coili768 – 80336Sequence AnalysisAdd
BLAST
Coiled coili850 – 89041Sequence AnalysisAdd
BLAST
Coiled coili1261 – 129333Sequence 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 fingeri1202 – 125251PHD-typePROSITE-ProRule annotationAdd
BLAST

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

« Hide

        10         20         30         40         50
MAPLLGRKPY PLVKPLSEPP GPGEEVYTIE HTKEAFRNKE EYEARLRRYG
60 70 80 90 100
ERIWTCKSTG SSQLTHKEAW EEEQEVTELL QEEYPVWFEK PVLEIVHHNT
110 120 130 140 150
VPLDKLVDQV WVEILTKYAV GEKCDLMVGN DKTLSVEVVK IHPLENPPEE
160 170 180 190 200
NAEKKMEGAC DSPSSDKENA SQENLKKEPQ SKEEESRRES LSDRARRSPR
210 220 230 240 250
KLPTTMKEEK KKWVMPKFLP HKYDVKLVNE DKVISDVPAD NLFRTERPPN
260 270 280 290 300
KEIMRYFIRH YALRLGSGES APWVVEDELV KKFSLPSKFS DFLLDPHKFL
310 320 330 340 350
AENPSTKRKS LSSPEGKPRK RLKNVETGTG GEGAKGDKKK NKDSQNIPLS
360 370 380 390 400
PTIWSHMQVK KVNGSPLKMK NSGTSKKSDE ENVLGTPKSS KKQGDKKSSD
410 420 430 440 450
PKRRRKSGLN KTPNSQRLSK KEDKSLGGAK KPRMKQMTLL DLAKSPAAAG
460 470 480 490 500
SPKKQRRSST TGSAKLGKPF PPMALHLLRF YKENKGKEDK KTTLSSLLSK
510 520 530 540 550
AAKALSPEDR SRLPEELKEL VQKRWELLEQ KRRWALMSEE EKQSVLKQKR
560 570 580 590 600
QEVKQKLREK AKERREKEMQ VRREMSRRYE DQELEGKNLP AFRLFDMPEG
610 620 630 640 650
LPNTIFGDVA MVVEFLHCYS GLLMPDDQYP ITSIALLEAL AGEKAGFLYL
660 670 680 690 700
NRVLVVLLQT LLQDELAEGY SELDMPLSEI PLTMHSVSEL VRLCLRPSDA
710 720 730 740 750
HEEESARGSD DWQSGADFDD MVSSEFLEKL ETAEVFELDP QEKVSLLLAL
760 770 780 790 800
CHRILMTYSV EDHVEAVHQK SAEMWKERVA TLKEANDRKR AEKQKRKEQM
810 820 830 840 850
ETKTDGDVLI KAEKKKESTV KKETPKVLPK EEPEPEDMIS TVKSRRLMSI
860 870 880 890 900
QAKKEKEEQE RLNKVRMEKE AEEERIRRQK AATEKAFQDA VTKAKLVLRR
910 920 930 940 950
TPLGTDRNHN RYWLFSDVVP GLYIEKGWVH ESIDYSFTLP PEEEPVLTEE
960 970 980 990 1000
EEEEEEVKKE EETEDGEKED EGSIISASND ISQQGAPSHE SSIETTVPKQ
1010 1020 1030 1040 1050
GQNLWFVCDT PKDFDELLES LHPQGVRESE LKIRLQINYQ EILHSIHLTK
1060 1070 1080 1090 1100
KGNPGLKTCD GHQELLKFLR SDIIEVASRL QKGGLGYLED TSEFEEFEER
1110 1120 1130 1140 1150
VKTLEKLPEF GECVIALQES VIKKFLQGFM APKQKKKKKT GGEESTTAEE
1160 1170 1180 1190 1200
VDDQKKLAEE ARVATAVEKW KTAVREAQTF SRMHVLLGML DACIKWDMSA
1210 1220 1230 1240 1250
ENARCKVCRR KGEDDKLILC DECNKAFHLF CLRPALYRIP AGEWLCPACQ
1260 1270 1280 1290 1300
PTIARRSSRG RNYKEDSEEE EDSEEEDEEE SEEEDSEEEH RNTGHSLRSR
1310 1320 1330 1340 1350
KKVKTSSKSK MQKKPAKPAS RSASKTDTNP SKTSPKSSAK PKSRAAPSSP
1360 1370 1380 1390 1400
VDIDELVRQS SKPPSRKKDV ELQKCEEILQ KIMKFRHSWP FREPVSAEEA
1410 1420 1430 1440 1450
EDYQDVITSP MDLTTMQGKF KSSEYHSASD FIEDMKLIFS NAEEYNQPSS
1460 1470 1480 1490 1500
NVLTCMSRTE EAFVELLQKS LPGVSYLRRR TRKRAATPSD NSDDDDDDEE
1510 1520 1530
EDERSKKQKN GKQGKKASSK RKVEHSRTEK YQTKQK
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 63 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