Reviewed, UniProtKB/Swiss-Prot A8DZJ1 (BAZ1B_XENLA)

Names and origin

Protein names

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 names

Name:	baz1b
Synonyms:	wstf

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	1441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	DNA damage Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain Coiled coil Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
Gene Ontology (GO)
Biological process	histone phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from sequence or structural similarity. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin remodeling complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP 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: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1441	1441	Tyrosine-protein kinase BAZ1B		PRO_0000378189
Regions
	Domain	26 – 132	107	WAC
	Domain	578 – 642	65	DDT
	Domain	1321 – 1391	71	Bromo
	Zinc finger	1151 – 1201	51	PHD-type
	Coiled coil	513 – 558	46	Potential
	Coiled coil	813 – 861	49	Potential
	Coiled coil	1080 – 1113	34	Potential
	Coiled coil	1213 – 1253	41	Potential
Experimental info
	Sequence conflict	275	1	A → P in AAI26048. Ref.2
	Sequence conflict	763	1	G → E in CAJ29032. Ref.1
	Sequence conflict	771	1	A → E in CAJ29032. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A8DZJ1-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 9124174FDBBC09ED	FASTA	1,441	166,153
	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

References

	« Hide 'large scale' referencesShow '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: 16448863] [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
EMBLGenBankDDBJ	AM084226 mRNA. Translation: CAJ29032.1. BC072944 mRNA. Translation: AAH72944.1. Sequence problems. BC126047 mRNA. Translation: AAI26048.1.
RefSeq	NP_001136259.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	443594.
KEGG	xla:443594.
Organism-specific databases
CTD	443594.
Xenbase	XB-FEAT-853543. baz1b.
Family and domain databases
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR018501. DDT_dom_superfamily. IPR013136. WSTF_Acf1_Cbp146. IPR019786. Zinc_finger_PHD-type_CS. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. [Graphical view]
Gene3D	G3DSA:1.20.920.10. Bromodomain. 1 hit.
Pfam	PF00439. Bromodomain. 1 hit. PF00628. PHD. 1 hit. PF10537. WAC_Acf1_DNA_bd. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00249. PHD. 1 hit. SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00633. BROMODOMAIN_1. False negative. 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]
ProtoNet	Search...

Entry information

Entry name

BAZ1B_XENLA

Accession

Primary (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:	September 22, 2009
This is version 14 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project