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Protein Page:
WSTF (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
WSTF plays a central role in chromatin remodeling and acts as a transcription regulator. Apparently possesses tyrosine-protein kinase activity, but bears no sequence resemblance classical tyrosine kinase proteins. Involved in DNA damage response by phosphorylating Y142 of histone H2AX. H2AXpY142 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 Y142, and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. 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), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association. Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA. Ubiquitously expressed with high levels of expression in heart, brain, placenta, skeletal muscle and ovary. Two alternatively-spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; DNA replication; Nuclear receptor co-regulator; EC 2.7.10.2; Protein kinase, Ser/Thr (non-receptor); ATYPICAL group; BAZ family
Cellular Component: centric heterochromatin; nuclear replication fork; condensed chromosome
Molecular Function: protein binding; vitamin D receptor binding; zinc ion binding; protein-tyrosine kinase activity; non-membrane spanning protein tyrosine kinase activity; histone kinase activity; chromatin binding; protein complex scaffold; ATP binding
Biological Process: heart morphogenesis; peptidyl-tyrosine phosphorylation; transcription, DNA-dependent; nucleosome disassembly; regulation of transcription, DNA-dependent; chromatin-mediated maintenance of transcription; double-strand break repair; histone phosphorylation; ATP-dependent chromatin remodeling; response to DNA damage stimulus
Reference #:  Q9UIG0 (UniProtKB)
Alt. Names/Synonyms: BAZ1B; Bromodomain adjacent to zinc finger domain protein 1B; bromodomain adjacent to zinc finger domain, 1B; hWALp2; transcription factor WSTF; Tyrosine-protein kinase BAZ1B; WBSC10; WBSCR10; WBSCR9; Williams syndrome transcription factor; Williams-Beuren syndrome chromosomal region 10 protein; Williams-Beuren syndrome chromosomal region 9 protein; Williams-Beuren syndrome chromosome region 10; Williams-Beuren syndrome chromosome region 9; WSTF
Gene Symbols: BAZ1B
Molecular weight: 170,903 Da
Basal Isoelectric point: 8.7  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

WSTF

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: S158‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S58-p TCKSTGSsQLTHKEA
0 1 S152 EEATEKKSDGACDsP
1 9 S158-p KSDGACDsPssDKEN
0 12 S160-p DGACDsPssDKENss
0 8 S161-p GACDsPssDKENssQ
0 6 S166-p PssDKENssQIAQDH
0 5 S167-p ssDKENssQIAQDHQ
0 4 S189-p EDEGRREsINDRARR
0 3 S197-p INDRARRsPRKLPts
0 1 T203-p RsPRKLPtsLKKGER
0 4 S204-p sPRKLPtsLKKGERK
0 1 T266-p HNALRAGtGENAPWV
0 2 Y296-p SDFLLDPykYMTLNP
0 2 K297-a DFLLDPykYMTLNPS
0 1 K297-u DFLLDPykYMTLNPS
0 4 S312-p TKRKNTGsPDRKPsK
0 3 S318-p GsPDRKPsKKsKTDN
0 1 S321-p DRKPsKKsKTDNSSL
0 5 N325 sKKsKTDNSSLSsPL
0 2 S326 KKsKTDNSSLSsPLN
0 1 S327 KsKTDNSSLSsPLNP
0 1 S329 KTDNSSLSsPLNPKL
0 4 S330-p TDNSSLSsPLNPKLW
0 3 S345-p CHVHLKKsLsGsPLK
0 4 S347-p VHLKKsLsGsPLKVK
0 10 S349-p LKKsLsGsPLKVKNS
0 1 S359-p KVKNSKNsKsPEEHL
0 14 S361-p KNSKNsKsPEEHLEE
0 7 S374-p EEMMKMMsPNKLHTN
0 23 K409-a LKAKGRSkGILNGQk
0 10 K416-a kGILNGQkSTGNSKS
0 2 K426-a GNSKSPKkGLKTPkT
0 4 K432-a KkGLKTPkTKMKQMT
0 1 T439 kTKMKQMTLLDMAKG
0 1 N456 KMTRAPRNsGGTPRT
0 2 S457-p MTRAPRNsGGTPRTS
0 1 S464 sGGTPRTSSKPHKHL
0 1 K501 ALSCVISKTARLLSS
0 2 K588-u EDQELTGkNLPAFRL
0 1 S699-p VRLCLRRsDVQEEsE
0 15 S705-p RsDVQEEsEGsDtDD
0 13 S708-p VQEEsEGsDtDDNKD
0 5 T710-p EEsEGsDtDDNKDsA
0 2 S716-p DtDDNKDsAAFEDNE
0 1 A717 tDDNKDsAAFEDNEV
0 1 K778-u QMSAELWkERLAVLK
0 1 T945-p NHHCKDHtVsGDEDy
0 3 S947-p HCKDHtVsGDEDyCP
0 1 Y952-p tVsGDEDyCPRSKKA
0 3 K1068-u EVATRLQkGGLGYVE
0 1 S1147-p VEEAKVAsALEKWKT
0 5 S1315-p KPHSTRRsQPKAPPV
0 46 K1335-a DELVLQTkRSsRRQs
0 1 K1335-u DELVLQTkRSsRRQs
0 2 S1338-p VLQTkRSsRRQsLEL
0 39 S1342-p kRSsRRQsLELQKCE
0 44 S1468-p LAEDEGDsEPEAVGQ
0 5 P1470 EDEGDsEPEAVGQSR
0 14 A1472 EGDsEPEAVGQSRGR
  mouse

 
S58 TCKSTGSSQLTHKEA
S152-p EEAVEKKsDGACDsP
S158-p KsDGACDsPssDKEN
S160-p DGACDsPssDKENsS
S161-p GACDsPssDKENsSQ
S166-p PssDKENsSQMAQDL
S167 ssDKENsSQMAQDLQ
S189-p EDEGRREsINDRARR
S197 INDRARRSPRKLPTs
T203 RSPRKLPTsLKKGER
S204-p SPRKLPTsLKKGERK
T266 HNALRAGTGENAPWV
Y296 SDFLLDPYKYMTLNP
K297 DFLLDPYKYMTLNPS
K297 DFLLDPYKYMTLNPS
S312-p TKRRNTGsPDRKPsK
S318-p GsPDRKPsKKPKRDs
P321 DRKPsKKPKRDsssL
S325-p sKKPKRDsssLssPL
S326-p KKPKRDsssLssPLN
S327-p KPKRDsssLssPLNP
S329-p KRDsssLssPLNPKL
S330-p RDsssLssPLNPKLW
S345-p CHVHLEKsLNGPPLK
N347 VHLEKsLNGPPLKVK
P349 LEKsLNGPPLKVKNS
S359-p KVKNSKNsKsPEEHL
S361-p KNSKNsKsPEEHLEG
S374-p EGVMKIMsPNNNKLH
K410-a LKAKGRGkGILNGQk
K417-a kGILNGQkSTGNSKS
K427 GNSKSPSKCVKTPKT
K433 SKCVKTPKTKMKQMt
T440-p KTKMKQMtLLDMAKG
S457-p KMTRTPRssGGVPRS
S458-p MTRTPRssGGVPRSs
S465-p sGGVPRSsGKPHKHL
K502-u ALSCVISkTARLLSN
R589 EDQELGGRNLPAFRL
C700 VRLCLRRCDVQEDsE
S706-p RCDVQEDsEGsEtDD
S709-p VQEDsEGsEtDDNKD
T711-p EDsEGsEtDDNKDst
S717-p EtDDNKDstPFEDNE
T718-p tDDNKDstPFEDNEV
K779 QVSAELWKERLAVLK
S946 KHHRKDHSNLPDDDY
- gap
Y953 SNLPDDDYCPRSKKA
K1068-u EVATRLQkGGLGYME
S1147 VEEAKVASALEKWKT
S1315-p KSHPARRsRPKDDPE
K1331-a DDLVLQTkRISRRQs
K1331 DDLVLQTKRISRRQs
S1334 VLQTkRISRRQsLEL
S1338-p kRISRRQsLELQKCE
S1464-p LADDEGDsDsEsVGQ
S1466-p DDEGDsDsEsVGQSR
S1468-p EGDsDsEsVGQSRGR
  rat

 
S58 TCKSTGSSQLTHKEA
S152 EEAAEKKSDGTCDSP
S158 KSDGTCDSPsSDKEN
S160-p DGTCDSPsSDKENSS
S161 GTCDSPsSDKENSSQ
S166 PsSDKENSSQMAQDH
S167 sSDKENSSQMAQDHQ
S188 EDGGRRESINDRARR
S196 INDRARRSPRKLPTS
T202 RSPRKLPTSLKKGER
S203 SPRKLPTSLKKGERK
T265 HNALRAGTGENAPWV
Y295 SDFLLDPYKYMTLNP
K296 DFLLDPYKYMTLNPS
K296 DFLLDPYKYMTLNPS
S311 TKRKNTGSPDRKPsK
S317-p GSPDRKPsKKPKRDN
P320 DRKPsKKPKRDNSSL
N324 sKKPKRDNSSLSSPL
S325 KKPKRDNSSLSSPLN
S326 KPKRDNSSLSSPLNP
S328 KRDNSSLSSPLNPKL
S329 RDNSSLSSPLNPKLW
S344 CHVHLEKSLNGPPLK
N346 VHLEKSLNGPPLKVK
P348 LEKSLNGPPLKVKNS
S358 KVKNSKNSKSPEEHL
S360 KNSKNSKSPEEHLEE
S373 EEVMKIMSPNKLHSF
K407 LKAKGRGKGILNGQK
K414 KGILNGQKSTGNSKS
K424 GNSKSPSKCVKTPKT
K430 SKCVKTPKTKMKQMT
T437 KTKMKQMTLLDMAKG
S454 KMTRTPRSSGGVPRS
S455 MTRTPRSSGGVPRSS
S462 SGGVPRSSGKPHKHL
K499 ALSCVISKTARLLSS
R586 EDQELGGRNLPTFRL
C697 VRLCLRRCDVQEDsE
S703-p RCDVQEDsEGsDTDD
S706-p VQEDsEGsDTDDNKD
T708 EDsEGsDTDDNKDST
S714 DTDDNKDSTPFEDNE
T715 TDDNKDSTPFEDNEV
K776 QMSAELWKERLAVLK
- gap
- gap
Y950 NNLPDDDYCPRSKKA
K1065 EVATRLQKGGLGYME
S1144 VEEAKVASALEKWKT
S1312 KSHAARRSRPKDDTE
K1328 DELVLQTKRSSRRQS
K1328 DELVLQTKRSSRRQS
S1331 VLQTKRSSRRQSLEL
S1335 KRSSRRQSLELQKCE
S1461-p LADDEGDsDsEsVGQ
S1463-p DDEGDsDsEsVGQSR
S1465-p EGDsDsEsVGQSRGR
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