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Protein Page:
WSTF (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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; Protein kinase, Ser/Thr (non-receptor); DNA replication; EC 2.7.10.2; Nuclear receptor co-regulator; ATYPICAL group; BAZ family
Chromosomal Location of Human Ortholog: 7q11.23
Cellular Component: centric heterochromatin; condensed chromosome; nuclear replication fork; nucleoplasm
Molecular Function: ATP binding; chromatin binding; histone kinase activity; non-membrane spanning protein tyrosine kinase activity; protein binding; protein-tyrosine kinase activity; zinc ion binding
Biological Process: chromatin assembly or disassembly; chromatin-mediated maintenance of transcription; DNA repair; double-strand break repair; gene expression; heart morphogenesis; histone phosphorylation; peptidyl-tyrosine phosphorylation; positive regulation of gene expression, epigenetic; regulation of gene expression, epigenetic; regulation of transcription, DNA-dependent; response to DNA damage stimulus; transcription, DNA-dependent
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  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 2 S58‑p TCKSTGSsQLTHKEA
0 1 K151‑ac DEEATEKksDGACDs
0 3 S152‑p EEATEKksDGACDsP
1 13 S158‑p ksDGACDsPssDKEN
0 14 S160‑p DGACDsPssDKENss
0 10 S161‑p GACDsPssDKENssQ
0 7 S166‑p PssDKENssQIAQDH
0 6 S167‑p ssDKENssQIAQDHQ
0 1 K175‑ac QIAQDHQkKETVVkE
0 1 K175‑m2 QIAQDHQkKETVVkE
0 1 K181‑m2 QkKETVVkEDEGRRE
0 8 S189‑p EDEGRREsINDRARR
0 4 S197‑p INDRARRsPRKLPts
0 1 T203‑p RsPRKLPtsLKKGER
0 6 S204‑p sPRKLPtsLKKGERK
0 1 K216‑ac ERKWAPPkFLPHkyD
0 1 K221‑ac PPkFLPHkyDVKLQN
0 1 Y222‑p PkFLPHkyDVKLQNE
0 1 S234‑p QNEDKIIsNVPADSL
0 1 T266‑p HNALRAGtGENAPWV
0 1 Y282‑p EDELVKKySLPSKFs
0 1 S289‑p ySLPSKFsDFLLDPy
0 2 Y296‑p sDFLLDPykyMTLNP
0 2 K297‑ac DFLLDPykyMTLNPS
0 1 K297‑ub DFLLDPykyMTLNPS
0 2 Y298‑p FLLDPykyMTLNPST
0 1 K306‑ac MTLNPSTkRKNTGsP
0 8 S312‑p TkRKNTGsPDRKPsK
0 4 S318‑p GsPDRKPsKKsKtDN
0 2 S321‑p DRKPsKKsKtDNSsL
0 1 T323‑p KPsKKsKtDNSsLSs
0 6 N325 sKKsKtDNSsLSsPL
0 2 S326 KKsKtDNSsLSsPLN
0 2 S327‑p KsKtDNSsLSsPLNP
0 1 S329 KtDNSsLSsPLNPKL
0 10 S330‑p tDNSsLSsPLNPKLW
0 5 S345‑p CHVHLKKsLsGsPLK
0 11 S347‑p VHLKKsLsGsPLKVK
0 18 S349‑p LKKsLsGsPLKVKNS
0 2 S359‑p KVKNSKNsKsPEEHL
0 27 S361‑p KNSKNsKsPEEHLEE
0 9 S374‑p EEMMKMMsPNKLHTN
0 24 K409‑ac LKAKGRSkGILNGQk
0 10 K416‑ac kGILNGQkSTGNSKS
0 2 K426‑ac GNSKSPKkGLkTPkT
0 1 K429‑ac KSPKkGLkTPkTKMK
0 4 K432‑ac KkGLkTPkTKMKQMT
0 1 T439 kTKMKQMTLLDMAKG
0 1 K449‑ac DMAKGTQkMtRAPRN
0 1 T451‑p AKGTQkMtRAPRNsG
0 1 N456 kMtRAPRNsGGTPRT
0 2 S457‑p MtRAPRNsGGTPRTS
0 1 S464 sGGTPRTSsKPHKHL
0 1 S465‑p GGTPRTSsKPHKHLP
0 2 K501‑ub ALSCVISkTARLLSS
0 3 K588‑ub EDQELTGkNLPAFRL
0 1 S699‑p VRLCLRRsDVQEEsE
0 27 S705‑p RsDVQEEsEGsDtDD
0 23 S708‑p VQEEsEGsDtDDNKD
0 7 T710‑p EEsEGsDtDDNKDsA
0 4 S716‑p DtDDNKDsAAFEDNE
0 1 A717 tDDNKDsAAFEDNEV
0 1 T759‑p LCHRILMtySVQDHM
0 1 Y760‑p CHRILMtySVQDHME
0 1 K778‑ub QMSAELWkERLAVLK
0 1 K810‑ac AKNKENGkVENGLGk
0 2 K817‑ac kVENGLGkTDRKKEI
0 2 T833‑p KFEPQVDtEAEDMIs
0 1 S840‑p tEAEDMIsAVKsRRL
0 1 S844‑p DMIsAVKsRRLLAIQ
0 1 K864‑ac EIQEREMkVKLERQA
0 1 S932‑p EKGWVHDsIDyRFNH
0 1 Y935‑p WVHDsIDyRFNHHCK
0 4 T945‑p NHHCKDHtVsGDEDy
0 13 S947‑p HCKDHtVsGDEDyCP
0 2 Y952‑p tVsGDEDyCPRSKKA
0 2 S966‑p ANLGKNAsMNtQHGt
0 1 T969‑p GKNAsMNtQHGtATE
0 1 T973‑p sMNtQHGtATEVAVE
0 1 K1043‑ub RKPNLGLkSCDGNQE
0 4 K1068‑ub EVATRLQkGGLGYVE
0 1 K1107 LQASVIKKFLQGFMA
0 1 K1116‑ac LQGFMAPkQkRRKLQ
0 1 K1118‑ac GFMAPkQkRRKLQSE
0 2 S1127‑p RKLQSEDsAKTEEVD
0 1 S1147‑p VEEAKVAsALEKWKT
0 10 S1315‑p KPHSTRRsQPKAPPV
0 49 K1335‑ac DELVLQTkRSsRRQs
0 2 K1335‑ub DELVLQTkRSsRRQs
0 2 S1338‑p VLQTkRSsRRQsLEL
0 54 S1342‑p kRSsRRQsLELQKCE
0 66 S1468‑p LAEDEGDsEPEAVGQ
0 7 P1470 EDEGDsEPEAVGQsR
0 19 A1472 EGDsEPEAVGQsRGR
0 2 S1476‑p EPEAVGQsRGRRQKK
  WSTF iso2  
S58 TCKSTGSSQLTHKEA
K151 DEEATEKKSDGACDS
S152 EEATEKKSDGACDSP
S158 KSDGACDSPSSDKEN
S160 DGACDSPSSDKENSS
S161 GACDSPSSDKENSSQ
S166 PSSDKENSSQIAQDH
S167 SSDKENSSQIAQDHQ
K175 QIAQDHQKKETVVKE
K175 QIAQDHQKKETVVKE
K181 QKKETVVKEDEGRRE
S189 EDEGRRESINDRARR
S197 INDRARRSPRKLPTS
T203 RSPRKLPTSLKKGER
S204 SPRKLPTSLKKGERK
K216 ERKWAPPKFLPHKYD
K221 PPKFLPHKYDVKLQN
Y222 PKFLPHKYDVKLQNE
S234 QNEDKIISNVPADSL
T266 HNALRAGTGENAPWV
Y282 EDELVKKYSLPSKFS
S289 YSLPSKFSDFLLDPY
Y296 SDFLLDPYKYMTLNP
K297 DFLLDPYKYMTLNPS
K297 DFLLDPYKYMTLNPS
Y298 FLLDPYKYMTLNPST
K306 MTLNPSTKRKNTGSP
S312 TKRKNTGSPDRKPSK
S318 GSPDRKPSKKSKTDN
S321 DRKPSKKSKTDNSSL
T323 KPSKKSKTDNSSLSS
N325 SKKSKTDNSSLSSPL
S326 KKSKTDNSSLSSPLN
S327 KSKTDNSSLSSPLNP
S329 KTDNSSLSSPLNPKL
S330 TDNSSLSSPLNPKLW
S345 CHVHLKKSLSGSPLK
S347 VHLKKSLSGSPLKVK
S349 LKKSLSGSPLKVKNS
S359 KVKNSKNSKSPEEHL
S361 KNSKNSKSPEEHLEE
S374 EEMMKMMSPNKLHTN
K409 LKAKGRSKGILNGQK
K416 KGILNGQKSTGNSKS
K426 GNSKSPKKGLKTPKT
K429 KSPKKGLKTPKTKMK
K432 KKGLKTPKTKMKQMT
T439 KTKMKQMTLLDMAKG
K449 DMAKGTQKMTRAPRN
T451 AKGTQKMTRAPRNSG
N456 KMTRAPRNSGGTPRT
S457 MTRAPRNSGGTPRTS
S464 SGGTPRTSSKPHKHL
S465 GGTPRTSSKPHKHLP
K501 ALSCVISKTARLLSS
K588 EDQELTGKNLPAFRL
S695 VRLCLRRSDVQEESE
S701 RSDVQEESEGSDTDD
S704 VQEESEGSDTDDNKD
T706 EESEGSDTDDNKDSA
S712 DTDDNKDSAAFEDNE
A713 TDDNKDSAAFEDNEV
T755 LCHRILMTYSVQDHM
Y756 CHRILMTYSVQDHME
K774 QMSAELWKERLAVLK
K806 AKNKENGKVENGLGK
K813 KVENGLGKTDRKKEI
T829 KFEPQVDTEAEDMIS
S836 TEAEDMISAVKSRRL
S840 DMISAVKSRRLLAIQ
K860 EIQEREMKVKLERQA
S928 EKGWVHDSIDYRFNH
Y931 WVHDSIDYRFNHHCK
T941 NHHCKDHTVSGDEDY
S943 HCKDHTVSGDEDYCP
Y948 TVSGDEDYCPRSKKA
S962 ANLGKNASMNTQHGT
T965 GKNASMNTQHGTATE
T969 SMNTQHGTATEVAVE
K1039 RKPNLGLKSCDGNQE
K1064 EVATRLQKGGLGYVE
K1103 LQASVIKKFLQGFMA
K1112 LQGFMAPKQKRRKLQ
K1114 GFMAPKQKRRKLQSE
S1123 RKLQSEDSAKTEEVD
S1143 VEEAKVASALEKWKT
S1311 KPHSTRRSQPKAPPV
K1331 DELVLQTKRSSRRQS
K1331 DELVLQTKRSSRRQS
S1334 VLQTKRSSRRQSLEL
S1338 KRSSRRQSLELQKCE
S1464 LAEDEGDSEPEAVGQ
P1466 EDEGDSEPEAVGQSR
A1468 EGDSEPEAVGQSRGR
S1472 EPEAVGQSRGRRQKK
  mouse

 
S58 TCKSTGSSQLTHKEA
K151 DEEAVEKKsDGACDs
S152‑p EEAVEKKsDGACDsP
S158‑p KsDGACDsPssDKEN
S160‑p DGACDsPssDKENsS
S161‑p GACDsPssDKENsSQ
S166‑p PssDKENsSQMAQDL
S167 ssDKENsSQMAQDLQ
K175 QMAQDLQKKETVVKE
K175 QMAQDLQKKETVVKE
K181 QKKETVVKEDEGRRE
S189‑p EDEGRREsINDRARR
S197 INDRARRSPRKLPTs
T203 RSPRKLPTsLKKGER
S204‑p SPRKLPTsLKKGERK
K216 ERKWAPPKFLPHKYD
K221 PPKFLPHKYDVKLQN
Y222 PKFLPHKYDVKLQNE
S234 QNEDKIISNVPADSL
T266 HNALRAGTGENAPWV
Y282 EDELVKKYSLPSKFS
S289 YSLPSKFSDFLLDPY
Y296 SDFLLDPYKYMTLNP
K297 DFLLDPYKYMTLNPS
K297 DFLLDPYKYMTLNPS
Y298 FLLDPYKYMTLNPST
K306 MTLNPSTKRRNTGsP
S312‑p TKRRNTGsPDRKPsK
S318‑p GsPDRKPsKKPKRDs
P321 DRKPsKKPKRDsssL
R323 KPsKKPKRDsssLss
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‑ac LKAKGRGkGILNGQk
K417‑ac kGILNGQkSTGNSKS
K427 GNSKSPSKCVKTPKT
K430 KSPSKCVKTPKTKMK
K433 SKCVKTPKTKMKQMt
T440‑p KTKMKQMtLLDMAKG
K450 DMAKGTQKMTRTPRs
T452 AKGTQKMTRTPRssG
S457‑p KMTRTPRssGGVPRS
S458‑p MTRTPRssGGVPRSs
S465‑p sGGVPRSsGKPHKHL
G466 GGVPRSsGKPHKHLP
K502‑ub ALSCVISkTARLLSN
R589 EDQELGGRNLPAFRL
C700 VRLCLRRCDVQEDsE
S706‑p RCDVQEDsEGsEtDD
S709‑p VQEDsEGsEtDDNKD
T711‑p EDsEGsEtDDNKDst
S717‑p EtDDNKDstPFEDNE
T718‑p tDDNKDstPFEDNEV
T760 LCHRILMTYSVQDHM
Y761 CHRILMTYSVQDHME
K779 QVSAELWKERLAVLK
K811 ARNKENGKEENVLGK
K818 KEENVLGKVDRKKEI
V834 KIEQQVEVEADDMIS
S841 VEADDMISAVKSRRL
S845 DMISAVKSRRLLSMQ
K865 EIQERETKVRLEREA
S933 EKGWVHNSIDYRFKH
Y936 WVHNSIDYRFKHHRK
S946 KHHRKDHSNLPDDDY
- gap
Y953 SNLPDDDYCPRSKKA
S967‑p ANLGKNAsVNAHHGP
- gap
- gap
K1043 RKPNLGLKSCDGNQE
K1068‑ub EVATRLQkGGLGYME
K1107 LQASVIKKFLQGFMA
K1116 LQGFMAPKQKKRKLQ
K1118 GFMAPKQKKRKLQSE
S1127 RKLQSEDSTKSEEVD
S1147 VEEAKVASALEKWKT
S1315‑p KSHPARRsRPKDDPE
K1331‑ac DDLVLQTkRISRRQs
K1331 DDLVLQTKRISRRQs
S1334 VLQTkRISRRQsLEL
S1338‑p kRISRRQsLELQKCE
S1464‑p LADDEGDsDsEsVGQ
S1466‑p DDEGDsDsEsVGQSR
S1468‑p EGDsDsEsVGQSRGR
S1472 DsEsVGQSRGRRQKK
  rat

 
S58 TCKSTGSSQLTHKEA
K151 DEEAAEKKSDGTCDS
S152 EEAAEKKSDGTCDSP
S158 KSDGTCDSPsSDKEN
S160‑p DGTCDSPsSDKENSS
S161 GTCDSPsSDKENSSQ
S166 PsSDKENSSQMAQDH
S167 sSDKENSSQMAQDHQ
K175 QMAQDHQKETVVKED
K175 QMAQDHQKETVVKED
K180 HQKETVVKEDGGRRE
S188‑p EDGGRREsINDRARR
S196 INDRARRSPRKLPTS
T202 RSPRKLPTSLKKGER
S203 SPRKLPTSLKKGERK
K215 ERKWAPPKFLPHKYD
K220 PPKFLPHKYDVKLQS
Y221 PKFLPHKYDVKLQSE
S233 QSEDKIISNVPADSL
T265 HNALRAGTGENAPWV
Y281 EDELVKKYSLPSKFS
S288 YSLPSKFSDFLLDPY
Y295 SDFLLDPYKYMTLNP
K296 DFLLDPYKYMTLNPS
K296 DFLLDPYKYMTLNPS
Y297 FLLDPYKYMTLNPST
K305 MTLNPSTKRKNTGSP
S311 TKRKNTGSPDRKPsK
S317‑p GSPDRKPsKKPKRDN
P320 DRKPsKKPKRDNSSL
R322 KPsKKPKRDNSSLSS
N324 sKKPKRDNSSLSSPL
S325 KKPKRDNSSLSSPLN
S326 KPKRDNSSLSSPLNP
S328 KRDNSSLSSPLNPKL
S329 RDNSSLSSPLNPKLW
S344 CHVHLEKSLNGPPLK
N346 VHLEKSLNGPPLKVK
P348 LEKSLNGPPLKVKNS
S358 KVKNSKNSKSPEEHL
S360 KNSKNSKSPEEHLEE
S373 EEVMKIMSPNKLHSF
K407‑ac LKAKGRGkGILNGQK
K414 kGILNGQKSTGNSKS
K424 GNSKSPSKCVKTPKT
K427 KSPSKCVKTPKTKMK
K430 SKCVKTPKTKMKQMT
T437 KTKMKQMTLLDMAKG
K447 DMAKGTQKMTRTPRS
T449 AKGTQKMTRTPRSSG
S454 KMTRTPRSSGGVPRS
S455 MTRTPRSSGGVPRSS
S462 SGGVPRSSGKPHKHL
G463 GGVPRSSGKPHKHLP
K499 ALSCVISKTARLLSS
R586 EDQELGGRNLPTFRL
C697 VRLCLRRCDVQEDsE
S703‑p RCDVQEDsEGsDTDD
S706‑p VQEDsEGsDTDDNKD
T708 EDsEGsDTDDNKDST
S714 DTDDNKDSTPFEDNE
T715 TDDNKDSTPFEDNEV
T757 LCHRILMTYSVQDHM
Y758 CHRILMTYSVQDHME
K776 QMSAELWKERLAVLK
K808 ARNKENGKEENVLGK
K815 KEENVLGKVDRKKEI
V831 KIENQVEVEADDMIS
S838 VEADDMISAVKSRRL
S842 DMISAVKSRRLLSMQ
K862 EIQERETKVRLEREA
S930 EKGWVHNSIDYRFKH
Y933 WVHNSIDYRFKHHRK
- gap
- gap
Y950 NNLPDDDYCPRSKKA
S964 ANLGKNASVNAHLGS
- gap
S971 SVNAHLGSALEAVET
K1040 RKPNLGLKSCDGNQE
K1065 EVATRLQKGGLGYME
K1104‑ub LQASVIKkFLQGFMA
K1113 LQGFMAPKQKKRKLQ
K1115 GFMAPKQKKRKLQSE
S1124 RKLQSEDSTKSEEVD
S1144 VEEAKVASALEKWKT
S1312 KSHAARRSRPKDDTE
K1328‑ac DELVLQTkRSSRRQs
K1328 DELVLQTKRSSRRQs
S1331 VLQTkRSSRRQsLEL
S1335‑p kRSSRRQsLELQKCE
S1461‑p LADDEGDsDsEsVGQ
S1463‑p DDEGDsDsEsVGQSR
S1465‑p EGDsDsEsVGQSRGR
S1469 DsEsVGQSRGRRQKK
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