BAZ1B_MOUSE - dbPTM
BAZ1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAZ1B_MOUSE
UniProt AC Q9Z277
Protein Name Tyrosine-protein kinase BAZ1B
Gene Name Baz1b
Organism Mus musculus (Mouse).
Sequence Length 1479
Subcellular Localization Nucleus . Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA (By similarity)..
Protein Description 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. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication..
Protein Sequence MAPLLGRKPFPLVKPLPGEEPLFTIPHTQEAFRTREEYEARLERYSERIWTCKSTGSSQLTHKEAWEEEQEVAELLKEEFPNWYEKLVLEMVHHNTASLEKLVDSAWLEIMTKYAVGEECDFEVGKEKMLKVKIVKIHPLEKVDEEAVEKKSDGACDSPSSDKENSSQMAQDLQKKETVVKEDEGRRESINDRARRSPRKLPTSLKKGERKWAPPKFLPHKYDVKLQNEDKIISNVPADSLIRTERPPNKEILRYFIRHNALRAGTGENAPWVVEDELVKKYSLPSKFSDFLLDPYKYMTLNPSTKRRNTGSPDRKPSKKPKRDSSSLSSPLNPKLWCHVHLEKSLNGPPLKVKNSKNSKSPEEHLEGVMKIMSPNNNKLHSFHIPKKGPAAKKPGKHSDKPLKAKGRGKGILNGQKSTGNSKSPSKCVKTPKTKMKQMTLLDMAKGTQKMTRTPRSSGGVPRSSGKPHKHLPPAALHLIAYYKENKDKEDKKSALSCVISKTARLLSNEDRARLPEELRALVQKRYELLEHKKRWASMSEEQRKEYLKKKRQELKERLREKAKERREREMLERLEKQKRFEDQELGGRNLPAFRLVDTPEGLPNTLFGDVALVVEFLSCYSGLLLPDAQYPITAVSLMEALSADKGGFLYLNRVLVILLQTLLQDEIAEDYGELGMKLSEIPLTLHSVSELVRLCLRRCDVQEDSEGSETDDNKDSTPFEDNEVQDEFLEKLETSEFFELTSEEKLRILTALCHRILMTYSVQDHMETRQQVSAELWKERLAVLKEENDKKRAEKQKRKEMEARNKENGKEENVLGKVDRKKEIVKIEQQVEVEADDMISAVKSRRLLSMQAKRKREIQERETKVRLEREAEEERMRKHKAAAEKAFQEGIAKAKLVLRRTPIGTDRNHNRYWLFSNEVPGLFIEKGWVHNSIDYRFKHHRKDHSNLPDDDYCPRSKKANLGKNASVNAHHGPALEAVETTVPKQGQNLWFLCDSQKELDELLSCLHPQGIRESQLKERLEKRYQEITHSIYLARKPNLGLKSCDGNQELLNFLRSDLIEVATRLQKGGLGYMEGTSEFEARVISLEKLKDFGECVIALQASVIKKFLQGFMAPKQKKRKLQSEDSTKSEEVDEEKKMVEEAKVASALEKWKTAIREAQTFSRMHVLLGMLDACIKWDMSAENARCKVCRKKGEDDKLILCDECNKAFHLFCLRPALYEVPDGEWQCPACQPPTARRNSRGRNYTEESTSEGSEGDESGEEEEEEEEEEEEEEDYEVAGLRLRPRKTIRGKQSVIPAARPGRPPGKKSHPARRSRPKDDPEVDDLVLQTKRISRRQSLELQKCEDILHKLVKYRFSWPFREPVTRDEAEDYYDVIEHPMDFQTIQNKCSCGNYRSVQEFLTDMKQVFANAELYNCRGSHVLSCMEKTEQCLLALLQKHLPGHPYVRRKRRKFPDRLADDEGDSDSESVGQSRGRRQKK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
58PhosphorylationTCKSTGSSQLTHKEA
EECCCCCCCCCCHHH		30.4727841257
150UbiquitinationVDEEAVEKKSDGACD
CCHHHHHHCCCCCCC		51.4827667366
152PhosphorylationEEAVEKKSDGACDSP
HHHHHHCCCCCCCCC		52.9623684622
158PhosphorylationKSDGACDSPSSDKEN
CCCCCCCCCCCCCCC		26.9427087446
160PhosphorylationDGACDSPSSDKENSS
CCCCCCCCCCCCCHH		55.9427087446
161PhosphorylationGACDSPSSDKENSSQ
CCCCCCCCCCCCHHH		56.9621082442
166PhosphorylationPSSDKENSSQMAQDL
CCCCCCCHHHHHHHH		24.0425619855
167PhosphorylationSSDKENSSQMAQDLQ
CCCCCCHHHHHHHHH		35.2425619855
169OxidationDKENSSQMAQDLQKK
CCCCHHHHHHHHHHH		3.8017242355
189PhosphorylationEDEGRRESINDRARR
CCCCCHHHHHHHHHC		25.5325159016
203PhosphorylationRSPRKLPTSLKKGER
CCCCCCCCCCCCCCC		58.0728066266
204PhosphorylationSPRKLPTSLKKGERK
CCCCCCCCCCCCCCC		35.9326745281
266PhosphorylationHNALRAGTGENAPWV
HCCHHCCCCCCCCCE		40.10-
282PhosphorylationEDELVKKYSLPSKFS
CHHHHHHCCCCCCHH		15.1023737553
283PhosphorylationDELVKKYSLPSKFSD
HHHHHHCCCCCCHHH		42.5619144319
286PhosphorylationVKKYSLPSKFSDFLL
HHHCCCCCCHHHHHC		52.1823737553
298PhosphorylationFLLDPYKYMTLNPST
HHCCHHHCCCCCCCC		6.8928576409
300PhosphorylationLDPYKYMTLNPSTKR
CCHHHCCCCCCCCCC		21.9422871156
304PhosphorylationKYMTLNPSTKRRNTG
HCCCCCCCCCCCCCC		45.5529176673
305PhosphorylationYMTLNPSTKRRNTGS
CCCCCCCCCCCCCCC		29.8129176673
310PhosphorylationPSTKRRNTGSPDRKP
CCCCCCCCCCCCCCC		36.9125159016
312PhosphorylationTKRRNTGSPDRKPSK
CCCCCCCCCCCCCCC		22.9126824392
318PhosphorylationGSPDRKPSKKPKRDS
CCCCCCCCCCCCCCC		57.2425159016
325PhosphorylationSKKPKRDSSSLSSPL
CCCCCCCCCCCCCCC		26.3426824392
326PhosphorylationKKPKRDSSSLSSPLN
CCCCCCCCCCCCCCC		39.3221082442
327PhosphorylationKPKRDSSSLSSPLNP
CCCCCCCCCCCCCCC		35.9027149854
329PhosphorylationKRDSSSLSSPLNPKL
CCCCCCCCCCCCCCC		31.6827149854
330PhosphorylationRDSSSLSSPLNPKLW
CCCCCCCCCCCCCCE		38.4026824392
345PhosphorylationCHVHLEKSLNGPPLK
EEEEEHHHCCCCCCC		20.0728066266
359PhosphorylationKVKNSKNSKSPEEHL
CCCCCCCCCCHHHHH		37.9425168779
361PhosphorylationKNSKNSKSPEEHLEG
CCCCCCCCHHHHHHH		37.0525521595
374PhosphorylationEGVMKIMSPNNNKLH
HHHHHHCCCCCCCEE		28.1326824392
382PhosphorylationPNNNKLHSFHIPKKG
CCCCCEEEEECCCCC		29.0227841257
410AcetylationLKAKGRGKGILNGQK
CCCCCCCCCCCCCCC		41.2223864654
417AcetylationKGILNGQKSTGNSKS
CCCCCCCCCCCCCCC		51.9271347
440PhosphorylationKTKMKQMTLLDMAKG
CCCHHHCHHHHHHCC		22.9820139300
446AcetylationMTLLDMAKGTQKMTR
CHHHHHHCCCCCCCC		56.7222826441
452PhosphorylationAKGTQKMTRTPRSSG
HCCCCCCCCCCCCCC		38.1329514104
454PhosphorylationGTQKMTRTPRSSGGV
CCCCCCCCCCCCCCC		17.5629514104
457PhosphorylationKMTRTPRSSGGVPRS
CCCCCCCCCCCCCCC		34.2420139300
458PhosphorylationMTRTPRSSGGVPRSS
CCCCCCCCCCCCCCC		40.6320139300
465PhosphorylationSGGVPRSSGKPHKHL
CCCCCCCCCCCCCCC		52.7120139300
502UbiquitinationALSCVISKTARLLSN
HHHHHHHHHHHHHCH		34.7722790023
502AcetylationALSCVISKTARLLSN
HHHHHHHHHHHHHCH		34.7723806337
706PhosphorylationRCDVQEDSEGSETDD
HCCCCCCCCCCCCCC		43.0025521595
709PhosphorylationVQEDSEGSETDDNKD
CCCCCCCCCCCCCCC		33.0225521595
711PhosphorylationEDSEGSETDDNKDST
CCCCCCCCCCCCCCC		50.8025521595
717PhosphorylationETDDNKDSTPFEDNE
CCCCCCCCCCCCCCH		39.3225521595
718PhosphorylationTDDNKDSTPFEDNEV
CCCCCCCCCCCCCHH		41.9725159016
760PhosphorylationLCHRILMTYSVQDHM
HHHHHHHHCCCHHHH		14.8130635358
761PhosphorylationCHRILMTYSVQDHME
HHHHHHHCCCHHHHH		7.9030635358
762PhosphorylationHRILMTYSVQDHMET
HHHHHHCCCHHHHHH		12.2530635358
769PhosphorylationSVQDHMETRQQVSAE
CCHHHHHHHHHHHHH		26.6330635358
850PhosphorylationVKSRRLLSMQAKRKR
HHHHHHHHHHHHHHH		17.2829176673
946PhosphorylationKHHRKDHSNLPDDDY
CCCCCCCCCCCCCCC		50.6327149854
953PhosphorylationSNLPDDDYCPRSKKA
CCCCCCCCCCHHHCC		16.0225159016
967PhosphorylationANLGKNASVNAHHGP
CCCCCCCCCCCCCCC		25.8726370283
1006GlutathionylationELDELLSCLHPQGIR
HHHHHHHHHCCCCCC		4.0024333276
1045GlutathionylationPNLGLKSCDGNQELL
CCCCCCCCCCCHHHH		8.1024333276
1068UbiquitinationEVATRLQKGGLGYME
HHHHHHHCCCCCCCC		60.5822790023
1315PhosphorylationKSHPARRSRPKDDPE
CCCCCHHCCCCCCCC		47.5926824392
1331AcetylationDDLVLQTKRISRRQS
HHHHHHHHHHHHHHC		34.4723806337
1334PhosphorylationVLQTKRISRRQSLEL
HHHHHHHHHHHCHHH		25.9928285833
1338PhosphorylationKRISRRQSLELQKCE
HHHHHHHCHHHHHHH		23.2327087446
1372PhosphorylationTRDEAEDYYDVIEHP
CHHHHHHHHHHHCCC		7.9625159016
1373PhosphorylationRDEAEDYYDVIEHPM
HHHHHHHHHHHCCCC		18.9625159016
1431GlutathionylationCMEKTEQCLLALLQK
HHHHHHHHHHHHHHH		2.4724333276
1464PhosphorylationLADDEGDSDSESVGQ
HCCCCCCCCCCCCCC		54.6227087446
1466PhosphorylationDDEGDSDSESVGQSR
CCCCCCCCCCCCCCC		35.4127087446
1468PhosphorylationEGDSDSESVGQSRGR
CCCCCCCCCCCCCCC		35.1827087446
1472PhosphorylationDSESVGQSRGRRQKK
CCCCCCCCCCCCCCC		30.6725619855
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BAZ1B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAZ1B_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BAZ1B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMCA5_MOUSESmarca5physical
11980720
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAZ1B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-1338 ANDSER-1464, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1338, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-1464; SER-1466AND SER-1468, AND MASS SPECTROMETRY.

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