BAZ1B_HUMAN - dbPTM
BAZ1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAZ1B_HUMAN
UniProt AC Q9UIG0
Protein Name Tyrosine-protein kinase BAZ1B
Gene Name BAZ1B
Organism Homo sapiens (Human).
Sequence Length 1483
Subcellular Localization Nucleus . Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA.
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 MAPLLGRKPFPLVKPLPGEEPLFTIPHTQEAFRTREEYEARLERYSERIWTCKSTGSSQLTHKEAWEEEQEVAELLKEEFPAWYEKLVLEMVHHNTASLEKLVDTAWLEIMTKYAVGEECDFEVGKEKMLKVKIVKIHPLEKVDEEATEKKSDGACDSPSSDKENSSQIAQDHQKKETVVKEDEGRRESINDRARRSPRKLPTSLKKGERKWAPPKFLPHKYDVKLQNEDKIISNVPADSLIRTERPPNKEIVRYFIRHNALRAGTGENAPWVVEDELVKKYSLPSKFSDFLLDPYKYMTLNPSTKRKNTGSPDRKPSKKSKTDNSSLSSPLNPKLWCHVHLKKSLSGSPLKVKNSKNSKSPEEHLEEMMKMMSPNKLHTNFHIPKKGPPAKKPGKHSDKPLKAKGRSKGILNGQKSTGNSKSPKKGLKTPKTKMKQMTLLDMAKGTQKMTRAPRNSGGTPRTSSKPHKHLPPAALHLIAYYKENKDREDKRSALSCVISKTARLLSSEDRARLPEELRSLVQKRYELLEHKKRWASMSEEQRKEYLKKKREELKKKLKEKAKERREKEMLERLEKQKRYEDQELTGKNLPAFRLVDTPEGLPNTLFGDVAMVVEFLSCYSGLLLPDAQYPITAVSLMEALSADKGGFLYLNRVLVILLQTLLQDEIAEDYGELGMKLSEIPLTLHSVSELVRLCLRRSDVQEESEGSDTDDNKDSAAFEDNEVQDEFLEKLETSEFFELTSEEKLQILTALCHRILMTYSVQDHMETRQQMSAELWKERLAVLKEENDKKRAEKQKRKEMEAKNKENGKVENGLGKTDRKKEIVKFEPQVDTEAEDMISAVKSRRLLAIQAKKEREIQEREMKVKLERQAEEERIRKHKAAAEKAFQEGIAKAKLVMRRTPIGTDRNHNRYWLFSDEVPGLFIEKGWVHDSIDYRFNHHCKDHTVSGDEDYCPRSKKANLGKNASMNTQHGTATEVAVETTTPKQGQNLWFLCDSQKELDELLNCLHPQGIRESQLKERLEKRYQDIIHSIHLARKPNLGLKSCDGNQELLNFLRSDLIEVATRLQKGGLGYVEETSEFEARVISLEKLKDFGECVIALQASVIKKFLQGFMAPKQKRRKLQSEDSAKTEEVDEEKKMVEEAKVASALEKWKTAIREAQTFSRMHVLLGMLDACIKWDMSAENARCKVCRKKGEDDKLILCDECNKAFHLFCLRPALYEVPDGEWQCPACQPATARRNSRGRNYTEESASEDSEDDESDEEEEEEEEEEEEEDYEVAGLRLRPRKTIRGKHSVIPPAARSGRRPGKKPHSTRRSQPKAPPVDDAEVDELVLQTKRSSRRQSLELQKCEEILHKIVKYRFSWPFREPVTRDEAEDYYDVITHPMDFQTVQNKCSCGSYRSVQEFLTDMKQVFTNAEVYNCRGSHVLSCMVKTEQCLVALLHKHLPGHPYVRRKRKKFPDRLAEDEGDSEPEAVGQSRGRRQKK
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
8AcetylationMAPLLGRKPFPLVKP
CCCCCCCCCCCCCCC
49.5726051181
8UbiquitinationMAPLLGRKPFPLVKP
CCCCCCCCCCCCCCC
49.5723000965
14AcetylationRKPFPLVKPLPGEEP
CCCCCCCCCCCCCCC
48.8226051181
14UbiquitinationRKPFPLVKPLPGEEP
CCCCCCCCCCCCCCC
48.8223000965
45PhosphorylationYEARLERYSERIWTC
HHHHHHHHHHCEEEE
12.9023312004
46PhosphorylationEARLERYSERIWTCK
HHHHHHHHHCEEEEC
26.9823312004
53UbiquitinationSERIWTCKSTGSSQL
HHCEEEECCCCCCCC
43.6129967540
54PhosphorylationERIWTCKSTGSSQLT
HCEEEECCCCCCCCC
39.9023312004
55PhosphorylationRIWTCKSTGSSQLTH
CEEEECCCCCCCCCC
26.9523312004
57PhosphorylationWTCKSTGSSQLTHKE
EEECCCCCCCCCCHH
18.2623312004
58PhosphorylationTCKSTGSSQLTHKEA
EECCCCCCCCCCHHH
30.4725159151
61PhosphorylationSTGSSQLTHKEAWEE
CCCCCCCCCHHHHHH
24.2223312004
63UbiquitinationGSSQLTHKEAWEEEQ
CCCCCCCHHHHHHHH
43.8429967540
77UbiquitinationQEVAELLKEEFPAWY
HHHHHHHHHHCHHHH
68.7529967540
126AcetylationECDFEVGKEKMLKVK
CCCCCCCCCCEEEEE
60.3826051181
126UbiquitinationECDFEVGKEKMLKVK
CCCCCCCCCCEEEEE
60.3833845483
128UbiquitinationDFEVGKEKMLKVKIV
CCCCCCCCEEEEEEE
53.68-
136UbiquitinationMLKVKIVKIHPLEKV
EEEEEEEEEEECHHC
38.4829967540
142AcetylationVKIHPLEKVDEEATE
EEEEECHHCCHHHHH
63.7726051181
142UbiquitinationVKIHPLEKVDEEATE
EEEEECHHCCHHHHH
63.7733845483
148PhosphorylationEKVDEEATEKKSDGA
HHCCHHHHHCCCCCC
52.1730576142
150UbiquitinationVDEEATEKKSDGACD
CCHHHHHCCCCCCCC
53.9033845483
151AcetylationDEEATEKKSDGACDS
CHHHHHCCCCCCCCC
47.777408827
152PhosphorylationEEATEKKSDGACDSP
HHHHHCCCCCCCCCC
52.9622167270
158PhosphorylationKSDGACDSPSSDKEN
CCCCCCCCCCCCCCC
26.9422167270
160PhosphorylationDGACDSPSSDKENSS
CCCCCCCCCCCCCHH
55.9422167270
161PhosphorylationGACDSPSSDKENSSQ
CCCCCCCCCCCCHHH
56.9622167270
163AcetylationCDSPSSDKENSSQIA
CCCCCCCCCCHHHHH
61.8225953088
166PhosphorylationPSSDKENSSQIAQDH
CCCCCCCHHHHHHHH
25.3922167270
167PhosphorylationSSDKENSSQIAQDHQ
CCCCCCHHHHHHHHH
36.8717525332
175"N6,N6-dimethyllysine"QIAQDHQKKETVVKE
HHHHHHHHHHHEECC
49.51-
175AcetylationQIAQDHQKKETVVKE
HHHHHHHHHHHEECC
49.517408839
175MethylationQIAQDHQKKETVVKE
HHHHHHHHHHHEECC
49.51-
181"N6,N6-dimethyllysine"QKKETVVKEDEGRRE
HHHHHEECCCCCCHH
55.93-
181MethylationQKKETVVKEDEGRRE
HHHHHEECCCCCCHH
55.93-
189PhosphorylationEDEGRRESINDRARR
CCCCCHHHHHHHHHC
25.5323401153
197PhosphorylationINDRARRSPRKLPTS
HHHHHHCCCCCCCCC
24.4125159151
203PhosphorylationRSPRKLPTSLKKGER
CCCCCCCCCCCCCCC
58.0730266825
204PhosphorylationSPRKLPTSLKKGERK
CCCCCCCCCCCCCCC
35.9330266825
207UbiquitinationKLPTSLKKGERKWAP
CCCCCCCCCCCCCCC
71.8924816145
216AcetylationERKWAPPKFLPHKYD
CCCCCCCCCCCCCCE
59.4826051181
221AcetylationPPKFLPHKYDVKLQN
CCCCCCCCCEEECCC
41.0026051181
221UbiquitinationPPKFLPHKYDVKLQN
CCCCCCCCCEEECCC
41.0029967540
222PhosphorylationPKFLPHKYDVKLQNE
CCCCCCCCEEECCCC
23.96-
225SumoylationLPHKYDVKLQNEDKI
CCCCCEEECCCCCCC
41.27-
225SumoylationLPHKYDVKLQNEDKI
CCCCCEEECCCCCCC
41.27-
225UbiquitinationLPHKYDVKLQNEDKI
CCCCCEEECCCCCCC
41.2733845483
231AcetylationVKLQNEDKIISNVPA
EECCCCCCCCCCCCH
35.4425953088
231UbiquitinationVKLQNEDKIISNVPA
EECCCCCCCCCCCCH
35.4433845483
234PhosphorylationQNEDKIISNVPADSL
CCCCCCCCCCCHHHH
34.94-
240PhosphorylationISNVPADSLIRTERP
CCCCCHHHHHCCCCC
28.0024719451
250AcetylationRTERPPNKEIVRYFI
CCCCCCCHHHHHHHH
55.3726051181
250UbiquitinationRTERPPNKEIVRYFI
CCCCCCCHHHHHHHH
55.3724816145
266PhosphorylationHNALRAGTGENAPWV
HCCHHCCCCCCCCCE
40.1020068231
280AcetylationVVEDELVKKYSLPSK
EECHHHHHHCCCCCC
59.6326051181
280UbiquitinationVVEDELVKKYSLPSK
EECHHHHHHCCCCCC
59.6329967540
281UbiquitinationVEDELVKKYSLPSKF
ECHHHHHHCCCCCCH
32.37-
282PhosphorylationEDELVKKYSLPSKFS
CHHHHHHCCCCCCHH
15.10-
283PhosphorylationDELVKKYSLPSKFSD
HHHHHHCCCCCCHHH
42.5619691289
286PhosphorylationVKKYSLPSKFSDFLL
HHHCCCCCCHHHHHC
52.1824719451
287UbiquitinationKKYSLPSKFSDFLLD
HHCCCCCCHHHHHCC
47.12-
289PhosphorylationYSLPSKFSDFLLDPY
CCCCCCHHHHHCCHH
31.0520068231
296PhosphorylationSDFLLDPYKYMTLNP
HHHHCCHHHCCCCCC
17.8926074081
297AcetylationDFLLDPYKYMTLNPS
HHHCCHHHCCCCCCC
33.6511688637
297UbiquitinationDFLLDPYKYMTLNPS
HHHCCHHHCCCCCCC
33.6523000965
297 (in isoform 1)Ubiquitination-33.6521890473
297 (in isoform 2)Ubiquitination-33.6521890473
298PhosphorylationFLLDPYKYMTLNPST
HHCCHHHCCCCCCCC
6.8926074081
300PhosphorylationLDPYKYMTLNPSTKR
CCHHHCCCCCCCCCC
21.9426074081
304PhosphorylationKYMTLNPSTKRKNTG
HCCCCCCCCCCCCCC
45.5523401153
305PhosphorylationYMTLNPSTKRKNTGS
CCCCCCCCCCCCCCC
35.8023401153
306AcetylationMTLNPSTKRKNTGSP
CCCCCCCCCCCCCCC
66.7625953088
306UbiquitinationMTLNPSTKRKNTGSP
CCCCCCCCCCCCCCC
66.7623000965
308UbiquitinationLNPSTKRKNTGSPDR
CCCCCCCCCCCCCCC
61.4923000965
310PhosphorylationPSTKRKNTGSPDRKP
CCCCCCCCCCCCCCC
41.9126074081
312PhosphorylationTKRKNTGSPDRKPSK
CCCCCCCCCCCCCCC
22.9125159151
316UbiquitinationNTGSPDRKPSKKSKT
CCCCCCCCCCCCCCC
62.1123000965
318PhosphorylationGSPDRKPSKKSKTDN
CCCCCCCCCCCCCCC
56.6128176443
319UbiquitinationSPDRKPSKKSKTDNS
CCCCCCCCCCCCCCC
70.3723000965
320UbiquitinationPDRKPSKKSKTDNSS
CCCCCCCCCCCCCCC
62.6223000965
321PhosphorylationDRKPSKKSKTDNSSL
CCCCCCCCCCCCCCC
44.5226055452
322UbiquitinationRKPSKKSKTDNSSLS
CCCCCCCCCCCCCCC
69.6323000965
323PhosphorylationKPSKKSKTDNSSLSS
CCCCCCCCCCCCCCC
47.7226055452
326PhosphorylationKKSKTDNSSLSSPLN
CCCCCCCCCCCCCCC
35.1525159151
327PhosphorylationKSKTDNSSLSSPLNP
CCCCCCCCCCCCCCH
38.2325159151
329PhosphorylationKTDNSSLSSPLNPKL
CCCCCCCCCCCCHHH
31.6830266825
330PhosphorylationTDNSSLSSPLNPKLW
CCCCCCCCCCCHHHE
38.4023401153
335AcetylationLSSPLNPKLWCHVHL
CCCCCCHHHEEEEEE
54.2525953088
335UbiquitinationLSSPLNPKLWCHVHL
CCCCCCHHHEEEEEE
54.2523000965
343UbiquitinationLWCHVHLKKSLSGSP
HEEEEEEEHHHCCCC
25.9929967540
344MethylationWCHVHLKKSLSGSPL
EEEEEEEHHHCCCCC
64.09115978471
344UbiquitinationWCHVHLKKSLSGSPL
EEEEEEEHHHCCCCC
64.0929967540
345PhosphorylationCHVHLKKSLSGSPLK
EEEEEEHHHCCCCCC
26.6123927012
347PhosphorylationVHLKKSLSGSPLKVK
EEEEHHHCCCCCCCC
44.2922167270
349PhosphorylationLKKSLSGSPLKVKNS
EEHHHCCCCCCCCCC
24.5522167270
352UbiquitinationSLSGSPLKVKNSKNS
HHCCCCCCCCCCCCC
55.3232015554
359PhosphorylationKVKNSKNSKSPEEHL
CCCCCCCCCCHHHHH
37.9422167270
361PhosphorylationKNSKNSKSPEEHLEE
CCCCCCCCHHHHHHH
37.0529255136
374PhosphorylationEEMMKMMSPNKLHTN
HHHHHHHCCCCCCCC
23.0927134283
380PhosphorylationMSPNKLHTNFHIPKK
HCCCCCCCCCCCCCC
50.4420068231
386UbiquitinationHTNFHIPKKGPPAKK
CCCCCCCCCCCCCCC
70.5229967540
409AcetylationLKAKGRSKGILNGQK
CCCCCCCCCCCCCCC
48.9271341
416AcetylationKGILNGQKSTGNSKS
CCCCCCCCCCCCCCC
51.9271345
421PhosphorylationGQKSTGNSKSPKKGL
CCCCCCCCCCCCCCC
35.5429888752
423PhosphorylationKSTGNSKSPKKGLKT
CCCCCCCCCCCCCCC
41.6024719451
426AcetylationGNSKSPKKGLKTPKT
CCCCCCCCCCCCCCH
73.2419608861
429AcetylationKSPKKGLKTPKTKMK
CCCCCCCCCCCHHHH
72.0226210075
430PhosphorylationSPKKGLKTPKTKMKQ
CCCCCCCCCCHHHHH
34.7524719451
432AcetylationKKGLKTPKTKMKQMT
CCCCCCCCHHHHHHH
67.0426210075
439PhosphorylationKTKMKQMTLLDMAKG
CHHHHHHHHHHHHHC
22.9829396449
445UbiquitinationMTLLDMAKGTQKMTR
HHHHHHHHCCHHHCC
56.7229967540
447PhosphorylationLLDMAKGTQKMTRAP
HHHHHHCCHHHCCCC
25.0629396449
449AcetylationDMAKGTQKMTRAPRN
HHHHCCHHHCCCCCC
41.9211791593
451PhosphorylationAKGTQKMTRAPRNSG
HHCCHHHCCCCCCCC
30.62-
457PhosphorylationMTRAPRNSGGTPRTS
HCCCCCCCCCCCCCC
39.6228102081
460PhosphorylationAPRNSGGTPRTSSKP
CCCCCCCCCCCCCCC
17.0828102081
465PhosphorylationGGTPRTSSKPHKHLP
CCCCCCCCCCCCCCC
49.98-
483UbiquitinationLHLIAYYKENKDRED
HHHHHHHHHCCCHHH
41.9823000965
486UbiquitinationIAYYKENKDREDKRS
HHHHHHCCCHHHHHH
60.2923000965
496PhosphorylationEDKRSALSCVISKTA
HHHHHHHHHHHHHHH
13.1724667141
501AcetylationALSCVISKTARLLSS
HHHHHHHHHHHHCCH
34.7725953088
501MalonylationALSCVISKTARLLSS
HHHHHHHHHHHHCCH
34.7726320211
501UbiquitinationALSCVISKTARLLSS
HHHHHHHHHHHHCCH
34.7723000965
507PhosphorylationSKTARLLSSEDRARL
HHHHHHCCHHHHHCC
35.9520873877
508PhosphorylationKTARLLSSEDRARLP
HHHHHCCHHHHHCCH
43.4119691289
526PhosphorylationRSLVQKRYELLEHKK
HHHHHHHHHHHHHHH
20.2628152594
5322-HydroxyisobutyrylationRYELLEHKKRWASMS
HHHHHHHHHHHHCCC
34.36-
532UbiquitinationRYELLEHKKRWASMS
HHHHHHHHHHHHCCC
34.3629967540
537PhosphorylationEHKKRWASMSEEQRK
HHHHHHHCCCHHHHH
18.8428555341
539PhosphorylationKKRWASMSEEQRKEY
HHHHHCCCHHHHHHH
35.1729083192
546PhosphorylationSEEQRKEYLKKKREE
CHHHHHHHHHHHHHH
27.1929083192
549UbiquitinationQRKEYLKKKREELKK
HHHHHHHHHHHHHHH
55.2424816145
561UbiquitinationLKKKLKEKAKERREK
HHHHHHHHHHHHHHH
64.2724816145
588AcetylationEDQELTGKNLPAFRL
HCCCCCCCCCCCEEE
50.5026051181
588UbiquitinationEDQELTGKNLPAFRL
HCCCCCCCCCCCEEE
50.5022817900
588 (in isoform 1)Ubiquitination-50.5021890473
588 (in isoform 2)Ubiquitination-50.5021890473
699PhosphorylationVRLCLRRSDVQEESE
HHHHHHCCCCCHHHC
35.3830278072
705PhosphorylationRSDVQEESEGSDTDD
CCCCCHHHCCCCCCC
46.6429255136
708PhosphorylationVQEESEGSDTDDNKD
CCHHHCCCCCCCCCC
33.0329255136
710PhosphorylationEESEGSDTDDNKDSA
HHHCCCCCCCCCCCH
47.1229255136
716PhosphorylationDTDDNKDSAAFEDNE
CCCCCCCCHHHCCCH
24.0930278072
759PhosphorylationLCHRILMTYSVQDHM
HHHHHHHHHCHHHHH
14.81-
760PhosphorylationCHRILMTYSVQDHME
HHHHHHHHCHHHHHH
7.90-
774 (in isoform 2)Ubiquitination-15.5721890473
778UbiquitinationQMSAELWKERLAVLK
HHHHHHHHHHHHHHH
45.6521890473
778 (in isoform 1)Ubiquitination-45.6521890473
790UbiquitinationVLKEENDKKRAEKQK
HHHHHHHHHHHHHHH
56.6024816145
810AcetylationAKNKENGKVENGLGK
HHHHHCCCCCCCCCC
58.9430584253
817AcetylationKVENGLGKTDRKKEI
CCCCCCCCCCCCHHH
52.9023749302
826SumoylationDRKKEIVKFEPQVDT
CCCHHHEEECCCCCC
50.07-
826SumoylationDRKKEIVKFEPQVDT
CCCHHHEEECCCCCC
50.0725114211
826UbiquitinationDRKKEIVKFEPQVDT
CCCHHHEEECCCCCC
50.0724816145
833PhosphorylationKFEPQVDTEAEDMIS
EECCCCCCCHHHHHH
37.9330266825
840PhosphorylationTEAEDMISAVKSRRL
CCHHHHHHHHHHHHH
22.00-
843AcetylationEDMISAVKSRRLLAI
HHHHHHHHHHHHHHH
37.6525953088
843UbiquitinationEDMISAVKSRRLLAI
HHHHHHHHHHHHHHH
37.6532015554
844PhosphorylationDMISAVKSRRLLAIQ
HHHHHHHHHHHHHHH
18.94-
853SumoylationRLLAIQAKKEREIQE
HHHHHHHHHHHHHHH
38.50-
8532-HydroxyisobutyrylationRLLAIQAKKEREIQE
HHHHHHHHHHHHHHH
38.50-
853AcetylationRLLAIQAKKEREIQE
HHHHHHHHHHHHHHH
38.5025953088
853SumoylationRLLAIQAKKEREIQE
HHHHHHHHHHHHHHH
38.5028112733
853UbiquitinationRLLAIQAKKEREIQE
HHHHHHHHHHHHHHH
38.5029967540
854UbiquitinationLLAIQAKKEREIQER
HHHHHHHHHHHHHHH
66.09-
864AcetylationEIQEREMKVKLERQA
HHHHHHHHHHHHHHH
31.3119821681
885AcetylationKHKAAAEKAFQEGIA
HHHHHHHHHHHHHHH
50.1825953088
885UbiquitinationKHKAAAEKAFQEGIA
HHHHHHHHHHHHHHH
50.18-
893AcetylationAFQEGIAKAKLVMRR
HHHHHHHHHEEEEEC
44.1025953088
893UbiquitinationAFQEGIAKAKLVMRR
HHHHHHHHHEEEEEC
44.1029967540
932PhosphorylationEKGWVHDSIDYRFNH
ECCCCCCCCCCCCCC
11.50-
935PhosphorylationWVHDSIDYRFNHHCK
CCCCCCCCCCCCCCC
18.55-
942AcetylationYRFNHHCKDHTVSGD
CCCCCCCCCCCCCCC
48.4626051181
942UbiquitinationYRFNHHCKDHTVSGD
CCCCCCCCCCCCCCC
48.4633845483
945PhosphorylationNHHCKDHTVSGDEDY
CCCCCCCCCCCCCCC
26.8823401153
947PhosphorylationHCKDHTVSGDEDYCP
CCCCCCCCCCCCCCC
41.5029255136
952PhosphorylationTVSGDEDYCPRSKKA
CCCCCCCCCCHHHCC
11.4229255136
963AcetylationSKKANLGKNASMNTQ
HHCCCCCCCCCCCCC
53.1326051181
966PhosphorylationANLGKNASMNTQHGT
CCCCCCCCCCCCCCC
23.2029214152
969PhosphorylationGKNASMNTQHGTATE
CCCCCCCCCCCCEEE
17.1921712546
973PhosphorylationSMNTQHGTATEVAVE
CCCCCCCCEEEEEEE
28.4321712546
983PhosphorylationEVAVETTTPKQGQNL
EEEEEECCCCCCCEE
35.59-
1025PhosphorylationKERLEKRYQDIIHSI
HHHHHHHHHHHHHHH
22.9328152594
1043AcetylationRKPNLGLKSCDGNQE
CCCCCCCCCCCCCHH
47.4426051181
1043SumoylationRKPNLGLKSCDGNQE
CCCCCCCCCCCCCHH
47.4428112733
1043UbiquitinationRKPNLGLKSCDGNQE
CCCCCCCCCCCCCHH
47.44-
1045GlutathionylationPNLGLKSCDGNQELL
CCCCCCCCCCCHHHH
8.1022555962
1064 (in isoform 2)Ubiquitination-36.7721890473
1068UbiquitinationEVATRLQKGGLGYVE
HHHHHHHHCCCCCCE
60.5822817900
1068 (in isoform 1)Ubiquitination-60.5821890473
1078PhosphorylationLGYVEETSEFEARVI
CCCCEECCCEEEEEE
43.50-
1089SumoylationARVISLEKLKDFGEC
EEEEEHHHHCCHHHH
67.16-
1089SumoylationARVISLEKLKDFGEC
EEEEEHHHHCCHHHH
67.1628112733
1089UbiquitinationARVISLEKLKDFGEC
EEEEEHHHHCCHHHH
67.1623000965
1091UbiquitinationVISLEKLKDFGECVI
EEEHHHHCCHHHHHH
63.1823000965
1107SumoylationLQASVIKKFLQGFMA
HHHHHHHHHHHHHCC
39.93-
1107SumoylationLQASVIKKFLQGFMA
HHHHHHHHHHHHHCC
39.9328112733
1116AcetylationLQGFMAPKQKRRKLQ
HHHHCCCHHHHHHCC
59.947465925
1118AcetylationGFMAPKQKRRKLQSE
HHCCCHHHHHHCCCC
61.367465937
1124PhosphorylationQKRRKLQSEDSAKTE
HHHHHCCCCCCCCHH
54.5325627689
1127PhosphorylationRKLQSEDSAKTEEVD
HHCCCCCCCCHHHCH
27.8425159151
1129SumoylationLQSEDSAKTEEVDEE
CCCCCCCCHHHCHHH
61.49-
1129AcetylationLQSEDSAKTEEVDEE
CCCCCCCCHHHCHHH
61.4926051181
1129SumoylationLQSEDSAKTEEVDEE
CCCCCCCCHHHCHHH
61.49-
1147PhosphorylationVEEAKVASALEKWKT
HHHHHHHHHHHHHHH
36.0522817900
1151UbiquitinationKVASALEKWKTAIRE
HHHHHHHHHHHHHHH
55.64-
1192UbiquitinationARCKVCRKKGEDDKL
CCCCCCCCCCCCCCE
61.0622505724
1193UbiquitinationRCKVCRKKGEDDKLI
CCCCCCCCCCCCCEE
48.4522505724
1198UbiquitinationRKKGEDDKLILCDEC
CCCCCCCCEEEECCC
50.1522505724
1207UbiquitinationILCDECNKAFHLFCL
EEECCCHHHHHHHHH
65.1822505724
1249PhosphorylationGRNYTEESASEDSED
CCCCCCCCCCCCCCC
30.7525137130
1251PhosphorylationNYTEESASEDSEDDE
CCCCCCCCCCCCCCC
51.7425137130
1254PhosphorylationEESASEDSEDDESDE
CCCCCCCCCCCCCCH
38.5825137130
1259PhosphorylationEDSEDDESDEEEEEE
CCCCCCCCCHHHHHH
58.2625137130
1291AcetylationPRKTIRGKHSVIPPA
CCCCCCCCCCCCCHH
23.9026051181
1291UbiquitinationPRKTIRGKHSVIPPA
CCCCCCCCCCCCCHH
23.9029967540
1293PhosphorylationKTIRGKHSVIPPAAR
CCCCCCCCCCCHHHH
25.8128555341
1315PhosphorylationKPHSTRRSQPKAPPV
CCCCCCCCCCCCCCC
47.7623401153
1318UbiquitinationSTRRSQPKAPPVDDA
CCCCCCCCCCCCCHH
66.9229967540
1331 (in isoform 2)Ubiquitination-3.3321890473
1334PhosphorylationVDELVLQTKRSSRRQ
HHHHHHHHHHHHHHH
25.0223312004
1335AcetylationDELVLQTKRSSRRQS
HHHHHHHHHHHHHHH
37.0023954790
1335UbiquitinationDELVLQTKRSSRRQS
HHHHHHHHHHHHHHH
37.0022817900
1335 (in isoform 1)Ubiquitination-37.0021890473
1337PhosphorylationLVLQTKRSSRRQSLE
HHHHHHHHHHHHHHH
29.7421406692
1338PhosphorylationVLQTKRSSRRQSLEL
HHHHHHHHHHHHHHH
35.2021406692
1342PhosphorylationKRSSRRQSLELQKCE
HHHHHHHHHHHHHHH
23.2329255136
1347UbiquitinationRQSLELQKCEEILHK
HHHHHHHHHHHHHHH
57.1329967540
1354AcetylationKCEEILHKIVKYRFS
HHHHHHHHHHHHHCC
45.8326051181
1354UbiquitinationKCEEILHKIVKYRFS
HHHHHHHHHHHHHCC
45.8329967540
1358PhosphorylationILHKIVKYRFSWPFR
HHHHHHHHHCCCCCC
13.1422210691
1361PhosphorylationKIVKYRFSWPFREPV
HHHHHHCCCCCCCCC
25.4922210691
1369PhosphorylationWPFREPVTRDEAEDY
CCCCCCCCHHHHHHH
43.0227642862
1376PhosphorylationTRDEAEDYYDVITHP
CHHHHHHHHHCCCCC
7.9628796482
1377PhosphorylationRDEAEDYYDVITHPM
HHHHHHHHHCCCCCC
18.9628796482
1381PhosphorylationEDYYDVITHPMDFQT
HHHHHCCCCCCCHHH
21.5622210691
1388PhosphorylationTHPMDFQTVQNKCSC
CCCCCHHHHCCCCCC
24.8522210691
1431AcetylationHVLSCMVKTEQCLVA
CHHHHEECHHHHHHH
21.3326051181
1435GlutathionylationCMVKTEQCLVALLHK
HEECHHHHHHHHHHH
2.4122555962
1442AcetylationCLVALLHKHLPGHPY
HHHHHHHHHCCCCHH
46.9726051181
1449PhosphorylationKHLPGHPYVRRKRKK
HHCCCCHHHHCCCCC
10.8328258704
1468PhosphorylationLAEDEGDSEPEAVGQ
HCCCCCCCCHHHHCC
66.9429255136
1476PhosphorylationEPEAVGQSRGRRQKK
CHHHHCCCCCCCCCC
30.6723927012

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
158SPhosphorylationKinaseMAPK3P27361
GPS
158SPhosphorylationKinaseMAPK9P45984
GPS
158SPhosphorylationKinaseMAPK14Q16539
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAZ1B_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMCA5_HUMANSMARCA5physical
16603771
ERCC6_HUMANERCC6physical
16603771
SF3B1_HUMANSF3B1physical
16603771
RHD_HUMANRHDphysical
16603771
DEK_HUMANDEKphysical
16603771
MBB1A_HUMANMYBBP1Aphysical
16603771
MYO1C_HUMANMYO1Cphysical
16603771
VDR_HUMANVDRphysical
17250953
SMCA5_HUMANSMARCA5physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SMCA4_HUMANSMARCA4physical
22939629
MBD3_HUMANMBD3physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
SRRM2_HUMANSRRM2physical
22939629
SMCA5_HUMANSMARCA5physical
23555303
MYO1C_HUMANMYO1Cphysical
23555303

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAZ1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-426, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705; SER-1315 ANDSER-1468, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-1468, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-345; SER-347;SER-349; SER-361; SER-374; SER-699; SER-705; SER-708; SER-716;SER-947; SER-1315; SER-1342 AND SER-1468, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-347; SER-349;SER-508; SER-1342 AND SER-1468, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705 AND SER-1468, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-361; SER-1147;SER-1342 AND SER-1468, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705; SER-708 ANDSER-1468, AND MASS SPECTROMETRY.

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