BAP1_HUMAN - dbPTM
BAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAP1_HUMAN
UniProt AC Q92560
Protein Name Ubiquitin carboxyl-terminal hydrolase BAP1
Gene Name BAP1
Organism Homo sapiens (Human).
Sequence Length 729
Subcellular Localization Cytoplasm . Nucleus . Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O (PubMed:24703950).
Protein Description Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration. [PubMed: 24703950 Acts as a tumor suppressor.]
Protein Sequence MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSSVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKSASNKSPLVLEANRAPAASEGNHTDGAEEAAGSCAQAPSHSPPNKPKLVVKPPGSSLNGVHPNPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPPQQYSDDEDDYEDDEEDDVQNTNSALRYKGKGTGKPGALSGSADGQLSVLQPNTINVLAEKLKESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSIRPIQGSQGSSSPVEKEVVEATDSREKTGMVRPGEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
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
120UbiquitinationSRMKDFTKGFSPESK
HHHHHHHCCCCHHHC		58.93-
123PhosphorylationKDFTKGFSPESKGYA
HHHHCCCCHHHCCCC		36.1029396449
126PhosphorylationTKGFSPESKGYAIGN
HCCCCHHHCCCCCCC		34.4627251275
127UbiquitinationKGFSPESKGYAIGNA
CCCCHHHCCCCCCCH		55.04-
139UbiquitinationGNAPELAKAHNSHAR
CCHHHHHHHHCCCCC		63.9021890473
139UbiquitinationGNAPELAKAHNSHAR
CCHHHHHHHHCCCCC		63.9021890473
143PhosphorylationELAKAHNSHARPEPR
HHHHHHCCCCCCCCC		14.5125554490
155AcetylationEPRHLPEKQNGLSAV
CCCCCCCHHCCHHHH		47.3123749302
155UbiquitinationEPRHLPEKQNGLSAV
CCCCCCCHHCCHHHH		47.31-
223PhosphorylationLATAGEPYHDIRFNL
CCCCCCCCCCCEEEE		14.0727642862
241PhosphorylationVPDRRIKYEARLHVL
CCCCCCHHEEEEEEE		16.67-
254PhosphorylationVLKVNRQTVLEALQQ
EEECCHHHHHHHHHH		24.6630622161
273PhosphorylationTQPELIQTHKSQESQ
HCHHHHHHCHHHHHC		25.0329214152
275UbiquitinationPELIQTHKSQESQLP
HHHHHHCHHHHHCCC		58.17-
276PhosphorylationELIQTHKSQESQLPE
HHHHHCHHHHHCCCH		31.4125159151
279PhosphorylationQTHKSQESQLPEESK
HHCHHHHHCCCHHHH		29.4028555341
285PhosphorylationESQLPEESKSASNKS
HHCCCHHHHCCCCCC		30.1926074081
287PhosphorylationQLPEESKSASNKSPL
CCCHHHHCCCCCCCE		46.3223927012
289PhosphorylationPEESKSASNKSPLVL
CHHHHCCCCCCCEEE		52.4630278072
292PhosphorylationSKSASNKSPLVLEAN
HHCCCCCCCEEEEEC		27.9319664994
305PhosphorylationANRAPAASEGNHTDG
ECCCCCHHCCCCCCC		48.4129970186
310PhosphorylationAASEGNHTDGAEEAA
CHHCCCCCCCHHHHC		39.8829970186
319PhosphorylationGAEEAAGSCAQAPSH
CHHHHCHHCCCCCCC		11.1027794612
325PhosphorylationGSCAQAPSHSPPNKP
HHCCCCCCCCCCCCC		39.3423401153
327PhosphorylationCAQAPSHSPPNKPKL
CCCCCCCCCCCCCCE		46.5225159151
366PhosphorylationAFLDNHNYAKSPMQE
HHHHCCCCCCCCCCH		14.0927642862
369PhosphorylationDNHNYAKSPMQEEED
HCCCCCCCCCCHHHH		19.8925159151
371SulfoxidationHNYAKSPMQEEEDLA
CCCCCCCCCHHHHHH		11.4821406390
384PhosphorylationLAAGVGRSRVPVRPP
HHCCCCCCCCCCCCC		31.5327794612
394PhosphorylationPVRPPQQYSDDEDDY
CCCCCCCCCCCCCCC		14.6021955146
395PhosphorylationVRPPQQYSDDEDDYE
CCCCCCCCCCCCCCC		33.9625159151
401PhosphorylationYSDDEDDYEDDEEDD
CCCCCCCCCCCCCCC		33.3121955146
412PhosphorylationEEDDVQNTNSALRYK
CCCCCCCHHHHHHHC		17.2926074081
414PhosphorylationDDVQNTNSALRYKGK
CCCCCHHHHHHHCCC		27.0026074081
425AcetylationYKGKGTGKPGALSGS
HCCCCCCCCCCCCCC		39.8726051181
451AcetylationTINVLAEKLKESQKD
HHHHHHHHHHHHHCC		60.2926051181
455PhosphorylationLAEKLKESQKDLSIP
HHHHHHHHHCCCCCC		40.7329083192
460PhosphorylationKESQKDLSIPLSIKT
HHHHCCCCCCEEEEC		32.0930266825
464PhosphorylationKDLSIPLSIKTSSGA
CCCCCCEEEECCCCC		19.3826329039
467PhosphorylationSIPLSIKTSSGAGSP
CCCEEEECCCCCCCC		26.8423312004
468PhosphorylationIPLSIKTSSGAGSPA
CCEEEECCCCCCCCC		23.0523312004
469PhosphorylationPLSIKTSSGAGSPAV
CEEEECCCCCCCCCE		37.5823312004
473PhosphorylationKTSSGAGSPAVAVPT
ECCCCCCCCCEEECC		14.7823312004
480PhosphorylationSPAVAVPTHSQPSPT
CCCEEECCCCCCCCC		27.7926074081
482PhosphorylationAVAVPTHSQPSPTPS
CEEECCCCCCCCCCC		46.3826074081
485PhosphorylationVPTHSQPSPTPSNES
ECCCCCCCCCCCCCC		33.4926074081
487PhosphorylationTHSQPSPTPSNESTD
CCCCCCCCCCCCCCC		43.6226074081
489PhosphorylationSQPSPTPSNESTDTA
CCCCCCCCCCCCCCH		56.5626074081
492PhosphorylationSPTPSNESTDTASEI
CCCCCCCCCCCHHHH		35.5126074081
493PhosphorylationPTPSNESTDTASEIG
CCCCCCCCCCHHHHH		31.0626074081
495PhosphorylationPSNESTDTASEIGSA
CCCCCCCCHHHHHHH		31.9730576142
497PhosphorylationNESTDTASEIGSAFN
CCCCCCHHHHHHHHC		31.6623312004
501PhosphorylationDTASEIGSAFNSPLR
CCHHHHHHHHCCCCC		35.0323312004
505PhosphorylationEIGSAFNSPLRSPIR
HHHHHHCCCCCCCCC		20.8930576142
509PhosphorylationAFNSPLRSPIRSANP
HHCCCCCCCCCCCCC		32.1527251275
513PhosphorylationPLRSPIRSANPTRPS
CCCCCCCCCCCCCCC		32.8723927012
517PhosphorylationPIRSANPTRPSSPVT
CCCCCCCCCCCCCCC		55.8323401153
520PhosphorylationSANPTRPSSPVTSHI
CCCCCCCCCCCCHHH		43.9423401153
521PhosphorylationANPTRPSSPVTSHIS
CCCCCCCCCCCHHHH		26.5222167270
524PhosphorylationTRPSSPVTSHISKVL
CCCCCCCCHHHHHHH		20.2622167270
525PhosphorylationRPSSPVTSHISKVLF
CCCCCCCHHHHHHHH		21.0323927012
528PhosphorylationSPVTSHISKVLFGED
CCCCHHHHHHHHCCC		15.9923927012
537PhosphorylationVLFGEDDSLLRVDCI
HHHCCCCCCEEHHHH		41.4423917254
571PhosphorylationLAEDGVLSPLALTEG
HHCCCCCCCEEECCC		18.56-
582PhosphorylationLTEGGKGSSPSIRPI
ECCCCCCCCCCCCCC		42.4330266825
583PhosphorylationTEGGKGSSPSIRPIQ
CCCCCCCCCCCCCCC		31.1925159151
585PhosphorylationGGKGSSPSIRPIQGS
CCCCCCCCCCCCCCC		32.9330266825
592PhosphorylationSIRPIQGSQGSSSPV
CCCCCCCCCCCCCCC		18.2617525332
595PhosphorylationPIQGSQGSSSPVEKE
CCCCCCCCCCCCCHH		21.7225159151
596PhosphorylationIQGSQGSSSPVEKEV
CCCCCCCCCCCCHHH		45.5529255136
597PhosphorylationQGSQGSSSPVEKEVV
CCCCCCCCCCCHHHH		34.3629255136
609PhosphorylationEVVEATDSREKTGMV
HHHHCCCCCCCCCCC		37.6725159151
615SulfoxidationDSREKTGMVRPGEPL
CCCCCCCCCCCCCCC		2.5321406390
630UbiquitinationSGEKYSPKELLALLK
CCCCCCHHHHHHHHH		55.8621890473
630UbiquitinationSGEKYSPKELLALLK
CCCCCCHHHHHHHHH		55.8621890473
656MethylationCLKEEVEKRKKFKID
HHHHHHHHHHCCCCC		74.76-
658MethylationKEEVEKRKKFKIDDQ
HHHHHHHHCCCCCCC		73.88-
659MethylationEEVEKRKKFKIDDQR
HHHHHHHCCCCCCCH		56.79-
705PhosphorylationVRRRQGVSIGRLHKQ
HHHHCCCCHHHHHHC		26.59-
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 BAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAP1_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 BAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HCFC1_HUMANHCFC1physical
19615732
FOXK2_HUMANFOXK2physical
19615732
IPO5_HUMANIPO5physical
19615732
PPM1G_HUMANPPM1Gphysical
19615732
RBBP7_HUMANRBBP7physical
19615732
OGT1_HUMANOGTphysical
19615732
HAT1_HUMANHAT1physical
19615732
4EBP3_HUMANEIF4EBP3physical
19615732
PSME3_HUMANPSME3physical
19615732
CBX1_HUMANCBX1physical
19615732
CBX3_HUMANCBX3physical
19615732
SAHH3_HUMANAHCYL2physical
19615732
ANR17_HUMANANKRD17physical
19615732
APC7_HUMANANAPC7physical
19615732
ASXL2_HUMANASXL2physical
19615732
UBE2O_HUMANUBE2Ophysical
19615732
IPO4_HUMANIPO4physical
19615732
ASXL1_HUMANASXL1physical
19615732
KDM1B_HUMANKDM1Bphysical
19615732
FOXK1_HUMANFOXK1physical
19615732
HCFC1_HUMANHCFC1physical
19815555
ASXL1_HUMANASXL1physical
19815555
ASXL2_HUMANASXL2physical
19815555
HSP72_HUMANHSPA2physical
19815555
FOXK2_HUMANFOXK2physical
19815555
FOXK1_HUMANFOXK1physical
19815555
KDM1B_HUMANKDM1Bphysical
19815555
HAT1_HUMANHAT1physical
19815555
ANR17_HUMANANKRD17physical
19815555
ASXL1_HUMANASXL1physical
20436459
H2A2C_HUMANHIST2H2ACphysical
20436459
ASXL1_HUMANASXL1physical
20805357
ZC3HD_HUMANZC3H13physical
20805357
HCFC1_HUMANHCFC1physical
20805357
ASXL2_HUMANASXL2physical
20805357
PRD10_HUMANPRDM10physical
20805357
OGT1_HUMANOGTphysical
20805357
FOXK1_HUMANFOXK1physical
20805357
GRP75_HUMANHSPA9physical
20805357
FOXK2_HUMANFOXK2physical
20805357
KDM1B_HUMANKDM1Bphysical
20805357
ZN131_HUMANZNF131physical
20805357
EFNA2_HUMANEFNA2physical
20805357
ELF2_HUMANELF2physical
20805357
TYY1_HUMANYY1physical
20805357
HCFC1_HUMANHCFC1physical
22683710
HCFC1_HUMANHCFC1physical
21642991
ASXL1_HUMANASXL1physical
21642991
HCFC1_HUMANHCFC1physical
19188440
BRCA1_HUMANBRCA1physical
9528852
ASXL1_HUMANASXL1physical
22897849
HCFC1_HUMANHCFC1physical
24703950
UBE2O_HUMANUBE2Ophysical
24703950
OGT1_HUMANOGTphysical
24703950
H2A2A_HUMANHIST2H2AA3physical
24703950
HCFC1_HUMANHCFC1physical
24211834
H2A2C_HUMANHIST2H2ACphysical
25283999
OGT1_MOUSEOgtphysical
22878500
FOXK2_HUMANFOXK2physical
25451922
FOXK1_HUMANFOXK1physical
25451922
MCRS1_HUMANMCRS1physical
26300492
ASXL3_HUMANASXL3physical
26647312
ASXL1_HUMANASXL1physical
26416890
ASXL2_HUMANASXL2physical
26416890
OGT1_HUMANOGTphysical
26416890
HCFC1_HUMANHCFC1physical
26416890
FOXK2_HUMANFOXK2physical
24748658
KLF5_HUMANKLF5physical
26419610
H2A2C_HUMANHIST2H2ACphysical
26739236
ASXL1_HUMANASXL1physical
26739236
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
156240Mesothelioma, malignant (MESOM)
614327Tumor predisposition syndrome (TPDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-327; SER-582 ANDSER-597, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND MASSSPECTROMETRY.
"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-583; SER-592 ANDSER-597, 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 THR-487 AND SER-489, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory