BAP1_MOUSE - dbPTM
BAP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAP1_MOUSE
UniProt AC Q99PU7
Protein Name Ubiquitin carboxyl-terminal hydrolase BAP1
Gene Name Bap1
Organism Mus musculus (Mouse).
Sequence Length 728
Subcellular Localization Cytoplasm . Nucleus . Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O.
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. Acts as a tumor suppressor (By similarity)..
Protein Sequence MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYETRLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPLGLEAGRTPVASECTQTDGAEEVAGSCPQTTTHSPPSKCKLVVKPPGSSLNGVPPNPAPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRAPQQYSEDEDDYEDEDEDVQNTNPAIRYKRKGTGKPGSLSNSSDGQLSVLQPNTINVLTEKLQESQKDLSVPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSTRSSQGSQGSSGLEEKEVVEVTESRDKPGLNRSSEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
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
276PhosphorylationELIQTHKSQESQLPE
HHHHHCHHHHHCCCC		31.41-
279PhosphorylationQTHKSQESQLPEESK
HHCHHHHHCCCCCCC		29.40-
285PhosphorylationESQLPEESKPASSKS
HHCCCCCCCCCCCCC		42.1325619855
289PhosphorylationPEESKPASSKSPLGL
CCCCCCCCCCCCCCC		46.9925619855
290PhosphorylationEESKPASSKSPLGLE
CCCCCCCCCCCCCCC		38.9825619855
292PhosphorylationSKPASSKSPLGLEAG
CCCCCCCCCCCCCCC		27.5725521595
301PhosphorylationLGLEAGRTPVASECT
CCCCCCCCCCCCCCC		22.6125619855
305PhosphorylationAGRTPVASECTQTDG
CCCCCCCCCCCCCCC		33.1825619855
308PhosphorylationTPVASECTQTDGAEE
CCCCCCCCCCCCHHH		30.3825619855
310PhosphorylationVASECTQTDGAEEVA
CCCCCCCCCCHHHCC		20.4625619855
319PhosphorylationGAEEVAGSCPQTTTH
CHHHCCCCCCCCCCC		16.9425619855
323PhosphorylationVAGSCPQTTTHSPPS
CCCCCCCCCCCCCCC		20.8523684622
324PhosphorylationAGSCPQTTTHSPPSK
CCCCCCCCCCCCCCC		19.7725619855
325PhosphorylationGSCPQTTTHSPPSKC
CCCCCCCCCCCCCCC		24.6025619855
327PhosphorylationCPQTTTHSPPSKCKL
CCCCCCCCCCCCCEE		36.0921082442
330PhosphorylationTTTHSPPSKCKLVVK
CCCCCCCCCCEEEEC		54.8125619855
366PhosphorylationAFLDNHNYAKSPMQE
HHHHCCCCCCCCCCH		14.0924759943
369PhosphorylationDNHNYAKSPMQEEED
HCCCCCCCCCCHHHH		19.8921082442
384PhosphorylationLAAGVGRSRVPVRAP
HHCCCCCCCCCCCCC		31.5327087446
394PhosphorylationPVRAPQQYSEDEDDY
CCCCCCCCCCCCCCC		14.5828833060
395PhosphorylationVRAPQQYSEDEDDYE
CCCCCCCCCCCCCCC		33.9425521595
401PhosphorylationYSEDEDDYEDEDEDV
CCCCCCCCCCCCHHH		37.2928833060
411PhosphorylationEDEDVQNTNPAIRYK
CCHHHHCCCHHHCEE		26.0323984901
492PhosphorylationPTPSNESTDTASEIG
CCCCCCCCCCHHHHH		31.06-
512PhosphorylationPLRSPIRSANPTRPS
CCCCCCCCCCCCCCC		32.8723684622
516PhosphorylationPIRSANPTRPSSPVT
CCCCCCCCCCCCCCC		55.8323684622
519PhosphorylationSANPTRPSSPVTSHI
CCCCCCCCCCCCHHH		43.9423684622
520PhosphorylationANPTRPSSPVTSHIS
CCCCCCCCCCCHHHH		26.5223684622
523PhosphorylationTRPSSPVTSHISKVL
CCCCCCCCHHHHHHH		20.2625159016
524PhosphorylationRPSSPVTSHISKVLF
CCCCCCCHHHHHHHH		21.0325159016
527PhosphorylationSPVTSHISKVLFGED
CCCCHHHHHHHHCCC		15.9925159016
536PhosphorylationVLFGEDDSLLRVDCI
HHHCCCCCCEEHHHH		41.44-
570PhosphorylationLAEDGVLSPLALTEG
HHCCCCCCCEEECCC		18.5626745281
575PhosphorylationVLSPLALTEGGKGSS
CCCCEEECCCCCCCC		27.2926239621
581PhosphorylationLTEGGKGSSPSTRSS
ECCCCCCCCCCCCCC		42.4326239621
582PhosphorylationTEGGKGSSPSTRSSQ
CCCCCCCCCCCCCCC		31.3826239621
584PhosphorylationGGKGSSPSTRSSQGS
CCCCCCCCCCCCCCC		38.1026160508
585PhosphorylationGKGSSPSTRSSQGSQ
CCCCCCCCCCCCCCC		37.6426160508
591PhosphorylationSTRSSQGSQGSSGLE
CCCCCCCCCCCCCCC		24.5927841257
595PhosphorylationSQGSQGSSGLEEKEV
CCCCCCCCCCCEEEE		54.9729109428
606PhosphorylationEKEVVEVTESRDKPG
EEEEEEEECCCCCCC		18.1026643407
608PhosphorylationEVVEVTESRDKPGLN
EEEEEECCCCCCCCC		36.0926643407
704PhosphorylationVRRRQGVSIGRLHKQ
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAP1_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 BAP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASXL2_HUMANASXL2physical
20360068
ASXL1_HUMANASXL1physical
20360068
HCFC1_HUMANHCFC1physical
20360068
BAP1_HUMANBAP1physical
20360068
HCFC1_MOUSEHcfc1physical
22878500
OGT1_MOUSEOgtphysical
22878500
KDM1B_MOUSEKdm1bphysical
22878500
ASXL1_MOUSEAsxl1physical
22878500
ASXL2_MOUSEAsxl2physical
22878500
OTUD4_MOUSEOtud4physical
22878500
FOXK1_MOUSEFoxk1physical
22878500
KPCA_MOUSEPrkcaphysical
22878500
PI51C_MOUSEPip5k1cphysical
22878500
KC1E_HUMANCSNK1Ephysical
26496610
HCFC1_HUMANHCFC1physical
26496610
COG1_HUMANCOG1physical
26496610
BRE1B_HUMANRNF40physical
26496610
DDX42_HUMANDDX42physical
26496610
DAAF5_HUMANDNAAF5physical
26496610
RAIN_HUMANRASIP1physical
26496610
CENPJ_HUMANCENPJphysical
26496610
HOMEZ_HUMANHOMEZphysical
26496610
DCTP1_HUMANDCTPP1physical
26496610
S35E1_HUMANSLC35E1physical
26496610
ASXL1_HUMANASXL1physical
26496610
KDM1B_HUMANKDM1Bphysical
26496610
FOXK1_HUMANFOXK1physical
26496610
PR14L_HUMANPRR14Lphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAP1_MOUSE

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Related Literatures of Post-Translational Modification

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