BGLR_HUMAN - dbPTM
BGLR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BGLR_HUMAN
UniProt AC P08236
Protein Name Beta-glucuronidase
Gene Name GUSB
Organism Homo sapiens (Human).
Sequence Length 651
Subcellular Localization Lysosome.
Protein Description Plays an important role in the degradation of dermatan and keratan sulfates..
Protein Sequence MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNVSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT
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
39UbiquitinationESPSRECKELDGLWS
CCCCCCCHHCCCCEE		57.4621963094
39UbiquitinationESPSRECKELDGLWS
CCCCCCCHHCCCCEE		57.46-
39 (in isoform 2)Ubiquitination-57.4621890473
39 (in isoform 1)Ubiquitination-57.4621890473
39UbiquitinationESPSRECKELDGLWS
CCCCCCCHHCCCCEE		57.4621890473
93UbiquitinationISQDWRLRHFVGWVW
CCCHHHHHHHCEEEE		16.7822817900
127UbiquitinationVLRIGSAHSYAIVWV
EEEECCCCEEEEEEE		24.0422817900
135UbiquitinationSYAIVWVNGVDTLEH
EEEEEEECCCEEEEE		29.1122817900
140UbiquitinationWVNGVDTLEHEGGYL
EECCCEEEEECCCCC		5.6822817900
144UbiquitinationVDTLEHEGGYLPFEA
CEEEEECCCCCCCEE		31.7722817900
149UbiquitinationHEGGYLPFEADISNL
ECCCCCCCEEEHHHC		12.8022817900
150UbiquitinationEGGYLPFEADISNLV
CCCCCCCEEEHHHCE		43.4222817900
169UbiquitinationLPSRLRITIAINNTL
CCCEEEEEEEECCCC		9.6422817900
173N-linked_GlycosylationLRITIAINNTLTPTT
EEEEEEECCCCCCCC		26.818505339
173N-linked_GlycosylationLRITIAINNTLTPTT
EEEEEEECCCCCCCC		26.818505339
178UbiquitinationAINNTLTPTTLPPGT
EECCCCCCCCCCCCC		26.8822817900
180O-linked_GlycosylationNNTLTPTTLPPGTIQ
CCCCCCCCCCCCCEE		38.17OGP
192UbiquitinationTIQYLTDTSKYPKGY
CEEEEECCCCCCCCE		23.1422817900
201UbiquitinationKYPKGYFVQNTYFDF
CCCCCEEECCCEECC		3.0222817900
213UbiquitinationFDFFNYAGLQRSVLL
ECCCCCCCCCCEEEE		16.3922817900
213UbiquitinationFDFFNYAGLQRSVLL
ECCCCCCCCCCEEEE		16.39-
222UbiquitinationQRSVLLYTTPTTYID
CCEEEEEECCCCEEC		26.6922817900
222UbiquitinationQRSVLLYTTPTTYID
CCEEEEEECCCCEEC		26.69-
251UbiquitinationVNYQISVKGSNLFKL
EEEEEEECCCCEEEE		50.24-
268UbiquitinationRLLDAENKVVANGTG
EEEECCCCEEECCCC		29.59-
272N-linked_GlycosylationAENKVVANGTGTQGQ
CCCCEEECCCCCCCC		36.6312754519
272N-linked_GlycosylationAENKVVANGTGTQGQ
CCCCEEECCCCCCCC		36.6312754519
274O-linked_GlycosylationNKVVANGTGTQGQLK
CCEEECCCCCCCCEE		36.5430059200
274PhosphorylationNKVVANGTGTQGQLK
CCEEECCCCCCCCEE		36.548505339
308 (in isoform 2)Ubiquitination-10.3021890473
317UbiquitinationQTSLGPVSDFYTLPV
CCCCCCHHHCEECCC		25.7422817900
317 (in isoform 2)Ubiquitination-25.7421890473
357UbiquitinationKHEDADIRGKGFDWP
CCCCCCCCCCCCCHH		41.1229967540
359 (in isoform 1)Ubiquitination-46.7021890473
359UbiquitinationEDADIRGKGFDWPLL
CCCCCCCCCCCHHEE		46.7022817900
366UbiquitinationKGFDWPLLVKDFNLL
CCCCHHEEECHHHHH		3.8421890473
368 (in isoform 1)Ubiquitination-57.4821890473
368UbiquitinationFDWPLLVKDFNLLRW
CCHHEEECHHHHHHH		57.4822817900
386UbiquitinationNAFRTSHYPYAEEVM
CCHHCCCCCHHHHHH		9.5629967540
400UbiquitinationMQMCDRYGIVVIDEC
HHHHHHHCEEEEECC		13.7021890473
417UbiquitinationVGLALPQFFNNVSLH
CCCCHHHHCCCCCHH		7.1721890473
420N-linked_GlycosylationALPQFFNNVSLHHHM
CHHHHCCCCCHHHHH		21.43UniProtKB CARBOHYD
420N-linked_GlycosylationALPQFFNNVSLHHHM
CHHHHCCCCCHHHHH		21.438505339
422UbiquitinationPQFFNNVSLHHHMQV
HHHCCCCCHHHHHHH		24.9021890473
423UbiquitinationQFFNNVSLHHHMQVM
HHCCCCCHHHHHHHH		3.7721890473
430UbiquitinationLHHHMQVMEEVVRRD
HHHHHHHHHHHHHHC		1.7329967540
447PhosphorylationHPAVVMWSVANEPAS
CCCEEEEEECCCCHH		8.0222210691
451UbiquitinationVMWSVANEPASHLES
EEEEECCCCHHHHHH		32.2921890473
454PhosphorylationSVANEPASHLESAGY
EECCCCHHHHHHHHH		39.0429978859
458PhosphorylationEPASHLESAGYYLKM
CCHHHHHHHHHHHHH		33.1029978859
461PhosphorylationSHLESAGYYLKMVIA
HHHHHHHHHHHHHHH		12.8229978859
462PhosphorylationHLESAGYYLKMVIAH
HHHHHHHHHHHHHHH		10.0329978859
470PhosphorylationLKMVIAHTKSLDPSR
HHHHHHHCCCCCCCC		17.2022210691
474UbiquitinationIAHTKSLDPSRPVTF
HHHCCCCCCCCCEEE		46.3421890473
495UbiquitinationAADKGAPYVDVICLN
CCCCCCCEEEEEEEE		14.5621890473
495UbiquitinationAADKGAPYVDVICLN
CCCCCCCEEEEEEEE		14.5621890473
495UbiquitinationAADKGAPYVDVICLN
CCCCCCCEEEEEEEE		14.56-
576UbiquitinationYHLGLDQKRRKYVVG
HCCCCCHHHHHHHHH		54.5629967540
590UbiquitinationGELIWNFADFMTEQS
HHHHHHHHHHHCCCC		13.1021890473
590 (in isoform 2)Ubiquitination-13.1021890473
631N-linked_GlycosylationERYWKIANETRYPHS
HHHHHHHHCCCCCHH		55.438505339
631N-linked_GlycosylationERYWKIANETRYPHS
HHHHHHHHCCCCCHH		55.438505339
641 (in isoform 1)Ubiquitination-38.6121890473
641UbiquitinationRYPHSVAKSQCLENS
CCCHHHHHHHHHHHC		38.6122817900
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 BGLR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BGLR_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 BGLR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EST1_HUMANCES1physical
10562416
FAHD1_HUMANFAHD1physical
26344197
HXA3_HUMANHOXA3physical
28514442
PMEL_HUMANPMELphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
253220Mucopolysaccharidosis 7 (MPS7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BGLR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-173; ASN-272 AND ASN-631,AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-272, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-272.

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