GLU2B_MOUSE - dbPTM
GLU2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLU2B_MOUSE
UniProt AC O08795
Protein Name Glucosidase 2 subunit beta
Gene Name Prkcsh
Organism Mus musculus (Mouse).
Sequence Length 521
Subcellular Localization Endoplasmic reticulum .
Protein Description Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins..
Protein Sequence MLLLLLLLLPLCWAVEVKRPRGVSLSNHHFYEESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEETEPKEEKPPVLPPTEEEEEEEEEPEEEEEEEEEEEEAPPPLQPPQPPSPTEDEKMPPYDEETQAIIDAAQEARSKFEEVERSLKEMEESIRSLEQEISFDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKHGGSPTSLGTWGSWAGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEAPSDGDHDEL
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
24PhosphorylationVKRPRGVSLSNHHFY
CCCCCCCCCCCCCCC
28.9827841257
62PhosphorylationYCDCKDGSDEPGTAA
CCCCCCCCCCCCCCC
49.2726525534
72N-linked_GlycosylationPGTAACPNGSFHCTN
CCCCCCCCCCEEECC
59.64-
89PhosphorylationYKPLYILSSRVNDGV
CCCEEEEECCCCCCC
13.41-
103PhosphorylationVCDCCDGTDEYNSGT
CCCCCCCCCCCCCCC
16.6526525534
142SuccinylationREGFRLKKILIEEWK
HHCHHHHHHHHHHHH
47.5423806337
142AcetylationREGFRLKKILIEEWK
HHCHHHHHHHHHHHH
47.5423806337
149AcetylationKILIEEWKTAREEKQ
HHHHHHHHHHHHHHH
35.2722826441
157PhosphorylationTAREEKQSKLLELQA
HHHHHHHHHHHHHHH
36.0228059163
166SuccinylationLLELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.0523806337
166AcetylationLLELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.0523806337
166SuccinylationLLELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.05-
168PhosphorylationELQAGKKSLEDQVET
HHHHCCCCHHHHHHH
40.2426824392
180 (in isoform 2)Acetylation-55.92-
180AcetylationVETLRAAKEEAERPE
HHHHHHHHHHHHCHH
55.9223201123
196AcetylationEAKDQHRKLWEEQQA
HHHHHHHHHHHHHHH
56.6919849947
342PhosphorylationLQPPQPPSPTEDEKM
CCCCCCCCCCCCCCC
51.6530635358
344PhosphorylationPPQPPSPTEDEKMPP
CCCCCCCCCCCCCCC
61.4830635358
368PhosphorylationDAAQEARSKFEEVER
HHHHHHHHHHHHHHH
49.0624719451
376PhosphorylationKFEEVERSLKEMEES
HHHHHHHHHHHHHHH
30.22-
383PhosphorylationSLKEMEESIRSLEQE
HHHHHHHHHHHHHHH
15.25-
427PhosphorylationLCPFKLVSQKPKHGG
HCCCCEECCCCCCCC
42.81-
452AcetylationWAGPDHDKFSAMKYE
CCCCCCCCCCCCEEE
37.4922826441
457AcetylationHDKFSAMKYEQGTGC
CCCCCCCEEECCCCC
45.4022826441
469N-linked_GlycosylationTGCWQGPNRSTTVRL
CCCCCCCCCCCCEEE
58.31-
514PhosphorylationEPPPEAPSDGDHDEL
CCCCCCCCCCCCCCC
62.3626525534

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
89SPhosphorylationKinasePKC-Uniprot
376SPhosphorylationKinasePKC-Uniprot
383SPhosphorylationKinasePKC-Uniprot
427SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLU2B_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 GLU2B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI67_MOUSETrim67physical
22337885
TRIM9_MOUSETrim9physical
22337885
PLPR4_MOUSELppr4physical
22337885

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLU2B_MOUSE

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Related Literatures of Post-Translational Modification

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