GLU2B_HUMAN - dbPTM
GLU2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLU2B_HUMAN
UniProt AC P14314
Protein Name Glucosidase 2 subunit beta
Gene Name PRKCSH
Organism Homo sapiens (Human).
Sequence Length 528
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 MLLPLLLLLPMCWAVEVKRPRGVSLTNHHFYDESKPFTCLDGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVCDCCDGTDEYNSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAAIRDKYRSEALPTDLPAPSAPDLTEPKEEQPPVPSSPTEEEEEEEEEEEEEAEEEEEEEDSEEAPPPLSPPQPASPAEEDKMPPYDEQTQAFIDAAQEARNKFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKLGGSPTSLGTWGSWIGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELMTPAACPEPPPEAPTEDDHDEL
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
24PhosphorylationVKRPRGVSLTNHHFY
CCCCCCCCCCCCCCC
32.0925849741
26PhosphorylationRPRGVSLTNHHFYDE
CCCCCCCCCCCCCCC
25.6226133373
31PhosphorylationSLTNHHFYDESKPFT
CCCCCCCCCCCCCCC
17.9128348404
72N-linked_GlycosylationPGTAACPNGSFHCTN
CCCCCCCCCCEEECC
59.64UniProtKB CARBOHYD
83UbiquitinationHCTNTGYKPLYIPSN
EECCCCCCCCEECCC
29.86-
83MethylationHCTNTGYKPLYIPSN
EECCCCCCCCEECCC
29.86115975685
89PhosphorylationYKPLYIPSNRVNDGV
CCCCEECCCCCCCCC
27.92-
117AcetylationVICENTCKEKGRKER
CCCCCHHHHCCHHHH
61.4926051181
126PhosphorylationKGRKERESLQQMAEV
CCHHHHHHHHHHHHH
37.3925159151
130SulfoxidationERESLQQMAEVTREG
HHHHHHHHHHHHHHH
1.9021406390
134O-linked_GlycosylationLQQMAEVTREGFRLK
HHHHHHHHHHHHHHH
17.9555826287
1422-HydroxyisobutyrylationREGFRLKKILIEDWK
HHHHHHHHHHHHHHH
47.54-
142UbiquitinationREGFRLKKILIEDWK
HHHHHHHHHHHHHHH
47.54-
1492-HydroxyisobutyrylationKILIEDWKKAREEKQ
HHHHHHHHHHHHHHH
49.21-
149SuccinylationKILIEDWKKAREEKQ
HHHHHHHHHHHHHHH
49.2123954790
149AcetylationKILIEDWKKAREEKQ
HHHHHHHHHHHHHHH
49.2127452117
1582-HydroxyisobutyrylationAREEKQKKLIELQAG
HHHHHHHHHHHHHHC
52.80-
166SuccinylationLIELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.05-
166AcetylationLIELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.0525953088
166UbiquitinationLIELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.05-
166SuccinylationLIELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.0523954790
1662-HydroxyisobutyrylationLIELQAGKKSLEDQV
HHHHHHCCCCHHHHH
42.05-
1672-HydroxyisobutyrylationIELQAGKKSLEDQVE
HHHHHCCCCHHHHHH
60.39-
167UbiquitinationIELQAGKKSLEDQVE
HHHHHCCCCHHHHHH
60.39-
168PhosphorylationELQAGKKSLEDQVEM
HHHHCCCCHHHHHHH
40.2428355574
175SulfoxidationSLEDQVEMLRTVKEE
CHHHHHHHHHHHHHH
3.0128465586
177MethylationEDQVEMLRTVKEEAE
HHHHHHHHHHHHHHH
35.84115488789
180SuccinylationVEMLRTVKEEAEKPE
HHHHHHHHHHHHCHH
49.5823954790
1962-HydroxyisobutyrylationEAKEQHQKLWEEQLA
HHHHHHHHHHHHHHH
54.14-
196UbiquitinationEAKEQHQKLWEEQLA
HHHHHHHHHHHHHHH
54.14-
206UbiquitinationEEQLAAAKAQQEQEL
HHHHHHHHHHHHHHH
41.84-
228PhosphorylationLDDDMDGTVSVTELQ
CCCCCCCEEEEEEEE
12.8226074081
230PhosphorylationDDMDGTVSVTELQTH
CCCCCEEEEEEEECC
24.1426074081
232PhosphorylationMDGTVSVTELQTHPE
CCCEEEEEEEECCCC
24.3826074081
263O-linked_GlycosylationLLSGDTQTDATSFYD
HHCCCCCCCHHHHHH
29.69OGP
280PhosphorylationWAAIRDKYRSEALPT
HHHHHHHHHHCCCCC
24.5426657352
282O-linked_GlycosylationAIRDKYRSEALPTDL
HHHHHHHHCCCCCCC
24.9123301498
282PhosphorylationAIRDKYRSEALPTDL
HHHHHHHHCCCCCCC
24.9126657352
287O-linked_GlycosylationYRSEALPTDLPAPSA
HHHCCCCCCCCCCCC
51.5223301498
287PhosphorylationYRSEALPTDLPAPSA
HHHCCCCCCCCCCCC
51.5226657352
293O-linked_GlycosylationPTDLPAPSAPDLTEP
CCCCCCCCCCCCCCC
55.3223301498
293PhosphorylationPTDLPAPSAPDLTEP
CCCCCCCCCCCCCCC
55.3225693802
298O-linked_GlycosylationAPSAPDLTEPKEEQP
CCCCCCCCCCCCCCC
58.5923301498
298PhosphorylationAPSAPDLTEPKEEQP
CCCCCCCCCCCCCCC
58.5925693802
335PhosphorylationEEEEEEDSEEAPPPL
HHHHHHCCCCCCCCC
40.3925137130
343O-linked_GlycosylationEEAPPPLSPPQPASP
CCCCCCCCCCCCCCC
40.06OGP
343PhosphorylationEEAPPPLSPPQPASP
CCCCCCCCCCCCCCC
40.0625137130
349PhosphorylationLSPPQPASPAEEDKM
CCCCCCCCCCCCCCC
31.18-
349O-linked_GlycosylationLSPPQPASPAEEDKM
CCCCCCCCCCCCCCC
31.18OGP
363O-linked_GlycosylationMPPYDEQTQAFIDAA
CCCCCHHHHHHHHHH
21.59OGP
376UbiquitinationAAQEARNKFEEAERS
HHHHHHHHHHHHHHH
48.91-
376AcetylationAAQEARNKFEEAERS
HHHHHHHHHHHHHHH
48.9126822725
3762-HydroxyisobutyrylationAAQEARNKFEEAERS
HHHHHHHHHHHHHHH
48.91-
383PhosphorylationKFEEAERSLKDMEES
HHHHHHHHHHHHHHH
31.14-
385UbiquitinationEEAERSLKDMEESIR
HHHHHHHHHHHHHHH
57.16-
385SuccinylationEEAERSLKDMEESIR
HHHHHHHHHHHHHHH
57.1623954790
3852-HydroxyisobutyrylationEEAERSLKDMEESIR
HHHHHHHHHHHHHHH
57.16-
387SulfoxidationAERSLKDMEESIRNL
HHHHHHHHHHHHHHH
6.1821406390
390PhosphorylationSLKDMEESIRNLEQE
HHHHHHHHHHHHHHH
17.3426546556
423PhosphorylationYELTTNEYVYRLCPF
EECCCCCHHHHHCCH
12.5925884760
431AcetylationVYRLCPFKLVSQKPK
HHHHCCHHHCCCCCC
32.8725953088
434PhosphorylationLCPFKLVSQKPKLGG
HCCHHHCCCCCCCCC
42.8121082442
435UbiquitinationCPFKLVSQKPKLGGS
CCHHHCCCCCCCCCC
59.6021890473
436UbiquitinationPFKLVSQKPKLGGSP
CHHHCCCCCCCCCCC
36.29-
438UbiquitinationKLVSQKPKLGGSPTS
HHCCCCCCCCCCCCC
67.7921890473
442PhosphorylationQKPKLGGSPTSLGTW
CCCCCCCCCCCCCCC
24.1728450419
444PhosphorylationPKLGGSPTSLGTWGS
CCCCCCCCCCCCCCC
37.9827251275
445PhosphorylationKLGGSPTSLGTWGSW
CCCCCCCCCCCCCCC
28.3427251275
448PhosphorylationGSPTSLGTWGSWIGP
CCCCCCCCCCCCCCC
31.7628450419
451PhosphorylationTSLGTWGSWIGPDHD
CCCCCCCCCCCCCCC
13.69-
459AcetylationWIGPDHDKFSAMKYE
CCCCCCCCCCCCEEE
37.4926051181
4592-HydroxyisobutyrylationWIGPDHDKFSAMKYE
CCCCCCCCCCCCEEE
37.49-
459UbiquitinationWIGPDHDKFSAMKYE
CCCCCCCCCCCCEEE
37.49-
464UbiquitinationHDKFSAMKYEQGTGC
CCCCCCCEEECCCCC
45.40-
464AcetylationHDKFSAMKYEQGTGC
CCCCCCCEEECCCCC
45.4027452117
465PhosphorylationDKFSAMKYEQGTGCW
CCCCCCEEECCCCCC
10.6228152594
471GlutathionylationKYEQGTGCWQGPNRS
EEECCCCCCCCCCCC
2.1722555962
476N-linked_GlycosylationTGCWQGPNRSTTVRL
CCCCCCCCCCCCEEE
58.31UniProtKB CARBOHYD
484UbiquitinationRSTTVRLLCGKETMV
CCCCEEEECCCCEEC
2.2521890473
485GlutathionylationSTTVRLLCGKETMVT
CCCEEEECCCCEECC
9.6622555962
487UbiquitinationTVRLLCGKETMVTST
CEEEECCCCEECCCC
49.362189047
4872-HydroxyisobutyrylationTVRLLCGKETMVTST
CEEEECCCCEECCCC
49.36-
490SulfoxidationLLCGKETMVTSTTEP
EECCCCEECCCCCCH
3.0421406390
494PhosphorylationKETMVTSTTEPSRCE
CCEECCCCCCHHHHH
26.3021712546
498PhosphorylationVTSTTEPSRCEYLME
CCCCCCHHHHHHHHH
43.2421712546

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
24SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
89SPhosphorylationKinasePKC-Uniprot
168SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
383SPhosphorylationKinasePKC-Uniprot
390SPhosphorylationKinasePKC-Uniprot
434SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLU2B_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 GLU2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU153_HUMANNUP153physical
22939629
PNPT1_HUMANPNPT1physical
22939629
PDIA1_HUMANP4HBphysical
22939629
RS6_HUMANRPS6physical
21988832
VDR_HUMANVDRphysical
21988832
ARMX3_HUMANARMCX3physical
22863883
BUB1B_HUMANBUB1Bphysical
22863883
PUR6_HUMANPAICSphysical
22863883
RNBP6_HUMANRANBP6physical
22863883
DNA2_HUMANDNA2physical
26186194
APC7_HUMANANAPC7physical
26186194
PREP_HUMANPITRM1physical
26186194
TSC2_HUMANTSC2physical
26186194
PEX14_HUMANPEX14physical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
S27A2_HUMANSLC27A2physical
26186194
BBS1_HUMANBBS1physical
26186194
AURKA_HUMANAURKAphysical
26186194
TBB3_HUMANTUBB3physical
26186194
COPG1_HUMANCOPG1physical
26186194
INT7_HUMANINTS7physical
26186194
DEN6A_HUMANDENND6Aphysical
26186194
FUK_HUMANFUKphysical
26186194
IPO9_HUMANIPO9physical
26344197
FUK_HUMANFUKphysical
28514442
TSC2_HUMANTSC2physical
28514442
DEN6A_HUMANDENND6Aphysical
28514442
PEX14_HUMANPEX14physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
AURKA_HUMANAURKAphysical
28514442
EFNB3_HUMANEFNB3physical
28514442
TBB3_HUMANTUBB3physical
28514442
PREP_HUMANPITRM1physical
28514442
S27A2_HUMANSLC27A2physical
28514442
COPG1_HUMANCOPG1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
174050Polycystic liver disease (PCLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLU2B_HUMAN

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Related Literatures of Post-Translational Modification

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