MOGS_HUMAN - dbPTM
MOGS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOGS_HUMAN
UniProt AC Q13724
Protein Name Mannosyl-oligosaccharide glucosidase
Gene Name MOGS
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein.
Protein Description Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner..
Protein Sequence MARGERRRRAVPAEGVRTAERAARGGPGRRDGRGGGPRSTAGGVALAVVVLSLALGMSGRWVLAWYRARRAVTLHSAPPVLPADSSSPAVAPDLFWGTYRPHVYFGMKTRSPKPLLTGLMWAQQGTTPGTPKLRHTCEQGDGVGPYGWEFHDGLSFGRQHIQDGALRLTTEFVKRPGGQHGGDWSWRVTVEPQDSGTSALPLVSLFFYVVTDGKEVLLPEVGAKGQLKFISGHTSELGDFRFTLLPPTSPGDTAPKYGSYNVFWTSNPGLPLLTEMVKSRLNSWFQHRPPGAPPERYLGLPGSLKWEDRGPSGQGQGQFLIQQVTLKIPISIEFVFESGSAQAGGNQALPRLAGSLLTQALESHAEGFRERFEKTFQLKEKGLSSGEQVLGQAALSGLLGGIGYFYGQGLVLPDIGVEGSEQKVDPALFPPVPLFTAVPSRSFFPRGFLWDEGFHQLVVQRWDPSLTREALGHWLGLLNADGWIGREQILGDEARARVPPEFLVQRAVHANPPTLLLPVAHMLEVGDPDDLAFLRKALPRLHAWFSWLHQSQAGPLPLSYRWRGRDPALPTLLNPKTLPSGLDDYPRASHPSVTERHLDLRCWVALGARVLTRLAEHLGEAEVAAELGPLAASLEAAESLDELHWAPELGVFADFGNHTKAVQLKPRPPQGLVRVVGRPQPQLQYVDALGYVSLFPLLLRLLDPTSSRLGPLLDILADSRHLWSPFGLRSLAASSSFYGQRNSEHDPPYWRGAVWLNVNYLALGALHHYGHLEGPHQARAAKLHGELRANVVGNVWRQYQATGFLWEQYSDRDGRGMGCRPFHGWTSLVLLAMAEDY
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
5 (in isoform 2)Phosphorylation-37.1429116813
11 (in isoform 2)Phosphorylation-4.3529116813
18PhosphorylationVPAEGVRTAERAARG
CCCHHHHHHHHHHHC		30.3929396449
52PhosphorylationALAVVVLSLALGMSG
HHHHHHHHHHHCCCH		10.45-
98PhosphorylationAPDLFWGTYRPHVYF
CCCCCCCCCCCEEEE		13.62-
99PhosphorylationPDLFWGTYRPHVYFG
CCCCCCCCCCEEEEE		20.43-
111PhosphorylationYFGMKTRSPKPLLTG
EEECCCCCCCCCHHH		42.37-
126PhosphorylationLMWAQQGTTPGTPKL
HHHHHCCCCCCCCCC		26.02-
127PhosphorylationMWAQQGTTPGTPKLR
HHHHCCCCCCCCCCC		26.92-
130PhosphorylationQQGTTPGTPKLRHTC
HCCCCCCCCCCCCCC		20.6029116813
174UbiquitinationRLTTEFVKRPGGQHG
EEEEEEECCCCCCCC		59.19-
228UbiquitinationVGAKGQLKFISGHTS
CCCCCCEEEECCCCC		32.53-
243PhosphorylationELGDFRFTLLPPTSP
CCCCEEEEECCCCCC		24.1122199227
248PhosphorylationRFTLLPPTSPGDTAP
EEEECCCCCCCCCCC		45.6822199227
249PhosphorylationFTLLPPTSPGDTAPK
EEECCCCCCCCCCCC		32.4322199227
253PhosphorylationPPTSPGDTAPKYGSY
CCCCCCCCCCCCCCC		51.2622199227
363PhosphorylationLLTQALESHAEGFRE
HHHHHHHHHHHHHHH		28.93-
3742-HydroxyisobutyrylationGFRERFEKTFQLKEK
HHHHHHHHHHHCHHC		52.51-
374UbiquitinationGFRERFEKTFQLKEK
HHHHHHHHHHHCHHC		52.51-
3792-HydroxyisobutyrylationFEKTFQLKEKGLSSG
HHHHHHCHHCCCCCH		46.74-
379UbiquitinationFEKTFQLKEKGLSSG
HHHHHHCHHCCCCCH		46.74-
436PhosphorylationFPPVPLFTAVPSRSF
CCCCCCEEECCCCCC		34.13-
576UbiquitinationLPTLLNPKTLPSGLD
CCCCCCCCCCCCCCC		62.712190698
580PhosphorylationLNPKTLPSGLDDYPR
CCCCCCCCCCCCCCC		55.9128634298
585PhosphorylationLPSGLDDYPRASHPS
CCCCCCCCCCCCCCC		8.3528634298
589PhosphorylationLDDYPRASHPSVTER
CCCCCCCCCCCCCHH		36.8930257219
592PhosphorylationYPRASHPSVTERHLD
CCCCCCCCCCHHHHH		35.9328634298
657N-linked_GlycosylationGVFADFGNHTKAVQL
EEEEECCCCCCEEEC		39.387635146
657N-linked_GlycosylationGVFADFGNHTKAVQL
EEEEECCCCCCEEEC		39.387635146
665UbiquitinationHTKAVQLKPRPPQGL
CCCEEECCCCCCCCC		23.14-
705PhosphorylationLLRLLDPTSSRLGPL
HHHHHCCCCCCHHHH		38.71-
706PhosphorylationLRLLDPTSSRLGPLL
HHHHCCCCCCHHHHH		20.88-
707PhosphorylationRLLDPTSSRLGPLLD
HHHCCCCCCHHHHHH		33.72-
719PhosphorylationLLDILADSRHLWSPF
HHHHHHCCCCCCCCC		18.9121712546
724PhosphorylationADSRHLWSPFGLRSL
HCCCCCCCCCHHHHH		19.40-
730PhosphorylationWSPFGLRSLAASSSF
CCCCHHHHHHHCCCC		27.6626437602
734PhosphorylationGLRSLAASSSFYGQR
HHHHHHHCCCCCCCC		22.4028152594
735PhosphorylationLRSLAASSSFYGQRN
HHHHHHCCCCCCCCC		21.5328152594
736PhosphorylationRSLAASSSFYGQRNS
HHHHHCCCCCCCCCC		21.7126437602
738PhosphorylationLAASSSFYGQRNSEH
HHHCCCCCCCCCCCC		17.8128152594
7822-HydroxyisobutyrylationPHQARAAKLHGELRA
HHHHHHHHHHHHHHH		39.78-
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 MOGS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOGS_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 MOGS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCG1_HUMANCHGBphysical
16169070
TECR_HUMANTECRphysical
22939629
NUP62_HUMANNUP62physical
22939629
RAB5A_HUMANRAB5Aphysical
22939629
RAP1B_HUMANRAP1Bphysical
22939629
RS24_HUMANRPS24physical
22939629
RL31_HUMANRPL31physical
22939629
Drug and Disease Associations
Kegg Disease
H00119 Congenital disorders of glycosylation (CDG) type II
OMIM Disease
606056Type IIb congenital disorder of glycosylation (CDGIIb)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOGS_HUMAN

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Related Literatures of Post-Translational Modification

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