EDEM1_MOUSE - dbPTM
EDEM1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDEM1_MOUSE
UniProt AC Q925U4
Protein Name ER degradation-enhancing alpha-mannosidase-like protein 1
Gene Name Edem1
Organism Mus musculus (Mouse).
Sequence Length 652
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2..
Protein Sequence MQWRALVLGLVLLRLGLHAVLWLVFGLGPSMGFYQRFPLSFGFQRLRDPDGSGPVGPPGGPAWLHRPRRGTEGRLETPPEPGPTPGPGVCGPAHWGYALGGGGCGPDEYERRYSGAFPPQLRAQMRDLARGMFVFGYDNYMAHAFPQDELNPIYCRGRGPDRGDPSNLNINDVLGNYSLTLVDALDTLAIMGNSSEFQKAVKLVINTVSFDKDSTVQVFEATIRVLGSLLSAHRIITDSKQPFGDMTIEDYDNELLYMAHDLAVRLLPAFENTKTGIPYPRVNLKTGVPPDSNNETCTAGAGSLLVEFGILSRLLGDSTFEWVARRAVKALWNLRSNDTGLLGNVVNIQTGHWVGKQSGLGAGLDSFYEYLLKSYILFGEKEDLEMFNAAYQSIQSYLRRGREACNEGEGDPPLYVNVNMFSGQLMNTWIDSLQAFFPGLQVLIGDVEDAICLHAFYYAIWKRYGALPERYNWQLQAPDVLFYPLRPELVESTYLLYQATKNPFYLHVGMDILQSLEKYTKVKCGYATLHHVIDKSKEDRMESFFLSETCKYLYLLFDEENPVHKSGTRYMFTTEGHIISVDKRLRELPWKEFFSEDGERDQEEKFVHRPKSQELRVINSSSNCNRVPDERRYSLPLKSIYMRQIDQMVGLI
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
84UbiquitinationTPPEPGPTPGPGVCG
CCCCCCCCCCCCCCC
46.9527667366
176N-linked_GlycosylationNINDVLGNYSLTLVD
CHHHHCCCCCEEHHH
21.04-
193N-linked_GlycosylationDTLAIMGNSSEFQKA
HHHHHCCCCHHHHHH
25.61-
274UbiquitinationLPAFENTKTGIPYPR
HHHHCCCCCCCCCCC
57.2327667366
294N-linked_GlycosylationGVPPDSNNETCTAGA
CCCCCCCCCCCCCCH
50.32-
337N-linked_GlycosylationALWNLRSNDTGLLGN
HHHHCCCCCCCCCCC
44.42-
505PhosphorylationQATKNPFYLHVGMDI
HHHCCCCEEECCHHH
9.3528059163
520PhosphorylationLQSLEKYTKVKCGYA
HHHHHHHHCCCCCEE
40.1928059163
634PhosphorylationVPDERRYSLPLKSIY
CCCCCCCCCCHHHHH
23.0027600695
638UbiquitinationRRYSLPLKSIYMRQI
CCCCCCHHHHHHHHH
32.63-

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 EDEM1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDEM1_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 EDEM1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SE1L1_HUMANSEL1Lphysical
22905195

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDEM1_MOUSE

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Related Literatures of Post-Translational Modification

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