UniProt ID | PDI2_CAEEL | |
---|---|---|
UniProt AC | Q17770 | |
Protein Name | Protein disulfide-isomerase 2 | |
Gene Name | pdi-2 | |
Organism | Caenorhabditis elegans. | |
Sequence Length | 493 | |
Subcellular Localization | Endoplasmic reticulum lumen. | |
Protein Description | Involved in cuticle formation. [PubMed: 10805750 May play a role in the unfolded protein response] | |
Protein Sequence | MFRLVGLFFLVLGASAAVIEEEENVIVLTKDNFDEVINGNEFILVEFYAPWCGHCKSLAPEYAKAATQLKEEGSDIKLGKLDATVHGEVSSKFEVRGYPTLKLFRNGKPQEYNGGRDHDSIIAWLKKKTGPVAKPLADADAVKELQESADVVVIGYFKDTTSDDAKTFLEVAAGIDDVPFGISTEDAVKSEIELKGEGIVLFKKFDDGRVAFDEKLTQDGLKTWIQANRLALVSEFTQETASVIFGGEIKSHNLLFVSKESSEFAKLEQEFKNAAKQFKGKVLFVYINTDVEENARIMEFFGLKKDELPAIRLISLEEDMTKFKPDFEEITTENISKFTQNYLDGSVKPHLMSEDIPEDWDKNPVKILVGKNFEQVARDNTKNVLVEFYAPWCGHCKQLAPTWDKLGEKFADDESIVIAKMDSTLNEVEDVKIQSFPTIKFFPAGSNKVVDYTGDRTIEGFTKFLETNGKEGAGASEEEKAEEEADEEGHTEL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of PDI2_CAEEL !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDI2_CAEEL !! |
* 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 PDI2_CAEEL !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PDI2_CAEEL !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins."; Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.; Mol. Cell. Proteomics 6:2100-2109(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-334, AND MASSSPECTROMETRY. |