| Tag | Content |
|---|
| CPLM ID | CPLM-018772 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ER degradation-enhancing alpha-mannosidase-like protein 1 |
Protein Synonyms/Alias | |
Gene Name | EDEM1 |
Gene Synonyms/Alias | EDEM; KIAA0212 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 116 | RGPDEYEKRYSGAFP | ubiquitination | [1] | | 279 | LPAFENTKTGIPYPR | ubiquitination | [1] | | 334 | WVARRAVKALWNLRS | ubiquitination | [1] | | 528 | LEKYTKVKCGYATLH | ubiquitination | [1] | | 570 | DEDNPVHKSGTRYMF | ubiquitination | [1] | | 596 | HLRELPWKEFFSEEG | ubiquitination | [1] | | 643 | RRYSLPLKSIYMRQI | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional 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 lacks mannosidase activity. |
Sequence Annotation | CARBOHYD 181 181 N-linked (GlcNAc...) (Potential).
CARBOHYD 198 198 N-linked (GlcNAc...) (Potential).
CARBOHYD 299 299 N-linked (GlcNAc...) (Potential).
CARBOHYD 342 342 N-linked (GlcNAc...) (Potential).
CARBOHYD 624 624 N-linked (GlcNAc...) (Potential). |
Keyword | Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; Unfolded protein response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 657 AA |
Protein Sequence | MQWRALVLGL VLLRLGLHGV LWLVFGLGPS MGFYQRFPLS FGFQRLRSPD GPASPTSGPV 60
GRPGGVSGPS WLQPPGTGAA QSPRKAPRRP GPGMCGPANW GYVLGGRGRG PDEYEKRYSG 120
AFPPQLRAQM RDLARGMFVF GYDNYMAHAF PQDELNPIHC RGRGPDRGDP SNLNINDVLG 180
NYSLTLVDAL DTLAIMGNSS EFQKAVKLVI NTVSFDKDST VQVFEATIRV LGSLLSAHRI 240
ITDSKQPFGD MTIKDYDNEL LYMAHDLAVR LLPAFENTKT GIPYPRVNLK TGVPPDTNNE 300
TCTAGAGSLL VEFGILSRLL GDSTFEWVAR RAVKALWNLR SNDTGLLGNV VNIQTGHWVG 360
KQSGLGAGLD SFYEYLLKSY ILFGEKEDLE MFNAAYQSIQ NYLRRGREAC NEGEGDPPLY 420
VNVNMFSGQL MNTWIDSLQA FFPGLQVLIG DVEDAICLHA FYYAIWKRYG ALPERYNWQL 480
QAPDVLFYPL RPELVESTYL LYQATKNPFY LHVGMDILQS LEKYTKVKCG YATLHHVIDK 540
STEDRMESFF LSETCKYLYL LFDEDNPVHK SGTRYMFTTE GHIVSVDEHL RELPWKEFFS 600
EEGGQDQGGK SVHRPKPHEL KVINSSSNCN RVPDERRYSL PLKSIYMRQI DQMVGLI 657 |
Gene Ontology | GO:0030176; C:integral to endoplasmic reticulum membrane; ISS:UniProtKB. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0051787; F:misfolded protein binding; IDA:UniProtKB. GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome. GO:0030433; P:ER-associated protein catabolic process; ISS:UniProtKB. GO:0043687; P:post-translational protein modification; TAS:Reactome. GO:0006457; P:protein folding; TAS:Reactome. GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |