CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020232
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ER degradation-enhancing alpha-mannosidase-like protein 2 
Protein Synonyms/Alias
  
Gene Name
 EDEM2 
Gene Synonyms/Alias
 C20orf31; C20orf49; UNQ573/PRO1135 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
402DAVESIEKISKVECGubiquitination[1]
405ESIEKISKVECGFATubiquitination[2]
492LHCCQRLKEEQWEVEubiquitination[1, 2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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
 Involved in endoplasmic reticulum-associated degradation (ERAD) that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner. It lacks mannosidase activity. Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. 
Sequence Annotation
 CARBOHYD 90 90 N-linked (GlcNAc...) (Potential).
 CARBOHYD 112 112 N-linked (GlcNAc...) (Potential).
 CARBOHYD 289 289 N-linked (GlcNAc...) (Potential).
 CARBOHYD 450 450 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Endoplasmic reticulum; Glycoprotein; Polymorphism; Reference proteome; Secreted; Signal; Unfolded protein response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 578 AA 
Protein Sequence
MPFRLLIPLG LLCALLPQHH GAPGPDGSAP DPAHYRERVK AMFYHAYDSY LENAFPFDEL 60
RPLTCDGHDT WGSFSLTLID ALDTLLILGN VSEFQRVVEV LQDSVDFDID VNASVFETNI 120
RVVGGLLSAH LLSKKAGVEV EAGWPCSGPL LRMAEEAARK LLPAFQTPTG MPYGTVNLLH 180
GVNPGETPVT CTAGIGTFIV EFATLSSLTG DPVFEDVARV ALMRLWESRS DIGLVGNHID 240
VLTGKWVAQD AGIGAGVDSY FEYLVKGAIL LQDKKLMAMF LEYNKAIRNY TRFDDWYLWV 300
QMYKGTVSMP VFQSLEAYWP GLQSLIGDID NAMRTFLNYY TVWKQFGGLP EFYNIPQGYT 360
VEKREGYPLR PELIESAMYL YRATGDPTLL ELGRDAVESI EKISKVECGF ATIKDLRDHK 420
LDNRMESFFL AETVKYLYLL FDPTNFIHNN GSTFDAVITP YGECILGAGG YIFNTEAHPI 480
DPAALHCCQR LKEEQWEVED LMREFYSLKR SRSKFQKNTV SSGPWEPPAR PGTLFSPENH 540
DQARERKPAK QKVPLLSCPS QPFTSKLALL GQVFLDSS 578 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 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.
 GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW. 
Interpro
 IPR001382; Glyco_hydro_47. 
Pfam
 PF01532; Glyco_hydro_47 
SMART
  
PROSITE
  
PRINTS
 PR00747; GLYHDRLASE47.