CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012100
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein OS-9 
Protein Synonyms/Alias
 Amplified in osteosarcoma 9 
Gene Name
 OS9 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
288PQVWSETKSGVAPQKubiquitination[1]
380KGGTKKGKPNIGQEQubiquitination[1]
564DEDTRNLKEIFFNILubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4. 
Sequence Annotation
 DOMAIN 108 178 PRKCSH.
 BINDING 130 130 Carbohydrate.
 BINDING 182 182 Carbohydrate.
 BINDING 188 188 Carbohydrate.
 BINDING 212 212 Carbohydrate.
 BINDING 218 218 Carbohydrate.
 CARBOHYD 177 177 N-linked (GlcNAc...) (Potential).
 DISULFID 110 123
 DISULFID 181 216
 DISULFID 196 228  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Polymorphism; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 667 AA 
Protein Sequence
MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV 60
VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 120
EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK 180
CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA 240
PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS 300
PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR 360
SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED 420
EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSEVKAGM ERELENIIQE TEKELDPDGL 480
KKESERDRAM LALTSTLNKL IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTGKIEIKI 540
VRPWAEGTEE GARWLTDEDT RNLKEIFFNI LVPGAEEAQK ERQRQKELES NYRRVWGSPG 600
GEGTGDLDEF DF 612 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
 GO:0000836; C:Hrd1p ubiquitin ligase complex; NAS:UniProtKB.
 GO:0001948; F:glycoprotein binding; IDA:UniProtKB.
 GO:0030433; P:ER-associated protein catabolic process; IMP:UniProtKB.
 GO:0006621; P:protein retention in ER lumen; IDA:UniProtKB.
 GO:0006605; P:protein targeting; IEA:Compara.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
 GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB. 
Interpro
 IPR009011; Man6P_isomerase_rcpt-bd_dom.
 IPR012913; PRKCSH. 
Pfam
 PF07915; PRKCSH 
SMART
  
PROSITE
  
PRINTS