| Tag | Content |
|---|
| 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 |
|---|
| 288 | PQVWSETKSGVAPQK | ubiquitination | [1] | | 380 | KGGTKKGKPNIGQEQ | ubiquitination | [1] | | 564 | DEDTRNLKEIFFNIL | ubiquitination | [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. |
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PRINTS | |