| Tag | Content |
|---|
| CPLM ID | CPLM-017233 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein OS-9 |
Protein Synonyms/Alias | |
Gene Name | Os9 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 113 | RDAPCLLKTKDWWTY | ubiquitination | [1] | | 462 | ERLRSEVKAGMEREL | ubiquitination | [1] | | 478 | NIIQETEKELDPEGL | ubiquitination | [1] | | 520 | QSPELVQKYKKRRVV | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 (By similarity). |
Sequence Annotation | DOMAIN 108 178 PRKCSH.
BINDING 130 130 Carbohydrate (By similarity).
BINDING 182 182 Carbohydrate (By similarity).
BINDING 188 188 Carbohydrate (By similarity).
BINDING 212 212 Carbohydrate (By similarity).
BINDING 218 218 Carbohydrate (By similarity).
CARBOHYD 177 177 N-linked (GlcNAc...) (Potential).
DISULFID 110 123 By similarity.
DISULFID 181 216 By similarity.
DISULFID 196 228 By similarity. |
Keyword | Alternative splicing; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Reference proteome; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 672 AA |
Protein Sequence | MAAEVLLSSL LGLLFLGLLL PARLTGGVGS LNLEELSEMR YGIQILPLPV MGGQSQASDV 60
VVVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY 120
EFCYGRHIQQ YHMEDSEIKG DVLYLGHYQS SFNWDDETAK ASKQHRLKRY HSQTYGNGSK 180
CDLNGKPREA EVRFLCDEGA GISGDYIDRV DEPVSCSYVL TIRTSRLCPH PLLRPPASAA 240
PQAILCHPAL QPDEYMAYLQ RQAESKQHEE KTTEEVQDTD RQVWSGSKAA GAPPKKEDVS 300
PAKEEKESEL WKLQGPEEQA AAREEAQAGE QDLNHEAAAD PAPSPPNDFQ NNVQVKLIRS 360
PADLIRLIEE LKAAEKGKPS VRREQPGDDT TEAPQREAEG TKAKGKDGEP PGLMEEEDGD 420
DEEEEEEEEE DEEEQQLLGE FEKELEGMLL PSNRERLRSE VKAGMERELE NIIQETEKEL 480
DPEGLRKESE REQAILALTS TLDKLIKRLQ ENQSPELVQK YKKRRVVPQK PPPSPHPTEE 540
EPEHRVRVRV TKLRPGGPNR DLTVLEMNRE NPQLKQIEGL VTEVLEREGL TAEGKIEIKI 600
VRPGAEGKEE DTRWLTDEDT RNLKEIFFNI LVQGAEEANK ERQRQSELES NYRRVWGSPG 660
GEDTGDLDEF DF 672 |
Gene Ontology | GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB. GO:0001948; F:glycoprotein binding; ISS:UniProtKB. GO:0030433; P:ER-associated protein catabolic process; ISS:UniProtKB. GO:0006621; P:protein retention in ER lumen; ISS:UniProtKB. GO:0006605; P:protein targeting; IEA:Compara. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB. GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |