CPLM-012099

Genbank Nucleotide ID

Protein Synonyms/Alias

Amplified in osteosarcoma 9

Homo sapiens (Human)

Position	Peptide	Type	References
66	DVVIVSSKYKQRYEC	ubiquitination	[1]
113	RDAPCLLKTKDWWTY	ubiquitination	[1]
115	APCLLKTKDWWTYEF	ubiquitination	[2]
180	QTYGNGSKCDLNGRP	ubiquitination	[2, 3]
271	DSKQYGDKIIEELQD	ubiquitination	[1]
288	PQVWSETKSGVAPQK	ubiquitination	[1, 3, 4]
303	MAGASPTKDDSKDSD	ubiquitination	[2]
307	SPTKDDSKDSDFWKM	ubiquitination	[2]
377	EELKGGTKKGKPNIG	ubiquitination	[2]
380	KGGTKKGKPNIGQEQ	ubiquitination	[1]
457	DRLRSEVKAGMEREL	ubiquitination	[1]
481	ELDPDGLKKESERDR	ubiquitination	[1]
507	LIKRLEEKQSPELVK	ubiquitination	[1]
563	DLTVLEMKRENPQLK	ubiquitination	[2]
594	AAGKIEIKIVRPWAE	ubiquitination	[2]
619	DEDTRNLKEIFFNIL	ubiquitination	[1, 5]
641	QKERQRQKELESNYR	ubiquitination	[1, 2]

[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]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] 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]
[5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]

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.

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

3D-structure; Alternative splicing; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Polymorphism; Reference proteome; Signal.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

IPR009011; Man6P_isomerase_rcpt-bd_dom.
IPR012913; PRKCSH.