dbPTM

CALX_CAEEL - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CALX_CAEEL
UniProt AC	P34652
Protein Name	Calnexin
Gene Name	cnx-1
Organism	Caenorhabditis elegans.
Sequence Length	619
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I membrane protein. Cytoplasm, perinuclear region . Cytoplasmic vesicle . Perinuclear localization in excretory and germ cells. In intestinal cells, clustered signals around vacuoles with vesicles are
Protein Description	Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). Required for embryogenesis and larval development under heat and ER stress conditions. May be important for germ cell development. Involved in neuronal necrotic cell death..
Protein Sequence	MVNRKWMYIFIQFLLVSSIRSDDDVFEDDEEEVTKGSDDKEEFVPSLFVAPKLSDKSTPNFFDYFPVGSKIGLTWIKSLAKKDDVDSDIAKYNGEWSIGAPTKVSIEGDLGLIVKTKARHHAIAAKLNTPFAFDANTFVVQYDIKFEEGQECGGGYLKLLSEGAEKDLANFQDKTAYTIMFGPDKCGATGKVHLIFRYKNPINGTISEYHANQPTTIGSTYWDDHNTHLFTLVVKPTGEYSVSVDGKSLYYGNMMSDVTPALTPPKQIFDETDLKPVDWDERENIEDESAVKPDDWDENEPQSVVDEAATKPYDWNEEENELIADPEAKKPQDWDEDMDGSWEAPLIDNPACKGLSGCGTWKAPTIKNPKYKGKWIRPKISNPAFKGKWTARLIDNPNYFEPKPFAGLAPITAVGIEMWTMSENILFDNILITSSEEDSSDVAKQTFYVKQKEEYRLAAATGNGNGFFQQIIDATNEKPWLWAVYILCVLLPLVAIGVFCFGKQSKPTPNFAKKSDAYSADDDRVPNLVDDDEEEIIGDEEDDVNQPGPSGSQSNPEPQDEEENAEQQSANSSQSSAAEEEDDEHVVPENEPVKPTEEFAKKSPKNTGGAKRRTARRGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
203	N-linked_Glycosylation	FRYKNPINGTISEYH EEECCCCCCCCEEEC	42.69	16256074
571	N-linked_Glycosylation	NAEQQSANSSQSSAA HHHHHHHHHHHCCCC	47.65	16256074

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of CALX_CAEEL !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CALX_CAEEL !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CALX_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CALX_CAEEL !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CALX_CAEEL

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Caenorhabditis elegans calnexin is N-glycosylated and required forstress response."; Lee W., Lee T.H., Park B.J., Chang J.W., Yu J.R., Koo H.S., Park H.,Yoo Y.J., Ahnn J.; Biochem. Biophys. Res. Commun. 338:1018-1030(2005). Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUESPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE,GLYCOSYLATION AT ASN-203 AND ASN-571, AND MUTAGENESIS OF ASN-203 ANDASN-571.	16256074 [Abstract]