dbPTM

CALX_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CALX_RAT
UniProt AC	P35565
Protein Name	Calnexin
Gene Name	Canx
Organism	Rattus norvegicus (Rat).
Sequence Length	591
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I membrane protein . Endoplasmic reticulum . Melanosome . The palmitoylated form preferentially localizes to the perinuclear rough ER.
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. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse..
Protein Sequence	MEGKWLLCLLLVLGTAAIQAHDGHDDDMIDIEDDLDDVIEEVEDSKSKSDTSTPPSPKVTYKAPVPTGEVYFADSFDRGSLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTSELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIADPDAVKPDDWDEDAPSKIPDEEATKPEGWLDDEPEYIPDPDAEKPEDWDEDMDGEWEAPQIANPKCESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIISGDRRVVDDWANDGWGLKKAADGAAEPGVVGQMLEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQSNAMEYKKTDAPQPDVKDEEGKEEEKNKGDEEEEEEKLEEKQKSDAEEDGGTGSQDEEDSKPKAEEDEILNRSPRNRKPRRE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	Phosphorylation	SDTSTPPSPKVTYKA CCCCCCCCCCEEEEC	38.26	22108457
80	Phosphorylation	ADSFDRGSLSGWILS ECCCCCCCCHHHHHH	21.91	27097102
82	Phosphorylation	SFDRGSLSGWILSKA CCCCCCCHHHHHHHH	33.50	22673903
87	Phosphorylation	SLSGWILSKAKKDDT CCHHHHHHHHCCCCC	22.79	22673903
91	Succinylation	WILSKAKKDDTDDEI HHHHHHCCCCCCCHH	66.74	26843850
135	Acetylation	KHHAISAKLNKPFLF HHHHHHHCCCCCCCC	45.89	22902405
138	Acetylation	AISAKLNKPFLFDTK HHHHCCCCCCCCCCC	47.81	-
171	Acetylation	AYVKLLSKTSELNLD HHHHHHHCCCCCCHH	56.91	22902405
172	Phosphorylation	YVKLLSKTSELNLDQ HHHHHHCCCCCCHHH	24.86	22673903
173	Phosphorylation	VKLLSKTSELNLDQF HHHHHCCCCCCHHHC	43.77	22673903
221	Acetylation	VYEEKHAKRPDADLK CCCHHHCCCCCCCHH	65.27	22902405
402	Succinylation	QGIWKPRKIPNPDFF CCCCCCCCCCCCCHH	71.67	26843850
459	Acetylation	ANDGWGLKKAADGAA HHCCCCCHHHHCCCC	36.11	140753
503	S-palmitoylation	VFLVILFCCSGKKQS HHHHHHHHCCCCHHH	1.29	-
504	S-palmitoylation	FLVILFCCSGKKQSN HHHHHHHCCCCHHHC	4.75	-
526	Succinylation	DAPQPDVKDEEGKEE CCCCCCCCCCCCHHH	67.79	26843850
537	Succinylation	GKEEEKNKGDEEEEE CHHHHHCCCCHHHHH	77.97	26843850
546	Succinylation	DEEEEEEKLEEKQKS CHHHHHHHHHHHHHH	65.56	26843850
546	Acetylation	DEEEEEEKLEEKQKS CHHHHHHHHHHHHHH	65.56	22902405
553	Phosphorylation	KLEEKQKSDAEEDGG HHHHHHHHHCCCCCC	39.29	23712012
561	Phosphorylation	DAEEDGGTGSQDEED HCCCCCCCCCCCHHH	38.91	19700791
563	Phosphorylation	EEDGGTGSQDEEDSK CCCCCCCCCCHHHCC	34.01	19700791
569	Phosphorylation	GSQDEEDSKPKAEED CCCCHHHCCCCHHHH	54.88	27097102
582	Phosphorylation	EDEILNRSPRNRKPR HHHHHHCCCCCCCCC	27.43	28825834

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
563	S	Phosphorylation	Kinase	MAPK3	P21708	Uniprot
582	S	Phosphorylation	Kinase	CDK1	P06493	PSP
582	S	Phosphorylation	Kinase	PRKACA	P00517	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
563	S	Phosphorylation		10393181
Phosphorylated at Ser-563 by MAPK3/ERK1.

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HOME3_RAT	Homer3	physical	22486777
PRS8_RAT	Psmc5	physical	22486777
GRM1_RAT	Grm1	physical	22486777

Drug and Disease Associations

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

Regulatory Network of CALX_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 ANDSER-582, AND MASS SPECTROMETRY.	16396499 [Abstract]
"Phosphorylation by CK2 and MAPK enhances calnexin association withribosomes."; Chevet E., Wong H.N., Gerber D., Cochet C., Fazel A., Cameron P.H.,Gushue J.N., Thomas D.Y., Bergeron J.J.; EMBO J. 18:3655-3666(1999). Cited for: PHOSPHORYLATION AT SER-563, AND INTERACTION WITH MAPK3/ERK1.	10393181 [Abstract]

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