CALX1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CALX1_ARATH
• UniProt AC: P29402
• Protein Name: Calnexin homolog 1
• Gene Name: CNX1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 530
• Subcellular Localization: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
• 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)..
• Protein Sequence: MRQRQLFSVFLLLLAFVSFQKLCYCDDQTVLYESFDEPFDGRWIVSKNSDYEGVWKHAKSEGHEDYGLLVSEKARKYGIVKELDEPLNLKEGTVVLQYEVRFQEGLECGGAYLKYLRPQEAGWTPQGFDSESPYSIMFGPDKCGGTNKVHFILKHKNPKSGEYVEHHLKFPPSVPYDKLSHVYTAILKPDNEVRILVDGEEKKKANLLSGEDFEPALIPAKTIPDPEDKKPEDWDERAKIPDPNAVKPEDWDEDAPMEIEDEEAEKPEGWLDDEPEEVDDPEATKPEDWDDEEDGMWEAPKIDNPKCEAAPGCGEWKRPMKRNPAYKGKWSSPLIDNPAYKGIWKPRDIPNPDYFELDRPDYEPIAAIGIEIWTMQDGILFDNILIAKDEKVAETYRQTTWKPKFDVEKEKQKAEEEAAGSADGLKSYQKVVFDLLNKVADLSFLSAYKSKITELIEKAEQQPNLTIGVLVAIVVVFFSLFLKLIFGGKKAAAPVEKKKPEVAESSKSGDEAEKKEETAAPRKRQPRRDN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
108	S-nitrosylation	RFQEGLECGGAYLKY ECCCCCEECCEEEEE	7.98	22115780
464	N-linked_Glycosylation	EKAEQQPNLTIGVLV HHHHHCCCCHHHHHH	45.54	-
505	Phosphorylation	KKPEVAESSKSGDEA CCHHHHHHCCCCCHH	33.07	23776212
506	Phosphorylation	KPEVAESSKSGDEAE CHHHHHHCCCCCHHH	23.50	23776212
508	Phosphorylation	EVAESSKSGDEAEKK HHHHHCCCCCHHHHH	54.12	30291188
518	Phosphorylation	EAEKKEETAAPRKRQ HHHHHHHCCCCCCCC	29.25	19376835

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

Oops, there are no upstream regulatory protein records of CALX1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CALX1_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CALX1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of CALX1_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASSSPECTROMETRY.
PubMed: 19376835