CAS_ARATH - dbPTM
CAS_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAS_ARATH
UniProt AC Q9FN48
Protein Name Calcium sensing receptor, chloroplastic
Gene Name CAS
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 387
Subcellular Localization Plastid, chloroplast thylakoid membrane
Single-pass membrane protein
Stromal side .
Protein Description Modulates cytoplasmic Ca(2+) concentration and is crucial for proper stomatal regulation in response to elevated levels of external Ca(2+). May function by regulating concentrations of inositol 1,4,5-trisphosphate (IP3), which in turn triggers release of Ca(2+) from internal stores. May play a role in de-etiolation..
Protein Sequence MAMAEMATKSSLSAKLTLPSSSTKKTLSLRQVSVSLPTSTSISLLSLFASPPHEAKAAVSIPKDQIVSSLTEVEKTINQVQETGSSVFDATQRVFQVVGDALKPALDTALPIAKQAGEEAMKLASPAFSEASKKAQEAMQSSGFDSEPVFNAAKTVTDVAQQTSKAIEDAKPIASSTMDTISSADPSVIVVAAGAAFLAYLLLPPVFSAISFNFRGYKGDLTPAQTLDLLCTKNYLMVDIRSEKDKEKAGIPRLPSNAKNRVISIPLEELPNKVKGIVRNSKRVEAEIAALKISYLKKINKGSNIIILDSYTDSAKIVAKTLKVLGYKNCYIVTDGFSGGRGWLQSRLGTDSYNFSFAQVLSPSRIIPAASRSFGTRSGTKFLPSSD
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 Orthologous
Protein Cluster
76PhosphorylationSLTEVEKTINQVQET
HHHHHHHHHHHHHHH
16.2029797451
264PhosphorylationNAKNRVISIPLEELP
CCCCCEEEEEHHHCC
18.4619880383
350PhosphorylationWLQSRLGTDSYNFSF
HHHHHHCCCCCCEEH
26.7719376835
352PhosphorylationQSRLGTDSYNFSFAQ
HHHHCCCCCCEEHHH
23.0919376835
353PhosphorylationSRLGTDSYNFSFAQV
HHHCCCCCCEEHHHH
24.0419376835
356PhosphorylationGTDSYNFSFAQVLSP
CCCCCCEEHHHHCCH
18.9430291188
362PhosphorylationFSFAQVLSPSRIIPA
EEHHHHCCHHHEEEH
23.2119376835
364PhosphorylationFAQVLSPSRIIPAAS
HHHHCCHHHEEEHHH
32.5119376835
371PhosphorylationSRIIPAASRSFGTRS
HHEEEHHHHCCCCCC
30.4819376835
373PhosphorylationIIPAASRSFGTRSGT
EEEHHHHCCCCCCCC
26.0719376835
376PhosphorylationAASRSFGTRSGTKFL
HHHHCCCCCCCCCCC
21.4619376835
378PhosphorylationSRSFGTRSGTKFLPS
HHCCCCCCCCCCCCC
51.1323111157
380PhosphorylationSFGTRSGTKFLPSSD
CCCCCCCCCCCCCCC
21.6230291188
385PhosphorylationSGTKFLPSSD-----
CCCCCCCCCC-----
49.6527545962
386PhosphorylationGTKFLPSSD------
CCCCCCCCC------
45.4519376835

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 CAS_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 CAS_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAS_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAS_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-373; SER-378 ANDTHR-380, AND IDENTIFICATION BY MASS SPECTROMETRY.
"Light regulation of CaS, a novel phosphoprotein in the thylakoidmembrane of Arabidopsis thaliana.";
Vainonen J.P., Sakuragi Y., Stael S., Tikkanen M., Allahverdiyeva Y.,Paakkarinen V., Aro E., Suorsa M., Scheller H.V., Vener A.V.,Aro E.M.;
FEBS J. 275:1767-1777(2008).
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-380, AND DISRUPTIONPHENOTYPE.

TOP