CASP_ARATH - dbPTM
CASP_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASP_ARATH
UniProt AC Q9LS42
Protein Name Protein CASP
Gene Name CASP
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 689
Subcellular Localization Golgi apparatus membrane
Single-pass type IV membrane protein .
Protein Description May be involved in intra-Golgi transport..
Protein Sequence MEVSQDGSERDKTPPPSSSSSSSSPIPVVTNFWKEFDLEKEKSLLDEQGLRIAENQENSQKNRRKLAESTRDFKKASPENKLSMFNSLLKGYQEEVDNITKRAKFGENAFLNIYQKLYEAPDPFPALASIAEQDRKLSEVESENRKMKVELEEFRTEATHLKNQQATIRRLEERNRQLEQQMEEKIKEVVEIKQRNLAEENQKTMELLKDREQALQDQLRQAKDSVSTMQKLHELAQNQLFELRAQSDEETAGKQSEVSLLMDEVERAQTRLLTLEREKGHLRSQLQTANEDTDNKKSDNIDSNSMLENSLTAKEKIISELNMEIHNVETALANERESHVAEIKKLNSLLNKKDTIIEEMKKELQERPSAKLVDDLRKKVKILQAVGYNSIEAEDWDAATTGEEMSKMESLLLDKNRKMEHEVTQLKVQLSEKASLLEKAEAKGEELTAKVNEQQRLIQKLEDDILKGYGSKERKGALFDEWEFSEAGVAEQSEPMDQKHVPSEQDQSSMLKVICSQRDRFRARLRETEEEIRRLKEKIGFLTDELEKTKADNVKLYGKIRYVQDYNHDKVVSRGSKKYVEDLESGFSSDVESKYKKIYEDDINPFAAFSKKEREQRIKDLGIRDRITLSSGRFLLGNKYARTFAFFYTIGLHVLVFTCLYRMSAYSYLSHGAEETLMTEATTNLPHGL
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
1Acetylation-------MEVSQDGS
-------CCCCCCCC
11.7922223895
247PhosphorylationLFELRAQSDEETAGK
HHHHHHCCCHHHCCH
46.1025561503
579PhosphorylationVSRGSKKYVEDLESG
EECCCHHHHHHHHHC
16.8919376835
585PhosphorylationKYVEDLESGFSSDVE
HHHHHHHHCCCCHHH
53.0523776212
588PhosphorylationEDLESGFSSDVESKY
HHHHHCCCCHHHHHH
29.2023776212
589PhosphorylationDLESGFSSDVESKYK
HHHHCCCCHHHHHHH
43.3330291188
593PhosphorylationGFSSDVESKYKKIYE
CCCCHHHHHHHHHHH
40.9323776212

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 CASP_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASP_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 CASP_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STP1_ARATHSTP1physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
PPA3_ARATHPAP3physical
24833385
RAA5A_ARATHRABA5aphysical
24833385
WAK3_ARATHWAK3physical
24833385
BETL2_ARATHAT1G29060physical
24833385

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

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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-589, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589, AND MASSSPECTROMETRY.

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