UniProt ID | ACA2_ARATH | |
---|---|---|
UniProt AC | O81108 | |
Protein Name | Calcium-transporting ATPase 2, plasma membrane-type | |
Gene Name | ACA2 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 1014 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein. |
|
Protein Description | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the endoplasmic reticulum.. | |
Protein Sequence | MESYLNENFDVKAKHSSEEVLEKWRNLCGVVKNPKRRFRFTANLSKRYEAAAMRRTNQEKLRIAVLVSKAAFQFISGVSPSDYTVPEDVKAAGFEICADELGSIVESHDVKKLKFHGGVDGLAGKLKASPTDGLSTEAAQLSQRQELFGINKFAESEMRGFWVFVWEALQDMTLMILGVCAFVSLIVGIATEGWPKGSHDGLGIAASILLVVFVTATSDYRQSLQFRDLDKEKKKITVQVTRNGFRQKLSIYDLLPGDIVHLAIGDQVPADGLFLSGFSVVIDESSLTGESEPVMVNAQNPFLMSGTKVQDGSCKMMITTVGMRTQWGKLMATLTEGGDDETPLQVKLNGVATIIGKIGLFFAVVTFAVLVQGMFMRKLSTGTHWVWSGDEALELLEYFAIAVTIVVVAVPEGLPLAVTLSLAFAMKKMMNDKALVRHLAACETMGSATTICSDKTGTLTTNHMTVVKSCICMNVQDVANKGSSLQSEIPESAVKLLIQSIFNNTGGEVVVNKHGKTELLGTPTETAILELGLSLGGKFQEERKSYKVIKVEPFNSTKKRMGVVIELPEGGRMRAHTKGASEIVLAACDKVVNSSGEVVPLDEESIKYLNVTINEFANEALRTLCLAYMDIEGGFSPDDAIPASGFTCVGIVGIKDPVRPGVKESVELCRRAGITVRMVTGDNINTAKAIARECGILTDDGIAIEGPVFREKNQEELLELIPKIQVMARSSPMDKHTLVKQLRTTFDEVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKESADVIILDDNFSTIVTVAKWGRSVYINIQKFVQFQLTVNVVALVVNFSSACLTGSAPLTAVQLLWVNMIMDTLGALALATEPPNDELMKRLPVGRRGNFITNAMWRNILGQAVYQFIVIWILQAKGKAMFGLDGPDSTLMLNTLIFNCFVFCQVFNEISSREMEEIDVFKGILDNYVFVVVIGATVFFQIIIIEFLGTFASTTPLTITQWIFSIFIGFLGMPIAAGLKTIPV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MESYLNEN -------CCCHHCCC | 35.61 | 22223895 | |
41 | Phosphorylation | PKRRFRFTANLSKRY CCCCEEEEECHHHHH | 15.47 | 25561503 | |
45 | Phosphorylation | FRFTANLSKRYEAAA EEEEECHHHHHHHHH | 18.20 | 10823962 | |
581 | Phosphorylation | RAHTKGASEIVLAAC EEECCCCCHHHHHHC | 36.20 | 19880383 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
45 | S | Phosphorylation | Kinase | CPK1 | Q06850 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACA2_ARATH !! |
* 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 ACA2_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NAC89_ARATH | NAC089 | physical | 21798944 | |
GDU4_ARATH | GDU4 | physical | 22737156 | |
CNG10_ARATH | CNGC10 | physical | 22737156 | |
UPS1_ARATH | UPS1 | physical | 22737156 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A calcium-dependent protein kinase can inhibit a calmodulin-stimulated Ca2+ pump (ACA2) located in the endoplasmic reticulum ofArabidopsis."; Hwang I., Sze H., Harper J.F.; Proc. Natl. Acad. Sci. U.S.A. 97:6224-6229(2000). Cited for: PHOSPHORYLATION AT SER-45 BY CPK1. |