dbPTM

ACA10_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACA10_ARATH
UniProt AC	Q9SZR1
Protein Name	Calcium-transporting ATPase 10, plasma membrane-type
Gene Name	ACA10
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1069
Subcellular Localization	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	MSGQFNNSPRGEDKDVEAGTSSFTEYEDSPFDIASTKNAPVERLRRWRQAALVLNASRRFRYTLDLKREEDKKQMLRKMRAHAQAIRAAHLFKAAASRVTGIASPLPTPGGGDFGIGQEQIVSISRDQNIGALQELGGVRGLSDLLKTNLEKGIHGDDDDILKRKSAFGSNTYPQKKGRSFWRFVWEASQDLTLIILIVAAVASLALGIKTEGIEKGWYDGISIAFAVLLVIVVTATSDYRQSLQFQNLNEEKRNIRLEVTRDGRRVEISIYDIVVGDVIPLNIGDQVPADGVLVAGHSLAVDESSMTGESKIVQKNSTKHPFLMSGCKVADGNGTMLVTGVGVNTEWGLLMASVSEDNGGETPLQVRLNGVATFIGIVGLTVAGVVLFVLVVRYFTGHTKNEQGGPQFIGGKTKFEHVLDDLVEIFTVAVTIVVVAVPEGLPLAVTLTLAYSMRKMMADKALVRRLSACETMGSATTICSDKTGTLTLNEMTVVECYAGLQKMDSPDSSSKLPSAFTSILVEGIAHNTTGSVFRSESGEIQVSGSPTERAILNWAIKLGMDFDALKSESSAVQFFPFNSEKKRGGVAVKSPDSSVHIHWKGAAEIVLGSCTHYMDESESFVDMSEDKMGGLKDAIDDMAARSLRCVAIAFRTFEADKIPTDEEQLSRWELPEDDLILLAIVGIKDPCRPGVKNSVLLCQQAGVKVRMVTGDNIQTAKAIALECGILASDSDASEPNLIEGKVFRSYSEEERDRICEEISVMGRSSPNDKLLLVQSLKRRGHVVAVTGDGTNDAPALHEADIGLAMGIQGTEVAKEKSDIIILDDNFESVVKVVRWGRSVYANIQKFIQFQLTVNVAALVINVVAAISAGEVPLTAVQLLWVNLIMDTLGALALATEPPTDHLMDRAPVGRREPLITNIMWRNLFIQAMYQVTVLLILNFRGISILHLKSKPNAERVKNTVIFNAFVICQVFNEFNARKPDEINIFRGVLRNHLFVGIISITIVLQVVIVEFLGTFASTTKLDWEMWLVCIGIGSISWPLAVIGKLIPVPETPVSQYFRINRWRRNSSG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGQFNNSP ------CCCCCCCCC	53.24	22223895
2	Phosphorylation	------MSGQFNNSP ------CCCCCCCCC	53.24	25561503
8	Phosphorylation	MSGQFNNSPRGEDKD CCCCCCCCCCCCCCC	19.65	27532006
20	Phosphorylation	DKDVEAGTSSFTEYE CCCCCCCCCCCCCCC	28.39	15308754
21	Phosphorylation	KDVEAGTSSFTEYED CCCCCCCCCCCCCCC	23.65	15308754
22	Phosphorylation	DVEAGTSSFTEYEDS CCCCCCCCCCCCCCC	35.71	30407730
24	Phosphorylation	EAGTSSFTEYEDSPF CCCCCCCCCCCCCCC	39.34	15308754
26	Phosphorylation	GTSSFTEYEDSPFDI CCCCCCCCCCCCCCC	23.21	30407730
29	Phosphorylation	SFTEYEDSPFDIAST CCCCCCCCCCCCCCC	18.61	19376835
35	Phosphorylation	DSPFDIASTKNAPVE CCCCCCCCCCCCCHH	40.00	30407730
36	Phosphorylation	SPFDIASTKNAPVER CCCCCCCCCCCCHHH	21.21	30407730
57	Phosphorylation	AALVLNASRRFRYTL HHHHHHHHHHHHHCC	23.94	23111157
62	Phosphorylation	NASRRFRYTLDLKRE HHHHHHHHCCCCCCH	14.67	25561503
63	Phosphorylation	ASRRFRYTLDLKREE HHHHHHHCCCCCCHH	15.00	25561503
100	Phosphorylation	KAAASRVTGIASPLP HHHHHHCCCEECCCC	23.04	26811356
104	Phosphorylation	SRVTGIASPLPTPGG HHCCCEECCCCCCCC	25.67	19880383
538	Phosphorylation	GSVFRSESGEIQVSG CCEEECCCCCEEECC	42.86	24243849
776	Phosphorylation	DKLLLVQSLKRRGHV CCEEHHHHHHHCCCE	28.51	19880383

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 ACA10_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACA10_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 ACA10_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ACA10_ARATH !!

Drug and Disease Associations

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

Regulatory Network of ACA10_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND MASSSPECTROMETRY.	17317660 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND MASSSPECTROMETRY.	14506206 [Abstract]