ALA1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ALA1_ARATH
• UniProt AC: P98204
• Protein Name: Phospholipid-transporting ATPase 1 {ECO:0000303|PubMed:11148289}
• Gene Name: ALA1 {ECO:0000303|PubMed:11148289}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1158
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Cell membrane ; Multi-pass membrane protein . Requires the presence of an ALIS protein to exit the endoplasmic reticulum to the cell membrane.
• Protein Description: Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Has activity with phosphatidylserine and with a much lower efficiency with phosphatidylethanolamine, but not with phosphatidylcholine..
• Protein Sequence: MDPRKSIDKPPHHDPILGVSSRWSVSSKDNKEVTFGDLGSKRIRHGSAGADSEMLSMSQKEIKDEDARLIYINDPDRTNERFEFTGNSIKTAKYSVFTFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASIMPLAFVLLVSAIKDAYEDFRRHRSDRVENNRLALVFEDHQFREKKWKHIRVGEVIKVQSNQTLPCDMVLLATSDPTGVVYVQTTNLDGESNLKTRYAKQETLLKAADMESFNGFIKCEKPNRNIYGFQANMEIDGRRLSLGPSNIILRGCELKNTAWALGVVVYAGGETKAMLNNSGAPSKRSRLETRMNLEIILLSLFLIVLCTIAAATAAVWLRTHRDDLDTILFYRRKDYSERPGGKNYKYYGWGWEIFFTFFMAVIVYQIMIPISLYISMELVRIGQAYFMTNDDQMYDESSDSSFQCRALNINEDLGQIKYLFSDKTGTLTDNKMEFQCACIEGVDYSDREPADSEHPGYSIEVDGIILKPKMRVRVDPVLLQLTKTGKATEEAKRANEFFLSLAACNTIVPIVSNTSDPNVKLVDYQGESPDEQALVYAAAAYGFLLIERTSGHIVINVRGETQRFNVLGLHEFDSDRKRMSVILGCPDMSVKLFVKGADSSMFGVMDESYGGVIHETKIQLHAYSSDGLRTLVVGMRELNDSEFEQWHSSFEAASTALIGRAGLLRKVAGNIETNLRIVGATAIEDKLQRGVPEAIESLRIAGIKVWVLTGDKQETAISIGFSSRLLTRNMRQIVINSNSLDSCRRSLEEANASIASNDESDNVALIIDGTSLIYVLDNDLEDVLFQVACKCSAILCCRVAPFQKAGIVALVKNRTSDMTLAIGDGANDVSMIQMADVGVGISGQEGRQAVMASDFAMGQFRFLVPLLLVHGHWNYQRMGYMILYNFYRNAVFVLILFWYVLFTCYTLTTAITEWSSVLYSVIYTAIPTIIIGILDKDLGRQTLLDHPQLYGVGQRAEGYSTTLFWYTMIDTIWQSAAIFFIPMFAYWGSTIDTSSLGDLWTIAAVVVVNLHLAMDVIRWNWITHAAIWGSIVAACICVIVIDVIPTLPGYWAIFQVGKTWMFWFCLLAIVVTSLLPRFAIKFLVEYYRPSDVRIAREAEKLGTFRESQPVGVEMNLIQDPPRR

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
6	Phosphorylation	--MDPRKSIDKPPHH --CCCCCCCCCCCCC	36.98	26811356
20	Phosphorylation	HDPILGVSSRWSVSS CCCCCCCCCCCEECC	16.64	26811356
34	Phosphorylation	SKDNKEVTFGDLGSK CCCCCEEEECCCCCC	24.00	19880383
40	Phosphorylation	VTFGDLGSKRIRHGS EEECCCCCCEECCCC	26.51	30291188
47	Phosphorylation	SKRIRHGSAGADSEM CCEECCCCCCCCHHH	19.87	17317660
52	Phosphorylation	HGSAGADSEMLSMSQ CCCCCCCHHHHCCCH	25.11	17317660
56	Phosphorylation	GADSEMLSMSQKEIK CCCHHHHCCCHHHHC	18.31	25561503
58	Phosphorylation	DSEMLSMSQKEIKDE CHHHHCCCHHHHCCC	34.42	17317660
517	Phosphorylation	DPVLLQLTKTGKATE CHHHHHHHCCCCCCH	17.38	19880383
774	Phosphorylation	QIVINSNSLDSCRRS EHHHCCCCHHHHHHH	33.12	24894044

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

Oops, there are no upstream regulatory protein records of ALA1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ALA1_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 ALA1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of ALA1_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-40, AND MASSSPECTROMETRY.
PubMed: 19376835