| UniProt ID | ALA2_ARATH | |
|---|---|---|
| UniProt AC | P98205 | |
| Protein Name | Phospholipid-transporting ATPase 2 {ECO:0000303|PubMed:11402198} | |
| Gene Name | ALA2 {ECO:0000303|PubMed:11402198} | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 1107 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Prevacuolar compartment membrane Multi-pass membrane protein . Requires the presence of an ALIS protein to exit the endoplasmic reticulum to the prevacuolar compartment. |
|
| Protein Description | Involved in transport of phospholipids. Contributes to transmembrane flipping of lipids. Requires an interaction with a protein of the ALIS family for activity. Specific for phosphatidylserine and has no activity with lysolipid, phosphatidylcholine or phosphatidylethanolamine.. | |
| Protein Sequence | MKRFVYINDDEASKELCCDNRISNRKYTLWNFLPKNLWEQFSRFMNQYFLLIACLQLWSLITPVNPASTWGPLIFIFAVSASKEAWDDYHRYLSDKKANEKEVWIVKQGIKKHIQAQDIQVGNIVWLRENDEVPCDLVLLGTSDPQGVCYVETAALDGETDLKTRVIPSACVGIDLELLHKMKGVIECPVPDKDIRRFDANMRLFPPFIDNDVCSLTIKNTLLQSCYLRNTEWACGVSVYTGNQTKLGMSRGIAEPKLTAMDAMIDKLTGAIFVFQIVVVLVLGIAGNVWKDTEARKQWYVQYPEEAPWYELLVIPLRFELLCSIMIPISIKVSLDLVKGLYAKFIEWDVEMIDQETGTASYAANTAISEDLGQVEYILTDKTGTLTDNKMIFRRCCIGGIFYGNENGDALKDAQLLNAITSGSTDVIRFLTVMAICNTVLPVQSKAGDIVYKAQSQDEDALVIAASKLHMVFVGKNANLLEIRFNGSVIRYEVLEILEFTSDRKRMSVVVKDCQNGKIILLSKGADEAILPYARAGQQTRTIGDAVEHYSQLGLRTLCLAWRELEENEYLEWSVKFKEASSLLVDREWRIAEVCQRLEHDLYILGVTAIEDRLQDGVPETIETLRKAGINFWMLTGDKQNTAIQIALSCNFISPEPKGQLLMIDGKTEEDVSRSLERVLLTMRITASEPKDVAFVIDGWALEIALKHHRKDFVELAILSRTAICCRVTPSQKAQLVEILKSCDYRTLAIGDGGNDVRMIQQADIGVGISGREGLQAARAADYSIGRFRFLKRLILVHGRYSYNRTAFLSQYSFYKSLLICFIQIFFSFISGVSGTSLFNSVSLMAYNVFYTSVPVLVSVIDKDLSEASVMQHPQILFYCQAGRLLNPSTFAGWFGRSLFHAIIVFVITIHAYAYEKSEMEELGMVALSGCIWLQAFVVAQETNSFTVLQHLSIWGNLVGFYAINFLFSAIPSSGMYTIMFRLCSQPSYWITMFLIVGAGMGPIFALKYFRYTYRPSKINILQQAERMGGPILTLGNIETQPRTIEKDLSPISITQPKNRSPVYEPLLSDSPNATRRSFGPGTPFEFFQSQSRLSSSSGYTRNCKDN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 28 | Phosphorylation | RISNRKYTLWNFLPK CCCCCCCCHHHCCCH | 28.47 | 19880383 | |
| 259 | Phosphorylation | GIAEPKLTAMDAMID CCCCCCHHHHHHHHH | 26.51 | 24894044 | |
| 608 | Phosphorylation | DLYILGVTAIEDRLQ CEEEEEEEHHHHHHH | 21.81 | 26811356 | |
| 624 | Phosphorylation | GVPETIETLRKAGIN CCCHHHHHHHHHCCC | 28.19 | 26811356 | |
| 1050 | Phosphorylation | RTIEKDLSPISITQP CCCCCCCCCCCCCCC | 30.26 | 19245862 | |
| 1061 | Phosphorylation | ITQPKNRSPVYEPLL CCCCCCCCCCCCCHH | 28.28 | 19376835 | |
| 1064 | Phosphorylation | PKNRSPVYEPLLSDS CCCCCCCCCCHHCCC | 18.40 | 19376835 | |
| 1069 | Phosphorylation | PVYEPLLSDSPNATR CCCCCHHCCCCCCCC | 43.66 | 19376835 | |
| 1071 | Phosphorylation | YEPLLSDSPNATRRS CCCHHCCCCCCCCCC | 19.37 | 30291188 | |
| 1075 | Phosphorylation | LSDSPNATRRSFGPG HCCCCCCCCCCCCCC | 33.00 | 19376835 | |
| 1078 | Phosphorylation | SPNATRRSFGPGTPF CCCCCCCCCCCCCCH | 31.12 | 19880383 | |
| 1083 | Phosphorylation | RRSFGPGTPFEFFQS CCCCCCCCCHHHHHC | 28.12 | 30407730 | |
| 1090 | Phosphorylation | TPFEFFQSQSRLSSS CCHHHHHCCHHHCCC | 25.60 | 30407730 | |
| 1092 | Phosphorylation | FEFFQSQSRLSSSSG HHHHHCCHHHCCCCC | 40.20 | 30407730 | |
| 1095 | Phosphorylation | FQSQSRLSSSSGYTR HHCCHHHCCCCCCCC | 27.36 | 25561503 | |
| 1096 | Phosphorylation | QSQSRLSSSSGYTRN HCCHHHCCCCCCCCC | 32.87 | 25561503 | |
| 1097 | Phosphorylation | SQSRLSSSSGYTRNC CCHHHCCCCCCCCCC | 25.14 | 29654922 |
| 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 ALA2_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ALA2_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 ALA2_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ALA2_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-1050, AND MASSSPECTROMETRY. | |