UniProt ID | ALA10_ARATH | |
---|---|---|
UniProt AC | Q9LI83 | |
Protein Name | Phospholipid-transporting ATPase 10 {ECO:0000303|PubMed:11402198} | |
Gene Name | ALA10 {ECO:0000303|PubMed:11402198} | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 1202 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
Protein Description | Involved in transport of phospholipids.. | |
Protein Sequence | MAGPSRRRRRLHLSKIYSYTCGKSSFQEDHSNIGGPGFSRVVYCNEPGSPAAERRNYAGNYVRSTKYTVASFFPKSLFEQFRRVANFYFLVTGILSLTDLSPYGAVSALLPLALVISATMVKEGIEDWRRKQQDIEVNNRKVKVHDGNGIFRQEEWRNLRVGDIVRVEKDEFFPADLLLLSSSYEDSVCYVETMNLDGETNLKVKQGLEATSSLLNQDSDFKDFRGVVRCEDPNVNLYVFVGTLALEEERFPLSIQQILLRDSKLRNTEYVYGAVVFTGHDTKVIQNSTDPPSKRSRIERTMDKIIYLMFGLVFLMSFVGSIIFGVETREDKVKNGRTERWYLKPDDADIFFDPERAPMAAIYHFFTATMLYSYFIPISLYVSIEIVKVLQSIFINRDIHMYYEETDKPAQARTSNLNEELGMVDTILSDKTGTLTCNSMEFIKCSIAGKAYGRGITEVERAMAVRSGGSPLVNEDLDVVVDQSGPKVKGFNFEDERVMNGNWVRQPEAAVLQKFFRLLAVCHTAIPETDEESGNVSYEAESPDEAAFVVAAREFGFEFFNRTQNGISFRELDLVSGEKVERVYRLLNVLEFNSTRKRMSVIVRDDDGKLLLLSKGADNVMFERLAKNGRQFEAKTQEHVNQYADAGLRTLVLAYREVDENEYIEFNKSFNEAKASVSEDREALIDEITDKMERDLILLGATAVEDKLQNGVPECIDKLAQAGIKIWVLTGDKMETAINIGFASSLLRQEMKQIIINLETPQIKSLEKSGGKDEIELASRESVVMQLQEGKALLAASGASSEAFALIIDGKSLTYALEDEIKKMFLDLATSCASVICCRSSPKQKALVTRLVKSGTGKTTLAIGDGANDVGMLQEADIGVGISGVEGMQAVMSSDIAIAQFRYLERLLLVHGHWCYSRIASMICYFFYKNITFGVTVFLYEAYTSFSGQPAYNDWFLSLFNVFFSSLPVIALGVFDQDVSARFCYKFPLLYQEGVQNILFSWKRIIGWMFNGFISALAIFFLCKESLKHQLFDPDGKTAGREILGGTMYTCVVWVVNLQMALSISYFTWVQHIVIWGSIAFWYIFLMIYGAMTPSFSTDAYMVFLEALAPAPSYWLTTLFVMIFALIPYFVYKSVQMRFFPKYHQMIQWIRYEGHSNDPEFVEMVRQRSIRPTTVGYTARRAASVRRSARFHDQIYKDLVGV | |
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 |
---|---|---|---|---|---|
18 | Phosphorylation | LHLSKIYSYTCGKSS HCHHHHHHHCCCCCC | 19.89 | 25561503 | |
25 | Phosphorylation | SYTCGKSSFQEDHSN HHCCCCCCCCCCCCC | 34.14 | 26811356 | |
31 | Phosphorylation | SSFQEDHSNIGGPGF CCCCCCCCCCCCCCC | 42.33 | 17317660 | |
301 | Phosphorylation | KRSRIERTMDKIIYL HHHHHHHHHHHHHHH | 19.55 | 24894044 | |
467 | Phosphorylation | ERAMAVRSGGSPLVN HHHHHHHCCCCCCCC | 40.69 | 26811356 | |
470 | Phosphorylation | MAVRSGGSPLVNEDL HHHHCCCCCCCCCCC | 20.70 | 17317660 | |
814 | Phosphorylation | IIDGKSLTYALEDEI EECCCCHHHHCHHHH | 17.53 | 24243849 | |
1169 | Phosphorylation | VEMVRQRSIRPTTVG HHHHHHCCCCCCCHH | 18.01 | 30407730 | |
1173 | Phosphorylation | RQRSIRPTTVGYTAR HHCCCCCCCHHHHHH | 25.02 | 25561503 | |
1174 | Phosphorylation | QRSIRPTTVGYTARR HCCCCCCCHHHHHHH | 18.02 | 25561503 |
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 ALA10_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ALA10_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 ALA10_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ALA10_ARATH !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, SUBCELLULARLOCATION, AND MASS SPECTROMETRY. | |
"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 SER-31, AND MASSSPECTROMETRY. |