| 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. | ||||||
loading...
| 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. | |