| UniProt ID | AP2A_DROME | |
|---|---|---|
| UniProt AC | P91926 | |
| Protein Name | AP-2 complex subunit alpha | |
| Gene Name | AP-2alpha | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 940 | |
| Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side . Membrane, coated pit Peripheral membrane protein Cytoplasmic side . Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. |
|
| Protein Description | Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP-2alpha is a subunit of the plasma membrane adapter.. | |
| Protein Sequence | MAPVRGDGMRGLAVFISDIRNCKSKEAEVKRINKELANIRSKFKGDKTLDGYQKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYSEKQIGYLFISVLVNTNSDLIRLIIQSIKNDLQSRNPVHVNLALQCIANIGSRDMAESFSNEIPKLLVSGDTMDVVKQSAALCLLRLFRSSPDIIPGGEWTSRIIHLLNDQHMGVVTAATSLIDALVKRNPDEYKGCVNLAVSRLSRIVTASYTDLQDYTYYFVPAPWLSVKLLRLLQNYNPVTEEAGVRARLNETLETILNKAQEPPKSKKVQHSNAKNAVLFEAINLIIHSDSEPNLLVRACNQLGQFLSNRETNLRYLALESMCHLATSEFSHEEVKKHQEVVILSMKMEKDVSVRQMAVDLLYAMCDRGNAEEIVQEMLNYLETADYSIREEMVLKVAILAEKYATDYTWYVDVILNLIRIAGDYVSEEVWYRVIQIVINREEVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDSRSAPLVQFKLLHSKYHLCSPMTRALLLSTYIKFINLFPEIRTNIQDVFRQHSNLRSADAELQQRASEYLQLSIVASTDVLATVLEEMPSFPERESSILAVLKKKKPGRVPENEIRESKSPAPLTSAAQNNALVNNSHSKLNNSNANTDLLGLSTPPSNNIGSGSNSNSTLIDVLGDMYGSNSNNNSSAVYNTKKFLFKNNGVLFENEMLQIGVKSEFRQNLGRLGLFYGNKTQVPLTNFNPVLQWSAEDALKLNVQMKVVEPTLEAGAQIQQLLTAECIEDYADAPTIEISFRYNGTQQKFSIKLPLSVNKFFEPTEMNAESFFARWKNLSGEQQRSQKVFKAAQPLDLPGARNKLMGFGMQLLDQVDPNPDNMVCAGIIHTQSQQVGCLMRLEPNKQAQMFRLTVRASKETVTREICDLLTDQF | |
| 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 |
|---|---|---|---|---|---|
| 632 | Phosphorylation | PENEIRESKSPAPLT CHHHCCCCCCCCCCC | 28.69 | 19429919 | |
| 634 | Phosphorylation | NEIRESKSPAPLTSA HHCCCCCCCCCCCHH | 35.26 | 19429919 | |
| 639 | Phosphorylation | SKSPAPLTSAAQNNA CCCCCCCCHHHHHCH | 18.43 | 19429919 | |
| 640 | Phosphorylation | KSPAPLTSAAQNNAL CCCCCCCHHHHHCHH | 29.32 | 19429919 | |
| 651 | Phosphorylation | NNALVNNSHSKLNNS HCHHCCCCCHHCCCC | 24.76 | 21082442 | |
| 653 | Phosphorylation | ALVNNSHSKLNNSNA HHCCCCCHHCCCCCC | 38.36 | 27794539 |
| 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 AP2A_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AP2A_DROME !! | ||||||
* 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 AP2A_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RLIP_DROME | Rlip | physical | 22036573 | |
| NOTCH_DROME | N | genetic | 22474327 | |
| DL_DROME | Dl | genetic | 22474327 | |
| FAT_DROME | ft | physical | 24114784 | |
| NUMB_DROME | numb | physical | 22474327 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-634, ANDMASS SPECTROMETRY. | |