| UniProt ID | AP3M_YEAST | |
|---|---|---|
| UniProt AC | P38153 | |
| Protein Name | AP-3 complex subunit mu | |
| Gene Name | APM3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 483 | |
| Subcellular Localization |
Golgi apparatus . Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side . Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. |
|
| Protein Description | Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for the transport via the ALP pathway, which directs the transport of the cargo proteins PHO8 and VAM3 to the vacuole.. | |
| Protein Sequence | MYLSFYITDTKNKLIFQYLLGATAPSFKHLWTRVQSTCPQLLEDSSSDDYLDHSMVGRDLEVYKYFSVINKLNYWCLASTSKSKGPLDCFTFLETIDRILLEYFDKDKLSIKKIVNNYDRISLIFNCCVEAGEPNVSDMLYVNKIKEAVPERSDLSKFISSTAHNLQQAVQLPQQRQQQLQQNQISRGSNSLIENEEIVPWRTSRASKHENNELYVDLLETFHVVFEKKKSHLRLLTGSIHGIVDVRSYLNDNPLVAVKLNTMGNDIGIPSLHDCVEINDGVFSPSNITFIPPDGKFRLLEYSVDLSSQVKQSGVRMNSIGLMSLHFQNGLGKDSDEFELSLNIENFKKVSQVDDLKIDLQFNVENADPNEIAYKIKILRNTHGRFENSIIMGQGQWIFDKSTATGTVPVLRGCIEYENTGPNFTKKVDLQTVSLEYSYIGQSASGIYVEAIDIVSGLTIGKNTKLYKGAKYKTQTGNFQVRL | |
| 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 |
|---|---|---|---|---|---|
| 106 | Acetylation | ILLEYFDKDKLSIKK HHHHHHCCCCCCHHH | 47.03 | 24489116 | |
| 113 | Ubiquitination | KDKLSIKKIVNNYDR CCCCCHHHHHCCCCH | 50.66 | 23749301 | |
| 189 | Phosphorylation | QNQISRGSNSLIENE HHCHHCCCCCCCCCC | 23.33 | 28889911 | |
| 191 | Phosphorylation | QISRGSNSLIENEEI CHHCCCCCCCCCCCC | 32.21 | 19779198 | |
| 459 | Phosphorylation | IDIVSGLTIGKNTKL EEECCCCEECCCCEE | 31.07 | 28889911 |
| 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 AP3M_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AP3M_YEAST !! | ||||||
* 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 AP3M_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-459, AND MASSSPECTROMETRY. | |
