| UniProt ID | ARP2_YEAST | |
|---|---|---|
| UniProt AC | P32381 | |
| Protein Name | Actin-related protein 2 | |
| Gene Name | ARP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 391 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, actin patch . | |
| Protein Description | Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity).. | |
| Protein Sequence | MDPHNPIVLDQGTGFVKIGRAGENFPDYTFPSIVGRPILRAEERASVATPLKDIMIGDEASEVRSYLQISYPMENGIIKNWTDMELLWDYAFFEQMKLPSTSNGKILLTEPPMNPLKNREKMCEVMFEKYDFGGVYVAIQAVLALYAQGLSSGVVVDSGDGVTHIVPVYESVVLSHLTRRLDVAGRDVTRHLIDLLSRRGYAFNRTADFETVRQIKEKLCYVSYDLDLDTKLARETTALVESYELPDGRTIKVGQERFEAPECLFQPGLVDVEQPGVGELLFNTVQSADVDIRSSLYKAIVLSGGSSMYPGLPSRLEKELKQLWFSRVLHNDPSRLDKFKVRIEDPPRRKHMVFIGGAVLASIMADKDHMWLSKQEWQESGPSAMTKFGPR | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDPHNPIV -------CCCCCCEE | 19.10 | 22814378 | |
| 17 | Acetylation | DQGTGFVKIGRAGEN ECCCCEEEECCCCCC | 36.86 | 24489116 | |
| 46 | Phosphorylation | LRAEERASVATPLKD CCHHHHHCCCCCHHH | 20.64 | 28889911 | |
| 49 | Phosphorylation | EERASVATPLKDIMI HHHHCCCCCHHHHCC | 27.31 | 19779198 | |
| 52 | Ubiquitination | ASVATPLKDIMIGDE HCCCCCHHHHCCCCC | 46.54 | 23749301 | |
| 52 | Acetylation | ASVATPLKDIMIGDE HCCCCCHHHHCCCCC | 46.54 | 24489116 | |
| 66 | Phosphorylation | EASEVRSYLQISYPM CHHHHHHHHHCCCCC | 7.64 | 28889911 | |
| 117 | Ubiquitination | EPPMNPLKNREKMCE CCCCCCCCCHHHHHH | 56.04 | 23749301 | |
| 121 | Ubiquitination | NPLKNREKMCEVMFE CCCCCHHHHHHHHHH | 45.68 | 22817900 | |
| 201 | Phosphorylation | DLLSRRGYAFNRTAD HHHHHCCCCCCCCCC | 13.25 | 27017623 | |
| 206 | Phosphorylation | RGYAFNRTADFETVR CCCCCCCCCCHHHHH | 31.51 | 27017623 | |
| 211 | Phosphorylation | NRTADFETVRQIKEK CCCCCHHHHHHHHHH | 22.45 | 27017623 | |
| 252 | Ubiquitination | LPDGRTIKVGQERFE CCCCCEEEECCCCCC | 39.43 | 23749301 | |
| 298 | Acetylation | DIRSSLYKAIVLSGG CHHHHHHHHHHHCCC | 36.61 | 24489116 | |
| 298 | Ubiquitination | DIRSSLYKAIVLSGG CHHHHHHHHHHHCCC | 36.61 | 17644757 | |
| 318 | Ubiquitination | GLPSRLEKELKQLWF CCCHHHHHHHHHHHH | 73.30 | 17644757 | |
| 321 | Acetylation | SRLEKELKQLWFSRV HHHHHHHHHHHHHHH | 44.42 | 24489116 | |
| 334 | Phosphorylation | RVLHNDPSRLDKFKV HHHCCCHHHHHHEEE | 48.62 | 29688323 | |
| 338 | Ubiquitination | NDPSRLDKFKVRIED CCHHHHHHEEEECCC | 52.23 | 17644757 |
| 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 ARP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARP2_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 ARP2_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 SER-46 AND TYR-66, AND MASSSPECTROMETRY. | |
