| UniProt ID | ARPC2_YEAST | |
|---|---|---|
| UniProt AC | P53731 | |
| Protein Name | Actin-related protein 2/3 complex subunit 2 | |
| Gene Name | ARC35 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 342 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, actin patch. | |
| Protein Description | Functions as actin-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 mother actin filament (By similarity).. | |
| Protein Sequence | MLHLQPQNLLIQKTLNEAIEALRKGSPLTMDRIVSDFDYTTYHISNTAEDKSILLLSVKTKAWVSVSECQLDGSLTLLKFLADHYSSLGGVTIPSEVEPGYDYTLQITLAELVQESILQLSVLKTIILSFPFELAISKFIELSQQQPAPVEAEITGGEVAANGDNTLFTIKYRDEENIFIKPSNDRVTIIFETIFQDETDKIFGKVFLQEFVDARKRNRQIQSAPQVLYSHEPPLELKRLYQPPKVAEQSRRFITFVLFPRHFQTKELQFHSICQLTLFRNYFHYHIKCSKAYMHSRMRFRVDSFIKVLNRAKVDEDDENDELSAEGRQQARRTFTGRKIVY | |
| 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 |
|---|---|---|---|---|---|
| 13 | Ubiquitination | PQNLLIQKTLNEAIE CHHHHHHHHHHHHHH | 48.24 | 17644757 | |
| 24 | Ubiquitination | EAIEALRKGSPLTMD HHHHHHHCCCCCCHH | 65.67 | 15699485 | |
| 51 | Ubiquitination | ISNTAEDKSILLLSV ECCCCCCCEEEEEEE | 30.79 | 15699485 | |
| 76 | Phosphorylation | CQLDGSLTLLKFLAD CCCCCCHHHHHHHHH | 31.57 | 22369663 | |
| 143 | Phosphorylation | ISKFIELSQQQPAPV HHHHHHHHCCCCCCE | 17.10 | 22369663 | |
| 155 | Phosphorylation | APVEAEITGGEVAAN CCEEEEEECCEEEEC | 30.55 | 22369663 | |
| 166 | Phosphorylation | VAANGDNTLFTIKYR EEECCCCCEEEEEEE | 28.17 | 22369663 | |
| 169 | Phosphorylation | NGDNTLFTIKYRDEE CCCCCEEEEEEECCC | 21.48 | 22369663 | |
| 205 | Ubiquitination | ETDKIFGKVFLQEFV CHHHHHHHHHHHHHH | 21.04 | 24961812 | |
| 238 | Acetylation | HEPPLELKRLYQPPK CCCCCHHHHHHCCCC | 30.86 | 24489116 | |
| 245 | Ubiquitination | KRLYQPPKVAEQSRR HHHHCCCCHHHHHHH | 61.84 | 23749301 | |
| 304 | Phosphorylation | RMRFRVDSFIKVLNR CHHHHHHHHHHHHHH | 26.47 | 22369663 | |
| 313 | Ubiquitination | IKVLNRAKVDEDDEN HHHHHHHCCCCCCCC | 47.16 | 23749301 | |
| 324 | Phosphorylation | DDENDELSAEGRQQA CCCCCCCCHHHHHHH | 23.40 | 17563356 | |
| 334 | Phosphorylation | GRQQARRTFTGRKIV HHHHHHHHHCCCCCC | 21.72 | 24961812 | |
| 336 | Phosphorylation | QQARRTFTGRKIVY- HHHHHHHCCCCCCC- | 35.15 | 21440633 |
| 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 ARPC2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARPC2_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 ARPC2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-155 AND SER-324, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASSSPECTROMETRY. | |
