| UniProt ID | ARP8_YEAST | |
|---|---|---|
| UniProt AC | Q12386 | |
| Protein Name | Actin-like protein ARP8 | |
| Gene Name | ARP8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 881 | |
| Subcellular Localization | Nucleus. Cytoplasm, cytoskeleton. | |
| Protein Description | Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Exhibits low basal ATPase activity, and unable to polymerize. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex.. | |
| Protein Sequence | MSQEEAESSIIYEEPIDIPLEDDDDEDELEEENSVPLSSQADQENAENESDDSVDNVVGSETPRSVTGLSVDPRDVADEEDEDEEGEDEDEDEDDNDVDNEDENDNDNANENENELGSSRDKRAPPAVQTSKRYKKYPKLDPAKAPPGKKVPLHLLEKRRLGRIKAAEEFAKTLKKIGIEKVETTTLPATGLFQPLMLINQKNYSSDYLKKDDQIFALRDRKFLRNNNTSQISSTNTPDVIDLKSLPHSEASAAPLNDEIDLNDPTATIVIHPGSNSIKIGFPKDDHPVVVPNCVAVPKKWLDLENSEHVENVCLQREQSEEFNNIKSEMEKNFRERMRYYKRKVPGNAHEQVVSFNENSKPEIISEKNDPSPIEWIFDDSKLYYGSDALRCVDEKFVIRKPFRGGSFNVKSPYYKSLAELISDVTKLLEHALNSETLNVKPTKFNQYKVVLVIPDIFKKSHVETFIRVLLTELQFQAVAIIQESLATCYGAGISTSTCVVNIGAAETRIACVDEGTVLEHSAITLDYGGDDITRLFALFLLQSDFPLQDWKIDSKHGWLLAERLKKNFTTFQDADVAVQLYNFMNRSPNQPTEKYEFKLFDEVMLAPLALFFPQIFKLIRTSSHKNSSLEFQLPESRDLFTNELNDWNSLSQFESKEGNLYCDLNDDLKILNRILDAHNIIDQLQDKPENYGNTLKENFAPLEKAIVQSIANASITADVTRMNSFYSNILIVGGSSKIPALDFILTDRINIWRPSLLSSASFPQFYKKLTKEIKDLEGHYVNAPDKTEDENKQILQAQIKEKIVEELEEQHQNIEHQNGNEHIFPVSIIPPPRDMNPALIIWKGASVLAQIKLVEELFITNSDWDVHGSRILQYKCIFTY | |
| 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 |
|---|---|---|---|---|---|
| 65 | Phosphorylation | VGSETPRSVTGLSVD CCCCCCCCCCCCCCC | 25.82 | 22369663 | |
| 67 | Phosphorylation | SETPRSVTGLSVDPR CCCCCCCCCCCCCHH | 33.38 | 22369663 | |
| 70 | Phosphorylation | PRSVTGLSVDPRDVA CCCCCCCCCCHHHCC | 26.31 | 22369663 | |
| 130 | Phosphorylation | RAPPAVQTSKRYKKY CCCCHHHCCHHHHCC | 29.62 | 24603354 | |
| 131 | Phosphorylation | APPAVQTSKRYKKYP CCCHHHCCHHHHCCC | 9.69 | 26447709 | |
| 144 | Acetylation | YPKLDPAKAPPGKKV CCCCCCCCCCCCCCC | 67.81 | 25381059 | |
| 205 | Phosphorylation | LINQKNYSSDYLKKD EECCCCCCCCCCCCC | 26.57 | 21440633 | |
| 229 | Phosphorylation | KFLRNNNTSQISSTN HHHHCCCCCCCCCCC | 24.92 | 22369663 | |
| 230 | Phosphorylation | FLRNNNTSQISSTNT HHHCCCCCCCCCCCC | 27.86 | 22369663 | |
| 233 | Phosphorylation | NNNTSQISSTNTPDV CCCCCCCCCCCCCCE | 24.39 | 22369663 | |
| 234 | Phosphorylation | NNTSQISSTNTPDVI CCCCCCCCCCCCCEE | 27.57 | 22369663 | |
| 235 | Phosphorylation | NTSQISSTNTPDVID CCCCCCCCCCCCEEE | 36.00 | 20377248 | |
| 237 | Phosphorylation | SQISSTNTPDVIDLK CCCCCCCCCCEEEHH | 22.43 | 22369663 | |
| 252 | Phosphorylation | SLPHSEASAAPLNDE CCCCCCCCCCCCCCC | 22.40 | 21440633 | |
| 320 | Phosphorylation | VCLQREQSEEFNNIK HHHHHHHHHHHHHHH | 34.05 | 27214570 | |
| 381 | Phosphorylation | IEWIFDDSKLYYGSD CEEEECCCCCEECCC | 26.80 | 28889911 | |
| 459 | Acetylation | LVIPDIFKKSHVETF EEECCHHCHHHHHHH | 54.42 | 24489116 | |
| 844 | Ubiquitination | NPALIIWKGASVLAQ CCCEEEECCHHHHHH | 33.90 | 23749301 |
| 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 ARP8_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARP8_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 ARP8_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 SER-65; SER-70; SER-230;THR-235 AND SER-320, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY. | |