UniProt ID | ADD37_YEAST | |
---|---|---|
UniProt AC | Q03233 | |
Protein Name | Alpha1-proteinase inhibitor-degradation deficient protein 37 | |
Gene Name | ADD37 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 198 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Involved in ER-associated protein degradation (ERAD).. | |
Protein Sequence | MAIKPTKSFQNCLEAEVPGYNDCPTVLFSIDPNSGPRSKSKQRTKSKRCVSGRLATEVLDLYGNTKTATTPPPVLRRPSVTAAQQESACEGVLVKDQGDRQLQPILCSKEELVAKINDLCVCGSKLSSKELEFYKKKLDSNITKILQNEHTKTVLSQIFNEKDKNMAVKTIKHWMVTDTTISNWCPAFLKIFENAMPN | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MAIKPTKSFQNCLEA CCCCCCHHHHCHHHC | 34.25 | 20377248 | |
34 | Phosphorylation | LFSIDPNSGPRSKSK EEEECCCCCCCCCCC | 56.41 | 21440633 | |
67 | Phosphorylation | DLYGNTKTATTPPPV HHHCCCCCCCCCCCC | 27.48 | 22369663 | |
69 | Phosphorylation | YGNTKTATTPPPVLR HCCCCCCCCCCCCCC | 45.10 | 21440633 | |
70 | Phosphorylation | GNTKTATTPPPVLRR CCCCCCCCCCCCCCC | 31.19 | 22369663 | |
79 | Phosphorylation | PPVLRRPSVTAAQQE CCCCCCCCCCHHHHH | 30.23 | 17330950 | |
81 | Phosphorylation | VLRRPSVTAAQQESA CCCCCCCCHHHHHHH | 22.18 | 17330950 | |
129 | Acetylation | CGSKLSSKELEFYKK CCCCCCHHHHHHHHH | 64.04 | 24489116 | |
143 | Phosphorylation | KKLDSNITKILQNEH HHHHHHHHHHHHCHH | 19.11 | 30377154 | |
151 | Phosphorylation | KILQNEHTKTVLSQI HHHHCHHHHHHHHHH | 23.41 | 29136822 | |
153 | Phosphorylation | LQNEHTKTVLSQIFN HHCHHHHHHHHHHHC | 28.03 | 29136822 | |
156 | Phosphorylation | EHTKTVLSQIFNEKD HHHHHHHHHHHCHHC | 19.52 | 29136822 | |
162 | Acetylation | LSQIFNEKDKNMAVK HHHHHCHHCCCHHHE | 75.10 | 24489116 |
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 ADD37_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ADD37_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 ADD37_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-79, AND MASSSPECTROMETRY. | |
"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-79, AND MASSSPECTROMETRY. | |
"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-70, AND MASSSPECTROMETRY. |