UniProt ID | TMA17_YEAST | |
---|---|---|
UniProt AC | Q12513 | |
Protein Name | Translation machinery-associated protein 17 | |
Gene Name | TMA17 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 150 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | ATPase-dedicated chaperone that assists the formation of the RPT6-RPT3 ATPase pair, an early step in proteasome assembly. Plays a key role in maintaining homeostatic proteasome levels and adjusting proteasome assembly when demands increase, such as during proteasome stresses. Function overlaps with RPN14.. | |
Protein Sequence | MCSAGGIRRPIQIEEFKTAISGMSDMELAQIKTEIENSINHLQRSNARLGKYIAKLEGADDRLEADDSDDLENIDSGDLALYKDSVRENEIVLNNYNERVDALEQETVYRKTGHGKSKHEVEAKDNTNKGPDVDMDNSNVDVVTPNSIFI | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MCSAGGIRRP -----CCCCCCCCCC | 28.75 | 30377154 | |
24 | Phosphorylation | KTAISGMSDMELAQI HHHHCCCCHHHHHHH | 37.01 | 28889911 | |
33 | Phosphorylation | MELAQIKTEIENSIN HHHHHHHHHHHHHHH | 43.77 | 28889911 | |
38 | Phosphorylation | IKTEIENSINHLQRS HHHHHHHHHHHHHHH | 16.39 | 28889911 | |
45 | Phosphorylation | SINHLQRSNARLGKY HHHHHHHHHHHHHHH | 23.14 | 28889911 | |
51 | Acetylation | RSNARLGKYIAKLEG HHHHHHHHHHHHHCC | 37.77 | 25381059 | |
52 | Phosphorylation | SNARLGKYIAKLEGA HHHHHHHHHHHHCCC | 12.33 | 28889911 | |
68 | Phosphorylation | DRLEADDSDDLENID CCCCCCCCCCHHCCC | 33.30 | 22369663 | |
76 | Phosphorylation | DDLENIDSGDLALYK CCHHCCCCCCEEEEE | 30.34 | 22369663 | |
82 | Phosphorylation | DSGDLALYKDSVREN CCCCEEEEECCCCCC | 13.72 | 22369663 | |
85 | Phosphorylation | DLALYKDSVRENEIV CEEEEECCCCCCEEE | 20.94 | 29136822 | |
127 | Phosphorylation | EVEAKDNTNKGPDVD EEECCCCCCCCCCCC | 48.73 | 28889911 | |
144 | Phosphorylation | NSNVDVVTPNSIFI- CCCCCEECCCCCCC- | 19.32 | 19779198 | |
147 | Phosphorylation | VDVVTPNSIFI---- CCEECCCCCCC---- | 21.78 | 19779198 |
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 TMA17_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMA17_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 TMA17_YEAST !! |
Kegg Drug | ||||||
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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-24 AND SER-68, AND MASSSPECTROMETRY. | |
"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-68, 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-68, AND MASSSPECTROMETRY. |