UniProt ID | TBCA_YEAST | |
---|---|---|
UniProt AC | P48606 | |
Protein Name | Tubulin-specific chaperone A | |
Gene Name | RBL2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 106 | |
Subcellular Localization | Cytoplasm, cytoskeleton. | |
Protein Description | Tubulin-folding protein; involved in the early step of the tubulin folding pathway.. | |
Protein Sequence | MAPTQLDIKVKALKRLTKEEGYYQQELKDQEAHVAKLKEDKSVDPYDLKKQEEVLDDTKRLLPTLYEKIREFKEDLEQFLKTYQGTEDVSDARSAITSAQELLDSK | |
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 |
---|---|---|---|---|---|
18 | Ubiquitination | KALKRLTKEEGYYQQ HHHHHHHHHCCCCHH | 59.36 | 23749301 | |
18 | Acetylation | KALKRLTKEEGYYQQ HHHHHHHHHCCCCHH | 59.36 | 24489116 | |
41 | Acetylation | VAKLKEDKSVDPYDL HHHHHHCCCCCHHCH | 54.17 | 24489116 | |
49 | Succinylation | SVDPYDLKKQEEVLD CCCHHCHHHHHHHHH | 49.89 | 23954790 | |
68 | Acetylation | LLPTLYEKIREFKED HHHHHHHHHHHHHHH | 33.24 | 24489116 | |
82 | Phosphorylation | DLEQFLKTYQGTEDV HHHHHHHHHCCCCCH | 24.19 | 22369663 | |
83 | Phosphorylation | LEQFLKTYQGTEDVS HHHHHHHHCCCCCHH | 11.89 | 22369663 | |
86 | Phosphorylation | FLKTYQGTEDVSDAR HHHHHCCCCCHHHHH | 17.31 | 22369663 | |
90 | Phosphorylation | YQGTEDVSDARSAIT HCCCCCHHHHHHHHH | 37.56 | 22369663 | |
94 | Phosphorylation | EDVSDARSAITSAQE CCHHHHHHHHHHHHH | 26.24 | 22369663 | |
97 | Phosphorylation | SDARSAITSAQELLD HHHHHHHHHHHHHHH | 20.09 | 22890988 | |
98 | Phosphorylation | DARSAITSAQELLDS HHHHHHHHHHHHHHC | 23.11 | 22890988 | |
105 | Phosphorylation | SAQELLDSK------ HHHHHHHCC------ | 39.99 | 22369663 |
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 TBCA_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TBCA_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 TBCA_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-94, 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-94, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY. |