UniProt ID | TDA3_YEAST | |
---|---|---|
UniProt AC | P38758 | |
Protein Name | Putative oxidoreductase TDA3 | |
Gene Name | TDA3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 523 | |
Subcellular Localization | Cytoplasm. Late endosome. The recruitment from the cytoplasm to endosomal structures is facilitated by BTN2. | |
Protein Description | Putative oxidoreductase that negatively regulates the retrieval of cargo from late endosomes to the Golgi. Regulates YIF1 and KEX2 localization. Required for fast DNA replication.. | |
Protein Sequence | MGEDFMHPPFQTYPSKNSEGKKHIVIVGGGIIGCCTAYYLTQHPSFSPSTHHITIIESRRIAGGASGKAGGLLASWAFPHQIVPLSFQLHQELSDEYDGENNWDYRRLTTVSLEADVREEVIENYERLSKKAYNLNVPPPKKRPGYISNKFNIGDSNSSLSSSGSSLKNDSASNEEEGSDIHVSSSVPSLHSLTNERMRSHTNSASDLDSVSPVEQLRETNIHNPLPADLDWIRRELVNDWSSLGGTDTTAQLHPYKFTHFILSKAMETGAVDLLLGKVVGLKCDEMDCVHSLKYLPSVVKNRRNSRGHAENPDIKLGTIFNDENAKPIEINDIQQIVLSMGPWTSKILKDCPISGLRAHSVTIKPSEKTVSPYAILAELKVNDREFFSPEMYARKDEVYVCGEGDTLVNIPESSDDVEVVSEKCDELYHYVSKLSPTLSKGHLLRKQACFLPVLNVPTSSGPLIGETNVKDLYIASGHSCWGINNAPATGKLMAEILLDGEATSAEISSLDPKLYFDATILS | |
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 |
---|---|---|---|---|---|
131 | Acetylation | NYERLSKKAYNLNVP HHHHHHHHHHCCCCC | 53.37 | 25381059 | |
150 | Acetylation | RPGYISNKFNIGDSN CCCCCCCCCCCCCCC | 32.75 | 22865919 | |
156 | Phosphorylation | NKFNIGDSNSSLSSS CCCCCCCCCCCCCCC | 33.14 | 22890988 | |
158 | Phosphorylation | FNIGDSNSSLSSSGS CCCCCCCCCCCCCCC | 36.29 | 22890988 | |
159 | Phosphorylation | NIGDSNSSLSSSGSS CCCCCCCCCCCCCCC | 36.20 | 22369663 | |
161 | Phosphorylation | GDSNSSLSSSGSSLK CCCCCCCCCCCCCCC | 25.14 | 22890988 | |
162 | Phosphorylation | DSNSSLSSSGSSLKN CCCCCCCCCCCCCCC | 43.97 | 22890988 | |
163 | Phosphorylation | SNSSLSSSGSSLKND CCCCCCCCCCCCCCC | 39.04 | 22890988 | |
165 | Phosphorylation | SSLSSSGSSLKNDSA CCCCCCCCCCCCCCC | 34.15 | 22890988 | |
166 | Phosphorylation | SLSSSGSSLKNDSAS CCCCCCCCCCCCCCC | 47.06 | 22890988 | |
171 | Phosphorylation | GSSLKNDSASNEEEG CCCCCCCCCCCCCCC | 42.88 | 22369663 | |
173 | Phosphorylation | SLKNDSASNEEEGSD CCCCCCCCCCCCCCC | 49.04 | 22369663 | |
179 | Phosphorylation | ASNEEEGSDIHVSSS CCCCCCCCCCEECCC | 36.35 | 22369663 | |
184 | Phosphorylation | EGSDIHVSSSVPSLH CCCCCEECCCCCCHH | 11.61 | 22369663 | |
185 | Phosphorylation | GSDIHVSSSVPSLHS CCCCEECCCCCCHHH | 33.98 | 22369663 | |
186 | Phosphorylation | SDIHVSSSVPSLHSL CCCEECCCCCCHHHH | 30.46 | 22369663 | |
189 | Phosphorylation | HVSSSVPSLHSLTNE EECCCCCCHHHHCHH | 36.24 | 22369663 | |
192 | Phosphorylation | SSVPSLHSLTNERMR CCCCCHHHHCHHHHH | 42.03 | 22369663 | |
194 | Phosphorylation | VPSLHSLTNERMRSH CCCHHHHCHHHHHHH | 37.74 | 22369663 | |
200 | Phosphorylation | LTNERMRSHTNSASD HCHHHHHHHCCCCHH | 25.89 | 22369663 | |
202 | Phosphorylation | NERMRSHTNSASDLD HHHHHHHCCCCHHHC | 31.92 | 22369663 | |
204 | Phosphorylation | RMRSHTNSASDLDSV HHHHHCCCCHHHCCC | 30.24 | 22369663 | |
206 | Phosphorylation | RSHTNSASDLDSVSP HHHCCCCHHHCCCCH | 38.23 | 22369663 | |
210 | Phosphorylation | NSASDLDSVSPVEQL CCCHHHCCCCHHHHH | 31.62 | 22369663 | |
212 | Phosphorylation | ASDLDSVSPVEQLRE CHHHCCCCHHHHHHH | 27.46 | 22369663 | |
220 | Phosphorylation | PVEQLRETNIHNPLP HHHHHHHCCCCCCCC | 32.79 | 27017623 | |
306 | Phosphorylation | VVKNRRNSRGHAENP HHHCCCCCCCCCCCC | 37.52 | 17287358 | |
369 | Acetylation | VTIKPSEKTVSPYAI EEECCCCCCCCCCEE | 59.57 | 24489116 | |
372 | Phosphorylation | KPSEKTVSPYAILAE CCCCCCCCCCEEEEE | 19.88 | 21440633 | |
436 | Phosphorylation | YHYVSKLSPTLSKGH HHHHHHHCCCCCCCC | 21.41 | 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 TDA3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TDA3_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 TDA3_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
VTS1_YEAST | VTS1 | physical | 11283351 | |
SSB1_YEAST | SSB1 | physical | 19536198 | |
BTN2_YEAST | BTN2 | genetic | 21441304 | |
HSP72_YEAST | SSA2 | physical | 22940862 | |
SSB1_YEAST | SSB1 | physical | 22940862 | |
TDA3_YEAST | TDA3 | physical | 22940862 | |
BTN2_YEAST | BTN2 | physical | 25512335 | |
PMP3_YEAST | PMP3 | genetic | 27708008 | |
RTG2_YEAST | RTG2 | genetic | 27708008 | |
ERG3_YEAST | ERG3 | genetic | 27708008 | |
VRP1_YEAST | VRP1 | genetic | 27708008 | |
MKS1_YEAST | MKS1 | genetic | 27708008 | |
IRA2_YEAST | IRA2 | genetic | 27708008 | |
NCBP2_YEAST | CBC2 | genetic | 27708008 | |
NAA30_YEAST | MAK3 | genetic | 27708008 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
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-158; SER-159; SER-184;SER-200; THR-202; SER-204; SER-206; SER-210 AND SER-212, 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-200; THR-202; SER-204;SER-206 AND SER-212, AND MASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASSSPECTROMETRY. |