UniProt ID | LAS17_YEAST | |
---|---|---|
UniProt AC | Q12446 | |
Protein Name | Proline-rich protein LAS17 | |
Gene Name | LAS17 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 633 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MGLLNSSDKEIIKRALPKASNKIIDVTVARLYIAYPDKNEWQYTGLSGALALVDDLVGNTFFLKLVDINGHRGVIWDQELYVNFEYYQDRTFFHTFEMEECFAGLLFVDINEASHFLKRVQKRERYANRKTLLNKNAVALTKKVREEQKSQVVHGPRGESLIDNQRKRYNYEDVDTIPTTKHKAPPPPPPTAETFDSDQTSSFSDINSTTASAPTTPAPALPPASPEVRKEETHPKHSLPPLPNQFAPLPDPPQHNSPPQNNAPSQPQSNPFPFPIPEIPSTQSATNPFPFPVPQQQFNQAPSMGIPQQNRPLPQLPNRNNRPVPPPPPMRTTTEGSGVRLPAPPPPPRRGPAPPPPPHRHVTSNTLNSAGGNSLLPQATGRRGPAPPPPPRASRPTPNVTMQQNPQQYNNSNRPFGYQTNSNMSSPPPPPVTTFNTLTPQMTAATGQPAVPLPQNTQAPSQATNVPVAPPPPPASLGQSQIPQSAPSAPIPPTLPSTTSAAPPPPPAFLTQQPQSGGAPAPPPPPQMPATSTSGGGSFAETTGDAGRDALLASIRGAGGIGALRKVDKSQLDKPSVLLQEARGESASPPAAAGNGGTPGGPPASLADALAAALNKRKTKVGAHDDMDNGDDW | |
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 |
---|---|---|---|---|---|
22 | Acetylation | ALPKASNKIIDVTVA HCHHCCCCEEEEEEE | 38.24 | 24489116 | |
160 | Phosphorylation | VHGPRGESLIDNQRK CCCCCCHHHHCCCHH | 33.19 | 21440633 | |
176 | Phosphorylation | YNYEDVDTIPTTKHK CCCCCCCCCCCCCCC | 28.80 | 21440633 | |
181 | Acetylation | VDTIPTTKHKAPPPP CCCCCCCCCCCCCCC | 45.66 | 24489116 | |
197 | Phosphorylation | PTAETFDSDQTSSFS CCCCCCCCCCCCCCC | 27.68 | 21551504 | |
201 | Phosphorylation | TFDSDQTSSFSDINS CCCCCCCCCCCCCCC | 24.61 | 21551504 | |
204 | Phosphorylation | SDQTSSFSDINSTTA CCCCCCCCCCCCCCC | 39.26 | 21551504 | |
210 | Phosphorylation | FSDINSTTASAPTTP CCCCCCCCCCCCCCC | 20.59 | 21551504 | |
212 | Phosphorylation | DINSTTASAPTTPAP CCCCCCCCCCCCCCC | 32.46 | 21551504 | |
216 | Phosphorylation | TTASAPTTPAPALPP CCCCCCCCCCCCCCC | 19.18 | 21551504 | |
225 | Phosphorylation | APALPPASPEVRKEE CCCCCCCCHHHHCCC | 27.63 | 27214570 | |
332 | Phosphorylation | PPPPPMRTTTEGSGV CCCCCCCCCCCCCCC | 31.64 | 22369663 | |
333 | Phosphorylation | PPPPMRTTTEGSGVR CCCCCCCCCCCCCCC | 16.69 | 22369663 | |
334 | Phosphorylation | PPPMRTTTEGSGVRL CCCCCCCCCCCCCCC | 37.42 | 22369663 | |
337 | Phosphorylation | MRTTTEGSGVRLPAP CCCCCCCCCCCCCCC | 28.08 | 22369663 | |
363 | Phosphorylation | PPPHRHVTSNTLNSA CCCCCCCCCCCCCCC | 15.33 | 28152593 | |
364 | Phosphorylation | PPHRHVTSNTLNSAG CCCCCCCCCCCCCCC | 27.08 | 19779198 | |
366 | Phosphorylation | HRHVTSNTLNSAGGN CCCCCCCCCCCCCCC | 27.38 | 19779198 | |
369 | Phosphorylation | VTSNTLNSAGGNSLL CCCCCCCCCCCCCCC | 31.25 | 19779198 | |
374 | Phosphorylation | LNSAGGNSLLPQATG CCCCCCCCCCCCCCC | 34.26 | 21440633 | |
380 | Phosphorylation | NSLLPQATGRRGPAP CCCCCCCCCCCCCCC | 26.44 | 23749301 | |
574 | Acetylation | VDKSQLDKPSVLLQE CCHHHCCCCCHHHHH | 48.02 | 24489116 | |
576 | Phosphorylation | KSQLDKPSVLLQEAR HHHCCCCCHHHHHHC | 31.01 | 21551504 | |
586 | Phosphorylation | LQEARGESASPPAAA HHHHCCCCCCCCHHH | 36.55 | 17563356 | |
588 | Phosphorylation | EARGESASPPAAAGN HHCCCCCCCCHHHCC | 40.47 | 21082442 | |
598 | Phosphorylation | AAAGNGGTPGGPPAS HHHCCCCCCCCCCHH | 21.84 | 21551504 | |
605 | Phosphorylation | TPGGPPASLADALAA CCCCCCHHHHHHHHH | 29.84 | 27017623 |
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 LAS17_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LAS17_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 LAS17_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-588, 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-586 AND SER-588, ANDMASS SPECTROMETRY. |