UniProt ID | SYQ_YEAST | |
---|---|---|
UniProt AC | P13188 | |
Protein Name | Glutamine--tRNA ligase | |
Gene Name | GLN4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 809 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MSSVEELTQLFSQVGFEDKKVKEIVKNKKVSDSLYKLIKETPSDYQWNKSTRALVHNLASFVKGTDLPKSELIVNGIINGDLKTSLQVDAAFKYVKANGEASTKMGMNENSGVGIEITEDQVRNYVMQYIQENKERILTERYKLVPGIFADVKNLKELKWADPRSFKPIIDQEVLKLLGPKDERDLIKKKTKNNEKKKTNSAKKSSDNSASSGPKRTMFNEGFLGDLHKVGENPQAYPELMKEHLEVTGGKVRTRFPPEPNGYLHIGHSKAIMVNFGYAKYHNGTCYLRFDDTNPEKEAPEYFESIKRMVSWLGFKPWKITYSSDYFDELYRLAEVLIKNGKAYVCHCTAEEIKRGRGIKEDGTPGGERYACKHRDQSIEQNLQEFRDMRDGKYKPGEAILRMKQDLNSPSPQMWDLIAYRVLNAPHPRTGTKWRIYPTYDFTHCLVDSMENITHSLCTTEFYLSRESYEWLCDQVHVFRPAQREYGRLNITGTVLSKRKIAQLVDEKFVRGWDDPRLFTLEAIRRRGVPPGAILSFINTLGVTTSTTNIQVVRFESAVRKYLEDTTPRLMFVLDPVEVVVDNLSDDYEELATIPYRPGTPEFGERTVPFTNKFYIERSDFSENVDDKEFFRLTPNQPVGLIKVSHTVSFKSLEKDEAGKIIRIHVNYDNKVEEGSKPKKPKTYIQWVPISSKYNSPLRVTETRVYNQLFKSENPSSHPEGFLKDINPESEVVYKESVMEHNFGDVVKNSPWVVDSVKNSEFYVEEDKDSKEVCRFQAMRVGYFTLDKESTTSKVILNRIVSLKDATSK | |
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 |
---|---|---|---|---|---|
28 | Acetylation | VKEIVKNKKVSDSLY HHHHHHCCCCCHHHH | 49.16 | 17397211 | |
29 | Acetylation | KEIVKNKKVSDSLYK HHHHHCCCCCHHHHH | 57.26 | 17397211 | |
36 | Acetylation | KVSDSLYKLIKETPS CCCHHHHHHHHHCCC | 49.37 | 24489116 | |
49 | Acetylation | PSDYQWNKSTRALVH CCHHCCCHHHHHHHH | 50.69 | 24489116 | |
63 | Acetylation | HNLASFVKGTDLPKS HHHHHHHCCCCCCHH | 54.83 | 24489116 | |
69 | Acetylation | VKGTDLPKSELIVNG HCCCCCCHHHEEEEC | 64.95 | 24489116 | |
134 | Acetylation | MQYIQENKERILTER HHHHHHHHHHHHHHH | 47.84 | 24489116 | |
139 | Phosphorylation | ENKERILTERYKLVP HHHHHHHHHHHHCCC | 18.95 | 19823750 | |
142 | Phosphorylation | ERILTERYKLVPGIF HHHHHHHHHCCCCCC | 11.48 | 19823750 | |
143 | Acetylation | RILTERYKLVPGIFA HHHHHHHHCCCCCCC | 49.59 | 24489116 | |
153 | Acetylation | PGIFADVKNLKELKW CCCCCCCCCHHHCCC | 58.05 | 24489116 | |
165 | Phosphorylation | LKWADPRSFKPIIDQ CCCCCCCCCCCCCCH | 42.90 | 28889911 | |
167 | Acetylation | WADPRSFKPIIDQEV CCCCCCCCCCCCHHH | 36.23 | 24489116 | |
181 | Acetylation | VLKLLGPKDERDLIK HHHHHCCCCHHHHHH | 71.12 | 24489116 | |
206 | Phosphorylation | TNSAKKSSDNSASSG CCCCCCCCCCCCCCC | 50.09 | 28889911 | |
211 | Phosphorylation | KSSDNSASSGPKRTM CCCCCCCCCCCCCCC | 35.33 | 28889911 | |
242 | Acetylation | QAYPELMKEHLEVTG CCCHHHHHHHHEECC | 55.39 | 24489116 | |
297 | Acetylation | FDDTNPEKEAPEYFE ECCCCHHHHCHHHHH | 61.50 | 24489116 | |
307 | Acetylation | PEYFESIKRMVSWLG HHHHHHHHHHHHHHC | 43.66 | 24489116 | |
316 | Ubiquitination | MVSWLGFKPWKITYS HHHHHCCCCCEEEEE | 48.44 | 23749301 | |
316 | Acetylation | MVSWLGFKPWKITYS HHHHHCCCCCEEEEE | 48.44 | 24489116 | |
339 | Acetylation | RLAEVLIKNGKAYVC HHHHHHHHCCEEEEE | 56.33 | 22865919 | |
364 | Phosphorylation | RGIKEDGTPGGERYA CCCCCCCCCCCCCCH | 30.96 | 23749301 | |
378 | Phosphorylation | ACKHRDQSIEQNLQE HHHCCCHHHHHHHHH | 32.17 | 28889911 | |
404 | Ubiquitination | GEAILRMKQDLNSPS HHHHHHHHCCCCCCC | 33.94 | 23749301 | |
409 | Phosphorylation | RMKQDLNSPSPQMWD HHHCCCCCCCHHHHH | 33.77 | 28889911 | |
411 | Phosphorylation | KQDLNSPSPQMWDLI HCCCCCCCHHHHHHH | 27.82 | 28889911 | |
420 | Phosphorylation | QMWDLIAYRVLNAPH HHHHHHHHHHHCCCC | 8.34 | 29688323 | |
497 | Phosphorylation | NITGTVLSKRKIAQL CCCCEECCHHHHHHH | 26.52 | 22369663 | |
498 | Acetylation | ITGTVLSKRKIAQLV CCCEECCHHHHHHHH | 54.25 | 24489116 | |
498 | 2-Hydroxyisobutyrylation | ITGTVLSKRKIAQLV CCCEECCHHHHHHHH | 54.25 | - | |
508 | Acetylation | IAQLVDEKFVRGWDD HHHHHCHHHCCCCCC | 44.70 | 24489116 | |
613 | Ubiquitination | RTVPFTNKFYIERSD CCCCCCCCEEEECCC | 36.16 | 24961812 | |
613 | Acetylation | RTVPFTNKFYIERSD CCCCCCCCEEEECCC | 36.16 | 24489116 | |
628 | Acetylation | FSENVDDKEFFRLTP CCCCCCCHHHEECCC | 52.54 | 24489116 | |
643 | Acetylation | NQPVGLIKVSHTVSF CCCEEEEEEEEEEEE | 42.60 | 24489116 | |
651 | Acetylation | VSHTVSFKSLEKDEA EEEEEEECCCCCCCC | 46.77 | 24489116 | |
671 | Acetylation | IHVNYDNKVEEGSKP EEEECCCCCCCCCCC | 48.39 | 24489116 | |
693 | Acetylation | QWVPISSKYNSPLRV EEEECCCCCCCCCEE | 41.48 | 24489116 | |
711 | Acetylation | RVYNQLFKSENPSSH HHHHHHHCCCCCCCC | 66.51 | 24489116 | |
712 | Phosphorylation | VYNQLFKSENPSSHP HHHHHHCCCCCCCCC | 34.96 | 19779198 | |
716 | Phosphorylation | LFKSENPSSHPEGFL HHCCCCCCCCCCCCC | 53.51 | 19779198 | |
724 | Acetylation | SHPEGFLKDINPESE CCCCCCCCCCCCCCC | 55.06 | 24489116 | |
748 | Acetylation | HNFGDVVKNSPWVVD CCCCHHHCCCCCEEE | 52.10 | 24489116 | |
768 | Acetylation | EFYVEEDKDSKEVCR CEEEECCCCHHHHHH | 68.15 | 24489116 | |
771 | Acetylation | VEEDKDSKEVCRFQA EECCCCHHHHHHHEE | 65.39 | 24489116 | |
785 | Phosphorylation | AMRVGYFTLDKESTT EEEEEEEEECCCCCC | 26.09 | 28889911 | |
788 | Acetylation | VGYFTLDKESTTSKV EEEEEECCCCCCCHH | 57.59 | 24489116 | |
790 | Phosphorylation | YFTLDKESTTSKVIL EEEECCCCCCCHHHH | 42.60 | 28889911 | |
794 | Acetylation | DKESTTSKVILNRIV CCCCCCCHHHHHHHH | 31.07 | 24489116 | |
802 | Phosphorylation | VILNRIVSLKDATSK HHHHHHHHHHHHCCC | 27.59 | 17563356 | |
804 | Acetylation | LNRIVSLKDATSK-- HHHHHHHHHHCCC-- | 37.50 | 25381059 |
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 SYQ_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYQ_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 SYQ_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
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-802, AND MASSSPECTROMETRY. |