UniProt ID | HBS1_YEAST | |
---|---|---|
UniProt AC | P32769 | |
Protein Name | Elongation factor 1 alpha-like protein | |
Gene Name | HBS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 611 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Involved in protein translation. Together with DOM34, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.. | |
Protein Sequence | MAYSDYSDGADDMPDFHDEGEFDDYLNDDEYDLMNEVFPTLKAQLQDYQGWDNLSLKLALFDNNFDLESTLAELKKTLKKKKTPKKPIAAANGSANVTQKLANISISQQRPNDRLPDWLDEEESEGERNGEEANDEKTVQRYYKTTVPTKPKKPHDISAFVKSALPHLSFVVLGHVDAGKSTLMGRLLYDLNIVNQSQLRKLQRESETMGKSSFKFAWIMDQTNEERERGVTVSICTSHFSTHRANFTIVDAPGHRDFVPNAIMGISQADMAILCVDCSTNAFESGFDLDGQTKEHMLLASSLGIHNLIIAMNKMDNVDWSQQRFEEIKSKLLPYLVDIGFFEDNINWVPISGFSGEGVYKIEYTDEVRQWYNGPNLMSTLENAAFKISKENEGINKDDPFLFSVLEIIPSKKTSNDLALVSGKLESGSIQPGESLTIYPSEQSCIVDKIQVGSQQGQSTNHEETDVAIKGDFVTLKLRKAYPEDIQNGDLAASVDYSSIHSAQCFVLELTTFDMNRPLLPGTPFILFIGVKEQPARIKRLISFIDKGNTASKKKIRHLGSKQRAFVEIELIEVKRWIPLLTAHENDRLGRVVLRKDGRTIAAGKISEITQ | |
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 |
---|---|---|---|---|---|
55 | Phosphorylation | YQGWDNLSLKLALFD CCCCCCCEEEEEEEC | 29.70 | 15665377 | |
105 | Phosphorylation | TQKLANISISQQRPN HHHHHCCCCCCCCCC | 18.92 | 19823750 | |
107 | Phosphorylation | KLANISISQQRPNDR HHHCCCCCCCCCCCC | 17.30 | 21440633 | |
124 | Phosphorylation | DWLDEEESEGERNGE CCCCCCCCCCCCCCC | 54.93 | 22369663 | |
248 | Phosphorylation | STHRANFTIVDAPGH CCCCCCEEEEECCCC | 21.65 | 28889911 | |
321 | Phosphorylation | KMDNVDWSQQRFEEI CCCCCCHHHHHHHHH | 16.39 | 27017623 | |
414 | Phosphorylation | EIIPSKKTSNDLALV ECCCCCCCCCCEEEE | 36.18 | 21440633 | |
543 | Phosphorylation | ARIKRLISFIDKGNT HHHHHHHHHHHCCCC | 22.27 | 21440633 | |
547 | Acetylation | RLISFIDKGNTASKK HHHHHHHCCCCCCHH | 49.60 | 24489116 | |
605 | Ubiquitination | GRTIAAGKISEITQ- CCEEEEEEHHHCCC- | 38.03 | 23749301 |
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 HBS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HBS1_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 HBS1_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-124, 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-124, AND MASSSPECTROMETRY. |