UniProt ID | SQS1_YEAST | |
---|---|---|
UniProt AC | P53866 | |
Protein Name | Protein SQS1 | |
Gene Name | SQS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 767 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | May be involved in splicing since overexpression antagonizes the suppression of splicing defects by SPP382 mutants.. | |
Protein Sequence | MAKRHSHYQGSRRRHARGSNSKKAGRGNAKGIQGRKIKKKPTPTNSWHNSSIPLGEGDLDDVGADFNPGRAFISPKTIEDYYFGRDAKSRSMKMGGLRPGNRYDSSTDLQAGRAAFRKRPMQFVKAKEVYDPSHNMIQKLRAKNETKNSEEIVEREADVFEEPGKMTSDVEYINNEDSENEDDDSQNSPSTDHSLSSNESKVEDGDLFFVDEEAQQSPDLTKIKRVCIEEIARPREVAIEFDPILTIGKVELSVSEGNESKEISVDVPNKGNKTYHPFAGYISNVLHGMHTSDSDNDELDYEIETENNSEPLYESSASSEVDQGFNYVGQRHNSRADNNLLPSPSPQLTEDIKCLSINGTKTFEGNNDNLPSPASEELEFGFKEEDFVINTNDIVVSNIRMGGVDNSYYLRCYRLLGDYDFHWIDQDLLTDFVVDELGLPEDRLPAYLNFIKNSLIPKIEPAEPTYSDIPISDSSDEGDSYEGDSYEDDEDMASSVVHSDIEEGLDDLIAYTLKHDTERFKTFETKSLETKGKGKKKKLLIDDALALDTETLETLQSKFSKRIETKAKKRKAKEDFIDQENRNSNDMLKKYPYGLHIQNIKDEFESFLSRNNDRLTFPPLDPHGNKTVMKIAKHYNMKSSKIGKANHTSVVVEKIKKTKWSSPNYSLIDQLMRQRPVFMRIDIRRPREEQAAFERTKTIRGKFHVKEGEIVGQNAPEIGNENIGRRMLEKLGWKSGEGLGIQGNKGISEPIFAKIKKNRSGLRHSES | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
42 | Phosphorylation | RKIKKKPTPTNSWHN CCCCCCCCCCCCCCC | 52.18 | 23749301 | |
76 | Ubiquitination | GRAFISPKTIEDYYF CCCEECCCCHHHHHC | 56.17 | 23749301 | |
77 | Phosphorylation | RAFISPKTIEDYYFG CCEECCCCHHHHHCC | 32.74 | 28889911 | |
103 | Phosphorylation | GLRPGNRYDSSTDLQ CCCCCCCCCCCCCHH | 24.95 | 22369663 | |
105 | Phosphorylation | RPGNRYDSSTDLQAG CCCCCCCCCCCHHHH | 26.63 | 22369663 | |
106 | Phosphorylation | PGNRYDSSTDLQAGR CCCCCCCCCCHHHHH | 24.04 | 22369663 | |
107 | Phosphorylation | GNRYDSSTDLQAGRA CCCCCCCCCHHHHHH | 44.68 | 22369663 | |
167 | Phosphorylation | FEEPGKMTSDVEYIN CCCCCCCCCCCEECC | 25.84 | 21551504 | |
168 | Phosphorylation | EEPGKMTSDVEYINN CCCCCCCCCCEECCC | 35.84 | 21551504 | |
178 | Phosphorylation | EYINNEDSENEDDDS EECCCCCCCCCCCCC | 35.82 | 21551504 | |
191 | Phosphorylation | DSQNSPSTDHSLSSN CCCCCCCCCCCCCCC | 40.91 | 21551504 | |
217 | Phosphorylation | VDEEAQQSPDLTKIK ECHHHHHCCCCHHHH | 14.33 | 22369663 | |
221 | Phosphorylation | AQQSPDLTKIKRVCI HHHCCCCHHHHHHHH | 37.80 | 22369663 | |
253 | Phosphorylation | TIGKVELSVSEGNES EEEEEEEEECCCCCC | 15.30 | 27017623 | |
255 | Phosphorylation | GKVELSVSEGNESKE EEEEEEECCCCCCCE | 36.09 | 28889911 | |
260 | Phosphorylation | SVSEGNESKEISVDV EECCCCCCCEEEEEC | 39.32 | 24961812 | |
264 | Phosphorylation | GNESKEISVDVPNKG CCCCCEEEEECCCCC | 17.23 | 28889911 | |
292 | Phosphorylation | VLHGMHTSDSDNDEL HHCCCCCCCCCCCCC | 22.04 | 28889911 | |
294 | Phosphorylation | HGMHTSDSDNDELDY CCCCCCCCCCCCCCE | 37.77 | 28889911 | |
334 | Phosphorylation | YVGQRHNSRADNNLL CCCHHCCCCCCCCCC | 23.79 | 17563356 | |
343 | Phosphorylation | ADNNLLPSPSPQLTE CCCCCCCCCCCCCCC | 37.67 | 22369663 | |
345 | Phosphorylation | NNLLPSPSPQLTEDI CCCCCCCCCCCCCCC | 29.61 | 22369663 | |
349 | Phosphorylation | PSPSPQLTEDIKCLS CCCCCCCCCCCEEEE | 26.77 | 22369663 | |
353 | Ubiquitination | PQLTEDIKCLSINGT CCCCCCCEEEEECCE | 41.25 | 23749301 | |
356 | Phosphorylation | TEDIKCLSINGTKTF CCCCEEEEECCEEEE | 24.39 | 30377154 | |
372 | Phosphorylation | GNNDNLPSPASEELE CCCCCCCCCCHHHHH | 35.94 | 19795423 | |
375 | Phosphorylation | DNLPSPASEELEFGF CCCCCCCHHHHHCCC | 34.68 | 19795423 | |
521 | Ubiquitination | KHDTERFKTFETKSL CCCHHHHHEEECCCC | 59.53 | 23749301 | |
616 | Phosphorylation | SRNNDRLTFPPLDPH CCCCCCCCCCCCCCC | 34.68 | 27017623 | |
662 | Phosphorylation | IKKTKWSSPNYSLID HHHCCCCCCCCHHHH | 18.95 | 28889911 | |
665 | Phosphorylation | TKWSSPNYSLIDQLM CCCCCCCCHHHHHHH | 14.29 | 28889911 | |
666 | Phosphorylation | KWSSPNYSLIDQLMR CCCCCCCHHHHHHHH | 26.03 | 28889911 | |
735 | Phosphorylation | LEKLGWKSGEGLGIQ HHHHCCCCCCCCCCC | 35.25 | 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 SQS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SQS1_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 SQS1_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-105; SER-106; SER-217;SER-255; SER-334; SER-343; SER-345 AND SER-372, AND MASS SPECTROMETRY. | |
"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-105; SER-334 ANDSER-343, AND MASS SPECTROMETRY. | |
"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-343 AND SER-345, ANDMASS SPECTROMETRY. |