UniProt ID | PSK2_YEAST | |
---|---|---|
UniProt AC | Q08217 | |
Protein Name | Serine/threonine-protein kinase PSK2 | |
Gene Name | PSK2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1101 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Serine/threonine-protein kinase involved in the control of sugar metabolism and translation. Phosphorylates UGP1, which is required for normal glycogen and beta-(1,6)-glucan synthesis. This phosphorylation shifts glucose partitioning toward cell wall glucan synthesis at the expense of glycogen synthesis. Phosphorylates also the glycogen synthase GSY2 and the translation factors CAF20, TIF11 and SRO9.. | |
Protein Sequence | MTYPVSAAAPADISYSKNTPLVGLSKPPCLYQHASSSVDSFSSTFSDDDRSDLVAVPNESPHAFSYNPISPNSLGVRLTILRRSLEIMVNSPDILHELKKKAPVIAYPPSLRHTRNLTETATLSASRDPLNGSLISPLVSNMPSPASRPVIQRATSLMVLPDNDTASKLNPAKSELENLLFLLNLALENNSFERASDLHMLSLLNIKKINFDSDIQKSETLKKVLLDSLAEPFFENYKKFPHKDLGSKSQYNEYEEKHDDIVSLADIKPQQDYSRILHPFTSAKNSGPEAIFTCSQQYPWNFKAANDLACLTFGISKNVIKALTLLDLIHTDSRNFVLEKIMNAEDDNQEIVFTGETIPIVQPNSTSNNNVPNLIWASLWAKRKNGLLVCVFEKTPCDYIDVMLNLRDFSVDSIIDTTHFLENFDKKKQQESTSPMTEKKTVKFANEIHDIGSVSHSLSKLIDDVRFGKVFSADDDLLPLSIRVANHVNEERYFTLNCLSENIPCAVTTSVLENEIKLKIHSLPYQAGLFIVDSHTLSLLSFNKSVAKNMFGLRLHELAGSSVTKLVPSLADMISYINKTYPMLNITLPENKGLVLTEHFFRKIEAEMHHDKDSFYTSIGLDGCHKDGNLIKVDVQLRVLNTNAVLLWITHSRDVVIENYTTVPSQLPMLKENEIDVVGSRGSSSASSKKSSEKIPVNTLKAMADLSISSAETISNSDDEVDLNQVNEKLRETSCGKVRGIESNDNNNYDDDMTMVDDPELKHKIELTKMYTQDKSKFVKDDNFKVDEKFIMRIIEPINGEEIKKETNELDKRNSTLKATYLTTPEANIGSQKRIKKFSDFTILQVMGEGAYGKVNLCIHNREHYIVVIKMIFKERILVDTWVRDRKLGTIPSEIQIMATLNKNSQENILKLLDFFEDDDYYYIETPVHGETGSIDLFDVIEFKKDMVEHEAKLVFKQVVASIKHLHDQGIVHRDIKDENVIVDSHGFVKLIDFGSAAYIKSGPFDVFVGTMDYAAPEVLGGSSYKGKPQDIWALGVLLYTIIYKENPYYNIDEILEGELRFDKSEHVSEECISLIKRILTREVDKRPTIDEIYEDKWLKI | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MTYPVSAAA ------CCCCCCCCC | 48.08 | 24909858 | |
3 | Phosphorylation | -----MTYPVSAAAP -----CCCCCCCCCC | 17.31 | 26447709 | |
6 | Phosphorylation | --MTYPVSAAAPADI --CCCCCCCCCCCCC | 14.00 | 24909858 | |
14 | Phosphorylation | AAAPADISYSKNTPL CCCCCCCCCCCCCCC | 24.73 | 30377154 | |
16 | Phosphorylation | APADISYSKNTPLVG CCCCCCCCCCCCCCC | 16.79 | 30377154 | |
118 | Phosphorylation | LRHTRNLTETATLSA CCCCCCCCCCEEEEC | 34.53 | 20489023 | |
124 | Phosphorylation | LTETATLSASRDPLN CCCCEEEECCCCCCC | 21.61 | 21440633 | |
155 | Phosphorylation | RPVIQRATSLMVLPD CCHHHHCCEEEECCC | 25.28 | 22369663 | |
156 | Phosphorylation | PVIQRATSLMVLPDN CHHHHCCEEEECCCC | 17.30 | 22369663 | |
222 | Ubiquitination | IQKSETLKKVLLDSL CCCCHHHHHHHHHHH | 48.53 | 15699485 | |
223 | Ubiquitination | QKSETLKKVLLDSLA CCCHHHHHHHHHHHH | 41.02 | 15699485 | |
263 | Phosphorylation | EKHDDIVSLADIKPQ HHHCCCCCHHHCCCC | 20.41 | 28889911 | |
433 | Phosphorylation | KKKQQESTSPMTEKK HHHHHHCCCCCCCHH | 35.78 | 27717283 | |
434 | Phosphorylation | KKQQESTSPMTEKKT HHHHHCCCCCCCHHH | 23.19 | 17563356 | |
437 | Phosphorylation | QESTSPMTEKKTVKF HHCCCCCCCHHHHHH | 48.30 | 30377154 | |
453 | Phosphorylation | NEIHDIGSVSHSLSK HHHHCHHHHHHHHHH | 22.30 | 21551504 | |
455 | Phosphorylation | IHDIGSVSHSLSKLI HHCHHHHHHHHHHHH | 14.73 | 21551504 | |
457 | Phosphorylation | DIGSVSHSLSKLIDD CHHHHHHHHHHHHHH | 27.17 | 21551504 | |
680 | Phosphorylation | NEIDVVGSRGSSSAS CCEEEECCCCCCCCC | 23.12 | 22369663 | |
683 | Phosphorylation | DVVGSRGSSSASSKK EEECCCCCCCCCCCC | 21.73 | 20377248 | |
684 | Phosphorylation | VVGSRGSSSASSKKS EECCCCCCCCCCCCC | 32.52 | 20377248 | |
685 | Phosphorylation | VGSRGSSSASSKKSS ECCCCCCCCCCCCCC | 33.59 | 21551504 | |
687 | Phosphorylation | SRGSSSASSKKSSEK CCCCCCCCCCCCCCC | 44.64 | 20377248 | |
688 | Phosphorylation | RGSSSASSKKSSEKI CCCCCCCCCCCCCCC | 43.76 | 21440633 | |
692 | Phosphorylation | SASSKKSSEKIPVNT CCCCCCCCCCCCHHH | 52.36 | 25752575 | |
699 | Phosphorylation | SEKIPVNTLKAMADL CCCCCHHHHHHHHHC | 29.84 | 20377248 | |
717 | Phosphorylation | SAETISNSDDEVDLN CCHHHCCCCCCCCHH | 39.38 | 27214570 | |
985 | Phosphorylation | DENVIVDSHGFVKLI CCCEEECCCCEEEEE | 18.02 | 28889911 | |
1024 | Phosphorylation | PEVLGGSSYKGKPQD CHHHCCCCCCCCHHH | 33.85 | 19779198 | |
1025 | Phosphorylation | EVLGGSSYKGKPQDI HHHCCCCCCCCHHHH | 26.00 | 19779198 | |
1065 | Phosphorylation | GELRFDKSEHVSEEC CCCCCCCCCCCCHHH | 34.48 | 19779198 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of PSK2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of PSK2_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 PSK2_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 THR-118; THR-155; SER-156;SER-680; SER-692 AND SER-717, 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-434, AND MASSSPECTROMETRY. |