UniProt ID | KPR5_YEAST | |
---|---|---|
UniProt AC | Q12265 | |
Protein Name | Ribose-phosphate pyrophosphokinase 5 | |
Gene Name | PRS5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 496 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5).. | |
Protein Sequence | MSMSNIVVFGGDSHPELVTKICENLDIHPSKVELGKFSNGETNIALRESVREKDVYIIQSGCGQVNDTFMQLLILISACKSASASRVTAVMPYLCYSRQPDIPYTAKGAPIISKPKENYTFESHPGTPVSSSLMTQRPGAESSLKSLDSAIRSTINLENPQPIRTPNSSATANNNFDIKKTLSFSRIPMIPGGKLQNTSNSTDAGELFNAQNAGYKLWVVQAGTLIAHLLSAAGADHVITMDLHDPQFPGFFDIPVDNLYCKPIAQNYIQHRIPDYQDAVIVSPDAGGAKRATAIADALELSFALIHKERRSQLLKGPPDATLTSGGSLPVSPRPLVTTLVSSQNTTSSGATGVAALEMKKTTSTSSTSSQSSNSSKFVQTTMLVGDVRNKVCIIVDDLVDTSYTITRAAKLLKDQGSTKVYALITHGVFSGDALERIGQSSIDKLIISNTVPQDRTLQYLGKDRVDVIDVSCIIGEAIRRIHNGESISMLFEHGW | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSMSNIVVF ------CCCCCEEEE | 30.80 | 30377154 | |
4 | Phosphorylation | ----MSMSNIVVFGG ----CCCCCEEEECC | 18.98 | 30377154 | |
13 | Phosphorylation | IVVFGGDSHPELVTK EEEECCCCCHHHHHH | 44.19 | 30377154 | |
31 | Acetylation | NLDIHPSKVELGKFS CCCCCHHHEEEECCC | 44.15 | 24489116 | |
36 | Acetylation | PSKVELGKFSNGETN HHHEEEECCCCCCCE | 59.24 | 24489116 | |
36 | Ubiquitination | PSKVELGKFSNGETN HHHEEEECCCCCCCE | 59.24 | 24961812 | |
81 | Phosphorylation | ILISACKSASASRVT HHHHHHHCCCCHHHE | 27.60 | 30377154 | |
83 | Phosphorylation | ISACKSASASRVTAV HHHHHCCCCHHHEEH | 33.59 | 30377154 | |
85 | Phosphorylation | ACKSASASRVTAVMP HHHCCCCHHHEEHHH | 25.45 | 30377154 | |
93 | Phosphorylation | RVTAVMPYLCYSRQP HHEEHHHHHHHCCCC | 7.42 | 30377154 | |
96 | Phosphorylation | AVMPYLCYSRQPDIP EHHHHHHHCCCCCCC | 12.32 | 30377154 | |
97 | Phosphorylation | VMPYLCYSRQPDIPY HHHHHHHCCCCCCCC | 24.36 | 30377154 | |
107 | Acetylation | PDIPYTAKGAPIISK CCCCCCCCCCCCCCC | 48.05 | 24489116 | |
119 | Phosphorylation | ISKPKENYTFESHPG CCCCCCCCEECCCCC | 17.56 | 22369663 | |
120 | Phosphorylation | SKPKENYTFESHPGT CCCCCCCEECCCCCC | 32.29 | 22369663 | |
123 | Phosphorylation | KENYTFESHPGTPVS CCCCEECCCCCCCCC | 30.69 | 22369663 | |
127 | Phosphorylation | TFESHPGTPVSSSLM EECCCCCCCCCCCHH | 25.60 | 22369663 | |
130 | Phosphorylation | SHPGTPVSSSLMTQR CCCCCCCCCCHHCCC | 18.53 | 22369663 | |
131 | Phosphorylation | HPGTPVSSSLMTQRP CCCCCCCCCHHCCCC | 27.94 | 22369663 | |
132 | Phosphorylation | PGTPVSSSLMTQRPG CCCCCCCCHHCCCCC | 18.04 | 20377248 | |
135 | Phosphorylation | PVSSSLMTQRPGAES CCCCCHHCCCCCCHH | 27.07 | 22369663 | |
142 | Phosphorylation | TQRPGAESSLKSLDS CCCCCCHHHHHHHHH | 40.20 | 22369663 | |
143 | Phosphorylation | QRPGAESSLKSLDSA CCCCCHHHHHHHHHH | 31.18 | 22369663 | |
145 | Ubiquitination | PGAESSLKSLDSAIR CCCHHHHHHHHHHHH | 51.42 | 24961812 | |
146 | Phosphorylation | GAESSLKSLDSAIRS CCHHHHHHHHHHHHH | 42.58 | 22369663 | |
149 | Phosphorylation | SSLKSLDSAIRSTIN HHHHHHHHHHHHHCC | 30.78 | 22369663 | |
153 | Phosphorylation | SLDSAIRSTINLENP HHHHHHHHHCCCCCC | 27.76 | 29136822 | |
154 | Phosphorylation | LDSAIRSTINLENPQ HHHHHHHHCCCCCCC | 12.20 | 29136822 | |
165 | Phosphorylation | ENPQPIRTPNSSATA CCCCCCCCCCCCCCC | 27.78 | 29136822 | |
168 | Phosphorylation | QPIRTPNSSATANNN CCCCCCCCCCCCCCC | 23.66 | 29136822 | |
169 | Phosphorylation | PIRTPNSSATANNNF CCCCCCCCCCCCCCC | 35.96 | 29136822 | |
171 | Phosphorylation | RTPNSSATANNNFDI CCCCCCCCCCCCCCC | 31.69 | 29136822 | |
181 | Phosphorylation | NNFDIKKTLSFSRIP CCCCCEEEEEECCCC | 23.72 | 22369663 | |
183 | Phosphorylation | FDIKKTLSFSRIPMI CCCEEEEEECCCCEE | 26.80 | 22369663 | |
185 | Phosphorylation | IKKTLSFSRIPMIPG CEEEEEECCCCEECC | 26.40 | 25521595 | |
194 | Acetylation | IPMIPGGKLQNTSNS CCEECCCCCCCCCCC | 53.46 | 24489116 | |
194 | Ubiquitination | IPMIPGGKLQNTSNS CCEECCCCCCCCCCC | 53.46 | 23749301 | |
198 | Phosphorylation | PGGKLQNTSNSTDAG CCCCCCCCCCCCCHH | 19.14 | 30377154 | |
199 | Phosphorylation | GGKLQNTSNSTDAGE CCCCCCCCCCCCHHH | 36.01 | 30377154 | |
201 | Phosphorylation | KLQNTSNSTDAGELF CCCCCCCCCCHHHHH | 27.68 | 30377154 | |
202 | Phosphorylation | LQNTSNSTDAGELFN CCCCCCCCCHHHHHH | 33.83 | 30377154 | |
290 | Ubiquitination | SPDAGGAKRATAIAD CCCCCCHHHHHHHHH | 45.93 | 23749301 | |
322 | Phosphorylation | LKGPPDATLTSGGSL HCCCCCCEECCCCCC | 37.64 | 26447709 | |
324 | Phosphorylation | GPPDATLTSGGSLPV CCCCCEECCCCCCCC | 22.44 | 30377154 | |
325 | Phosphorylation | PPDATLTSGGSLPVS CCCCEECCCCCCCCC | 44.24 | 20377248 | |
328 | Phosphorylation | ATLTSGGSLPVSPRP CEECCCCCCCCCCCC | 32.78 | 21440633 | |
332 | Phosphorylation | SGGSLPVSPRPLVTT CCCCCCCCCCCCEEE | 17.16 | 24961812 | |
338 | Phosphorylation | VSPRPLVTTLVSSQN CCCCCCEEEEECCCC | 23.30 | 20377248 | |
343 | Phosphorylation | LVTTLVSSQNTTSSG CEEEEECCCCCCCCC | 21.70 | 30377154 | |
346 | Phosphorylation | TLVSSQNTTSSGATG EEECCCCCCCCCCCE | 22.03 | 20377248 | |
347 | Phosphorylation | LVSSQNTTSSGATGV EECCCCCCCCCCCEE | 28.57 | 21551504 | |
349 | Phosphorylation | SSQNTTSSGATGVAA CCCCCCCCCCCEEEE | 30.29 | 21440633 | |
362 | Phosphorylation | AALEMKKTTSTSSTS EEEEEEEECCCCCCC | 22.06 | 19823750 | |
363 | Phosphorylation | ALEMKKTTSTSSTSS EEEEEEECCCCCCCC | 38.60 | 19823750 | |
364 | Phosphorylation | LEMKKTTSTSSTSSQ EEEEEECCCCCCCCC | 31.37 | 16445868 | |
365 | Phosphorylation | EMKKTTSTSSTSSQS EEEEECCCCCCCCCC | 25.30 | 28889911 | |
366 | Phosphorylation | MKKTTSTSSTSSQSS EEEECCCCCCCCCCC | 31.24 | 21440633 | |
367 | Phosphorylation | KKTTSTSSTSSQSSN EEECCCCCCCCCCCC | 32.18 | 16445868 | |
368 | Phosphorylation | KTTSTSSTSSQSSNS EECCCCCCCCCCCCC | 31.97 | 27214570 | |
369 | Phosphorylation | TTSTSSTSSQSSNSS ECCCCCCCCCCCCCC | 28.47 | 16445868 | |
370 | Phosphorylation | TSTSSTSSQSSNSSK CCCCCCCCCCCCCCC | 33.88 | 27214570 | |
372 | Phosphorylation | TSSTSSQSSNSSKFV CCCCCCCCCCCCCEE | 33.17 | 28889911 | |
373 | Phosphorylation | SSTSSQSSNSSKFVQ CCCCCCCCCCCCEEE | 32.85 | 27214570 | |
414 | Acetylation | TRAAKLLKDQGSTKV HHHHHHHHHCCCCEE | 59.44 | 24489116 | |
420 | Ubiquitination | LKDQGSTKVYALITH HHHCCCCEEEEEEEC | 34.64 | 17644757 | |
445 | Ubiquitination | IGQSSIDKLIISNTV HCCCCCCEEEECCCC | 39.66 | 23749301 | |
445 | Acetylation | IGQSSIDKLIISNTV HCCCCCCEEEECCCC | 39.66 | 24489116 | |
449 | Phosphorylation | SIDKLIISNTVPQDR CCCEEEECCCCCCCC | 21.32 | 30377154 |
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 KPR5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KPR5_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 KPR5_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-123; THR-127; THR-154;THR-165; SER-328 AND SER-332, 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-123 AND THR-127, ANDMASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-185, ANDMASS 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 TYR-119; THR-120; SER-123AND THR-127, AND MASS SPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-367 ANDSER-369, AND MASS SPECTROMETRY. |