UniProt ID | RL3_YEAST | |
---|---|---|
UniProt AC | P14126 | |
Protein Name | 60S ribosomal protein L3 {ECO:0000303|PubMed:9559554} | |
Gene Name | RPL3 {ECO:0000303|PubMed:9559554} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 387 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL3 plays a role in coordinating processes of accommodating the aminoacyl-tRNA in the PTC.. | |
Protein Sequence | MSHRKYEAPRHGHLGFLPRKRAASIRARVKAFPKDDRSKPVALTSFLGYKAGMTTIVRDLDRPGSKFHKREVVEAVTVVDTPPVVVVGVVGYVETPRGLRSLTTVWAEHLSDEVKRRFYKNWYKSKKKAFTKYSAKYAQDGAGIERELARIKKYASVVRVLVHTQIRKTPLAQKKAHLAEIQLNGGSISEKVDWAREHFEKTVAVDSVFEQNEMIDAIAVTKGHGFEGVTHRWGTKKLPRKTHRGLRKVACIGAWHPAHVMWSVARAGQRGYHSRTSINHKIYRVGKGDDEANGATSFDRTKKTITPMGGFVHYGEIKNDFIMVKGCIPGNRKRIVTLRKSLYTNTSRKALEEVSLKWIDTASKFGKGRFQTPAEKHAFMGTLKKDL | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MSHRKYEAPRHGH --CCCCCCCCCCCCC | 19.78 | 25533186 | |
20 | Ubiquitination | HLGFLPRKRAASIRA CCCCCCCHHHHHHHH | 44.44 | 17644757 | |
24 | Phosphorylation | LPRKRAASIRARVKA CCCHHHHHHHHHHHC | 16.18 | 24909858 | |
30 | Ubiquitination | ASIRARVKAFPKDDR HHHHHHHHCCCCCCC | 38.46 | 22817900 | |
34 | Ubiquitination | ARVKAFPKDDRSKPV HHHHCCCCCCCCCCC | 66.85 | 23749301 | |
38 | Phosphorylation | AFPKDDRSKPVALTS CCCCCCCCCCCEEHH | 48.59 | 21440633 | |
39 | Acetylation | FPKDDRSKPVALTSF CCCCCCCCCCEEHHH | 44.39 | 24489116 | |
39 | Ubiquitination | FPKDDRSKPVALTSF CCCCCCCCCCEEHHH | 44.39 | 23749301 | |
44 | Phosphorylation | RSKPVALTSFLGYKA CCCCCEEHHHHCHHC | 14.01 | 23749301 | |
45 | Phosphorylation | SKPVALTSFLGYKAG CCCCEEHHHHCHHCC | 21.23 | 21440633 | |
49 | Phosphorylation | ALTSFLGYKAGMTTI EEHHHHCHHCCCEEE | 10.38 | 28889911 | |
50 | Ubiquitination | LTSFLGYKAGMTTIV EHHHHCHHCCCEEEE | 36.34 | 23749301 | |
54 | Phosphorylation | LGYKAGMTTIVRDLD HCHHCCCEEEEECCC | 16.68 | 21440633 | |
55 | Phosphorylation | GYKAGMTTIVRDLDR CHHCCCEEEEECCCC | 14.48 | 21440633 | |
65 | Phosphorylation | RDLDRPGSKFHKREV ECCCCCCCCCCCCCE | 34.53 | 21440633 | |
66 | Acetylation | DLDRPGSKFHKREVV CCCCCCCCCCCCCEE | 58.36 | 24489116 | |
95 | Phosphorylation | GVVGYVETPRGLRSL EEEEEECCCCCHHHH | 14.29 | 27214570 | |
101 | Phosphorylation | ETPRGLRSLTTVWAE CCCCCHHHHHHHHHH | 34.80 | 22369663 | |
103 | Phosphorylation | PRGLRSLTTVWAEHL CCCHHHHHHHHHHHC | 22.13 | 22369663 | |
104 | Phosphorylation | RGLRSLTTVWAEHLS CCHHHHHHHHHHHCC | 21.24 | 22369663 | |
115 | 2-Hydroxyisobutyrylation | EHLSDEVKRRFYKNW HHCCHHHHHHHHHHH | 35.49 | - | |
115 | Acetylation | EHLSDEVKRRFYKNW HHCCHHHHHHHHHHH | 35.49 | 24489116 | |
115 | Ubiquitination | EHLSDEVKRRFYKNW HHCCHHHHHHHHHHH | 35.49 | 22817900 | |
120 | Acetylation | EVKRRFYKNWYKSKK HHHHHHHHHHHHHHH | 37.99 | 24489116 | |
120 | Ubiquitination | EVKRRFYKNWYKSKK HHHHHHHHHHHHHHH | 37.99 | 23749301 | |
124 | Ubiquitination | RFYKNWYKSKKKAFT HHHHHHHHHHHHHHH | 47.62 | 22817900 | |
127 | Ubiquitination | KNWYKSKKKAFTKYS HHHHHHHHHHHHHHH | 57.32 | 22817900 | |
128 | Ubiquitination | NWYKSKKKAFTKYSA HHHHHHHHHHHHHHH | 53.09 | 22817900 | |
131 | Phosphorylation | KSKKKAFTKYSAKYA HHHHHHHHHHHHHHH | 33.65 | 23749301 | |
132 | 2-Hydroxyisobutyrylation | SKKKAFTKYSAKYAQ HHHHHHHHHHHHHHH | 30.65 | - | |
132 | Acetylation | SKKKAFTKYSAKYAQ HHHHHHHHHHHHHHH | 30.65 | 24489116 | |
132 | Ubiquitination | SKKKAFTKYSAKYAQ HHHHHHHHHHHHHHH | 30.65 | 22817900 | |
134 | Phosphorylation | KKAFTKYSAKYAQDG HHHHHHHHHHHHHCC | 21.60 | 23749301 | |
136 | 2-Hydroxyisobutyrylation | AFTKYSAKYAQDGAG HHHHHHHHHHHCCCC | 34.87 | - | |
136 | Acetylation | AFTKYSAKYAQDGAG HHHHHHHHHHHCCCC | 34.87 | 24489116 | |
136 | Succinylation | AFTKYSAKYAQDGAG HHHHHHHHHHHCCCC | 34.87 | 23954790 | |
136 | Ubiquitination | AFTKYSAKYAQDGAG HHHHHHHHHHHCCCC | 34.87 | 23749301 | |
152 | Ubiquitination | ERELARIKKYASVVR HHHHHHHHHHHHHHH | 33.89 | 22817900 | |
153 | Acetylation | RELARIKKYASVVRV HHHHHHHHHHHHHHH | 43.61 | 25381059 | |
153 | Ubiquitination | RELARIKKYASVVRV HHHHHHHHHHHHHHH | 43.61 | 23749301 | |
156 | Phosphorylation | ARIKKYASVVRVLVH HHHHHHHHHHHHHHH | 20.32 | 17287358 | |
164 | Phosphorylation | VVRVLVHTQIRKTPL HHHHHHHHCCCCCCH | 20.43 | 17287358 | |
168 | Ubiquitination | LVHTQIRKTPLAQKK HHHHCCCCCCHHHHH | 57.00 | 23749301 | |
174 | 2-Hydroxyisobutyrylation | RKTPLAQKKAHLAEI CCCCHHHHHHHEEEE | 46.44 | - | |
174 | Succinylation | RKTPLAQKKAHLAEI CCCCHHHHHHHEEEE | 46.44 | 23954790 | |
174 | Ubiquitination | RKTPLAQKKAHLAEI CCCCHHHHHHHEEEE | 46.44 | 17644757 | |
175 | Ubiquitination | KTPLAQKKAHLAEIQ CCCHHHHHHHEEEEE | 29.03 | 17644757 | |
187 | Phosphorylation | EIQLNGGSISEKVDW EEEECCCCHHHHHHH | 25.08 | 22369663 | |
189 | Phosphorylation | QLNGGSISEKVDWAR EECCCCHHHHHHHHH | 32.82 | 22369663 | |
191 | Acetylation | NGGSISEKVDWAREH CCCCHHHHHHHHHHH | 38.41 | 24489116 | |
191 | Ubiquitination | NGGSISEKVDWAREH CCCCHHHHHHHHHHH | 38.41 | 23749301 | |
201 | Ubiquitination | WAREHFEKTVAVDSV HHHHHHHHHHHHCCH | 47.56 | 23749301 | |
222 | Acetylation | IDAIAVTKGHGFEGV EEEEEEECCCCCCCC | 42.16 | 24489116 | |
222 | Ubiquitination | IDAIAVTKGHGFEGV EEEEEEECCCCCCCC | 42.16 | 23749301 | |
230 | Phosphorylation | GHGFEGVTHRWGTKK CCCCCCCCCCCCCCC | 19.31 | 23749301 | |
236 | Ubiquitination | VTHRWGTKKLPRKTH CCCCCCCCCCCCCCC | 48.66 | 22817900 | |
237 | Ubiquitination | THRWGTKKLPRKTHR CCCCCCCCCCCCCCC | 64.66 | 22817900 | |
241 | Ubiquitination | GTKKLPRKTHRGLRK CCCCCCCCCCCCCHH | 46.90 | 22817900 | |
243 | Methylation | KKLPRKTHRGLRKVA CCCCCCCCCCCHHEE | 25.50 | 20864530 | |
248 | Acetylation | KTHRGLRKVACIGAW CCCCCCHHEEEEECC | 38.95 | 25381059 | |
248 | Ubiquitination | KTHRGLRKVACIGAW CCCCCCHHEEEEECC | 38.95 | 23749301 | |
263 | Phosphorylation | HPAHVMWSVARAGQR CHHHHHHHHHHCCCC | 6.44 | 21440633 | |
281 | 2-Hydroxyisobutyrylation | SRTSINHKIYRVGKG CCCCCCCEEEEECCC | 36.62 | - | |
281 | Acetylation | SRTSINHKIYRVGKG CCCCCCCEEEEECCC | 36.62 | 22865919 | |
281 | Succinylation | SRTSINHKIYRVGKG CCCCCCCEEEEECCC | 36.62 | 23954790 | |
281 | Ubiquitination | SRTSINHKIYRVGKG CCCCCCCEEEEECCC | 36.62 | 23749301 | |
283 | Phosphorylation | TSINHKIYRVGKGDD CCCCCEEEEECCCCC | 12.21 | 19823750 | |
287 | 2-Hydroxyisobutyrylation | HKIYRVGKGDDEANG CEEEEECCCCCCCCC | 57.20 | - | |
287 | Succinylation | HKIYRVGKGDDEANG CEEEEECCCCCCCCC | 57.20 | 23954790 | |
287 | Ubiquitination | HKIYRVGKGDDEANG CEEEEECCCCCCCCC | 57.20 | 23749301 | |
296 | Phosphorylation | DDEANGATSFDRTKK CCCCCCCCCCCCCCC | 31.18 | 22369663 | |
297 | Phosphorylation | DEANGATSFDRTKKT CCCCCCCCCCCCCCE | 25.31 | 22369663 | |
301 | Phosphorylation | GATSFDRTKKTITPM CCCCCCCCCCEEECC | 38.44 | 24961812 | |
302 | Ubiquitination | ATSFDRTKKTITPMG CCCCCCCCCEEECCC | 49.14 | 22817900 | |
303 | 2-Hydroxyisobutyrylation | TSFDRTKKTITPMGG CCCCCCCCEEECCCC | 44.54 | - | |
303 | Acetylation | TSFDRTKKTITPMGG CCCCCCCCEEECCCC | 44.54 | 25381059 | |
303 | Ubiquitination | TSFDRTKKTITPMGG CCCCCCCCEEECCCC | 44.54 | 23749301 | |
304 | Phosphorylation | SFDRTKKTITPMGGF CCCCCCCEEECCCCE | 31.47 | 28889911 | |
306 | Phosphorylation | DRTKKTITPMGGFVH CCCCCEEECCCCEEE | 16.68 | 29688323 | |
314 | Phosphorylation | PMGGFVHYGEIKNDF CCCCEEEEEEEECCE | 15.91 | 29688323 | |
318 | Acetylation | FVHYGEIKNDFIMVK EEEEEEEECCEEEEE | 46.27 | 24489116 | |
318 | Ubiquitination | FVHYGEIKNDFIMVK EEEEEEEECCEEEEE | 46.27 | 23749301 | |
325 | Acetylation | KNDFIMVKGCIPGNR ECCEEEEECCCCCCC | 30.59 | 24489116 | |
325 | Ubiquitination | KNDFIMVKGCIPGNR ECCEEEEECCCCCCC | 30.59 | 22817900 | |
337 | Phosphorylation | GNRKRIVTLRKSLYT CCCHHEEEEHHHHHC | 20.62 | 27017623 | |
340 | Ubiquitination | KRIVTLRKSLYTNTS HHEEEEHHHHHCCCC | 48.18 | 23749301 | |
341 | Phosphorylation | RIVTLRKSLYTNTSR HEEEEHHHHHCCCCH | 21.85 | 19823750 | |
343 | Phosphorylation | VTLRKSLYTNTSRKA EEEHHHHHCCCCHHH | 12.68 | 19823750 | |
344 | Phosphorylation | TLRKSLYTNTSRKAL EEHHHHHCCCCHHHH | 37.00 | 19823750 | |
346 | Phosphorylation | RKSLYTNTSRKALEE HHHHHCCCCHHHHHH | 23.31 | 19823750 | |
347 | Phosphorylation | KSLYTNTSRKALEEV HHHHCCCCHHHHHHC | 33.58 | 21440633 | |
349 | Acetylation | LYTNTSRKALEEVSL HHCCCCHHHHHHCHH | 58.03 | 24489116 | |
349 | Ubiquitination | LYTNTSRKALEEVSL HHCCCCHHHHHHCHH | 58.03 | 23749301 | |
355 | Phosphorylation | RKALEEVSLKWIDTA HHHHHHCHHHHHHCC | 27.75 | 22369663 | |
357 | Acetylation | ALEEVSLKWIDTASK HHHHCHHHHHHCCHH | 34.30 | 24489116 | |
357 | Ubiquitination | ALEEVSLKWIDTASK HHHHCHHHHHHCCHH | 34.30 | 23749301 | |
361 | Phosphorylation | VSLKWIDTASKFGKG CHHHHHHCCHHHCCC | 24.56 | 30377154 | |
363 | Phosphorylation | LKWIDTASKFGKGRF HHHHHCCHHHCCCCC | 30.52 | 23749301 | |
364 | 2-Hydroxyisobutyrylation | KWIDTASKFGKGRFQ HHHHCCHHHCCCCCC | 56.52 | - | |
364 | Acetylation | KWIDTASKFGKGRFQ HHHHCCHHHCCCCCC | 56.52 | 24489116 | |
364 | Ubiquitination | KWIDTASKFGKGRFQ HHHHCCHHHCCCCCC | 56.52 | 23749301 | |
367 | Ubiquitination | DTASKFGKGRFQTPA HCCHHHCCCCCCCHH | 50.47 | 22817900 | |
372 | Phosphorylation | FGKGRFQTPAEKHAF HCCCCCCCHHHHCCC | 23.04 | 23749301 | |
376 | Acetylation | RFQTPAEKHAFMGTL CCCCHHHHCCCHHCC | 42.19 | 24489116 | |
376 | Ubiquitination | RFQTPAEKHAFMGTL CCCCHHHHCCCHHCC | 42.19 | 23749301 | |
382 | Phosphorylation | EKHAFMGTLKKDL-- HHCCCHHCCCCCC-- | 24.50 | 23749301 | |
384 | Acetylation | HAFMGTLKKDL---- CCCHHCCCCCC---- | 44.04 | 24489116 | |
384 | Methylation | HAFMGTLKKDL---- CCCHHCCCCCC---- | 44.04 | 20137074 | |
384 | Succinylation | HAFMGTLKKDL---- CCCHHCCCCCC---- | 44.04 | 23954790 | |
384 | Ubiquitination | HAFMGTLKKDL---- CCCHHCCCCCC---- | 44.04 | 23749301 | |
385 | Ubiquitination | AFMGTLKKDL----- CCHHCCCCCC----- | 68.33 | 17644757 |
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 RL3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
243 | H | Methylation |
| 20864530 |
* 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 RL3_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Methylation | |
Reference | PubMed |
"A novel 3-methylhistidine modification of yeast ribosomal proteinRpl3 is dependent upon the YIL110W methyltransferase."; Webb K.J., Zurita-Lopez C.I., Al-Hadid Q., Laganowsky A., Young B.D.,Lipson R.S., Souda P., Faull K.F., Whitelegge J.P., Clarke S.G.; J. Biol. Chem. 285:37598-37606(2010). Cited for: METHYLATION AT HIS-243. | |
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-95 AND SER-297, AND MASSSPECTROMETRY. | |
"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-297 AND SER-355, 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-24; SER-156; THR-164 ANDSER-297, AND MASS SPECTROMETRY. | |
"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-24, 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 THR-103, AND MASSSPECTROMETRY. |