| UniProt ID | RS2_YEAST | |
|---|---|---|
| UniProt AC | P25443 | |
| Protein Name | 40S ribosomal protein S2 {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPS2 {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 254 | |
| Subcellular Localization | Cytoplasm . Nucleus, nucleolus . | |
| 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. [PubMed: 22096102 uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly] | |
| Protein Sequence | MSAPEAQQQKRGGFGGRNRGRPNRRGPRNTEEKGWVPVTKLGRLVKAGKITTIEEIFLHSLPVKEFQIIDTLLPGLQDEVMNIKPVQKQTRAGQRTRFKAVVVVGDSNGHVGLGIKTAKEVAGAIRAGIIIAKLSVIPIRRGYWGTNLGQPHSLATKTTGKCGSVTVRLIPAPRGSGIVASPAVKKLLQLAGVEDVYTQSNGKTRTLENTLKAAFVAIGNTYGFLTPNLWAEQPLPVSPLDIYSDEASAQKKRF | |
| 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 | ------MSAPEAQQQ ------CCCHHHHHH | 53.16 | 22369663 | |
| 2 | Acetylation | ------MSAPEAQQQ ------CCCHHHHHH | 53.16 | 10601260 | |
| 10 | Succinylation | APEAQQQKRGGFGGR CHHHHHHHCCCCCCC | 48.98 | 23954790 | |
| 10 | Acetylation | APEAQQQKRGGFGGR CHHHHHHHCCCCCCC | 48.98 | 22865919 | |
| 11 | Asymmetric dimethylarginine | PEAQQQKRGGFGGRN HHHHHHHCCCCCCCC | 46.24 | - | |
| 11 | Methylation | PEAQQQKRGGFGGRN HHHHHHHCCCCCCCC | 46.24 | 20035717 | |
| 30 | Phosphorylation | NRRGPRNTEEKGWVP CCCCCCCCCCCCCEE | 46.96 | 27214570 | |
| 33 | Ubiquitination | GPRNTEEKGWVPVTK CCCCCCCCCCEEHHH | 52.41 | 23749301 | |
| 33 | Succinylation | GPRNTEEKGWVPVTK CCCCCCCCCCEEHHH | 52.41 | 23954790 | |
| 33 | Acetylation | GPRNTEEKGWVPVTK CCCCCCCCCCEEHHH | 52.41 | 24489116 | |
| 39 | Phosphorylation | EKGWVPVTKLGRLVK CCCCEEHHHHHHHHC | 17.93 | 21440633 | |
| 40 | Ubiquitination | KGWVPVTKLGRLVKA CCCEEHHHHHHHHCC | 49.53 | 24961812 | |
| 40 | Acetylation | KGWVPVTKLGRLVKA CCCEEHHHHHHHHCC | 49.53 | 24489116 | |
| 40 | 2-Hydroxyisobutyrylation | KGWVPVTKLGRLVKA CCCEEHHHHHHHHCC | 49.53 | - | |
| 46 | 2-Hydroxyisobutyrylation | TKLGRLVKAGKITTI HHHHHHHCCCCCEEH | 56.89 | - | |
| 49 | Ubiquitination | GRLVKAGKITTIEEI HHHHCCCCCEEHHHH | 41.56 | 24961812 | |
| 60 | Phosphorylation | IEEIFLHSLPVKEFQ HHHHHHHCCCCCCEE | 36.19 | 21440633 | |
| 64 | Ubiquitination | FLHSLPVKEFQIIDT HHHCCCCCCEEHHHH | 51.36 | 17644757 | |
| 84 | Ubiquitination | QDEVMNIKPVQKQTR CHHHHCCCCCCCCCC | 33.85 | 24961812 | |
| 84 | Succinylation | QDEVMNIKPVQKQTR CHHHHCCCCCCCCCC | 33.85 | 23954790 | |
| 99 | Ubiquitination | AGQRTRFKAVVVVGD CCCCCEEEEEEEECC | 36.66 | 17644757 | |
| 116 | Ubiquitination | GHVGLGIKTAKEVAG CCEECCHHHHHHHHH | 40.40 | 17644757 | |
| 119 | Acetylation | GLGIKTAKEVAGAIR ECCHHHHHHHHHHHH | 58.93 | 22865919 | |
| 119 | Ubiquitination | GLGIKTAKEVAGAIR ECCHHHHHHHHHHHH | 58.93 | 23749301 | |
| 119 | 2-Hydroxyisobutyrylation | GLGIKTAKEVAGAIR ECCHHHHHHHHHHHH | 58.93 | - | |
| 119 | Succinylation | GLGIKTAKEVAGAIR ECCHHHHHHHHHHHH | 58.93 | 23954790 | |
| 133 | Ubiquitination | RAGIIIAKLSVIPIR HHCEEEEEEEEEEEC | 30.77 | 17644757 | |
| 133 | Acetylation | RAGIIIAKLSVIPIR HHCEEEEEEEEEEEC | 30.77 | 24489116 | |
| 135 | Phosphorylation | GIIIAKLSVIPIRRG CEEEEEEEEEEECCC | 19.79 | 28889911 | |
| 143 | Phosphorylation | VIPIRRGYWGTNLGQ EEEECCCCCCCCCCC | 10.00 | 21440633 | |
| 146 | Phosphorylation | IRRGYWGTNLGQPHS ECCCCCCCCCCCCCC | 17.08 | 23749301 | |
| 153 | Phosphorylation | TNLGQPHSLATKTTG CCCCCCCCCCCCCCC | 26.78 | 21440633 | |
| 156 | Phosphorylation | GQPHSLATKTTGKCG CCCCCCCCCCCCCCC | 33.93 | 28889911 | |
| 157 | 2-Hydroxyisobutyrylation | QPHSLATKTTGKCGS CCCCCCCCCCCCCCE | 38.18 | - | |
| 157 | Acetylation | QPHSLATKTTGKCGS CCCCCCCCCCCCCCE | 38.18 | 24489116 | |
| 157 | Ubiquitination | QPHSLATKTTGKCGS CCCCCCCCCCCCCCE | 38.18 | 17644757 | |
| 161 | Ubiquitination | LATKTTGKCGSVTVR CCCCCCCCCCEEEEE | 33.07 | 23749301 | |
| 164 | Phosphorylation | KTTGKCGSVTVRLIP CCCCCCCEEEEEEEE | 24.88 | 30377154 | |
| 166 | Phosphorylation | TGKCGSVTVRLIPAP CCCCCEEEEEEEECC | 11.12 | 21440633 | |
| 176 | Phosphorylation | LIPAPRGSGIVASPA EEECCCCCCCCCCHH | 26.99 | 22369663 | |
| 181 | Phosphorylation | RGSGIVASPAVKKLL CCCCCCCCHHHHHHH | 11.51 | 22369663 | |
| 185 | Ubiquitination | IVASPAVKKLLQLAG CCCCHHHHHHHHHHC | 39.55 | 23749301 | |
| 185 | Succinylation | IVASPAVKKLLQLAG CCCCHHHHHHHHHHC | 39.55 | 23954790 | |
| 186 | Ubiquitination | VASPAVKKLLQLAGV CCCHHHHHHHHHHCC | 48.07 | 23749301 | |
| 186 | 2-Hydroxyisobutyrylation | VASPAVKKLLQLAGV CCCHHHHHHHHHHCC | 48.07 | - | |
| 186 | Acetylation | VASPAVKKLLQLAGV CCCHHHHHHHHHHCC | 48.07 | 24489116 | |
| 203 | Ubiquitination | VYTQSNGKTRTLENT EEECCCCCEEEHHHH | 38.80 | 24961812 | |
| 203 | Acetylation | VYTQSNGKTRTLENT EEECCCCCEEEHHHH | 38.80 | 24489116 | |
| 206 | Phosphorylation | QSNGKTRTLENTLKA CCCCCEEEHHHHHHH | 43.59 | 21440633 | |
| 238 | Phosphorylation | AEQPLPVSPLDIYSD CCCCCCCCCCCCCCC | 20.15 | 24961812 | |
| 244 | Phosphorylation | VSPLDIYSDEASAQK CCCCCCCCCHHHHHH | 29.34 | 28889911 | |
| 248 | Phosphorylation | DIYSDEASAQKKRF- CCCCCHHHHHHHCC- | 29.23 | 24961812 | |
| 251 | Ubiquitination | SDEASAQKKRF---- CCHHHHHHHCC---- | 45.71 | 24961812 | |
| 252 | Ubiquitination | DEASAQKKRF----- CHHHHHHHCC----- | 47.13 | 24961812 |
| 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 RS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS2_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 RS2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "The action of N-terminal acetyltransferases on yeast ribosomalproteins."; Arnold R.J., Polevoda B., Reilly J.P., Sherman F.; J. Biol. Chem. 274:37035-37040(1999). Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA. | |
| "NH2-terminal acetylation of ribosomal proteins of Saccharomycescerevisiae."; Takakura H., Tsunasawa S., Miyagi M., Warner J.R.; J. Biol. Chem. 267:5442-5445(1992). Cited for: PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT SER-2. | |
| 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-181 AND SER-244, ANDMASS SPECTROMETRY. | |
