| UniProt ID | RS11A_YEAST | |
|---|---|---|
| UniProt AC | P0CX47 | |
| Protein Name | 40S ribosomal protein S11-A {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPS11A {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 156 | |
| 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.. | |
| Protein Sequence | MSTELTVQSERAFQKQPHIFNNPKVKTSKRTKRWYKNAGLGFKTPKTAIEGSYIDKKCPFTGLVSIRGKILTGTVVSTKMHRTIVIRRAYLHYIPKYNRYEKRHKNVPVHVSPAFRVQVGDIVTVGQCRPISKTVRFNVVKVSAAAGKANKQFAKF | |
| 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 | ------MSTELTVQS ------CCCEEEHHC | 30.50 | 22369663 | |
| 2 | Acetylation | ------MSTELTVQS ------CCCEEEHHC | 30.50 | 10601260 | |
| 3 | Phosphorylation | -----MSTELTVQSE -----CCCEEEHHCH | 33.44 | 22369663 | |
| 6 | Phosphorylation | --MSTELTVQSERAF --CCCEEEHHCHHHH | 15.40 | 22369663 | |
| 9 | Phosphorylation | STELTVQSERAFQKQ CCEEEHHCHHHHHHC | 25.39 | 24909858 | |
| 15 | Acetylation | QSERAFQKQPHIFNN HCHHHHHHCCCCCCC | 60.38 | 24489116 | |
| 15 | Ubiquitination | QSERAFQKQPHIFNN HCHHHHHHCCCCCCC | 60.38 | 22106047 | |
| 24 | Ubiquitination | PHIFNNPKVKTSKRT CCCCCCCCCCCCHHC | 59.49 | - | |
| 36 | Acetylation | KRTKRWYKNAGLGFK HHCHHHHHHCCCCCC | 33.10 | 24489116 | |
| 36 | Ubiquitination | KRTKRWYKNAGLGFK HHCHHHHHHCCCCCC | 33.10 | - | |
| 43 | Succinylation | KNAGLGFKTPKTAIE HHCCCCCCCCCCCEE | 63.22 | 23954790 | |
| 43 | Ubiquitination | KNAGLGFKTPKTAIE HHCCCCCCCCCCCEE | 63.22 | - | |
| 43 | Acetylation | KNAGLGFKTPKTAIE HHCCCCCCCCCCCEE | 63.22 | 24489116 | |
| 44 | Phosphorylation | NAGLGFKTPKTAIEG HCCCCCCCCCCCEEC | 27.96 | 22369663 | |
| 46 | Acetylation | GLGFKTPKTAIEGSY CCCCCCCCCCEECCC | 56.68 | 24489116 | |
| 46 | Ubiquitination | GLGFKTPKTAIEGSY CCCCCCCCCCEECCC | 56.68 | 22106047 | |
| 46 | Succinylation | GLGFKTPKTAIEGSY CCCCCCCCCCEECCC | 56.68 | 23954790 | |
| 47 | Phosphorylation | LGFKTPKTAIEGSYI CCCCCCCCCEECCCC | 33.79 | 28889911 | |
| 52 | Phosphorylation | PKTAIEGSYIDKKCP CCCCEECCCCCCCCC | 13.21 | 22369663 | |
| 53 | Phosphorylation | KTAIEGSYIDKKCPF CCCEECCCCCCCCCC | 24.81 | 21440633 | |
| 56 | Succinylation | IEGSYIDKKCPFTGL EECCCCCCCCCCCEE | 46.87 | 23954790 | |
| 56 | Ubiquitination | IEGSYIDKKCPFTGL EECCCCCCCCCCCEE | 46.87 | 22106047 | |
| 56 | Acetylation | IEGSYIDKKCPFTGL EECCCCCCCCCCCEE | 46.87 | 24489116 | |
| 57 | Ubiquitination | EGSYIDKKCPFTGLV ECCCCCCCCCCCEEE | 43.31 | 22106047 | |
| 57 | Acetylation | EGSYIDKKCPFTGLV ECCCCCCCCCCCEEE | 43.31 | 24489116 | |
| 61 | Phosphorylation | IDKKCPFTGLVSIRG CCCCCCCCEEEEECC | 18.10 | 22369663 | |
| 65 | Phosphorylation | CPFTGLVSIRGKILT CCCCEEEEECCEEEC | 16.17 | 22369663 | |
| 69 | Ubiquitination | GLVSIRGKILTGTVV EEEEECCEEECCEEE | 25.37 | - | |
| 69 | Acetylation | GLVSIRGKILTGTVV EEEEECCEEECCEEE | 25.37 | 24489116 | |
| 72 | Phosphorylation | SIRGKILTGTVVSTK EECCEEECCEEEECC | 33.99 | 22369663 | |
| 74 | Phosphorylation | RGKILTGTVVSTKMH CCEEECCEEEECCCC | 16.70 | 22369663 | |
| 77 | Phosphorylation | ILTGTVVSTKMHRTI EECCEEEECCCCEEE | 20.27 | 20377248 | |
| 78 | Phosphorylation | LTGTVVSTKMHRTIV ECCEEEECCCCEEEE | 22.30 | 21440633 | |
| 79 | Acetylation | TGTVVSTKMHRTIVI CCEEEECCCCEEEEE | 25.79 | 24489116 | |
| 79 | Ubiquitination | TGTVVSTKMHRTIVI CCEEEECCCCEEEEE | 25.79 | 22106047 | |
| 90 | Phosphorylation | TIVIRRAYLHYIPKY EEEEEHHHHHHHHCC | 7.69 | 28889911 | |
| 96 | Ubiquitination | AYLHYIPKYNRYEKR HHHHHHHCCCCCHHH | 45.67 | 22106047 | |
| 96 | Acetylation | AYLHYIPKYNRYEKR HHHHHHHCCCCCHHH | 45.67 | 24489116 | |
| 105 | Ubiquitination | NRYEKRHKNVPVHVS CCCHHHHCCCCEEEC | 64.77 | 22106047 | |
| 105 | Acetylation | NRYEKRHKNVPVHVS CCCHHHHCCCCEEEC | 64.77 | 24489116 | |
| 112 | Phosphorylation | KNVPVHVSPAFRVQV CCCCEEECCCEEEEC | 8.81 | 28889911 | |
| 132 | Phosphorylation | VGQCRPISKTVRFNV EEECEECCCEEEEEE | 25.59 | 24909858 | |
| 133 | Ubiquitination | GQCRPISKTVRFNVV EECEECCCEEEEEEE | 52.32 | 22106047 | |
| 133 | Acetylation | GQCRPISKTVRFNVV EECEECCCEEEEEEE | 52.32 | 24489116 | |
| 141 | Ubiquitination | TVRFNVVKVSAAAGK EEEEEEEEEEECCHH | 26.62 | 22106047 | |
| 141 | Acetylation | TVRFNVVKVSAAAGK EEEEEEEEEEECCHH | 26.62 | 24489116 | |
| 143 | Phosphorylation | RFNVVKVSAAAGKAN EEEEEEEEECCHHHH | 13.38 | 21440633 | |
| 148 | Ubiquitination | KVSAAAGKANKQFAK EEEECCHHHHHHHCC | 44.02 | 22106047 | |
| 151 | Ubiquitination | AAAGKANKQFAKF-- ECCHHHHHHHCCC-- | 52.21 | - | |
| 151 | Succinylation | AAAGKANKQFAKF-- ECCHHHHHHHCCC-- | 52.21 | 23954790 | |
| 155 | Ubiquitination | KANKQFAKF------ HHHHHHCCC------ | 53.55 | - |
| 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 RS11A_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS11A_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 RS11A_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 2-21, AND ACETYLATION AT SER-2 BY NATA. | |
| Phosphorylation | |
| Reference | PubMed |
| "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 THR-74, AND MASSSPECTROMETRY. | |
