| UniProt ID | RL40A_YEAST | |
|---|---|---|
| UniProt AC | P0CH08 | |
| Protein Name | Ubiquitin-60S ribosomal protein L40 | |
| Gene Name | RPL40A {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 128 | |
| Subcellular Localization |
Ubiquitin: Cytoplasm. Nucleus. 60S ribosomal protein L40-A: Cytoplasm . |
|
| Protein Description | Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).; 60S ribosomal protein L40-A: 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 eL40 is essential for translation of a subset of cellular transcripts, including stress response transcripts, such as DDR2] | |
| Protein Sequence | MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCDKSVCRKCYARLPPRATNCRKRKCGHTNQLRPKKKLK | |
| 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 |
|---|---|---|---|---|---|
| 6 | Ubiquitination | --MQIFVKTLTGKTI --CEEEEEECCCCEE | - | ||
| 11 | Ubiquitination | FVKTLTGKTITLEVE EEEECCCCEEEEEEE | - | ||
| 12 | Phosphorylation | VKTLTGKTITLEVES EEECCCCEEEEEEEC | 23749301 | ||
| 14 | Phosphorylation | TLTGKTITLEVESSD ECCCCEEEEEEECCC | 23749301 | ||
| 19 | Phosphorylation | TITLEVESSDTIDNV EEEEEEECCCCHHHH | 23749301 | ||
| 22 | Phosphorylation | LEVESSDTIDNVKSK EEEECCCCHHHHHHH | 23749301 | ||
| 27 | Ubiquitination | SDTIDNVKSKIQDKE CCCHHHHHHHHHCCC | - | ||
| 29 | Ubiquitination | TIDNVKSKIQDKEGI CHHHHHHHHHCCCCC | - | ||
| 48 | Ubiquitination | QRLIFAGKQLEDGRT HEEEEEEEECCCCCC | - | ||
| 55 | Phosphorylation | KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC | 22369663 | ||
| 57 | Phosphorylation | LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH | 22369663 | ||
| 59 | Phosphorylation | DGRTLSDYNIQKEST CCCCCCCCCCCCHHH | 22369663 | ||
| 63 | Ubiquitination | LSDYNIQKESTLHLV CCCCCCCCHHHHHHH | - | ||
| 65 | Phosphorylation | DYNIQKESTLHLVLR CCCCCCHHHHHHHHH | 23749301 | ||
| 66 | Phosphorylation | YNIQKESTLHLVLRL CCCCCHHHHHHHHHH | 23749301 | ||
| 81 | Phosphorylation | RGGIIEPSLKALASK CCCCCHHHHHHHHHH | 23749301 | ||
| 83 | Ubiquitination | GIIEPSLKALASKYN CCCHHHHHHHHHHCC | - | ||
| 87 | Phosphorylation | PSLKALASKYNCDKS HHHHHHHHHCCCCHH | 30377154 | ||
| 88 | Acetylation | SLKALASKYNCDKSV HHHHHHHHCCCCHHH | 24489116 | ||
| 88 | Ubiquitination | SLKALASKYNCDKSV HHHHHHHHCCCCHHH | - | ||
| 93 | Acetylation | ASKYNCDKSVCRKCY HHHCCCCHHHHHHHH | 24489116 | ||
| 93 | Ubiquitination | ASKYNCDKSVCRKCY HHHCCCCHHHHHHHH | - | ||
| 94 | Phosphorylation | SKYNCDKSVCRKCYA HHCCCCHHHHHHHHH | 30377154 | ||
| 100 | Phosphorylation | KSVCRKCYARLPPRA HHHHHHHHHHCCCCC | 19684113 |
| 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 RL40A_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL40A_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 RL40A_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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