Search Results
Overview
| Uniprot ID | P62983 |
|---|---|
| Protein Name | Ubiquitin-ribosomal protein eS31 fusion protein |
| Gene Name | Rps27a |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 48 | QRLIFAGKQLEDGRT |
| 6 | **MQIFVKTLTGKTI |
Function
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 proteotoxic stress response and cell cycle; 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, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. 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
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0022626 | cytosolic ribosome |
| Cellular Component | GO:0022627 | cytosolic small ribosomal subunit |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0043209 | myelin sheath |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0098794 | postsynapse |
| Cellular Component | GO:0098793 | presynapse |
| Cellular Component | GO:0005840 | ribosome |
| Cellular Component | GO:0032040 | small-subunit processome |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0031386 | protein tag activity |
| Molecular Function | GO:0003735 | structural constituent of ribosome |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0002181 | cytoplasmic translation |
| Biological Process | GO:0019941 | modification-dependent protein catabolic process |
| Biological Process | GO:0016567 | protein ubiquitination |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
| Biological Process | GO:0140242 | translation at postsynapse |
| Biological Process | GO:0140236 | translation at presynapse |
Reference
[1] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.