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RPS27A (Ubiquitin-ribosomal protein eS31 fusion protein) is a gene. The public catalogues list it as a drug target, and clinical evidence ties its variants to diagnosis, prognosis or drug response.
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 signalling processes leading to activation of the transcription factor NF-kappa-B.
Open Targets scores its association with cancer at 0.64 (direct and indirect evidence; datatypes clinical 0.11, genetic literature 0.76, affected pathway 0.83, literature 0.93, genetic association 0.05).
In plain words · RPS27A (Ubiquitin-ribosomal protein eS31 fusion protein) is a gene. The public catalogues list it as a drug target, and clinical evidence ties its variants to diagnosis, prognosis or drug response.
RPS27A (Ubiquitin-ribosomal protein eS31 fusion protein) is a gene. The public catalogues list it as a drug target, and clinical evidence ties its variants to diagnosis, prognosis or drug response.
Exists either covalently attached to another protein, or free (unanchored).
No product in this corpus aims at RPS27A yet. Drugs bind the molecule precisely: to switch it off, flag the cell for the immune system, or deliver a payload.
Broadly expressed or essential: HPA lists RPS27A among essential proteins and finds the RNA at low tissue specificity; a medicine acting on the wild-type protein would expose normal tissue too. HPA RPS27A: RNA low tissue specificity; high antibody staining in 29 normal tissues; highest cancer staining prostate cancer (6 of 7 high). Distribution: no corpus cancer carries a prevalence row, threshold or catalogue link for it; Open Targets associates it with 0 specific cancer types at or above 0.5. (Rule 7 of scripts/fetch-target-specificity.ts.)
Sources: Human Protein Atlas RPS27A tissue; Open Targets ENSG00000143947 associations
First described 1975. Earliest sequence paper UniProt cites for the protein: Schlesinger D.H. et al, Nature, 1975, "Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man". Source.
Sources: HGNC HGNC:10417 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P62979 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000143947 (association with cancer (MONDO_0004992) 0.64; (GraphQL API, CC0))
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 signalling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signalling. 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 signalling. Location: Cytoplasm; Nucleus, nucleolus; Nucleus (UniProt). Locus 2p16.1 (HGNC).
RNA: low tissue specificity, detected in all normal tissues.
Medium: Adipose tissue, Appendix, Bone marrow, Colon, Duodenum, Epididymis, Hippocampus, Kidney.
Medium only: cervical cancer, stomach cancer.
HPA RPS27A tissue · HPA RPS27A pathology · HPA protein class: Essential proteins
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"RPS27A" OR ABSTRACT:"RPS27A" OR TITLE:"ribosomal protein S27a" OR ABSTRACT:"ribosomal protein S27a" OR TITLE:"Ubiquitin-ribosomal protein eS31 fusion protein" OR ABSTRACT:"Ubiquitin-ribosomal protein eS31 fusion protein" OR TITLE:"UBCEP80" OR ABSTRACT:"UBCEP80" OR TITLE:"Uba80" OR ABSTRACT:"Uba80" OR TITLE:"S27A" OR ABSTRACT:"S27A") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about RPS27A, not a curated reading list.