lmmol · Proteins

Ubiquitin-ribosomal protein eS31 fusion protein

UniProt P62979 Organism Homo sapiens Gene RPS27A, UBA80, UBCEP1

Also known as: RPS27A, UBA80, UBCEP1

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.

Classification

Family (Pfam)
PF01599 Ribosomal_S27, PF00240 ubiquitin
InterPro
Ribosomal_eS31, Ribosomal_eS31_euk_sf, Ribosomal_zn-bd, Ubiquitin-like_dom, Ubiquitin-like_domsf, Ubiquitin_CS, Ubiquitin_dom, Ubiquitin_ubiquitin-like
Functional cluster
Ras-like GTPases & Nucleoid Proteins

Experimental structures · PDB · 212

A predicted model is available from AlphaFold.

Gene Ontology · 26

Drugs targeting this protein · 2

Related proteins · sequence + function similarity

Co-cited proteins · studied together in the literature

Literature · 32 cited papers

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