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Details on Person UniProt:P62979 RPS27A
| Class:Id | ReferenceGeneProduct:72362 |
|---|---|
| _chainChangeLog | chain:1-76 added on Fri February 6 2015;chain:77-156 added on Fri February 6 2015 |
| _displayName | UniProt:P62979 RPS27A |
| _timestamp | 2024-11-03 19:38:38 |
| chain | chain:1-76 chain:77-156 |
| checksum | 617BC63DF3A904F7 |
| comment | 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.FUNCTION Component of the 40S subunit of the ribosome (PubMed:23636399, PubMed:9582194). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:23636399, PubMed:34516797).SUBUNIT Part of the 40S ribosomal subunit (PubMed:23636399, PubMed:9582194). Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:23636399, PubMed:34516797).INTERACTION Phosphorylated at Ser-65 by PINK1 during mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30 (PubMed:25527291).PTM Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones.PTM (Microbial infection) Mono-ADP-ribosylated at Thr-66 by the C.violaceum CteC virulence factor. ADP-ribosylation causes the shutdown of polyubiquitin synthesis and disrupts the recognition and reversal of polyubiquitin.PTM Monoubiquitinated at Lys-107 and Lys-113 by RNF25 in response to ribosome collisions (ribosome stalling): ubiquitination promotes subsequent activation of RNF14, leading to EEF1A1 ubiquitination and degradation and rescue of stalled ribosomes (PubMed:36638793). Deubiquitination at Lys-113 by USP16 is required for maturation of the 40S ribosomal complex (PubMed:32129764).MISCELLANEOUS Ubiquitin is encoded by 4 different genes. UBA52 and RPS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins eL40 and eS31, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.MISCELLANEOUS For a better understanding, features related to ubiquitin are only indicated for the first chain.SIMILARITY In the N-terminal section; belongs to the ubiquitin family.SIMILARITY In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family. |
| description | recommendedName: fullName evidence="24"Ubiquitin-ribosomal protein eS31 fusion protein alternativeName: Ubiquitin carboxyl extension protein 80 component recommendedName: Ubiquitin /component component recommendedName: fullName evidence="23"Small ribosomal subunit protein eS31 alternativeName: 40S ribosomal protein S27a /component |
| geneName | RPS27A UBA80 UBCEP1 |
| identifier | P62979 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation ADP-ribosylation Cytoplasm Direct protein sequencing Isopeptide bond Metal-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation Zinc Zinc-finger |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9909836] Weiser, Joel, 2024-05-14 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | RPS27A |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8958142] ENSEMBL:ENSG00000143947 RPS27A [Homo sapiens] |
| secondaryIdentifier | RS27A_HUMAN P02248 P02249 P02250 P14798 P62988 Q29120 Q6LBL4 Q6LDU5 Q8WYN8 Q91887 Q91888 Q9BQ77 Q9BWD6 Q9BX98 Q9UEF2 Q9UEG1 Q9UEK8 Q9UPK7 |
| sequenceLength | 156 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:72363] RPS27A(77-156) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939202] Ub-48-RPS27A(1-76) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939205] RPS27A(1-76) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939208] RPS27A(1-76) [endocytic vesicle membrane] [Homo sapiens] [EntityWithAccessionedSequence:939222] Ub-63-RPS27A(1-76) [endosome membrane] [Homo sapiens] [EntityWithAccessionedSequence:939238] RPS27A(1-76) [endosome membrane] [Homo sapiens] [EntityWithAccessionedSequence:939248] Ub-63-RPS27A(1-76) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939849] RPS27A(1-76) [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:939855] Ub-63-RPS27A(1-76) [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:3095933] Ub-11-RPS27A(1-76) [cytosol] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:912737] ubiquitinylated lysine at 63 [ModifiedResidue:941610] ubiquitinylated lysine at 48 [ModifiedResidue:3095908] ubiquitinylated lysine at 11 [ModifiedResidue:5689109] ubiquitinylated lysine at 6 [ModifiedResidue:5689160] ubiquitinylated lysine at 29 [ModifiedResidue:5689168] ubiquitinylated lysine at 27 [ModifiedResidue:5689190] ubiquitinylated lysine at 33 [ModifiedResidue:8852043] glycyl phospho-5'-adenosine at 76 [ModifiedResidue:8869038] N6-glycyl-L-lysine at 76 [ModifiedResidue:9764635] modified L-methionine residue at 1 |
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No pathways have been reviewed or authored by UniProt:P62979 RPS27A (72362)
