RPS27A
entrez
6233
canonical
uniprot
P62979
canonical
ensembl
ENSG00000143947
resolver
ensp
ENSP00000272317
resolver
ensp
ENSP00000383981
resolver
ensp
ENSP00000385659
resolver
ensp
ENSP00000529898
resolver
ensp
ENSP00000609295
resolver
ensp
ENSP00000609296
resolver
ensp
ENSP00000609297
resolver
ensp
ENSP00000609298
resolver
ensp
ENSP00000609299
resolver
ensp
ENSP00000609300
resolver
ensp
ENSP00000636079
resolver
enst
ENST00000272317
resolver
enst
ENST00000402285
resolver
enst
ENST00000404735
resolver
enst
ENST00000859839
resolver
enst
ENST00000939236
resolver
enst
ENST00000939237
resolver
enst
ENST00000939238
resolver
enst
ENST00000939239
resolver
enst
ENST00000939240
resolver
enst
ENST00000939241
resolver
enst
ENST00000966020
resolver
genesymbol
RPS27A
resolver
genesymbol_syn
HEL112
resolver
genesymbol_syn
UBA80
resolver
genesymbol_syn
UBCEP1
resolver
hgnc
HGNC:10417
resolver
uniprot
B2RDW1
resolver
uniprot
D6W5C9
resolver
uniprot
P02248
resolver
uniprot
P02249
resolver
uniprot
P02250
resolver
uniprot
P14798
resolver
uniprot
P62988
resolver
uniprot
Q29120
resolver
uniprot
Q6LBL4
resolver
uniprot
Q6LDU5
resolver
uniprot
Q8WYN8
resolver
uniprot
Q91887
resolver
uniprot
Q91888
resolver
uniprot
Q9BQ77
resolver
uniprot
Q9BWD6
resolver
uniprot
Q9BX98
resolver
uniprot
Q9UEF2
resolver
uniprot
Q9UEG1
resolver
uniprot
Q9UEK8
resolver
uniprot
Q9UPK7
resolver
uniprot_entry
B2RDW1_HUMAN
resolver
uniprot_entry
RS27A_HUMAN
resolver
uniprot_sec
D6W5C9
resolver
uniprot_sec
P02248
resolver
uniprot_sec
P02249
resolver
uniprot_sec
P02250
resolver
uniprot_sec
P14798
resolver
uniprot_sec
P62988
resolver
uniprot_sec
Q29120
resolver
uniprot_sec
Q6LBL4
resolver
uniprot_sec
Q6LDU5
resolver
uniprot_sec
Q8WYN8
resolver
uniprot_sec
Q91887
resolver
uniprot_sec
Q91888
resolver
uniprot_sec
Q9BQ77
resolver
uniprot_sec
Q9BWD6
resolver
uniprot_sec
Q9BX98
resolver
uniprot_sec
Q9UEF2
resolver
uniprot_sec
Q9UEG1
resolver
uniprot_sec
Q9UEK8
resolver
uniprot_sec
Q9UPK7
resolver
amino_acid_sequence
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK
uniprot
proteins
function
FUNCTION: [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 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. {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127, ECO:0000303|PubMed:19754430}.; FUNCTION: [Small ribosomal subunit protein eS31]: 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). {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797, ECO:0000305|PubMed:9582194}.
uniprot
proteins
mass_dalton
17965
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="K->R: No effect on HLTF-mediated polyubiquitination of PCNA."; /evidence="ECO:0000269|PubMed:18719106"; MUTAGEN 63; /note="K->R: Abolishes HLTF-mediated polyubiquitination of PCNA."; /evidence="ECO:0000269|PubMed:18719106"; MUTAGEN 65; /note="S->A: Prevents phosphorylation in case of mitophagy. Impaired translocation of PRKN to mitochondria."; /evidence="ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007"; MUTAGEN 65; /note="S->D: Phosphomimetic mutant that binds and activates PRKN."; /evidence="ECO:0000269|PubMed:24751536"; MUTAGEN 65; /note="S->G: Phosphomimetic mutant that can recruit PRKN to mitochondria."; /evidence="ECO:0000269|PubMed:25474007"; MUTAGEN 68; /note="H->G: Loss of DTX3L-mediated polyubiquitination of histone H3 and H4."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 72; /note="R->G: No effect on ADP-ribosylation."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 72; /note="R->K: No effect on ADP-ribosylation, when associated with K-74."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 74; /note="R->G: No effect on ADP-ribosylation."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 74; /note="R->K: No effect on ADP-ribosylation, when associated with K-72."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 76; /note="G->A: Loss of ADP-ribosylation."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 107; /note="K->R: Abolished monoubiquitination by RNF25, leading to impaired ability to rescue stalled ribosomes; when associated with R-113."; /evidence="ECO:0000269|PubMed:36638793"; MUTAGEN 113; /note="K->R: Abolished monoubiquitination by RNF25, leading to impaired ability to rescue stalled ribosomes; when associated with R-107. Abolished deubiquitination by USP16, without affecting maturation of the 40S ribosomal complex."; /evidence="ECO:0000269|PubMed:32129764, ECO:0000269|PubMed:36638793
uniprot
proteins
post_translational_modification
PTM: [Ubiquitin]: 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). {ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291}.; PTM: [Ubiquitin]: 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. {ECO:0000269|PubMed:28525742}.; PTM: [Ubiquitin]: (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. {ECO:0000269|PubMed:32330457}.; PTM: [Small ribosomal subunit protein eS31]: 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). {ECO:0000269|PubMed:32129764, ECO:0000269|PubMed:36638793}.
uniprot
proteins
protein_family
Ubiquitin family; Eukaryotic ribosomal protein eS31 family
uniprot
proteins
pubmed
1128706
uniprot
proteins
pubmed
11875025
uniprot
proteins
pubmed
1370760
uniprot
proteins
pubmed
15466860
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16443603
uniprot
proteins
pubmed
16543144
uniprot
proteins
pubmed
1657614
uniprot
proteins
pubmed
18719106
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19754430
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23636399
uniprot
proteins
pubmed
24524803
uniprot
proteins
pubmed
24660806
uniprot
proteins
pubmed
24751536
uniprot
proteins
pubmed
24784582
uniprot
proteins
pubmed
25474007
uniprot
proteins
pubmed
25527291
uniprot
proteins
pubmed
25752573
uniprot
proteins
pubmed
25752577
uniprot
proteins
pubmed
2581967
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28525742
uniprot
proteins
pubmed
32129764
uniprot
proteins
pubmed
32330457
uniprot
proteins
pubmed
34239127
uniprot
proteins
pubmed
34516797
uniprot
proteins
pubmed
36638793
uniprot
proteins
pubmed
8706699
uniprot
proteins
pubmed
9582194
uniprot
proteins
sequence_length
156
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.; SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
uniprot
proteins