EXOSC10
entrez
5394
canonical
uniprot
Q01780
canonical
ensembl
ENSG00000171824
resolver
ensp
ENSP00000307307
resolver
ensp
ENSP00000366135
resolver
ensp
ENSP00000539417
resolver
genesymbol
EXOSC10
resolver
genesymbol_syn
PMSCL
resolver
genesymbol_syn
PMSCL2
resolver
genesymbol_syn
RRP6
resolver
hgnc
HGNC:9138
resolver
uniprot
B1AKQ0
resolver
uniprot
B1AKQ1
resolver
uniprot
Q15158
resolver
uniprot_entry
EXOSX_HUMAN
resolver
uniprot_sec
B1AKQ0
resolver
uniprot_sec
B1AKQ1
resolver
uniprot_sec
Q15158
resolver
activity_regulation
ACTIVITY REGULATION: Arginine-rich dipeptide repeat proteins expressed from C9orf72-derived repeat RNA interact with EXOSC10 and inhibit its ability to promote degradation of this RNA. {ECO:0000269|PubMed:32830871}.
uniprot
proteins
amino_acid_sequence
MAPPSTREPRVLSATSATKSDGEMVLPGFPDADSFVKFALGSVVAVTKASGGLPQFGDEYDFYRSFPGFQAFCETQGDRLLQCMSRVMQYHGCRSNIKDRSKVTELEDKFDLLVDANDVILERVGILLDEASGVNKNQQPVLPAGLQVPKTVVSSWNRKAAEYGKKAKSETFRLLHAKNIIRPQLKFREKIDNSNTPFLPKIFIKPNAQKPLPQALSKERRERPQDRPEDLDVPPALADFIHQQRTQQVEQDMFAHPYQYELNHFTPADAVLQKPQPQLYRPIEETPCHFISSLDELVELNEKLLNCQEFAVDLEHHSYRSFLGLTCLMQISTRTEDFIIDTLELRSDMYILNESLTDPAIVKVFHGADSDIEWLQKDFGLYVVNMFDTHQAARLLNLGRHSLDHLLKLYCNVDSNKQYQLADWRIRPLPEEMLSYARDDTHYLLYIYDKMRLEMWERGNGQPVQLQVVWQRSRDICLKKFIKPIFTDESYLELYRKQKKHLNTQQLTAFQLLFAWRDKTARREDESYGYVLPNHMMLKIAEELPKEPQGIIACCNPVPPLVRQQINEMHLLIQQAREMPLLKSEVAAGVKKSGPLPSAERLENVLFGPHDCSHAPPDGYPIIPTSGSVPVQKQASLFPDEKEDNLLGTTCLIATAVITLFNEPSAEDSKKGPLTVAQKKAQNIMESFENPFRMFLPSLGHRAPVSQAAKFDPSTKIYEISNRWKLAQVQVQKDSKEAVKKKAAEQTAAREQAKEACKAAAEQAISVRQQVVLENAAKKRERATSDPRTTEQKQEKKRLKISKKPKDPEPPEKEFTPYDYSQSDFKAFAGNSKSKVSSQFDPNKQTPSGKKCIAAKKIKQSVGNKSMSFPTGKSDRGFRYNWPQR
uniprot
proteins
ec_number
3.1.13.-
uniprot
proteins
function
FUNCTION: Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. 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:34516797). The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination (PubMed:25632158, PubMed:31086179). Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage (PubMed:31086179). Plays a role in oocyte development, maturation and survival (By similarity). Required for normal testis development and mitotic division of spermatogonia (By similarity). Plays a role in proper embryo development (By similarity). Required for global protein translation (PubMed:26857222, PubMed:36912080). Required for cell proliferation (PubMed:36912080). Regulates metabolism of C9orf72-derived repeat RNA that can be translated into toxic dipeptide repeat proteins (PubMed:32830871). {ECO:0000250|UniProtKB:P56960, ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:16455498, ECO:0000269|PubMed:17412707, ECO:0000269|PubMed:17545563, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:19056938, ECO:0000269|PubMed:20368444, ECO:0000269|PubMed:20699273, ECO:0000269|PubMed:25632158, ECO:0000269|PubMed:26857222, ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36912080}.
uniprot
proteins
mass_dalton
100831
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="K->R: No effect on sumoylation by USP36."; /evidence="ECO:0000269|PubMed:36912080"; MUTAGEN 168; /note="K->R: No effect on sumoylation by USP36. Reduces sumoylation levels and increases steady-state expression; when associated with R-201 and R-583."; /evidence="ECO:0000269|PubMed:26857222, ECO:0000269|PubMed:36912080"; MUTAGEN 201; /note="K->R: Reduces sumoylation levels and increases steady-state expression; when associated with R-168 and R-583."; /evidence="ECO:0000269|PubMed:26857222"; MUTAGEN 313; /note="D->N: Abolishes exoribonuclease activity."; /evidence="ECO:0000269|PubMed:21705430"; MUTAGEN 315; /note="E->Q: Abolishes exoribonuclease activity."; /evidence="ECO:0000269|PubMed:21705430"; MUTAGEN 316; /note="H->A: Slightly reduces exoribonuclease activity."; /evidence="ECO:0000269|PubMed:21705430"; MUTAGEN 371; /note="D->N: Abolishes exoribonuclease activity."; /evidence="ECO:0000269|PubMed:21705430"; MUTAGEN 404; /note="D->A: Increases exoribonuclease activity."; /evidence="ECO:0000269|PubMed:21705430"; MUTAGEN 436; /note="Y->A: Significantly reduces exoribonuclease activity."; /evidence="ECO:0000269|PubMed:21705430"; MUTAGEN 583; /note="K->R: Reduces sumoylation by USP36. Significantly attenuates binding to pre-rRNA across the 5.8S-ITS2 and 18S-ITS1 junctions. Reduces sumoylation levels and increases steady-state expression; when associated with R-168 and R-201."; /evidence="ECO:0000269|PubMed:26857222, ECO:0000269|PubMed:36912080"; MUTAGEN 710; /note="K->R: No effect on sumoylation by USP36."; /evidence="ECO:0000269|PubMed:36912080"; MUTAGEN 826; /note="K->R: No effect on sumoylation by USP36."; /evidence="ECO:0000269|PubMed:36912080"; MUTAGEN 833; /note="K->R: No effect on sumoylation by USP36."; /evidence="ECO:0000269|PubMed:36912080"; MUTAGEN 859; /note="K->R: No effect on sumoylation by USP36."; /evidence="ECO:0000269|PubMed:36912080"; MUTAGEN 873; /note="K->R: No effect on sumoylation by USP36."; /evidence="ECO:0000269|PubMed:36912080
uniprot
proteins
post_translational_modification
PTM: Sumoylated by USP36; sumoylation does not significantly affect EXOSC10 nucleolar localization and association with core exosome and USP36, but regulates the nucleolar RNA exosome activity in rRNA processing by promoting binding of EXOSC10 to pre-rRNAs (PubMed:36912080). Effects of sumoylation on EXOSC10 levels vary between different studies (PubMed:26857222, PubMed:36912080). Sumoylation of EXOSC10 is required for the modulation of EXOSC10 effects on cellular protein translation and cell proliferation (PubMed:36912080). Sumoylation is promoted by mild hypothermia (PubMed:26857222). {ECO:0000269|PubMed:26857222, ECO:0000269|PubMed:36912080}.
uniprot
proteins
protein_family
Exosome component 10/RRP6 family
uniprot
proteins
pubmed
10465791
uniprot
proteins
pubmed
11426320
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
1383382
uniprot
proteins
pubmed
14527413
uniprot
proteins
pubmed
14731398
uniprot
proteins
pubmed
15231747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1644924
uniprot
proteins
pubmed
16455498
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17234882
uniprot
proteins
pubmed
17412707
uniprot
proteins
pubmed
17545563
uniprot
proteins
pubmed
18172165
uniprot
proteins
pubmed
19056938
uniprot
proteins
pubmed
20368444
uniprot
proteins
pubmed
20531386
uniprot
proteins
pubmed
20531389
uniprot
proteins
pubmed
20699273
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21705430
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25632158
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26166824
uniprot
proteins
pubmed
26857222
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29906447
uniprot
proteins
pubmed
30047866
uniprot
proteins
pubmed
30538148
uniprot
proteins
pubmed
31086179
uniprot
proteins
pubmed
32830871
uniprot
proteins
pubmed
34516797
uniprot
proteins
pubmed
36912080
uniprot
proteins
sequence_length
885
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531386}. Nucleus {ECO:0000269|PubMed:36912080}. Nucleus, nucleolus {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:36912080}. Nucleus, nucleoplasm {ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:36912080}. Note=Strongly enriched in the nucleolus and a small amount has been found in cytoplasm supporting the existence of a nucleolar RNA exosome complex form (PubMed:20531386, PubMed:34516797). Arginine-rich dipeptide repeat proteins expressed from C9orf72-derived repeat RNA cause diffuse nuclear misdistribution of EXOSC10 (PubMed:32830871). Relocates to the DNA double-strand breaks in response to irradiation (PubMed:31086179). {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:31086179, ECO:0000269|PubMed:32830871, ECO:0000269|PubMed:34516797}.
uniprot
proteins