Eri1
entrez
67276
canonical
uniprot
Q7TMF2
canonical
ensembl
ENSMUSG00000031527
resolver
ensp
ENSMUSP00000033927
resolver
enst
ENSMUST00000033927
resolver
genesymbol
Eri1
resolver
genesymbol_syn
3'exo
resolver
genesymbol_syn
Thex1
resolver
uniprot
A0A0R4J0C8
resolver
uniprot
Q3TA98
resolver
uniprot
Q3TNT0
resolver
uniprot
Q80UN4
resolver
uniprot
Q8BV98
resolver
uniprot
Q8BWR6
resolver
uniprot
Q9CQ63
resolver
uniprot_entry
A0A0R4J0C8_MOUSE
resolver
uniprot_entry
ERI1_MOUSE
resolver
uniprot_entry
Q8BV98_MOUSE
resolver
uniprot_sec
Q3TA98
resolver
uniprot_sec
Q3TNT0
resolver
uniprot_sec
Q80UN4
resolver
uniprot_sec
Q8BWR6
resolver
uniprot_sec
Q9CQ63
resolver
activity_regulation
ACTIVITY REGULATION: Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity. {ECO:0000250|UniProtKB:Q8IV48}.
uniprot
proteins
amino_acid_sequence
MEDERGRERGGDAAQQKTPRPECEESRPLSVEKKQRCRLDGKETDGSKFISSNGSDFSDPVYKEIAMTNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESSAGDSYYDYICIIDFEATCEEGNPAEFLHEIIEFPVVLLNTHTLEIEDTFQQYVRPEVNAQLSEFCIGLTGITQDQVDRADAFPQVLKKVIEWMKSKELGTKYKYCILTDGSWDMSKFLSIQCRLSRLKHPAFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHSGLDDSKNIARIAVRMLQDGCELRINEKILGGQLMSVSSSLPVEGAPAPQMPHSRK
uniprot
proteins
ec_number
3.1.13.1
uniprot
proteins
function
FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient 3'-end histone mRNA exonuclease activity and degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Required for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA (PubMed:18438418). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. In vitro, does not have sequence specificity. In vitro, has weak DNA exonuclease activity. In vitro, shows biphasic kinetics such that there is rapid hydrolysis of the last three unpaired RNA nucleotides in the 39 flanking sequence followed by a much slower cleavage through the stem that occurs over a longer incubation period in the order of hours (By similarity). ERI1-mediated RNA metabolism plays a key role in chondrogenesis (PubMed:37352860). {ECO:0000250|UniProtKB:Q8IV48, ECO:0000269|PubMed:18438418, ECO:0000269|PubMed:37352860}.
uniprot
proteins
mass_dalton
39493
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="K->A: Impairs binding to and processing of 5.8S rRNA; when associated with A-108."; /evidence="ECO:0000269|PubMed:18438418"; MUTAGEN 108; /note="K->A: Impairs binding to and processing of 5.8S rRNA; when associated with A-107."; /evidence="ECO:0000269|PubMed:18438418"; MUTAGEN 130; /note="D->G: No effect on binding to 5.8S rRNA; when associated with G-132."; /evidence="ECO:0000269|PubMed:18438418"; MUTAGEN 132; /note="E->G: No effect on binding to 5.8S rRNA; when associated with G-130."; /evidence="ECO:0000269|PubMed:18438418
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18438418
uniprot
proteins
pubmed
19470752
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
37352860
uniprot
proteins
sequence_length
345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18438418}. Nucleus {ECO:0000269|PubMed:18438418}. Nucleus, nucleolus {ECO:0000269|PubMed:18438418}.
uniprot
proteins