ERI1
entrez
90459
canonical
uniprot
Q8IV48
canonical
ensembl
ENSG00000104626
resolver
ensp
ENSP00000250263
resolver
ensp
ENSP00000430190
resolver
ensp
ENSP00000790239
resolver
ensp
ENSP00000793297
resolver
enst
ENST00000250263
resolver
enst
ENST00000519292
resolver
genesymbol
ERI1
resolver
genesymbol_syn
3'EXO
resolver
genesymbol_syn
THEX1
resolver
hgnc
HGNC:23994
resolver
uniprot
A8K4U7
resolver
uniprot
Q9NSX3
resolver
uniprot_entry
ERI1_HUMAN
resolver
uniprot_sec
A8K4U7
resolver
uniprot_sec
Q9NSX3
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:0000269|PubMed:14536070}.
uniprot
proteins
amino_acid_sequence
MEDPQSKEPAGEAVALALLESPRPEGGEEPPRPSPEETQQCKFDGQETKGSKFITSSASDFSDPVYKEIAITNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESNFADSYYDYICIIDFEATCEEGNPPEFVHEIIEFPVVLLNTHTLEIEDTFQQYVRPEINTQLSDFCISLTGITQDQVDRADTFPQVLKKVIDWMKLKELGTKYKYSLLTDGSWDMSKFLNIQCQLSRLKYPPFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHCGLDDSKNIARIAVRMLQDGCELRINEKMHAGQLMSVSSSLPIEGTPPPQMPHFRK
uniprot
proteins
disease_involvement
DISEASE: Hoxha-Aliu syndrome (HXAL) [MIM:620662]: An autosomal recessive disorder characterized by mild intellectual disability, eyelid ptosis, and limb anomalies including brachydactyly, clinodactyly, dysplastic or absent nails, brachytelephalangy, short metacarpals, and toe syndactyly. {ECO:0000269|PubMed:36208065, ECO:0000269|PubMed:37352860}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondyloepimetaphyseal dysplasia, Guo-Campeau type (SEMDGC) [MIM:620663]: An autosomal recessive, severe bone disease characterized by short stature, scoliosis, platyspondyly, irregular vertebral plates, facial dysmorphism, and variable anomalies of the pelvis, hips, and extremities including short, rudimentary, or absent digits. {ECO:0000269|PubMed:16912046, ECO:0000269|PubMed:37352860}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:14536070, PubMed:16912046, PubMed:17135487, PubMed:37352860). 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 (PubMed:14536070, PubMed:16912046, PubMed:17135487). Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi) (PubMed:14961122). Required for binding the 5'-ACCCA-3' sequence present in stem-loop structure (PubMed:14536070, PubMed:16912046). Able to bind other mRNAs (PubMed:14536070, PubMed:16912046). Required for 5.8S rRNA 3'-end processing (PubMed:37352860). Also binds to 5.8s ribosomal RNA (By similarity). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs (PubMed:14536070, PubMed:16912046, PubMed:17135487). In vitro, does not have sequence specificity (PubMed:17135487). In vitro, has weak DNA exonuclease activity (PubMed:17135487). 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 (PubMed:17135487). ERI1-mediated RNA metabolism plays a key role in chondrogenesis (PubMed:37352860). {ECO:0000250|UniProtKB:Q7TMF2, ECO:0000269|PubMed:14536070, ECO:0000269|PubMed:14961122, ECO:0000269|PubMed:16912046, ECO:0000269|PubMed:17135487, ECO:0000269|PubMed:37352860}.
uniprot
proteins
mass_dalton
40064
uniprot
proteins
mutagenesis
MUTAGEN 92; /note="K->A: Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-104."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 96; /note="R->A: Does not inhibit RNA-binding to the stem-loop structure."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 99; /note="K->A: Reduces slightly RNA-binding to the stem-loop structure."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 104; /note="K->A: Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-92."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 105; /note="R->A: Inhibits RNA-binding to the stem-loop structure."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 109; /note="Y->A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-110."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 110; /note="Y->A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-109."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 111; /note="K->A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-112."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 112; /note="K->A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-111."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 234; /note="D->A: Inhibits 3'-end histone mRNA exonuclease activity."; /evidence="ECO:0000269|PubMed:16912046"; MUTAGEN 235; /note="M->A: Inhibits RNA-binding to the stem-loop structure and 3'-end histone mRNA exonuclease activity."; /evidence="ECO:0000269|PubMed:16912046
uniprot
proteins
pubmed
14536070
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14961122
uniprot
proteins
pubmed
15451662
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16912046
uniprot
proteins
pubmed
17135487
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
36208065
uniprot
proteins
pubmed
37352860
uniprot
proteins
sequence_length
349
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16912046}. Nucleus {ECO:0000269|PubMed:16912046}. Nucleus, nucleolus {ECO:0000269|PubMed:16912046}.
uniprot
proteins