TRIR
entrez
79002
canonical
uniprot
Q9BQ61
canonical
ensembl
ENSG00000123144
resolver
ensp
ENSP00000242784
resolver
ensp
ENSP00000466196
resolver
ensp
ENSP00000466801
resolver
enst
ENST00000242784
resolver
enst
ENST00000588213
resolver
enst
ENST00000592273
resolver
genesymbol
TRIR
resolver
genesymbol_syn
C19orf43
resolver
hgnc
HGNC:28424
resolver
uniprot
K7ELS0
resolver
uniprot
K7EN60
resolver
uniprot_entry
K7ELS0_HUMAN
resolver
uniprot_entry
K7EN60_HUMAN
resolver
uniprot_entry
TRIR_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Zn(2+) inhibits the RNase activity while Mg(2+), Ca(2+), Mn(2+), K(+), Na(+), EDTA and EGTA show little effect on the exoribonuclease activity (PubMed:28322335). {ECO:0000269|PubMed:28322335}.
uniprot
proteins
amino_acid_sequence
MAARGRRAEPQGREAPGPAGGGGGGSRWAESGSGTSPESGDEEVSGAGSSPVSGGVNLFANDGSFLELFKRKMEEEQRQRQEEPPPGPQRPDQSAAAAGPGDPKRKGGPGSTLSFVGKRRGGNKLALKTGIVAKKQKTEDEVLTSKGDAWAKYMAEVKKYKAHQCGDDDKTRPLVK
uniprot
proteins
ec_number
3.1.13.-
uniprot
proteins
function
FUNCTION: Exoribonuclease that is part of the telomerase RNA 3' end processing complex and which has the ability to cleave all four unpaired RNA nucleotides from the 5' end or 3' end with higher efficiency for purine bases (PubMed:28322335). {ECO:0000269|PubMed:28322335}.
uniprot
proteins
mass_dalton
18419
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
28322335
uniprot
proteins
sequence_length
176
uniprot
proteins