RLIG1
entrez
91298
canonical
uniprot
Q8N999
canonical
ensembl
ENSG00000133641
resolver
ensp
ENSP00000349358
resolver
genesymbol
RLIG1
resolver
genesymbol_syn
C12orf29
resolver
hgnc
HGNC:25322
resolver
uniprot
Q569K5
resolver
uniprot
Q6AWA8
resolver
uniprot
Q6PEK5
resolver
uniprot
Q8IYQ5
resolver
uniprot
Q9NT75
resolver
uniprot_entry
RLIG1_HUMAN
resolver
uniprot_sec
Q569K5
resolver
uniprot_sec
Q6AWA8
resolver
uniprot_sec
Q6PEK5
resolver
uniprot_sec
Q8IYQ5
resolver
uniprot_sec
Q9NT75
resolver
amino_acid_sequence
MKRLGSVQRKMPCVFVTEVKEEPSSKREHQPFKVLATETVSHKALDADIYSAIPTEKVDGTCCYVTTYKDQPYLWARLDRKPNKQAEKRFKNFLHSKENPKEFFWNVEEDFKPAPECWIPAKETEQINGNPVPDENGHIPGWVPVEKNNKQYCWHSSVVNYEFEIALVLKHHPDDSGLLEISAVPLSDLLEQTLELIGTNINGNPYGLGSKKHPLHLLIPHGAFQIRNLPSLKHNDLVSWFEDCKEGKIEGIVWHCSDGCLIKVHRHHLGLCWPIPDTYMNSRPVIINMNLNKCDSAFDIKCLFNHFLKIDNQKFVRLKDIIFDV
uniprot
proteins
ec_number
6.5.1.3
uniprot
proteins
function
FUNCTION: Functions as an RNA ligase, in vitro (PubMed:36792600). The ligation reaction entails three nucleotidyl transfer steps (PubMed:36792600). In the first step, the RNA ligase reacts with ATP in the absence of nucleic acid to form a covalent ligase-AMP intermediate and release pyrophosphate (PubMed:36792600). In step 2, the ligase-AMP binds to the nucleic acid and transfers the adenylate to the 5'-PO4 terminus to form an adenylylated intermediate (PubMed:36792600). In step 3, the RNA ligase directs the attack of the 3'-OH on the 5'-phosphoanhydride linkage, resulting in a repaired 3'-5' phosphodiester and release of AMP (PubMed:36792600). Exhibits selectivity for single-stranded RNA substrates and may not have nick-sealing activity on double-stranded DNA-RNA hybrids (PubMed:36792600). May play a role in maintaining RNA integrity under stress conditions, for example in response to reactive oxygen species (ROS) (PubMed:36792600). {ECO:0000269|PubMed:36792600, ECO:0000303|PubMed:36792600}.
uniprot
proteins
mass_dalton
37490
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="T->A: Abolishes RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 57; /note="K->A: Deficient in auto-AMPylation activity, in vitro. Abolishes RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 59; /note="D->N: Abolishes RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 77; /note="R->L: Reduces RNA ligation activity to about 12%, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 123; /note="E->D: Has no effect on RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 123; /note="E->Q: Has no effect on RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 250; /note="E->A: Abolishes RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 250; /note="E->Q: Abolishes RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600"; MUTAGEN 263; /note="K->N: Abolishes RNA ligation activity, in vitro."; /evidence="ECO:0000269|PubMed:36792600
uniprot
proteins
post_translational_modification
PTM: AMPylates itself (auto-AMPylation). {ECO:0000269|PubMed:36792600}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
36792600
uniprot
proteins
sequence_length
325
uniprot
proteins