Q9UN81
uniprot
Q9UN81
canonical
amino_acid_sequence
MGKKQNRKTGNSKTQSASPPPKERSSSPATEQSWMENDFDELREEGFRRSNYSELREDIQTKGKEVENFEKNLEECITRITNTEKCLKELMELKTKARELREECRSLRSRCDQLEERVSAMEDEMNEMKREGKFREKRIKRNEQSLQEIWDYVKRPNLRLIGVPESDVENGTKLENTLQDIIQENFPNLARQANVQIQEIQRTPQRYSSRRATPRHIIVRFTKVEMKEKMLRAAREKGRVTLKGKPIRLTADLSAETLQARREWGPIFNILKEKNFQPRISYPAKLSFISEGEIKYFIDKQMLRDFVTTRPALKELLKEALNMERNNRYQPLQNHAKM
uniprot
proteins
function
FUNCTION: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded. {ECO:0000269|PubMed:11158327, ECO:0000269|PubMed:21937507, ECO:0000269|PubMed:28806172, ECO:0000269|PubMed:30122351, ECO:0000269|PubMed:8945518}.
uniprot
proteins
mass_dalton
40056
uniprot
proteins
mutagenesis
MUTAGEN 93; /note="L->A: Small decrease in localization to stress granules; when associated with A-100 and A-114."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 100; /note="L->A: Small decrease in localization to stress granules; when associated with A-93 and A-114."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 114; /note="L->A: Small decrease in localization to stress granules; when associated with A-93 and A-100."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 116; /note="E->A: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with A-123."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 123; /note="D->A: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with A-116."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 132; /note="G->I: Loss of LINE-1 retrotransposition without affecting RNA-binding; when associated with I-135 and I-142."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 133; /note="K->S: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with A-137, A-140 and S-141."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 135; /note="R->I: Loss of LINE-1 retrotransposition without effect on RNA-binding; when associated with I-132 and I-142."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 137; /note="K->A: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-140 and S-141."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 140; /note="K->A: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-137 and S-141."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 141; /note="R->S: Loss of LINE-1 retrotransposition with decreased RNA-binding; when associated with S-133, A-137 and A-140."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 142; /note="N->I: Loss of LINE-1 retrotransposition without effect on RNA-binding; when associated with I-132 and I-135."; /evidence="ECO:0000269|PubMed:21822284"; MUTAGEN 155; /note="R->A: No effect on subcellular localization; when associated with A-157."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 157; /note="N->A: No effect on subcellular localization; when associated with A-155. Complete loss of localization to stress granules, slightly increased localization to the nucleus; when associated with G-159."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 159; /note="R->A: Moderately alters RNA-binding activity."; /evidence="ECO:0000269|PubMed:19139409"; MUTAGEN 159; /note="R->G: Decreased localization to stress granules. Complete loss of localization to stress granules, slightly increased localization to the nucleus; when associated with A-157."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 165; /note="E->G: No effect on cytoplasmic localization, may increase nucleolar localization."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 206; /note="R->A: Loss of RNA-binding activity; when associated with A-210 and A-211."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 210; /note="R->A: Loss of RNA-binding activity; when associated with A-206 and A-211."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 211; /note="R->A: Loss of RNA-binding activity; when associated with A-206 and A-210."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 218; /note="I->Y: Moderately alters RNA-binding activity."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 220; /note="R->A: Loss of LINE-1 retrotransposition without affecting RNA-binding."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 235; /note="R->A: Loss of LINE-1 retrotransposition with decreased RNA-binding."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 261..262; /note="RR->AA: Small decrease in localization to stress granules."; /evidence="ECO:0000269|PubMed:17562864"; MUTAGEN 261; /note="R->A: Loss of LINE-1 retrotransposition with decreased RNA-binding."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 261; /note="R->K: Loss of LINE-1 retrotransposition without affecting RNA-binding."; /evidence="ECO:0000269|PubMed:19139409, ECO:0000269|PubMed:21822284"; MUTAGEN 282; /note="Y->A: Loss of LINE-1 retrotransposition without affecting RNA-binding."; /evidence="ECO:0000269|PubMed:21822284
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated, probably by UBR2, which induces its degradation. {ECO:0000269|PubMed:28806172}.
uniprot
proteins
protein_family
Transposase 22 family
uniprot
proteins
pubmed
10401005
uniprot
proteins
pubmed
10655552
uniprot
proteins
pubmed
11158327
uniprot
proteins
pubmed
16183655
uniprot
proteins
pubmed
17562864
uniprot
proteins
pubmed
19139409
uniprot
proteins
pubmed
21822284
uniprot
proteins
pubmed
21937507
uniprot
proteins
pubmed
23093941
uniprot
proteins
pubmed
27428332
uniprot
proteins
pubmed
28806172
uniprot
proteins
pubmed
30122351
uniprot
proteins
pubmed
8945518
uniprot
proteins
sequence_length
338
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17562864}. Cytoplasm {ECO:0000269|PubMed:27428332}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:16183655, ECO:0000269|PubMed:30122351}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17562864, ECO:0000269|PubMed:23093941}. Note=Colocalizes with its encoding RNA in cytoplasmic ribonucleoprotein particle (PubMed:16183655). Mainly cytoplasmic, rarely detected in the nucleus, possibly within the nucleolus (PubMed:17562864). {ECO:0000269|PubMed:16183655, ECO:0000269|PubMed:17562864}.
uniprot
proteins