Lin28a
entrez
83557
canonical
uniprot
Q8K3Y3
canonical
ensembl
ENSMUSG00000050966
resolver
ensp
ENSMUSP00000050488
resolver
enst
ENSMUST00000051674
resolver
genesymbol
Lin28a
resolver
genesymbol_syn
Lin28
resolver
genesymbol_syn
Tex17
resolver
uniprot
Q6NV62
resolver
uniprot_entry
LN28A_MOUSE
resolver
uniprot_sec
Q6NV62
resolver
amino_acid_sequence
MGSVSNQQFAGGCAKAAEKAPEEAPPDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKNMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSINHMVASCPLKAQQGPSSQGKPAYFREEEEEIHSPALLPEAQN
uniprot
proteins
function
FUNCTION: RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:17473174, PubMed:18292307, PubMed:18566191, PubMed:18604195, PubMed:19703396, PubMed:23102813, PubMed:24209617). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (PubMed:26045559). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression (PubMed:17473174). Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 and TUT7 uridylyltransferaseS. This results in the terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:19703396, PubMed:28671666). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins (PubMed:23102813). Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (PubMed:24209617). {ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:18292307, ECO:0000269|PubMed:18566191, ECO:0000269|PubMed:18604195, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:23102813, ECO:0000269|PubMed:24209617, ECO:0000269|PubMed:26045559, ECO:0000269|PubMed:28671666}.
uniprot
proteins
mass_dalton
22720
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="G->S: Erroneous subcellular location. No positive effect on terminal myogenic differentiation."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 44..47; /note="Missing: Erroneous subcellular location. No positive effect on terminal myogenic differentiation."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 81; /note="M->I: Erroneous subcellular location; when associated with Q-85. No positive effect on terminal myogenic differentiation; when associated with Q-85."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 85; /note="R->Q: Erroneous subcellular location; when associated with I-81. No positive effect on terminal myogenic differentiation; when associated with I-81."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 119; /note="G->R: Erroneous subcellular location; when associated with S-124. No positive effect on terminal myogenic differentiation; when associated with S-124."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 124; /note="P->S: Erroneous subcellular location; when associated with R-119. No positive effect on terminal myogenic differentiation; when associated with R-119."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 138..139; /note="Missing: No effect on subcellular location; when associated with S-142. Normal terminal myogenic differentiation; when associated with S-142."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 139..142; /note="CYNC->AYNA: Disrupts 5'-GGAG-3' motif interaction. Disrupts oligoU-addition to pre-miRNA pre-let-7 by TUT4."; /evidence="ECO:0000269|PubMed:28671666"; MUTAGEN 142; /note="C->S: No effect on subcellular location; when associated with 44-C--F-47. Normal terminal myogenic differentiation; when associated with 44-C--F-47."; /evidence="ECO:0000269|PubMed:17473174"; MUTAGEN 161..164; /note="CHFC->AHFA: Disrupts 5'-GGAG-3' motif interaction. Binds miRNA but not TUT4."; /evidence="ECO:0000269|PubMed:28671666
uniprot
proteins
protein_family
Lin-28 family
uniprot
proteins
pubmed
11279525
uniprot
proteins
pubmed
12798299
uniprot
proteins
pubmed
14643679
uniprot
proteins
pubmed
15003116
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15722555
uniprot
proteins
pubmed
16227573
uniprot
proteins
pubmed
17473174
uniprot
proteins
pubmed
18292307
uniprot
proteins
pubmed
18566191
uniprot
proteins
pubmed
18604195
uniprot
proteins
pubmed
19703396
uniprot
proteins
pubmed
22078496
uniprot
proteins
pubmed
23102813
uniprot
proteins
pubmed
24209617
uniprot
proteins
pubmed
26045559
uniprot
proteins
pubmed
28671666
uniprot
proteins
sequence_length
209
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:17473174}. Rough endoplasmic reticulum {ECO:0000269|PubMed:23102813}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9H9Z2}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17473174}. Nucleus, nucleolus {ECO:0000269|PubMed:17473174}. Note=Predominantly cytoplasmic (PubMed:12798299). In the cytoplasm, localizes to peri-endoplasmic reticulum regions and detected in the microsomal fraction derived from rough endoplasmic reticulum (RER) following subcellular fractionation. May be bound to the cytosolic surface of RER on which ER-associated mRNAs are translated (PubMed:23102813). Shuttle from the nucleus to the cytoplasm requires RNA-binding (PubMed:17473174). Nucleolar localization observed in 10-15% of the nuclei in differentiated myotubes (PubMed:17473174). {ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:23102813}.
uniprot
proteins