LIN28A
entrez
79727
canonical
uniprot
Q9H9Z2
canonical
ensembl
ENSG00000131914
resolver
ensp
ENSP00000254231
resolver
ensp
ENSP00000363314
resolver
enst
ENST00000254231
resolver
enst
ENST00000326279
resolver
genesymbol
LIN28A
resolver
genesymbol_syn
CSDD1
resolver
genesymbol_syn
LIN28
resolver
genesymbol_syn
ZCCHC1
resolver
hgnc
HGNC:15986
resolver
uniprot_entry
LN28A_HUMAN
resolver
amino_acid_sequence
MGSVSNQQFAGGCAKAAEEAPEEAPEDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKSMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSISHMVASCPLKAQQGPSAQGKPTYFREEEEEIHSPTLLPEAQN
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:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). '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. 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 (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). This results in the terminal uridylation of target pre-miRNAs (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). 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:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). 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. 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 (By similarity). {ECO:0000250|UniProtKB:Q8K3Y3, ECO:0000269|PubMed:18951094, ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:21247876, ECO:0000269|PubMed:22118463, ECO:0000269|PubMed:22898984, ECO:0000305}.
uniprot
proteins
mass_dalton
22743
uniprot
proteins
mutagenesis
MUTAGEN 46; /note="W->A: Does not affect localization to P-bodies; when associated with A-55 and A-73."; /evidence="ECO:0000269|PubMed:17617744"; MUTAGEN 55; /note="F->A: Does not affect localization to P-bodies; when associated with A-46 and A-73."; /evidence="ECO:0000269|PubMed:17617744"; MUTAGEN 73; /note="F->A: Does not affect localization to P-bodies; when associated with A-46 and A-55."; /evidence="ECO:0000269|PubMed:17617744"; MUTAGEN 147; /note="H->A: Abolishes ability to suppress pre-let-7 biogenesis and localization to P-bodies without affecting pre-let-7 binding; when associated with A-169."; /evidence="ECO:0000269|PubMed:17617744, ECO:0000269|PubMed:18951094"; MUTAGEN 169; /note="H->A: Abolishes ability to suppress pre-let-7 biogenesis and localization to P-bodies without affecting pre-let-7 binding; when associated with A-147."; /evidence="ECO:0000269|PubMed:17617744, ECO:0000269|PubMed:18951094
uniprot
proteins
protein_family
Lin-28 family
uniprot
proteins
pubmed
12798299
uniprot
proteins
pubmed
14688391
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15003116
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15614775
uniprot
proteins
pubmed
15722555
uniprot
proteins
pubmed
16227573
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17617744
uniprot
proteins
pubmed
18951094
uniprot
proteins
pubmed
19483683
uniprot
proteins
pubmed
19703396
uniprot
proteins
pubmed
21247876
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22118463
uniprot
proteins
pubmed
22157959
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22898984
uniprot
proteins
sequence_length
209
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18951094, ECO:0000269|PubMed:22118463}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q8K3Y3}. Cytoplasm, P-body {ECO:0000269|PubMed:17617744}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17617744}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8K3Y3}. Note=Predominantly cytoplasmic (PubMed:22118463). 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 (By similarity). Shuttle from the nucleus to the cytoplasm requires RNA-binding (PubMed:17617744). Nucleolar localization is observed in 10-15% of the nuclei in differentiated myotubes (By similarity). {ECO:0000250|UniProtKB:Q8K3Y3, ECO:0000269|PubMed:17617744, ECO:0000269|PubMed:22118463}.
uniprot
proteins