Elavl1
entrez
15568
canonical
uniprot
P70372
canonical
ensembl
ENSMUSG00000040028
resolver
ensp
ENSMUSP00000096549
resolver
ensp
ENSMUSP00000146866
resolver
ensp
ENSMUSP00000288009
resolver
ensp
ENSMUSP00000288012
resolver
enst
ENSMUST00000098950
resolver
enst
ENSMUST00000209010
resolver
genesymbol
Elavl1
resolver
genesymbol_syn
Elra
resolver
genesymbol_syn
Hua
resolver
uniprot
Q60745
resolver
uniprot
Q78QY3
resolver
uniprot_entry
ELAV1_MOUSE
resolver
uniprot_sec
Q60745
resolver
uniprot_sec
Q78QY3
resolver
amino_acid_sequence
MSNGYEDHMAEDCRDDIGRTNLIVNYLPQNMTQEELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAISTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNMALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGISGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK
uniprot
proteins
function
FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (PubMed:24394384). Has also been shown to be capable of binding to m6A-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (By similarity). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (By similarity). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA (PubMed:21402775). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (PubMed:27616329). {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:21402775, ECO:0000269|PubMed:24394384, ECO:0000269|PubMed:27616329}.
uniprot
proteins
mass_dalton
36169
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by MAPKAPK2. Phosphorylated by PRKCD. {ECO:0000250|UniProtKB:Q15717}.; PTM: Methylated at Arg-217 by CARM1 in T-cells in response to LPS challenge. {ECO:0000269|PubMed:12237300}.
uniprot
proteins
protein_family
RRM elav family
uniprot
proteins
pubmed
12237300
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21402775
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24394384
uniprot
proteins
pubmed
27616329
uniprot
proteins
pubmed
7753842
uniprot
proteins
pubmed
9763509
uniprot
proteins
sequence_length
326
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9763509}. Nucleus {ECO:0000269|PubMed:9763509}. Cytoplasm, Stress granule {ECO:0000269|PubMed:27616329}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q15717}. Note=Translocates into the cytoplasm following phosphorylation by MAPKAPK2. Likewise, phosphorylation by PRKCD promotes translocation from the nucleus into the cytoplasm, where it is associated with free and cytoskeleton-bound polysomes (By similarity). Localizes to the stress granules in the presence of PLEKHN1. {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:27616329}.
uniprot
proteins