ELAVL1
entrez
1994
canonical
uniprot
Q15717
canonical
ensembl
ENSG00000066044
resolver
ensp
ENSP00000385269
resolver
ensp
ENSP00000661388
resolver
genesymbol
ELAVL1
resolver
genesymbol_syn
HUR
resolver
hgnc
HGNC:3312
resolver
uniprot
B4DVB8
resolver
uniprot
Q53XN6
resolver
uniprot
Q9BTT1
resolver
uniprot_entry
ELAV1_HUMAN
resolver
uniprot_sec
B4DVB8
resolver
uniprot_sec
Q53XN6
resolver
uniprot_sec
Q9BTT1
resolver
amino_acid_sequence
MSNGYEDHMAEDCRGDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNVALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGLSGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK
uniprot
proteins
function
FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability (PubMed:14517288, PubMed:18285462, PubMed:31358969). Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (By similarity). 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 (PubMed:32245947). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398, PubMed:17632515, PubMed:18285462, PubMed:23519412, PubMed:8626503). 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 (PubMed:8626503). 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 (By similarity). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (PubMed:29180010). {ECO:0000250|UniProtKB:P70372, ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:14731398, ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23519412, ECO:0000269|PubMed:29180010, ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:32245947, ECO:0000269|PubMed:8626503}.
uniprot
proteins
mass_dalton
36092
uniprot
proteins
mutagenesis
MUTAGEN 158; /note="S->A: Decreases phosphorylation by PRKCD."; /evidence="ECO:0000269|PubMed:18285462"; MUTAGEN 221; /note="S->A: Decreases phosphorylation by PRKCD. Nearly abolishes phosphorylation by PRKCD and translocation from the nucleus into the cytoplasm; when associated with A-318."; /evidence="ECO:0000269|PubMed:18285462"; MUTAGEN 318; /note="S->A: Decreases phosphorylation by PRKCD. Nearly abolishes phosphorylation by PRKCD and translocation from the nucleus into the cytoplasm; when associated with A-221."; /evidence="ECO:0000269|PubMed:18285462
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by MAPKAPK2 (PubMed:14517288). Phosphorylated by PRKCD (PubMed:18285462). {ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:18285462}.; PTM: Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge. {ECO:0000269|PubMed:12237300}.
uniprot
proteins
protein_family
RRM elav family
uniprot
proteins
pubmed
11729309
uniprot
proteins
pubmed
12237300
uniprot
proteins
pubmed
14517288
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14731398
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17632515
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17932509
uniprot
proteins
pubmed
18161049
uniprot
proteins
pubmed
18191643
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18285462
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19029303
uniprot
proteins
pubmed
19561594
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20219472
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23519412
uniprot
proteins
pubmed
23640942
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27616329
uniprot
proteins
pubmed
27974568
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29180010
uniprot
proteins
pubmed
29476152
uniprot
proteins
pubmed
30067974
uniprot
proteins
pubmed
31358969
uniprot
proteins
pubmed
32245947
uniprot
proteins
pubmed
8626503
uniprot
proteins
sequence_length
326
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462, ECO:0000269|PubMed:19029303}. Nucleus {ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P70372}. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Note=Translocates into the cytoplasm following phosphorylation by MAPKAPK2 (PubMed:14517288). Likewise, phosphorylation by PRKCD promotes translocation from the nucleus into the cytoplasm, where it is associated with free and cytoskeleton-bound polysomes (PubMed:18285462). Localizes to the stress granules in the presence of PLEKHN1 (By similarity). {ECO:0000250|UniProtKB:P70372, ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:18285462}.
uniprot
proteins