{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q15717","secondaryAccessions":["B4DVB8","Q53XN6","Q9BTT1"],"uniProtkbId":"ELAV1_HUMAN","entryAudit":{"firstPublicDate":"2001-02-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2002-05-15","entryVersion":234,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"ELAV-like protein 1"}},"alternativeNames":[{"fullName":{"value":"Hu-antigen R"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8626503"}],"value":"HuR"}]}]},"genes":[{"geneName":{"value":"ELAVL1"},"synonyms":[{"value":"HUR"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70372"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14731398"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17632515"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18285462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19029303"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23519412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29180010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31358969"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32245947"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8626503"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70372"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11729309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14731398"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17632515"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17932509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18161049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18191643"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19029303"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20219472"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23640942"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27616329"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27974568"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30067974"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32245947"}],"value":"Monomer and homodimer (in vitro) (PubMed:17632515, PubMed:20219472). Interacts with ANP32A (PubMed:11729309). Interacts with ZNF385A; the interaction is indirect and mRNA-dependent and may regulate p53/TP53 expression (By similarity). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303). Interacts with AGO1 and AGO2 (PubMed:17932509). Interacts with IGF2BP1; the interaction is enhanced by SEPIN14P20 peptide RBPR (PubMed:29476152, PubMed:32245947). Interacts with IGF2BP2 and IGF2BP3 (PubMed:23640942, PubMed:29476152). Interacts with HNRNPL (PubMed:18161049). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (PubMed:14731398). Interacts with ILF3; this interaction occurs in a RNA-dependent manner (PubMed:14731398). Interacts with PLEKHN1 (PubMed:18191643, PubMed:27616329). Interacts with SHFL; the interaction increases in presence of RNA (PubMed:27974568). Interacts with YBX1; interaction recruits ELAVL1 on C5-methylcytosine (m5C)-containing mRNAs, thereby promoting mRNA stability (PubMed:31358969). Interacts with FXR1 (PubMed:30067974)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q15717","intActId":"EBI-374260"},"interactantTwo":{"uniProtKBAccession":"P54253","geneName":"ATXN1","intActId":"EBI-930964"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q15717","intActId":"EBI-374260"},"interactantTwo":{"uniProtKBAccession":"O00560","geneName":"SDCBP","intActId":"EBI-727004"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q15717","intActId":"EBI-374260"},"interactantTwo":{"uniProtKBAccession":"Q13148","geneName":"TARDBP","intActId":"EBI-372899"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q15717","intActId":"EBI-374260"},"interactantTwo":{"uniProtKBAccession":"P0CG48","geneName":"UBC","intActId":"EBI-3390054"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70372"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18285462"}],"value":"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)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17632515"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18285462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19029303"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14517288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17632515"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18285462"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70372"}],"value":"Cytoplasm, Stress granule","id":"SL-0496"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29476152"}],"value":"Cytoplasm, P-body","id":"SL-0230"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q15717-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q15717-2"],"sequenceIds":["VSP_056148"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8626503"}],"value":"Ubiquitous. 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Phosphorylated by PRKCD (PubMed:18285462)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12237300"}],"value":"Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the RRM elav family"}],"commentType":"SIMILARITY"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/44237/ELAVL1","ftp":false}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21406692"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"ELAV-like protein 1","featureId":"PRO_0000081577"},{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"RRM 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00176"}]},{"type":"Domain","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"RRM 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00176"}]},{"type":"Domain","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"RRM 3","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00176"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21406692"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21406692"}]},{"type":"Modified residue","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"18285462"}]},{"type":"Modified residue","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"18669648"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19690332"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"20068231"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"21406692"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Omega-N-methylarginine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70372"}]},{"type":"Modified residue","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Asymmetric dimethylarginine; 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