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Q15717 (ELAV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ELAV-like protein 1
Alternative name(s):
Hu-antigen R
Short name=HuR
Gene names
Name:ELAVL1
Synonyms:HUR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation. 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. 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. Ref.14

Subunit structure

Interacts with ANP32A By similarity. Interact 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. Interacts with ANP32A, AGO1 and AGO2. Interacts with IGF2BP2 and IGF2BP3. Ref.5 Ref.9 Ref.14 Ref.19

Subcellular location

Cytoplasm. Nucleus. Note: Translocates into the cytoplasm following phosphorylation by MAPKAPK2. Ref.7 Ref.14

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated by MAPKAPK2. Ref.7

Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge. Ref.6

Sequence similarities

Belongs to the RRM elav family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process3'-UTR-mediated mRNA stabilization

Inferred from direct assay Ref.7. Source: UniProtKB

RNA metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA stabilization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

multicellular organismal development

Traceable author statement PubMed 9003489. Source: ProtInc

positive regulation of translation

Inferred from direct assay PubMed 21613615. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.7Ref.14. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionAU-rich element binding

Inferred from direct assay Ref.7. Source: UniProtKB

RNA binding

Inferred from direct assay Ref.13. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

mRNA 3'-UTR AU-rich region binding

Inferred from direct assay PubMed 23056314. Source: MGI

mRNA binding

Traceable author statement PubMed 10660597. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBCP0CG484EBI-374260,EBI-3390054

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 326325ELAV-like protein 1
PRO_0000081577

Regions

Domain20 – 9879RRM 1
Domain106 – 18681RRM 2
Domain244 – 32279RRM 3

Amino acid modifications

Modified residue21N-acetylserine Ref.18
Modified residue21Phosphoserine Ref.18
Modified residue2021Phosphoserine Ref.12 Ref.15 Ref.16 Ref.18
Modified residue2171Omega-N-methylated arginine; by CARM1 Ref.6

Experimental info

Sequence conflict1801T → A in AAB41913. Ref.1

Secondary structure

.............................. 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15717 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 0B86143805264DEF

FASTA32636,092
        10         20         30         40         50         60 
MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK LIRDKVAGHS 

        70         80         90        100        110        120 
LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS EVIKDANLYI SGLPRTMTQK 

       130        140        150        160        170        180 
DVEDMFSRFG RIINSRVLVD QTTGLSRGVA FIRFDKRSEA EEAITSFNGH KPPGSSEPIT 

       190        200        210        220        230        240 
VKFAANPNQN KNVALLSQLY HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA 

       250        260        270        280        290        300 
SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM 

       310        320 
AIASLNGYRL GDKILQVSFK TNKSHK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein."
Ma W.-J., Cheng S., Campbell C., Wright A., Furneaux H.M.
J. Biol. Chem. 271:8144-8151(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix.
[5]"Delineation of mRNA export pathways by the use of cell-permeable peptides."
Gallouzi I.-E., Steitz J.A.
Science 294:1895-1901(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANP32A.
[6]"Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase."
Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., Laird-Offringa I.A.
J. Biol. Chem. 277:44623-44630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-217.
[7]"Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2."
Tran H., Maurer F., Nagamine Y.
Mol. Cell. Biol. 23:7177-7188(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION BY MAPKAPK2.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[10]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[14]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[19]"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
Wachter K., Kohn M., Stohr N., Huttelmaier S.
Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38175 mRNA. Translation: AAB41913.1.
BT009793 mRNA. Translation: AAP88795.1.
CH471139 Genomic DNA. Translation: EAW68949.1.
BC003376 mRNA. Translation: AAH03376.1.
RefSeqNP_001410.2. NM_001419.2.
UniGeneHs.184492.
Hs.713744.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HI9X-ray2.00A/B/C/D18-99[»]
4ED5X-ray2.00A/B18-186[»]
4EGLX-ray2.90A18-186[»]
4FXVX-ray1.90A/B/C/D20-99[»]
ProteinModelPortalQ15717.
SMRQ15717. Positions 18-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108309. 1733 interactions.
DIPDIP-31291N.
IntActQ15717. 34 interactions.
MINTMINT-5001300.
STRING9606.ENSP00000385269.

Chemistry

BindingDBQ15717.
ChEMBLCHEMBL1250379.

PTM databases

PhosphoSiteQ15717.

Polymorphism databases

DMDM20981691.

Proteomic databases

PaxDbQ15717.
PeptideAtlasQ15717.
PRIDEQ15717.

Protocols and materials databases

DNASU1994.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000407627; ENSP00000385269; ENSG00000066044.
ENST00000596459; ENSP00000472197; ENSG00000066044.
GeneID1994.
KEGGhsa:1994.
UCSCuc002mjb.3. human.

Organism-specific databases

CTD1994.
GeneCardsGC19M008023.
HGNCHGNC:3312. ELAVL1.
HPACAB005256.
MIM603466. gene.
neXtProtNX_Q15717.
PharmGKBPA27740.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000231162.
HOVERGENHBG002295.
InParanoidQ15717.
KOK13088.
OrthoDBEOG77T14R.
PhylomeDBQ15717.
TreeFamTF313377.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15717.
BgeeQ15717.
CleanExHS_ELAVL1.
GenevestigatorQ15717.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSPR00961. HUDSXLRNA.
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15717.
GeneWikiELAVL1.
GenomeRNAi1994.
NextBio8063.
PROQ15717.
SOURCESearch...

Entry information

Entry nameELAV1_HUMAN
AccessionPrimary (citable) accession number: Q15717
Secondary accession number(s): Q53XN6, Q9BTT1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 15, 2002
Last modified: April 16, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM