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Q15717 (ELAV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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

Involved in 3'-UTR ARE-mediated MYC stabilization. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, HUR 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. Ref.14

Subunit structure

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, EIF2C1 and EIF2C2. Ref.5 Ref.9 Ref.14

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.

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 EIF2C1 AND EIF2C2.
[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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
+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.
IPIIPI00940851.
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.
ModBaseSearch...

Protein-protein interaction databases

IntActQ15717. 21 interactions.
MINTMINT-5001300.
STRING9606.ENSP00000385269.

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.
OrthoDBEOG4Z8XWZ.
PhylomeDBQ15717.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15717.
BgeeQ15717.
CleanExHS_ELAVL1.
GenevestigatorQ15717.
GermOnlineENSG00000066044. Homo sapiens.

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

BindingDBQ15717.
ChEMBLCHEMBL1250379.
EvolutionaryTraceQ15717.
GenomeRNAi1994.
NextBio8063.
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: May 1, 2013
This is version 136 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

Human chromosome 19

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families