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Q15717

- ELAV1_HUMAN

UniProt

Q15717 - ELAV1_HUMAN

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Protein
ELAV-like protein 1
Gene
ELAVL1, HUR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. AU-rich element binding Source: UniProtKB
  2. RNA binding Source: UniProtKB
  3. double-stranded RNA binding Source: MGI
  4. mRNA 3'-UTR AU-rich region binding Source: MGI
  5. mRNA 3'-UTR binding Source: UniProtKB
  6. mRNA binding Source: ProtInc
  7. nucleotide binding Source: InterPro
  8. poly(A) RNA binding Source: UniProtKB
  9. protein binding Source: UniProtKB
  10. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  2. RNA metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. mRNA stabilization Source: UniProtKB
  6. multicellular organismal development Source: ProtInc
  7. positive regulation of translation Source: MGI
  8. regulation of stem cell maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_25218. HuR stabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
ELAV-like protein 1
Alternative name(s):
Hu-antigen R
Short name:
HuR
Gene namesi
Name:ELAVL1
Synonyms:HUR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3312. ELAVL1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Translocates into the cytoplasm following phosphorylation by MAPKAPK2.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 326325ELAV-like protein 1
PRO_0000081577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei202 – 2021Phosphoserine4 Publications
Modified residuei217 – 2171Omega-N-methylated arginine; by CARM11 Publication

Post-translational modificationi

Phosphorylated by MAPKAPK2.1 Publication
Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ15717.
PaxDbiQ15717.
PeptideAtlasiQ15717.
PRIDEiQ15717.

PTM databases

PhosphoSiteiQ15717.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ15717.
BgeeiQ15717.
CleanExiHS_ELAVL1.
GenevestigatoriQ15717.

Organism-specific databases

HPAiCAB005256.

Interactioni

Subunit structurei

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 IGF2BP3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBCP0CG484EBI-374260,EBI-3390054

Protein-protein interaction databases

BioGridi108309. 1744 interactions.
DIPiDIP-31291N.
IntActiQ15717. 34 interactions.
MINTiMINT-5001300.
STRINGi9606.ENSP00000385269.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 267
Helixi33 – 419
Beta strandi46 – 538
Beta strandi55 – 573
Beta strandi60 – 7011
Helixi71 – 8111
Beta strandi92 – 954
Helixi101 – 1033
Beta strandi107 – 1115
Helixi119 – 1268
Helixi127 – 1293
Beta strandi132 – 1398
Turni141 – 1433
Beta strandi146 – 15611
Helixi157 – 16711
Beta strandi180 – 1834

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ15717.
SMRiQ15717. Positions 18-326.

Miscellaneous databases

EvolutionaryTraceiQ15717.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9879RRM 1
Add
BLAST
Domaini106 – 18681RRM 2
Add
BLAST
Domaini244 – 32279RRM 3
Add
BLAST

Sequence similaritiesi

Belongs to the RRM elav family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ15717.
KOiK13088.
OrthoDBiEOG77T14R.
PhylomeDBiQ15717.
TreeFamiTF313377.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSiPR00961. HUDSXLRNA.
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15717-1 [UniParc]FASTAAdd to Basket

« Hide

MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK    50
LIRDKVAGHS LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS 100
EVIKDANLYI SGLPRTMTQK DVEDMFSRFG RIINSRVLVD QTTGLSRGVA 150
FIRFDKRSEA EEAITSFNGH KPPGSSEPIT VKFAANPNQN KNVALLSQLY 200
HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA SSGWCIFIYN 250
LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM 300
AIASLNGYRL GDKILQVSFK TNKSHK 326
Length:326
Mass (Da):36,092
Last modified:May 15, 2002 - v2
Checksum:i0B86143805264DEF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801T → A in AAB41913. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38175 mRNA. Translation: AAB41913.1.
BT009793 mRNA. Translation: AAP88795.1.
CH471139 Genomic DNA. Translation: EAW68949.1.
BC003376 mRNA. Translation: AAH03376.1.
CCDSiCCDS12193.1.
RefSeqiNP_001410.2. NM_001419.2.
UniGeneiHs.184492.
Hs.713744.

Genome annotation databases

EnsembliENST00000407627; ENSP00000385269; ENSG00000066044.
ENST00000596459; ENSP00000472197; ENSG00000066044.
GeneIDi1994.
KEGGihsa:1994.
UCSCiuc002mjb.3. human.

Polymorphism databases

DMDMi20981691.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38175 mRNA. Translation: AAB41913.1 .
BT009793 mRNA. Translation: AAP88795.1 .
CH471139 Genomic DNA. Translation: EAW68949.1 .
BC003376 mRNA. Translation: AAH03376.1 .
CCDSi CCDS12193.1.
RefSeqi NP_001410.2. NM_001419.2.
UniGenei Hs.184492.
Hs.713744.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3HI9 X-ray 2.00 A/B/C/D 18-99 [» ]
4ED5 X-ray 2.00 A/B 18-186 [» ]
4EGL X-ray 2.90 A 18-186 [» ]
4FXV X-ray 1.90 A/B/C/D 20-99 [» ]
ProteinModelPortali Q15717.
SMRi Q15717. Positions 18-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108309. 1744 interactions.
DIPi DIP-31291N.
IntActi Q15717. 34 interactions.
MINTi MINT-5001300.
STRINGi 9606.ENSP00000385269.

Chemistry

BindingDBi Q15717.
ChEMBLi CHEMBL1250379.

PTM databases

PhosphoSitei Q15717.

Polymorphism databases

DMDMi 20981691.

Proteomic databases

MaxQBi Q15717.
PaxDbi Q15717.
PeptideAtlasi Q15717.
PRIDEi Q15717.

Protocols and materials databases

DNASUi 1994.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000407627 ; ENSP00000385269 ; ENSG00000066044 .
ENST00000596459 ; ENSP00000472197 ; ENSG00000066044 .
GeneIDi 1994.
KEGGi hsa:1994.
UCSCi uc002mjb.3. human.

Organism-specific databases

CTDi 1994.
GeneCardsi GC19M008023.
HGNCi HGNC:3312. ELAVL1.
HPAi CAB005256.
MIMi 603466. gene.
neXtProti NX_Q15717.
PharmGKBi PA27740.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000231162.
HOVERGENi HBG002295.
InParanoidi Q15717.
KOi K13088.
OrthoDBi EOG77T14R.
PhylomeDBi Q15717.
TreeFami TF313377.

Enzyme and pathway databases

Reactomei REACT_25218. HuR stabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei Q15717.
GeneWikii ELAVL1.
GenomeRNAii 1994.
NextBioi 8063.
PROi Q15717.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15717.
Bgeei Q15717.
CleanExi HS_ELAVL1.
Genevestigatori Q15717.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 3 hits.
[Graphical view ]
PRINTSi PR00961. HUDSXLRNA.
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
TIGRFAMsi TIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiELAV1_HUMAN
AccessioniPrimary (citable) accession number: Q15717
Secondary accession number(s): Q53XN6, Q9BTT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 15, 2002
Last modified: September 3, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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