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Protein

ELAV-like protein 1

Gene

ELAVL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (PubMed:14517288, PubMed:18285462). Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation (By similarity). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:8626503, PubMed:17632515, PubMed:18285462, PubMed:23519412). 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).By similarity6 Publications

GO - Molecular functioni

  • AU-rich element binding Source: UniProtKB
  • double-stranded RNA binding Source: MGI
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA binding Source: ProtInc
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • mRNA stabilization Source: UniProtKB
  • multicellular organism development Source: ProtInc
  • negative regulation of gene silencing by miRNA Source: BHF-UCL
  • positive regulation of translation Source: MGI
  • regulation of mRNA stability Source: Reactome
  • regulation of stem cell population maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000066044-MONOMER.
ReactomeiR-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-72163. mRNA Splicing - Major Pathway.
SIGNORiQ15717.

Names & Taxonomyi

Protein namesi
Recommended name:
ELAV-like protein 1
Alternative name(s):
Hu-antigen R
Short name:
HuR1 Publication
Gene namesi
Name:ELAVL1
Synonyms:HUR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3312. ELAVL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi158S → A: Decreases phosphorylation by PRKCD. 1 Publication1
Mutagenesisi221S → A: Decreases phosphorylation by PRKCD. Nearly abolishes phosphorylation by PRKCD and translocation from the nucleus into the cytoplasm; when associated with A-318. 1 Publication1
Mutagenesisi318S → A: Decreases phosphorylation by PRKCD. Nearly abolishes phosphorylation by PRKCD and translocation from the nucleus into the cytoplasm; when associated with A-221. 1 Publication1

Organism-specific databases

DisGeNETi1994.
OpenTargetsiENSG00000066044.
PharmGKBiPA27740.

Chemistry databases

ChEMBLiCHEMBL1250379.

Polymorphism and mutation databases

BioMutaiELAVL1.
DMDMi20981691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000815772 – 326ELAV-like protein 1Add BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei158Phosphoserine1 Publication1
Modified residuei197PhosphoserineCombined sources1
Modified residuei202PhosphoserineCombined sources1
Modified residuei206Omega-N-methylarginineBy similarity1
Modified residuei217Omega-N-methylarginine; alternateCombined sources1
Modified residuei217Omega-N-methylated arginine; by CARM1; alternate1 Publication1
Modified residuei221Phosphoserine1 Publication1
Modified residuei318Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated by MAPKAPK2 (PubMed:14517288). Phosphorylated by PRKCD (PubMed:18285462).2 Publications
Methylated at Arg-217 by CARM1 in macrophages in response to LPS challenge.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ15717.
MaxQBiQ15717.
PaxDbiQ15717.
PeptideAtlasiQ15717.
PRIDEiQ15717.

PTM databases

iPTMnetiQ15717.
PhosphoSitePlusiQ15717.
SwissPalmiQ15717.

Expressioni

Tissue specificityi

Ubiquitous. Detected in brain, liver, thymus and muscle.1 Publication

Gene expression databases

BgeeiENSG00000066044.
CleanExiHS_ELAVL1.
ExpressionAtlasiQ15717. baseline and differential.
GenevisibleiQ15717. HS.

Organism-specific databases

HPAiCAB005256.
HPA046298.

Interactioni

Subunit structurei

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 IGF2BP2 and IGF2BP3 (PubMed:23640942). Interacts with HNRNPL (PubMed:18161049).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SDCBPO005603EBI-374260,EBI-727004
UBCP0CG484EBI-374260,EBI-3390054

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108309. 1766 interactors.
DIPiDIP-31291N.
IntActiQ15717. 45 interactors.
MINTiMINT-5001300.
STRINGi9606.ENSP00000385269.

Chemistry databases

BindingDBiQ15717.

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 26Combined sources7
Helixi33 – 41Combined sources9
Beta strandi46 – 53Combined sources8
Beta strandi55 – 57Combined sources3
Beta strandi60 – 70Combined sources11
Helixi71 – 81Combined sources11
Beta strandi92 – 95Combined sources4
Helixi101 – 103Combined sources3
Beta strandi107 – 111Combined sources5
Helixi119 – 126Combined sources8
Helixi127 – 129Combined sources3
Beta strandi132 – 139Combined sources8
Turni141 – 143Combined sources3
Beta strandi146 – 156Combined sources11
Helixi157 – 167Combined sources11
Beta strandi180 – 183Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15717.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 98RRM 1PROSITE-ProRule annotationAdd BLAST79
Domaini106 – 186RRM 2PROSITE-ProRule annotationAdd BLAST81
Domaini244 – 322RRM 3PROSITE-ProRule annotationAdd BLAST79

Domaini

The first RRM (RNA recognition motif) domain is essential for binding to AU-rich elements.1 Publication

Sequence similaritiesi

Belongs to the RRM elav family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0145. Eukaryota.
ENOG410XP7S. LUCA.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ15717.
KOiK13088.
OMAiNNIDEQK.
OrthoDBiEOG091G0G9L.
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]
SUPFAMiSSF54928. SSF54928. 3 hits.
TIGRFAMsiTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15717-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK
60 70 80 90 100
LIRDKVAGHS LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS
110 120 130 140 150
EVIKDANLYI SGLPRTMTQK DVEDMFSRFG RIINSRVLVD QTTGLSRGVA
160 170 180 190 200
FIRFDKRSEA EEAITSFNGH KPPGSSEPIT VKFAANPNQN KNVALLSQLY
210 220 230 240 250
HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA SSGWCIFIYN
260 270 280 290 300
LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
310 320
AIASLNGYRL GDKILQVSFK TNKSHK
Length:326
Mass (Da):36,092
Last modified:May 15, 2002 - v2
Checksum:i0B86143805264DEF
GO
Isoform 2 (identifier: Q15717-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGSGGRSAQVSTGQRAWLLPCRFLKNTM

Note: No experimental confirmation available.
Show »
Length:353
Mass (Da):38,996
Checksum:i3398C72FC8B54012
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti180T → A in AAB41913 (PubMed:8626503).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0561481M → MGSGGRSAQVSTGQRAWLLP CRFLKNTM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38175 mRNA. Translation: AAB41913.1.
BT009793 mRNA. Translation: AAP88795.1.
AK301013 mRNA. Translation: BAG62630.1.
AC008975 Genomic DNA. No translation available.
AC010336 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68949.1.
BC003376 mRNA. Translation: AAH03376.1.
CCDSiCCDS12193.1. [Q15717-1]
RefSeqiNP_001410.2. NM_001419.2. [Q15717-1]
UniGeneiHs.184492.
Hs.713744.

Genome annotation databases

EnsembliENST00000407627; ENSP00000385269; ENSG00000066044. [Q15717-1]
ENST00000596459; ENSP00000472197; ENSG00000066044. [Q15717-1]
GeneIDi1994.
KEGGihsa:1994.
UCSCiuc002mjb.4. human. [Q15717-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38175 mRNA. Translation: AAB41913.1.
BT009793 mRNA. Translation: AAP88795.1.
AK301013 mRNA. Translation: BAG62630.1.
AC008975 Genomic DNA. No translation available.
AC010336 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68949.1.
BC003376 mRNA. Translation: AAH03376.1.
CCDSiCCDS12193.1. [Q15717-1]
RefSeqiNP_001410.2. NM_001419.2. [Q15717-1]
UniGeneiHs.184492.
Hs.713744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108309. 1766 interactors.
DIPiDIP-31291N.
IntActiQ15717. 45 interactors.
MINTiMINT-5001300.
STRINGi9606.ENSP00000385269.

Chemistry databases

BindingDBiQ15717.
ChEMBLiCHEMBL1250379.

PTM databases

iPTMnetiQ15717.
PhosphoSitePlusiQ15717.
SwissPalmiQ15717.

Polymorphism and mutation databases

BioMutaiELAVL1.
DMDMi20981691.

Proteomic databases

EPDiQ15717.
MaxQBiQ15717.
PaxDbiQ15717.
PeptideAtlasiQ15717.
PRIDEiQ15717.

Protocols and materials databases

DNASUi1994.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000407627; ENSP00000385269; ENSG00000066044. [Q15717-1]
ENST00000596459; ENSP00000472197; ENSG00000066044. [Q15717-1]
GeneIDi1994.
KEGGihsa:1994.
UCSCiuc002mjb.4. human. [Q15717-1]

Organism-specific databases

CTDi1994.
DisGeNETi1994.
GeneCardsiELAVL1.
HGNCiHGNC:3312. ELAVL1.
HPAiCAB005256.
HPA046298.
MIMi603466. gene.
neXtProtiNX_Q15717.
OpenTargetsiENSG00000066044.
PharmGKBiPA27740.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0145. Eukaryota.
ENOG410XP7S. LUCA.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ15717.
KOiK13088.
OMAiNNIDEQK.
OrthoDBiEOG091G0G9L.
PhylomeDBiQ15717.
TreeFamiTF313377.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000066044-MONOMER.
ReactomeiR-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-72163. mRNA Splicing - Major Pathway.
SIGNORiQ15717.

Miscellaneous databases

EvolutionaryTraceiQ15717.
GeneWikiiELAVL1.
GenomeRNAii1994.
PROiQ15717.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000066044.
CleanExiHS_ELAVL1.
ExpressionAtlasiQ15717. baseline and differential.
GenevisibleiQ15717. HS.

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]
SUPFAMiSSF54928. SSF54928. 3 hits.
TIGRFAMsiTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiELAV1_HUMAN
AccessioniPrimary (citable) accession number: Q15717
Secondary accession number(s): B4DVB8, Q53XN6, Q9BTT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 15, 2002
Last modified: November 30, 2016
This is version 171 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.