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Protein

ELAV-like protein 1

Gene

ELAVL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • miRNA binding Source: UniProtKB
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA binding Source: ProtInc
  • 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: MGI
  • multicellular organism development Source: ProtInc
  • negative regulation of gene silencing by miRNA Source: UniProtKB
  • positive regulation of translation Source: MGI
  • protein homooligomerization Source: UniProtKB
  • regulation of mRNA stability Source: Reactome
  • regulation of stem cell population maintenance Source: UniProtKB

Keywordsi

Molecular functionRNA-binding

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000066044.13
HGNCiHGNC:3312 ELAVL1
MIMi603466 gene
neXtProtiNX_Q15717

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15717
MaxQBiQ15717
PaxDbiQ15717
PeptideAtlasiQ15717
PRIDEiQ15717
ProteomicsDBi60716

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

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi108309, 1780 interactors
CORUMiQ15717
DIPiDIP-31291N
IntActiQ15717, 51 interactors
MINTiQ15717
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
Turni7 – 10Combined sources4
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[»]
5SZWNMR-A1-99[»]
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

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd12650 RRM1_Hu, 1 hit
cd12773 RRM2_HuR, 1 hit
Gene3Di3.30.70.330, 3 hits
InterProiView protein in InterPro
IPR006548 ELAD_HU_SF
IPR034775 ELAV/Hu_RRM1
IPR002343 Hud_Sxl_RNA
IPR034996 HuR_RRM2
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PfamiView protein in Pfam
PF00076 RRM_1, 3 hits
PRINTSiPR00961 HUDSXLRNA
SMARTiView protein in SMART
SM00360 RRM, 3 hits
SUPFAMiSSF54928 SSF54928, 3 hits
TIGRFAMsiTIGR01661 ELAV_HUD_SF, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 3 hits

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

Similar proteinsi

Entry informationi

Entry nameiELAV1_HUMAN
AccessioniPrimary (citable) accession number: Q15717
Secondary accession number(s): B4DVB8, Q53XN6, Q9BTT1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 15, 2002
Last modified: June 20, 2018
This is version 186 of the entry and version 2 of the sequence. See 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

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