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Protein

ELAV-like protein 4

Gene

Elavl4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA (By similarity). May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR.By similarity1 Publication

GO - Molecular functioni

  • AU-rich element binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: RGD
  • mRNA binding Source: RGD
  • nucleotide binding Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • associative learning Source: RGD
  • cellular response to nerve growth factor stimulus Source: RGD
  • nervous system development Source: RGD
  • neuron differentiation Source: RGD
  • positive regulation of dendrite development Source: RGD
  • regeneration Source: RGD
  • regulation of mRNA stability Source: RGD
  • response to cocaine Source: RGD
  • response to endoplasmic reticulum stress Source: RGD
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ELAV-like protein 4
Alternative name(s):
Hu-antigen D
Short name:
HuD
Paraneoplastic encephalomyelitis antigen HuD
Gene namesi
Name:Elavl4
Synonyms:Hud
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1560027. Elavl4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytoskeleton Source: RGD
  • cytosol Source: RGD
  • dendrite Source: RGD
  • growth cone Source: RGD
  • membrane Source: RGD
  • neuronal cell body Source: RGD
  • nuclear envelope Source: RGD
  • nucleus Source: RGD
  • polysomal ribosome Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373ELAV-like protein 4PRO_0000081585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei221 – 2211PhosphoserineCombined sources
Modified residuei236 – 2361Omega-N-methylated arginine; by CARM11 Publication

Post-translational modificationi

Methylation at Arg-236 by CARM1 weakens protective binding to the 3'-UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state. Methylation is inhibited by NGF, which facilitates neurite outgrowth.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiO09032.

PTM databases

iPTMnetiO09032.
PhosphoSiteiO09032.

Expressioni

Gene expression databases

GenevisibleiO09032. RN.

Interactioni

Subunit structurei

Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP.By similarity

Protein-protein interaction databases

BioGridi268628. 1 interaction.
STRINGi10116.ENSRNOP00000037614.

Structurei

3D structure databases

ProteinModelPortaliO09032.
SMRiO09032. Positions 37-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 11779RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 20581RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini290 – 36879RRM 3PROSITE-ProRule annotationAdd
BLAST

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.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiO09032.
OMAiGYKWEIL.
OrthoDBiEOG77T14R.
PhylomeDBiO09032.

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]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: At least 3 isoforms are produced.

Isoform 1 (identifier: O09032-1) [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
MEPQVSNGPT SNTSNGPSSN NRNCPSPMQT GAATDDSKTN LIVNYLPQNM
60 70 80 90 100
TQEEFRSLFG SIGEIESCKL VRDKITGQSL GYGFVNYIDP KDAEKAINTL
110 120 130 140 150
NGLRLQTKTI KVSYARPSSA SIRDANLYVS GLPKTMTQKE LEQLFSQYGR
160 170 180 190 200
IITSRILVDQ VTGVSRGVGF IRFDKRIEAE EAIKGLNGQK PSGATEPITV
210 220 230 240 250
KFANNPSQKS SQALLSQLYQ SPNRRYPGPL HHQAQRFRLD NLLNMAYGVK
260 270 280 290 300
RLMSGPVPPS ACPPRFSPIT IDGMTSLVGM NIPGHTGTGW CIFVYNLSPD
310 320 330 340 350
SDESVLWQLF GPFGAVNNVK VIRDFNTNKC KGFGFVTMTN YDEAAMAIAS
360 370
LNGYRLGDRV LQVSFKTNKA HKS
Length:373
Mass (Da):40,964
Last modified:July 1, 1997 - v1
Checksum:i05DB21C4272CAC62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83320 mRNA. Translation: AAB50733.1.
UniGeneiRn.134702.

Genome annotation databases

UCSCiRGD:1560027. rat. [O09032-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83320 mRNA. Translation: AAB50733.1.
UniGeneiRn.134702.

3D structure databases

ProteinModelPortaliO09032.
SMRiO09032. Positions 37-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi268628. 1 interaction.
STRINGi10116.ENSRNOP00000037614.

PTM databases

iPTMnetiO09032.
PhosphoSiteiO09032.

Proteomic databases

PaxDbiO09032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1560027. rat. [O09032-1]

Organism-specific databases

RGDi1560027. Elavl4.

Phylogenomic databases

eggNOGiKOG0145. Eukaryota.
ENOG410XP7S. LUCA.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiO09032.
OMAiGYKWEIL.
OrthoDBiEOG77T14R.
PhylomeDBiO09032.

Miscellaneous databases

PROiO09032.

Gene expression databases

GenevisibleiO09032. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The RNA binding protein HuD: rat cDNA and analysis of the alternative spliced mRNA in neuronal differentiating cell lines P19 and PC12."
    Steller U., Kohls S., Muller B., Soller R., Muller R., Schlender J., Blohm D.H.
    Brain Res. Mol. Brain Res. 35:285-296(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: FUNCTION, METHYLATION AT ARG-236.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiELAV4_RAT
AccessioniPrimary (citable) accession number: O09032
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.