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Entry version 200 (16 Oct 2019)
Sequence version 2 (15 May 2002)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability (PubMed:14517288, PubMed:18285462, PubMed:31358969). 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, PubMed:14731398). 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). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (PubMed:29180010).By similarity9 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-450520 HuR (ELAVL1) binds and stabilizes mRNA
R-HSA-72163 mRNA Splicing - Major Pathway

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q15717

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ELAV-like protein 1
Alternative name(s):
Hu-antigen R
Short name:
HuR1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ELAVL1
Synonyms:HUR
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3312 ELAVL1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
603466 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15717

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
1994

Open Targets

More...
OpenTargetsi
ENSG00000066044

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27740

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q15717

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1250379

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ELAVL1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
20981691

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000815772 – 326ELAV-like protein 1Add BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei158Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

The CPTAC Assay portal

More...
CPTACi
CPTAC-923

Encyclopedia of Proteome Dynamics

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EPDi
Q15717

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15717

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q15717

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q15717

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q15717

PeptideAtlas

More...
PeptideAtlasi
Q15717

PRoteomics IDEntifications database

More...
PRIDEi
Q15717

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
60716 [Q15717-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q15717

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q15717

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q15717

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000066044 Expressed in 237 organ(s), highest expression level in endothelial cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15717 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15717 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB005256
HPA046298

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

Interacts with DHX36; this interaction occurs in a RNA-dependent manner (PubMed:14731398).

Interacts with ILF3; this interaction occurs in a RNA-dependent manner (PubMed:14731398).

Interacts with PLEKHN1 (PubMed:18191643, PubMed:27616329).

Interacts with SHFL; the interaction increases in presence of RNA (PubMed:27974568).

Interacts with YBX1; interaction recruits ELAVL1 on C5-methylcytosine (m5C)-containing mRNAs, thereby promoting mRNA stability (PubMed:31358969).

By similarity11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108309, 1802 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q15717

Database of interacting proteins

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DIPi
DIP-31291N

Protein interaction database and analysis system

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IntActi
Q15717, 66 interactors

Molecular INTeraction database

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MINTi
Q15717

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000385269

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q15717

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q15717

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q15717

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini20 – 98RRM 1PROSITE-ProRule annotationAdd BLAST79
Domaini106 – 186RRM 2PROSITE-ProRule annotationAdd BLAST81
Domaini244 – 322RRM 3PROSITE-ProRule annotationAdd BLAST79

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RRM elav family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0145 Eukaryota
ENOG410XP7S LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155528

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231162

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15717

KEGG Orthology (KO)

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KOi
K13088

Identification of Orthologs from Complete Genome Data

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OMAi
WQKHVTS

Database of Orthologous Groups

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OrthoDBi
614259at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q15717

TreeFam database of animal gene trees

More...
TreeFami
TF313377

Family and domain databases

Conserved Domains Database

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CDDi
cd12650 RRM1_Hu, 1 hit
cd12773 RRM2_HuR, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.330, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00076 RRM_1, 3 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00961 HUDSXLRNA

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00360 RRM, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54928 SSF54928, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01661 ELAV_HUD_SF, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50102 RRM, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R055M0R055_HUMAN
ELAV-like protein 1
ELAVL1
133Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0QZR9M0QZR9_HUMAN
ELAV-like protein 1
ELAVL1
153Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti180T → A in AAB41913 (PubMed:8626503).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0561481M → MGSGGRSAQVSTGQRAWLLP CRFLKNTM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS12193.1 [Q15717-1]

NCBI Reference Sequences

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RefSeqi
NP_001410.2, NM_001419.2 [Q15717-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000407627; ENSP00000385269; ENSG00000066044 [Q15717-1]
ENST00000596459; ENSP00000472197; ENSG00000066044 [Q15717-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
1994

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1994

UCSC genome browser

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UCSCi
uc002mjb.4 human [Q15717-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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]

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
6G2KX-ray2.01A/B/C243-326[»]
6GC5X-ray1.90A/B/C/D241-326[»]
6GD1X-ray2.01A/B243-326[»]
6GD2X-ray1.90A/B/C243-326[»]
6GD3X-ray1.35A/B/C243-326[»]
SMRiQ15717
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108309, 1802 interactors
CORUMiQ15717
DIPiDIP-31291N
IntActiQ15717, 66 interactors
MINTiQ15717
STRINGi9606.ENSP00000385269

Chemistry databases

BindingDBiQ15717
ChEMBLiCHEMBL1250379

PTM databases

iPTMnetiQ15717
PhosphoSitePlusiQ15717
SwissPalmiQ15717

Polymorphism and mutation databases

BioMutaiELAVL1
DMDMi20981691

Proteomic databases

CPTACiCPTAC-923
EPDiQ15717
jPOSTiQ15717
MassIVEiQ15717
MaxQBiQ15717
PaxDbiQ15717
PeptideAtlasiQ15717
PRIDEiQ15717
ProteomicsDBi60716 [Q15717-1]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
1994

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1994
DisGeNETi1994

GeneCards: human genes, protein and diseases

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GeneCardsi
ELAVL1
HGNCiHGNC:3312 ELAVL1
HPAiCAB005256
HPA046298
MIMi603466 gene
neXtProtiNX_Q15717
OpenTargetsiENSG00000066044
PharmGKBiPA27740

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0145 Eukaryota
ENOG410XP7S LUCA
GeneTreeiENSGT00940000155528
HOGENOMiHOG000231162
InParanoidiQ15717
KOiK13088
OMAiWQKHVTS
OrthoDBi614259at2759
PhylomeDBiQ15717
TreeFamiTF313377

Enzyme and pathway databases

ReactomeiR-HSA-450520 HuR (ELAVL1) binds and stabilizes mRNA
R-HSA-72163 mRNA Splicing - Major Pathway
SIGNORiQ15717

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ELAVL1 human
EvolutionaryTraceiQ15717

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ELAVL1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1994
PharosiQ15717

Protein Ontology

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PROi
PR:Q15717

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000066044 Expressed in 237 organ(s), highest expression level in endothelial cell
ExpressionAtlasiQ15717 baseline and differential
GenevisibleiQ15717 HS

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, 2 hits
TIGRFAMsiTIGR01661 ELAV_HUD_SF, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiELAV1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15717
Secondary accession number(s): B4DVB8, Q53XN6, Q9BTT1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 15, 2002
Last modified: October 16, 2019
This is version 200 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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