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Protein

ELAV-like protein 2

Gene

ELAVL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds RNA. Seems to recognize a GAAA motif. Can bind to its own 3'-UTR, the FOS 3'-UTR and the ID 3'-UTR.

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: ProtInc
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA splicing, via spliceosome Source: Reactome
  • regulation of transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
ELAV-like protein 2
Alternative name(s):
ELAV-like neuronal protein 1
Hu-antigen B
Short name:
HuB
Nervous system-specific RNA-binding protein Hel-N1
Gene namesi
Name:ELAVL2
Synonyms:HUB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:3313. ELAVL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27741.

Polymorphism and mutation databases

BioMutaiELAVL2.
DMDMi93141258.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359ELAV-like protein 2PRO_0000081579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei221 – 2211PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ12926.
MaxQBiQ12926.
PaxDbiQ12926.
PRIDEiQ12926.

PTM databases

iPTMnetiQ12926.
PhosphoSiteiQ12926.

Expressioni

Tissue specificityi

Brain; neural-specific.

Gene expression databases

BgeeiQ12926.
CleanExiHS_ELAVL2.
ExpressionAtlasiQ12926. baseline and differential.
GenevisibleiQ12926. HS.

Organism-specific databases

HPAiCAB022222.

Interactioni

Subunit structurei

Interacts with IGF2BP1.1 Publication

Protein-protein interaction databases

BioGridi108308. 113 interactions.
IntActiQ12926. 1 interaction.
STRINGi9606.ENSP00000369460.

Structurei

3D structure databases

ProteinModelPortaliQ12926.
SMRiQ12926. Positions 37-251, 275-355.
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
Domaini276 – 35479RRM 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.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ12926.
KOiK13208.
OrthoDBiEOG77T14R.
PhylomeDBiQ12926.
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.

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

Isoform 1 (identifier: Q12926-1) [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
METQLSNGPT CNNTANGPTT INNNCSSPVD SGNTEDSKTN LIVNYLPQNM
60 70 80 90 100
TQEELKSLFG SIGEIESCKL VRDKITGQSL GYGFVNYIDP KDAEKAINTL
110 120 130 140 150
NGLRLQTKTI KVSYARPSSA SIRDANLYVS GLPKTMTQKE LEQLFSQYGR
160 170 180 190 200
IITSRILVDQ VTGISRGVGF IRFDKRIEAE EAIKGLNGQK PPGATEPITV
210 220 230 240 250
KFANNPSQKT NQAILSQLYQ SPNRRYPGPL AQQAQRFRLD NLLNMAYGVK
260 270 280 290 300
RFSPMTIDGM TSLAGINIPG HPGTGWCIFV YNLAPDADES ILWQMFGPFG
310 320 330 340 350
AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA AMAIASLNGY RLGDRVLQVS

FKTNKTHKA
Length:359
Mass (Da):39,504
Last modified:April 18, 2006 - v2
Checksum:i15E87088FC546DDC
GO
Isoform 2 (identifier: Q12926-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     239-251: Missing.

Show »
Length:346
Mass (Da):38,015
Checksum:iF1EC0F69EE5D15DD
GO

Sequence cautioni

The sequence BAD92531.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351A → R (PubMed:8158249).Curated
Sequence conflicti335 – 3351A → R (PubMed:7972035).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei239 – 25113Missing in isoform 2. 2 PublicationsVSP_005788Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12431 mRNA. Translation: AAA69698.1.
U29943 mRNA. Translation: AAA70417.1.
AB209294 mRNA. Translation: BAD92531.1. Different initiation.
AL161628, AL445623 Genomic DNA. Translation: CAI13376.1.
AL161628 Genomic DNA. Translation: CAC22160.1.
CH471071 Genomic DNA. Translation: EAW58581.1.
CH471071 Genomic DNA. Translation: EAW58582.1.
BC030692 mRNA. Translation: AAH30692.1.
CCDSiCCDS55298.1. [Q12926-2]
CCDS6515.1. [Q12926-1]
PIRiI38726.
I39077.
RefSeqiNP_001164666.1. NM_001171195.1. [Q12926-2]
NP_001164668.1. NM_001171197.1. [Q12926-2]
NP_004423.2. NM_004432.3. [Q12926-1]
UniGeneiHs.166109.

Genome annotation databases

EnsembliENST00000223951; ENSP00000223951; ENSG00000107105. [Q12926-2]
ENST00000380117; ENSP00000369460; ENSG00000107105. [Q12926-1]
ENST00000397312; ENSP00000380479; ENSG00000107105. [Q12926-1]
ENST00000544538; ENSP00000440998; ENSG00000107105. [Q12926-1]
GeneIDi1993.
KEGGihsa:1993.
UCSCiuc003zps.4. human. [Q12926-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12431 mRNA. Translation: AAA69698.1.
U29943 mRNA. Translation: AAA70417.1.
AB209294 mRNA. Translation: BAD92531.1. Different initiation.
AL161628, AL445623 Genomic DNA. Translation: CAI13376.1.
AL161628 Genomic DNA. Translation: CAC22160.1.
CH471071 Genomic DNA. Translation: EAW58581.1.
CH471071 Genomic DNA. Translation: EAW58582.1.
BC030692 mRNA. Translation: AAH30692.1.
CCDSiCCDS55298.1. [Q12926-2]
CCDS6515.1. [Q12926-1]
PIRiI38726.
I39077.
RefSeqiNP_001164666.1. NM_001171195.1. [Q12926-2]
NP_001164668.1. NM_001171197.1. [Q12926-2]
NP_004423.2. NM_004432.3. [Q12926-1]
UniGeneiHs.166109.

3D structure databases

ProteinModelPortaliQ12926.
SMRiQ12926. Positions 37-251, 275-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108308. 113 interactions.
IntActiQ12926. 1 interaction.
STRINGi9606.ENSP00000369460.

PTM databases

iPTMnetiQ12926.
PhosphoSiteiQ12926.

Polymorphism and mutation databases

BioMutaiELAVL2.
DMDMi93141258.

Proteomic databases

EPDiQ12926.
MaxQBiQ12926.
PaxDbiQ12926.
PRIDEiQ12926.

Protocols and materials databases

DNASUi1993.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223951; ENSP00000223951; ENSG00000107105. [Q12926-2]
ENST00000380117; ENSP00000369460; ENSG00000107105. [Q12926-1]
ENST00000397312; ENSP00000380479; ENSG00000107105. [Q12926-1]
ENST00000544538; ENSP00000440998; ENSG00000107105. [Q12926-1]
GeneIDi1993.
KEGGihsa:1993.
UCSCiuc003zps.4. human. [Q12926-1]

Organism-specific databases

CTDi1993.
GeneCardsiELAVL2.
HGNCiHGNC:3313. ELAVL2.
HPAiCAB022222.
MIMi601673. gene.
neXtProtiNX_Q12926.
PharmGKBiPA27741.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0145. Eukaryota.
ENOG410XP7S. LUCA.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000231162.
HOVERGENiHBG002295.
InParanoidiQ12926.
KOiK13208.
OrthoDBiEOG77T14R.
PhylomeDBiQ12926.
TreeFamiTF313377.

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

GeneWikiiELAVL2.
GenomeRNAii1993.
PROiQ12926.
SOURCEiSearch...

Gene expression databases

BgeeiQ12926.
CleanExiHS_ELAVL2.
ExpressionAtlasiQ12926. baseline and differential.
GenevisibleiQ12926. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian homologs of Drosophila ELAV localized to a neuronal subset can bind in vitro to the 3' UTR of mRNA encoding the Id transcriptional repressor."
    King P.H., Levine T.D., Fremeau R.T. Jr., Keene J.D.
    J. Neurosci. 14:1943-1952(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Selection of a subset of mRNAs from combinatorial 3' untranslated region libraries using neuronal RNA-binding protein Hel-N1."
    Gao F.B., Carson C.C., Levine T., Keene J.D.
    Proc. Natl. Acad. Sci. U.S.A. 91:11207-11211(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Medulloblastoma.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 2).
    Tissue: Testis.
  7. Cited for: INTERACTION WITH IGF2BP1.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiELAV2_HUMAN
AccessioniPrimary (citable) accession number: Q12926
Secondary accession number(s): D3DRK3
, Q13235, Q59G15, Q8NEM4, Q9H1Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 18, 2006
Last modified: June 8, 2016
This is version 138 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.