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Reviewed, UniProtKB/Swiss-Prot Q12926 (ELAV2_HUMAN)

Last modified February 9, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ELAV-like protein 2
Alternative name(s):
    Hu-antigen B
      Short name=HuB
    ELAV-like neuronal protein 1
    Nervous system-specific RNA-binding protein Hel-N1
Gene names
Name: ELAVL2
Synonyms: HUB
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Subunit structure

Interacts with IGF2BP1. Ref.6

Tissue specificity

Brain; neural-specific.

Sequence similarities

Belongs to the RRM elav family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processregulation of transcription, DNA-dependent Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionmRNA 3'-UTR binding Ref.1

Traceable author statement. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding Ref.6

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12926-1)

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.
Isoform 2 (identifier: Q12926-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359ELAV-like protein 2
PRO_0000081579

Regions

Domain39 – 11779RRM 1
Domain125 – 20581RRM 2
Domain276 – 35479RRM 3

Amino acid modifications

Modified residue2211Phosphoserine Ref.7 Ref.8

Natural variations

Alternative sequence239 – 25113Missing in isoform 2.
VSP_005788

Experimental info

Sequence conflict3351A → R Ref.1
Sequence conflict3351A → R Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: 15E87088FC546DDC

FASTA35939,504
        10         20         30         40         50         60 
METQLSNGPT CNNTANGPTT INNNCSSPVD SGNTEDSKTN LIVNYLPQNM TQEELKSLFG 

        70         80         90        100        110        120 
SIGEIESCKL VRDKITGQSL GYGFVNYIDP KDAEKAINTL NGLRLQTKTI KVSYARPSSA 

       130        140        150        160        170        180 
SIRDANLYVS GLPKTMTQKE LEQLFSQYGR IITSRILVDQ VTGISRGVGF IRFDKRIEAE 

       190        200        210        220        230        240 
EAIKGLNGQK PPGATEPITV KFANNPSQKT NQAILSQLYQ SPNRRYPGPL AQQAQRFRLD 

       250        260        270        280        290        300 
NLLNMAYGVK RFSPMTIDGM TSLAGINIPG HPGTGWCIFV YNLAPDADES ILWQMFGPFG 

       310        320        330        340        350 
AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA AMAIASLNGY RLGDRVLQVS FKTNKTHKA 

« Hide

Isoform 2.

Checksum: F1EC0F69EE5D15DD
Show »

FASTA34638,015

References

« Hide 'large scale' references
[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: 8158249] [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: 7972035] [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. expand/collapse author list , 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: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[6]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed: 17289661] [Abstract]
Cited for: INTERACTION WITH IGF2BP1.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, MASS SPECTROMETRY.
[8]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
BC030692 mRNA. Translation: AAH30692.1.
IPIIPI00030250.
IPI00219967.
PIRI38726.
I39077.
RefSeqNP_004423.2.
UniGeneHs.166109

3D structure databases

SMRQ12926. Positions 37-203, 39-355.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12926.

PTM databases

PhosphoSiteQ12926.

Proteomic databases

PRIDEQ12926.

Genome annotation databases

EnsemblENST00000359598; ENSP00000352612; ENSG00000107105; Homo sapiens. [Genome view]
ENST00000380117; ENSP00000369460; ENSG00000107105; Homo sapiens. [Genome view]
ENST00000397312; ENSP00000380479; ENSG00000107105; Homo sapiens. [Genome view]
GeneID1993.
KEGGhsa:1993.
UCSCuc003zps.1. human.
uc003zpu.1. human.

Organism-specific databases

CTD1993.
GeneCardsGC09M023680.
H-InvDBHIX0007958.
HGNCHGNC:3313. ELAVL2.
HPACAB022222.
MIM601673. gene.
PharmGKBPA27741.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13608.
HOVERGENQ12926.
InParanoidQ12926.
OrthoDBEOG9VHNS4.
PhylomeDBQ12926.

Gene expression databases

ArrayExpressQ12926.
BgeeQ12926.
CleanExHS_ELAVL2.
GenevestigatorQ12926.
GermOnlineENSG00000107105. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSPR00961. HUDSXLRNA.
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01661. ELAV_HUD_SF. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8059.
SOURCESearch...

Entry information

Entry nameELAV2_HUMAN
AccessionPrimary (citable) accession number: Q12926
Secondary accession number(s): Q13235 expand/collapse secondary AC list , Q59G15, Q8NEM4, Q9H1Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 18, 2006
Last modified: February 9, 2010
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents