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P26378 (ELAV4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ELAV-like protein 4
Alternative name(s):
Hu-antigen D
Short name=HuD
Paraneoplastic encephalomyelitis antigen HuD
Gene names
Name:ELAVL4
Synonyms:HUD, PNEM
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR By similarity. Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA. Ref.5 Ref.6

Subunit structure

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

Tissue specificity

Brain.

Post-translational modification

Methylation at Arg-243 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 By similarity.

Sequence similarities

Belongs to the RRM elav family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   PTMMethylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmRNA processing

Traceable author statement. Source: ProtInc

   Molecular functionAU-rich element binding

Inferred from direct assay Ref.6. Source: UniProtKB

mRNA 3'-UTR binding

Traceable author statement. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P26378-1)

Also known as: HUD1PRO;

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: P26378-2)

Also known as: HUD1;

The sequence of this isoform differs from the canonical sequence as follows:
     259-272: Missing.
Isoform 3 (identifier: P26378-3)

Also known as: HUD4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MV → MRLLLLREIVINESRNCSF
     259-272: Missing.
Isoform 4 (identifier: P26378-4)

Also known as: HUD3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MVM → MEQ
     259-272: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380ELAV-like protein 4
PRO_0000081583

Regions

Domain46 – 12479RRM 1
Domain132 – 21281RRM 2
Domain297 – 37579RRM 3

Amino acid modifications

Modified residue2431Omega-N-methylated arginine; by CARM1 Ref.7

Natural variations

Alternative sequence1 – 33MVM → MEQ in isoform 4.
VSP_037608
Alternative sequence1 – 22MV → MRLLLLREIVINESRNCSF in isoform 3.
VSP_014150
Alternative sequence259 – 27214Missing in isoform 2, isoform 3 and isoform 4.
VSP_005791
Natural variant1661D → G. Ref.4
Corresponds to variant rs17853533 [ dbSNP | Ensembl ].
VAR_058091
Natural variant2701P → S. Ref.1 Ref.2 Ref.5
Corresponds to variant rs2494876 [ dbSNP | Ensembl ].
VAR_052204
Natural variant3561A → T. Ref.4
Corresponds to variant rs17853531 [ dbSNP | Ensembl ].
VAR_058092

Secondary structure

1 .............................. 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HUD1PRO) [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 80E82D40FA5A05DE

FASTA38041,770
        10         20         30         40         50         60 
MVMIISTMEP QVSNGPTSNT SNGPSSNNRN CPSPMQTGAT TDDSKTNLIV NYLPQNMTQE 

        70         80         90        100        110        120 
EFRSLFGSIG EIESCKLVRD KITGQSLGYG FVNYIDPKDA EKAINTLNGL RLQTKTIKVS 

       130        140        150        160        170        180 
YARPSSASIR DANLYVSGLP KTMTQKELEQ LFSQYGRIIT SRILVDQVTG VSRGVGFIRF 

       190        200        210        220        230        240 
DKRIEAEEAI KGLNGQKPSG ATEPITVKFA NNPSQKSSQA LLSQLYQSPN RRYPGPLHHQ 

       250        260        270        280        290        300 
AQRFRLDNLL NMAYGVKRLM SGPVPPSACP PRFSPITIDG MTSLVGMNIP GHTGTGWCIF 

       310        320        330        340        350        360 
VYNLSPDSDE SVLWQLFGPF GAVNNVKVIR DFNTNKCKGF GFVTMTNYDE AAMAIASLNG 

       370        380 
YRLGDRVLQV SFKTNKAHKS

« Hide

Isoform 2 (HUD1) [UniParc].

Checksum: 9BB102A0AD7495F1
Show »

FASTA36640,379
Isoform 3 (HUD4) [UniParc].

Checksum: 4FA0B4DC38E805A2
Show »

FASTA38342,437
Isoform 4 (HUD3) [UniParc].

Checksum: B26D48737B9BCACB
Show »

FASTA36640,406

References

« Hide 'large scale' references
[1]"HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal."
Szabo A., Dalmau J., Manley G., Rosenfeld M., Wong E., Henson J., Posner J.B., Furneaux H.M.
Cell 67:325-333(1991) [PubMed: 1655278] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT SER-270.
Tissue: Brain.
[2]"Novel products of the HuD, HuC, NNP-1 and alpha-internexin genes identified by autologous antibody screening of a pediatric neuroblastoma library."
Behrends U., Jandl T., Golbeck A., Lechner B., Mueller-Weihrich S., Schmid I., Till H., Berthold F., Voltz R., Mautner J.M.
Int. J. Cancer 100:669-677(2002) [PubMed: 12209604] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), VARIANT SER-270.
Tissue: Neuroblastoma.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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), VARIANTS GLY-166 AND THR-356.
Tissue: Hypothalamus.
[5]"Paraneoplastic encephalomyelitis antigens bind to the AU-rich elements of mRNA."
Liu J., Dalmau J., Szabo A., Rosenfeld M., Huber J., Furneaux H.
Neurology 45:544-550(1995) [PubMed: 7898713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 240-279 (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, VARIANT SER-270.
[6]"RNA-binding analyses of HuC and HuD with the VEGF and c-myc 3'-untranslated regions using a novel ELISA-based assay."
King P.H.
Nucleic Acids Res. 28:E20-E20(2000) [PubMed: 10710437] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[7]"CARM1 regulates proliferation of PC12 cells by methylating HuD."
Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H., Yachi K., Kubo T., Yoshikawa H., Tohyama M.
Mol. Cell. Biol. 26:2273-2285(2006) [PubMed: 16508003] [Abstract]
Cited for: METHYLATION AT ARG-243.
[8]"Structural basis for recognition of AU-rich element RNA by the HuD protein."
Wang X., Tanaka Hall T.M.
Nat. Struct. Biol. 8:141-145(2001) [PubMed: 11175903] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 44-210 IN COMPLEX WITH RNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M62843 mRNA. Translation: AAA58396.1.
AY033995 mRNA. Translation: AAK57538.1.
AY033996 mRNA. Translation: AAK57539.1.
AY033997 mRNA. Translation: AAK57540.1.
AY033998 mRNA. Translation: AAK57541.1.
AL583843, AL592182 Genomic DNA. Translation: CAI14634.1.
AL583843, AL592182 Genomic DNA. Translation: CAI14635.1.
AL583843, AL592182 Genomic DNA. Translation: CAI14636.1.
AL583843, AL592182 Genomic DNA. Translation: CAI14637.1.
AL592182, AL583843 Genomic DNA. Translation: CAI15788.1.
AL592182, AL583843 Genomic DNA. Translation: CAI15789.1.
AL592182, AL583843 Genomic DNA. Translation: CAI15790.1.
AL592182, AL583843 Genomic DNA. Translation: CAI15791.1.
BC036071 mRNA. Translation: AAH36071.1.
IPIIPI00395507.
IPI00479625.
IPI00607677.
IPI00644588.
PIRA40348.
RefSeqNP_001138246.1. NM_001144774.1.
NP_001138247.1. NM_001144775.1.
NP_001138248.1. NM_001144776.1.
NP_068771.2. NM_021952.3.
UniGeneHs.213050.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXLX-ray1.80A44-210[»]
1G2EX-ray2.30A44-210[»]
ProteinModelPortalP26378.
SMRP26378. Positions 44-379.
ModBaseSearch...

Protein-protein interaction databases

IntActP26378. 2 interactions.
MINTMINT-1471928.
STRINGP26378.

PTM databases

PhosphoSiteP26378.

Polymorphism databases

DMDM223590202.

Proteomic databases

PRIDEP26378.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371823; ENSP00000360888; ENSG00000162374.
GeneID1996.
KEGGhsa:1996.
UCSCuc001csa.2. human.
uc001csb.1. human.
uc001csc.2. human.

Organism-specific databases

CTD1996.
GeneCardsGC01P050513.
HGNCHGNC:3315. ELAVL4.
HPACAB004442.
MIM168360. gene.
neXtProtNX_P26378.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17583.
GeneTreeENSGT00560000077064.
HOVERGENHBG002295.
PhylomeDBP26378.

Gene expression databases

ArrayExpressP26378.
BgeeP26378.
CleanExHS_ELAVL4.
GenevestigatorP26378.
GermOnlineENSG00000162374. Homo sapiens.

Family and domain databases

InterProIPR006548. ELAD_HUD_SF.
IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.
KOK13208.
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

NextBio8073.
SOURCESearch...

Entry information

Entry nameELAV4_HUMAN
AccessionPrimary (citable) accession number: P26378
Secondary accession number(s): B1APY6 expand/collapse secondary AC list , B1APY7, Q8IYD4, Q96J74, Q96J75, Q9UD24
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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