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UniProtKB/Swiss-Prot entry P26378


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ELAV4_HUMAN
Primary accession number P26378
Secondary accession number Q96J74
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on February 10, 2009 (Sequence version 2)
Annotations were last modified on    May 5, 2009 (Entry version 91)
Name and origin of the protein
Protein name ELAV-like protein 4
Synonyms Paraneoplastic encephalomyelitis antigen HuD
Hu-antigen D
Gene name
Name: ELAVL4
Synonyms: HUD, PNEM
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT SER-270.
TISSUE=Brain;
DOI=10.1016/0092-8674(91)90184-Z; PubMed=1655278 [NCBI, ExPASy, EBI, Israel, Japan]
Szabo A., Dalmau J., Manley G., Rosenfeld M., Wong E., Henson J., Posner J.B., Furneaux H.M.;
"HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal.";
Cell 67:325-333(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT SER-270.
TISSUE=Neuroblastoma;
DOI=10.1002/ijc.10550; PubMed=12209604 [NCBI, ExPASy, EBI, Israel, Japan]
Behrends U., Jandl T., Golbeck A., Lechner B., Mueller-Weihrich S., Schmid I., Till H., Berthold F., Voltz R., Mautner J.M.;
"Novel products of the HuD, HuC, NNP-1 and alpha-internexin genes identified by autologous antibody screening of a pediatric neuroblastoma library.";
Int. J. Cancer 100:669-677(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
METHYLATION AT ARG-243.
DOI=10.1128/MCB.26.6.2273-2285.2006; PubMed=16508003 [NCBI, ExPASy, EBI, Israel, Japan]
Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H., Yachi K., Kubo T., Yoshikawa H., Tohyama M.;
"CARM1 regulates proliferation of PC12 cells by methylating HuD.";
Mol. Cell. Biol. 26:2273-2285(2006).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 44-210 IN COMPLEX WITH RNA.
DOI=10.1038/84131; PubMed=11175903 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Tanaka Hall T.M.;
"Structural basis for recognition of AU-rich element RNA by the HuD protein.";
Nat. Struct. Biol. 8:141-145(2001).
Comments
  • FUNCTION: May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR (By similarity).
  • SUBUNIT: Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP (By similarity).
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsHUD1PRO
    Isoform IDP26378-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsHUD1
    Isoform IDP26378-2
    Features which should be applied to build the isoform sequence: VSP_005791.
    Name3
    SynonymsHUD4
    Isoform IDP26378-3
    Features which should be applied to build the isoform sequence: VSP_014150, VSP_005791.
  • TISSUE SPECIFICITY: Brain.
  • PTM: 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).
  • DISEASE: Paraneoplastic encephalomyelitis sensory neuropathy is associated with small cell lung cancer and is characterized by dementia, sensory loss, and other neurological disabilities. It may result from an immune response primarily directed against a small cell lung tumor antigen which is misdirected against similar antigens expressed in brain.
  • SIMILARITY: Belongs to the RRM elav family.
  • SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M62843; AAA58396.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY033996; AAK57539.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY033997; AAK57540.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY033998; AAK57541.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL583843; CAI14635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592182; CAI14635.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL592182; CAI15789.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL583843; CAI15789.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00395507; -.
IPI00479625; -.
IPI00607677; -.
PIR A40348; A40348.
RefSeq NP_001138246.1; -.
NP_001138247.1; -.
NP_068771.2; -.
UniGene Hs.213050
3D structure databases
PDB
1FXL; X-ray; 1.80 A; A=44-210.[ExPASy / RCSB / EBI]
1G2E; X-ray; 2.30 A; A=44-210.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FXL; -.
1G2E; -.
ModBase P26378.
PTM databases
PhosphoSite P26378; -.
Organism-specific databases
GeneCards GC01P050283; -.
H-InvDB HIX0023614; -.
HGNC HGNC:3315; ELAVL4.
GenAtlas ELAVL4.
HPA CAB004442; -.
MIM 168360; gene. [NCBI / EBI]
PharmGKB PA27743; -.
Gene expression databases
ArrayExpress P26378; -.
Bgee P26378; -.
CleanEx HS_ELAVL4; -.
GermOnline ENSG00000162374; Homo sapiens.
Ontologies
GO
GO:0003730; Molecular function: mRNA 3'-UTR binding (traceable author statement from ProtInc).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0006397; Biological process: mRNA processing (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR006548; ELAD_HUD_SF.
IPR002343; Hud_Sxl_RNA.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
Pfam PF00076; RRM_1; 3.
Pfam graphical view of domain structure.
PRINTS PR00961; HUDSXLRNA.
SMART SM00360; RRM; 3.
SMART graphical view of domain structure.
TIGRFAMs TIGR01661; ELAV_HUD_SF; 1.
PROSITE PS50102; RRM; 3.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000162374; Homo sapiens. [Contig view]
GeneID 1996; -.
KEGG hsa:1996; -.
Phylogenomic databases
HOVERGEN P26378; -.
Other
NextBio 8073; -.
SOURCE ELAVL4; Homo sapiens.
ProtoNet P26378.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Methylation; Polymorphism; Repeat; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   380  380     ELAV-like protein 4. PRO_0000081583
DOMAIN   46   124  79     RRM 1. 
DOMAIN   132   212  81     RRM 2. 
DOMAIN   297   375  79     RRM 3. 
MOD_RES   243   243        Omega-N-methylated arginine; by CARM1. 
VAR_SEQ   1     2        MV -> MRLLLLREIVINESRNCSF (in isoform 3). VSP_014150
VAR_SEQ   259   272        Missing (in isoform 2 and isoform 3). VSP_005791
VARIANT   270   270  1     P -> S (in dbSNP:rs2494876 [NCBI]). VAR_052204 
STRAND   46    52  7      
HELIX   59    67  9      
STRAND   72    79  8      
TURN   81    83  3      
STRAND   86    96  11      
HELIX   97   107  11      
STRAND   118   121  4      
HELIX   127   129  3      
STRAND   133   138  6      
HELIX   145   152  8      
HELIX   153   155  3      
STRAND   158   165  8      
TURN   167   169  3      
STRAND   172   182  11      
HELIX   183   193  11      
STRAND   206   209  4      
Sequence information
Length: 380 AA [This is the length of the unprocessed precursor] Molecular weight: 41770 Da [This is the MW of the unprocessed precursor] CRC64: 80E82D40FA5A05DE [This is a checksum on the sequence]
        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 

P26378 in FASTA format

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