ID   ELAV2_HUMAN             Reviewed;         359 AA.
AC   Q12926; Q13235; Q59G15; Q8NEM4; Q9H1Q8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-NOV-2009, entry version 81.
DE   RecName: Full=ELAV-like protein 2;
DE   AltName: Full=Hu-antigen B;
DE            Short=HuB;
DE   AltName: Full=ELAV-like neuronal protein 1;
DE   AltName: Full=Nervous system-specific RNA-binding protein Hel-N1;
GN   Name=ELAVL2; Synonyms=HUB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=94210033; PubMed=8158249;
RA   King P.H., Levine T.D., Fremeau R.T. Jr., Keene J.D.;
RT   "Mammalian homologs of Drosophila ELAV localized to a neuronal subset
RT   can bind in vitro to the 3' UTR of mRNA encoding the Id
RT   transcriptional repressor.";
RL   J. Neurosci. 14:1943-1952(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Medulloblastoma;
RX   MEDLINE=95062235; PubMed=7972035; DOI=10.1073/pnas.91.23.11207;
RA   Gao F.B., Carson C.C., Levine T., Keene J.D.;
RT   "Selection of a subset of mRNAs from combinatorial 3' untranslated
RT   region libraries using neuronal RNA-binding protein Hel-N1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:11207-11211(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH IGF2BP1.
RX   PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA   Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA   Johnsen A.H., Christiansen J., Nielsen F.C.;
RT   "Molecular composition of IMP1 ribonucleoprotein granules.";
RL   Mol. Cell. Proteomics 6:798-811(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- FUNCTION: Binds RNA. Seems to recognize a GAAA motif. Can bind to
CC       its own 3'-UTR, the FOS 3'-UTR and the ID 3'-UTR.
CC   -!- SUBUNIT: Interacts with IGF2BP1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q12926-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12926-2; Sequence=VSP_005788;
CC   -!- TISSUE SPECIFICITY: Brain; neural-specific.
CC   -!- SIMILARITY: Belongs to the RRM elav family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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DR   EMBL; U12431; AAA69698.1; -; mRNA.
DR   EMBL; U29943; AAA70417.1; -; mRNA.
DR   EMBL; AB209294; BAD92531.1; ALT_INIT; mRNA.
DR   EMBL; AL161628; CAI13376.1; -; Genomic_DNA.
DR   EMBL; AL445623; CAI13376.1; JOINED; Genomic_DNA.
DR   EMBL; AL161628; CAC22160.1; -; Genomic_DNA.
DR   EMBL; BC030692; AAH30692.1; -; mRNA.
DR   IPI; IPI00030250; -.
DR   IPI; IPI00219967; -.
DR   PIR; I38726; I38726.
DR   PIR; I39077; I39077.
DR   RefSeq; NP_004423.2; -.
DR   UniGene; Hs.166109; -.
DR   HSSP; P26378; 1FXL.
DR   SMR; Q12926; 37-203.
DR   STRING; Q12926; -.
DR   PhosphoSite; Q12926; -.
DR   PRIDE; Q12926; -.
DR   Ensembl; ENST00000223951; ENSP00000223951; ENSG00000107105; Homo sapiens.
DR   Ensembl; ENST00000359598; ENSP00000352612; ENSG00000107105; Homo sapiens.
DR   Ensembl; ENST00000380110; ENSP00000369453; ENSG00000107105; Homo sapiens.
DR   Ensembl; ENST00000380117; ENSP00000369460; ENSG00000107105; Homo sapiens.
DR   Ensembl; ENST00000397312; ENSP00000380479; ENSG00000107105; Homo sapiens.
DR   Ensembl; ENST00000423281; ENSP00000391757; ENSG00000107105; Homo sapiens.
DR   Ensembl; ENST00000440102; ENSP00000412602; ENSG00000107105; Homo sapiens.
DR   GeneID; 1993; -.
DR   KEGG; hsa:1993; -.
DR   UCSC; uc003zps.1; human.
DR   UCSC; uc003zpu.1; human.
DR   CTD; 1993; -.
DR   GeneCards; GC09M023680; -.
DR   H-InvDB; HIX0007958; -.
DR   HGNC; HGNC:3313; ELAVL2.
DR   HPA; CAB022222; -.
DR   MIM; 601673; gene.
DR   PharmGKB; PA27741; -.
DR   HOVERGEN; Q12926; -.
DR   NextBio; 8059; -.
DR   ArrayExpress; Q12926; -.
DR   Bgee; Q12926; -.
DR   CleanEx; HS_ELAVL2; -.
DR   Genevestigator; Q12926; -.
DR   GermOnline; ENSG00000107105; Homo sapiens.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; TAS:ProtInc.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; TAS:ProtInc.
DR   InterPro; IPR012677; a_b_plait_nuc_bd.
DR   InterPro; IPR006548; ELAD_HUD_SF.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
DR   InterPro; IPR000504; RRM_RNP1.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Phosphoprotein; Repeat;
KW   RNA-binding.
FT   CHAIN         1    359       ELAV-like protein 2.
FT                                /FTId=PRO_0000081579.
FT   DOMAIN       39    117       RRM 1.
FT   DOMAIN      125    205       RRM 2.
FT   DOMAIN      276    354       RRM 3.
FT   MOD_RES     221    221       Phosphoserine.
FT   VAR_SEQ     239    251       Missing (in isoform 2).
FT                                /FTId=VSP_005788.
FT   CONFLICT    335    335       A -> R (in Ref. 1 and 2).
SQ   SEQUENCE   359 AA;  39504 MW;  15E87088FC546DDC CRC64;
     METQLSNGPT CNNTANGPTT INNNCSSPVD SGNTEDSKTN LIVNYLPQNM TQEELKSLFG
     SIGEIESCKL VRDKITGQSL GYGFVNYIDP KDAEKAINTL NGLRLQTKTI KVSYARPSSA
     SIRDANLYVS GLPKTMTQKE LEQLFSQYGR IITSRILVDQ VTGISRGVGF IRFDKRIEAE
     EAIKGLNGQK PPGATEPITV KFANNPSQKT NQAILSQLYQ SPNRRYPGPL AQQAQRFRLD
     NLLNMAYGVK RFSPMTIDGM TSLAGINIPG HPGTGWCIFV YNLAPDADES ILWQMFGPFG
     AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA AMAIASLNGY RLGDRVLQVS FKTNKTHKA
//