ELAV2_HUMAN
ID ELAV2_HUMAN Reviewed; 359 AA.
AC Q12926; D3DRK3; Q13235; Q59G15; Q8NEM4; Q9H1Q8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=ELAV-like protein 2;
DE AltName: Full=ELAV-like neuronal protein 1;
DE AltName: Full=Hu-antigen B;
DE Short=HuB;
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8158249; DOI=10.1523/jneurosci.14-04-01943.1994;
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 can
RT bind in vitro to the 3' UTR of mRNA encoding the Id transcriptional
RT repressor.";
RL J. Neurosci. 14:1943-1952(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Medulloblastoma;
RX 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 region
RT 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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: RNA-binding protein that binds to the 3' untranslated region
CC (3'UTR) of target mRNAs (By similarity). Seems to recognize a GAAA
CC motif (By similarity). Can bind to its own 3'UTR, the FOS 3'UTR and the
CC ID 3'UTR (By similarity). {ECO:0000250|UniProtKB:Q60899}.
CC -!- SUBUNIT: Interacts with IGF2BP1 (PubMed:17289661). Interacts with MAP1B
CC light chain LC1 (By similarity). {ECO:0000250|UniProtKB:Q60899,
CC ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC Q12926-2; Q9NWZ8: GEMIN8; NbExp=3; IntAct=EBI-11075944, EBI-2626001;
CC Q12926-2; Q03403: TFF2; NbExp=3; IntAct=EBI-11075944, EBI-4314702;
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92531.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58581.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58582.1; -; Genomic_DNA.
DR EMBL; BC030692; AAH30692.1; -; mRNA.
DR CCDS; CCDS55298.1; -. [Q12926-2]
DR CCDS; CCDS6515.1; -. [Q12926-1]
DR PIR; I38726; I38726.
DR PIR; I39077; I39077.
DR RefSeq; NP_001164666.1; NM_001171195.1. [Q12926-2]
DR RefSeq; NP_001164668.1; NM_001171197.1. [Q12926-2]
DR RefSeq; NP_004423.2; NM_004432.3. [Q12926-1]
DR RefSeq; XP_016869908.1; XM_017014419.1.
DR RefSeq; XP_016869909.1; XM_017014420.1.
DR RefSeq; XP_016869910.1; XM_017014421.1.
DR RefSeq; XP_016869911.1; XM_017014422.1.
DR RefSeq; XP_016869912.1; XM_017014423.1.
DR RefSeq; XP_016869913.1; XM_017014424.1.
DR RefSeq; XP_016869914.1; XM_017014425.1.
DR AlphaFoldDB; Q12926; -.
DR SMR; Q12926; -.
DR BioGRID; 108308; 155.
DR IntAct; Q12926; 114.
DR STRING; 9606.ENSP00000380479; -.
DR GlyGen; Q12926; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12926; -.
DR PhosphoSitePlus; Q12926; -.
DR SwissPalm; Q12926; -.
DR BioMuta; ELAVL2; -.
DR DMDM; 93141258; -.
DR EPD; Q12926; -.
DR jPOST; Q12926; -.
DR MassIVE; Q12926; -.
DR MaxQB; Q12926; -.
DR PaxDb; Q12926; -.
DR PeptideAtlas; Q12926; -.
DR PRIDE; Q12926; -.
DR ProteomicsDB; 59031; -. [Q12926-1]
DR ProteomicsDB; 59032; -. [Q12926-2]
DR Antibodypedia; 10496; 345 antibodies from 31 providers.
DR DNASU; 1993; -.
DR Ensembl; ENST00000223951.10; ENSP00000223951.5; ENSG00000107105.15. [Q12926-2]
DR Ensembl; ENST00000380117.5; ENSP00000369460.1; ENSG00000107105.15. [Q12926-1]
DR Ensembl; ENST00000397312.7; ENSP00000380479.2; ENSG00000107105.15. [Q12926-1]
DR Ensembl; ENST00000544538.5; ENSP00000440998.1; ENSG00000107105.15. [Q12926-1]
DR GeneID; 1993; -.
DR KEGG; hsa:1993; -.
DR MANE-Select; ENST00000397312.7; ENSP00000380479.2; NM_004432.5; NP_004423.2.
DR UCSC; uc003zps.4; human. [Q12926-1]
DR CTD; 1993; -.
DR DisGeNET; 1993; -.
DR GeneCards; ELAVL2; -.
DR HGNC; HGNC:3313; ELAVL2.
DR HPA; ENSG00000107105; Group enriched (brain, testis).
DR MIM; 601673; gene.
DR neXtProt; NX_Q12926; -.
DR OpenTargets; ENSG00000107105; -.
DR PharmGKB; PA27741; -.
DR VEuPathDB; HostDB:ENSG00000107105; -.
DR eggNOG; KOG0145; Eukaryota.
DR GeneTree; ENSGT00940000156823; -.
DR HOGENOM; CLU_026186_2_2_1; -.
DR InParanoid; Q12926; -.
DR OMA; YPSCHSA; -.
DR OrthoDB; 775799at2759; -.
DR PhylomeDB; Q12926; -.
DR TreeFam; TF313377; -.
DR PathwayCommons; Q12926; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q12926; -.
DR SIGNOR; Q12926; -.
DR BioGRID-ORCS; 1993; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; ELAVL2; human.
DR GeneWiki; ELAVL2; -.
DR GenomeRNAi; 1993; -.
DR Pharos; Q12926; Tbio.
DR PRO; PR:Q12926; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q12926; protein.
DR Bgee; ENSG00000107105; Expressed in Brodmann (1909) area 23 and 128 other tissues.
DR ExpressionAtlas; Q12926; baseline and differential.
DR Genevisible; Q12926; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR CDD; cd12650; RRM1_Hu; 1.
DR CDD; cd12775; RRM2_HuB; 1.
DR CDD; cd12654; RRM3_HuB; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006548; ELAD_HU_SF.
DR InterPro; IPR034775; ELAV/Hu_RRM1.
DR InterPro; IPR034999; HuB_RRM2.
DR InterPro; IPR034914; HuB_RRM3.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..359
FT /note="ELAV-like protein 2"
FT /id="PRO_0000081579"
FT DOMAIN 39..117
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 125..205
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 276..354
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 239..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7972035"
FT /id="VSP_005788"
FT CONFLICT 335
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
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
