ELAV2_MOUSE
ID ELAV2_MOUSE Reviewed; 360 AA.
AC Q60899;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 Mel-N1;
GN Name=Elavl2; Synonyms=Hub;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8668530; DOI=10.1093/nar/24.11.2011;
RA Abe R., Yamamoto K., Sakamoto H.;
RT "Target specificity of neuronal RNA-binding protein, Mel-N1: direct binding
RT to the 3' untranslated region of its own mRNA.";
RL Nucleic Acids Res. 24:2011-2016(1996).
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION BY MEMORY TRAINING.
RX PubMed=11573004; DOI=10.1073/pnas.191388398;
RA Quattrone A., Pascale A., Nogues X., Zhao W., Gusev P., Pacini A.,
RA Alkon D.L.;
RT "Posttranscriptional regulation of gene expression in learning by the
RT neuronal ELAV-like mRNA-stabilizing proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11668-11673(2001).
RN [3]
RP INTERACTION WITH MAP1B LIGHT CHAIN LC1.
RX PubMed=21288476; DOI=10.1016/j.biochi.2011.01.008;
RA Fujiwara Y., Kasashima K., Saito K., Fukuda M., Fukao A., Sasano Y.,
RA Inoue K., Fujiwara T., Sakamoto H.;
RT "Microtubule association of a neuronal RNA-binding protein HuD through its
RT binding to the light chain of MAP1B.";
RL Biochimie 93:817-822(2011).
CC -!- FUNCTION: RNA-binding protein that binds to the 3' untranslated region
CC (3'UTR) of target mRNAs (PubMed:8668530). Seems to recognize a GAAA
CC motif (PubMed:8668530). Can bind to its own 3'UTR, the FOS 3'UTR and
CC the ID 3'UTR (PubMed:8668530). {ECO:0000269|PubMed:8668530}.
CC -!- SUBUNIT: Interacts with IGF2BP1 (By similarity). Interacts with MAP1B
CC light chain LC1 (PubMed:21288476). {ECO:0000250|UniProtKB:Q12926,
CC ECO:0000269|PubMed:21288476}.
CC -!- TISSUE SPECIFICITY: Brain; neural-specific (PubMed:8668530). Expressed
CC in the hippocampus (PubMed:11573004). {ECO:0000269|PubMed:11573004,
CC ECO:0000269|PubMed:8668530}.
CC -!- INDUCTION: Up-regulated after memory training in radial arm maze
CC experiments. {ECO:0000269|PubMed:11573004}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
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DR EMBL; U29088; AAC52644.1; -; mRNA.
DR CCDS; CCDS18355.1; -.
DR PIR; JC6057; JC6057.
DR RefSeq; NP_034616.1; NM_010486.2.
DR RefSeq; XP_006502852.1; XM_006502789.2.
DR RefSeq; XP_006502853.1; XM_006502790.2.
DR RefSeq; XP_006502854.1; XM_006502791.2.
DR AlphaFoldDB; Q60899; -.
DR SMR; Q60899; -.
DR BioGRID; 200483; 34.
DR IntAct; Q60899; 6.
DR MINT; Q60899; -.
DR STRING; 10090.ENSMUSP00000099863; -.
DR iPTMnet; Q60899; -.
DR PhosphoSitePlus; Q60899; -.
DR MaxQB; Q60899; -.
DR PaxDb; Q60899; -.
DR PRIDE; Q60899; -.
DR ProteomicsDB; 277817; -.
DR Antibodypedia; 10496; 345 antibodies from 31 providers.
DR DNASU; 15569; -.
DR Ensembl; ENSMUST00000008633; ENSMUSP00000008633; ENSMUSG00000008489.
DR GeneID; 15569; -.
DR KEGG; mmu:15569; -.
DR UCSC; uc008ton.2; mouse.
DR CTD; 1993; -.
DR MGI; MGI:1100887; Elavl2.
DR VEuPathDB; HostDB:ENSMUSG00000008489; -.
DR eggNOG; KOG0145; Eukaryota.
DR GeneTree; ENSGT00940000156823; -.
DR HOGENOM; CLU_026186_2_2_1; -.
DR InParanoid; Q60899; -.
DR OMA; YPSCHSA; -.
DR OrthoDB; 775799at2759; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 15569; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Elavl2; mouse.
DR PRO; PR:Q60899; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60899; protein.
DR Bgee; ENSMUSG00000008489; Expressed in superior cervical ganglion and 215 other tissues.
DR ExpressionAtlas; Q60899; baseline and differential.
DR Genevisible; Q60899; MM.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
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 Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..360
FT /note="ELAV-like protein 2"
FT /id="PRO_0000081580"
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 277..355
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12926"
SQ SEQUENCE 360 AA; 39577 MW; 780CDD07F2E97D74 CRC64;
METQLSNGPT CNNTANGPTT VNNNCSSPVD SGNTEDSKTN LIVNYLPQNM TQEELKSLFG
SIGEIESCKL VRDKITGQSL GYGFVNYIDP KDAEKAINTL NGLRLQTKTI KVSYARPSSA
SIRDANLYVS GLPKTMTQKE LEQLFSQYGR IITSRILVDQ VTGISRGVGF IRFDKRIEAE
EAIKGLNGQK PPGATEPITV KFANNPSQKT NQAILSQLYQ SPNRRYPGPL AQQAQRFRLD
NLLNMAYGVK SRFSPMTIDG MTSLAGINIP GHPGTGWCIF VYNLAPDADE SILWQMFGPF
GAVTNVKVIR DFNTNKCKGF GFVTMTNYDE AAMAIASLNG YRLGDRVLQV SFKTNKTHKA
