CELF3_HUMAN
ID CELF3_HUMAN Reviewed; 465 AA.
AC Q5SZQ8; B7ZKK6; O15414; Q499Y6; Q5SZQ7; Q6NVK0; Q8IZ98; Q9BZC2; Q9HB30;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=CUGBP Elav-like family member 3;
DE Short=CELF-3;
DE AltName: Full=Bruno-like protein 1;
DE AltName: Full=CAG repeat protein 4;
DE AltName: Full=CUG-BP- and ETR-3-like factor 3;
DE AltName: Full=ELAV-type RNA-binding protein 1;
DE Short=ETR-1;
DE AltName: Full=Expanded repeat domain protein CAG/CTG 4;
DE AltName: Full=RNA-binding protein BRUNOL-1;
DE AltName: Full=Trinucleotide repeat-containing gene 4 protein;
GN Name=CELF3; Synonyms=BRUNOL1, CAGH4, ERDA4, TNRC4;
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), FUNCTION, RNA-BINDING, TISSUE
RP SPECIFICITY, AND POLYMORPHISM.
RC TISSUE=Brain;
RX PubMed=11158314; DOI=10.1128/mcb.21.4.1285-1296.2001;
RA Ladd A.N., Charlet-B N., Cooper T.A.;
RT "The CELF family of RNA binding proteins is implicated in cell-specific and
RT developmentally regulated alternative splicing.";
RL Mol. Cell. Biol. 21:1285-1296(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA d'Apolito M., Savino M., Grifa A., Quattrone A.;
RT "The RNA binding protein CELF3 associates to the DMPK mRNA and is a
RT negative regulator of mRNA stability involved in neuronal
RT differentiation.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Retinoblastoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-465 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9225980; DOI=10.1007/s004390050476;
RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
RT "cDNAs with long CAG trinucleotide repeats from human brain.";
RL Hum. Genet. 100:114-122(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 326-465.
RX PubMed=10893231; DOI=10.1074/jbc.m003083200;
RA Good P.J., Chen Q., Warner S.J., Herring D.C.;
RT "A family of human RNA-binding proteins related to the Drosophila Bruno
RT translational regulator.";
RL J. Biol. Chem. 275:28583-28592(2000).
RN [8]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [9]
RP STRUCTURE BY NMR OF 90-178.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in trinucleotide repeat
RT containing 4 variant.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein involved in the regulation of pre-mRNA
CC alternative splicing. Mediates exon inclusion and/or exclusion in pre-
CC mRNA that are subject to tissue-specific and developmentally regulated
CC alternative splicing. Specifically activates exon 5 inclusion of
CC cardiac isoforms of TNNT2 during heart remodeling at the juvenile to
CC adult transition. Activates the splicing of MAPT/Tau exon 10. Binds to
CC muscle-specific splicing enhancer (MSE) intronic sites flanking the
CC alternative exon 5 of TNNT2 pre-mRNA. {ECO:0000269|PubMed:11158314,
CC ECO:0000269|PubMed:15009664}.
CC -!- INTERACTION:
CC Q5SZQ8-2; Q8IV36: HID1; NbExp=3; IntAct=EBI-12258670, EBI-743438;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5SZQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SZQ8-2; Sequence=VSP_026825;
CC Name=3;
CC IsoId=Q5SZQ8-3; Sequence=VSP_026824;
CC Name=4;
CC IsoId=Q5SZQ8-4; Sequence=VSP_046642;
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11158314}.
CC -!- POLYMORPHISM: The poly-Gln tract in AAK07474 may be polymorphic.
CC {ECO:0000305|PubMed:11158314}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB91444.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF329264; AAK07474.1; -; mRNA.
DR EMBL; AY165003; AAN73884.1; -; mRNA.
DR EMBL; AL589765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53422.1; -; Genomic_DNA.
DR EMBL; BC052491; AAH52491.1; -; mRNA.
DR EMBL; BC068008; AAH68008.1; -; mRNA.
DR EMBL; BC104758; AAI04759.1; -; mRNA.
DR EMBL; BC143226; AAI43227.1; -; mRNA.
DR EMBL; U80746; AAB91444.1; ALT_FRAME; mRNA.
DR EMBL; AF284423; AAG14457.1; -; mRNA.
DR CCDS; CCDS1002.1; -. [Q5SZQ8-1]
DR CCDS; CCDS53367.1; -. [Q5SZQ8-4]
DR RefSeq; NP_001166120.1; NM_001172649.3. [Q5SZQ8-4]
DR RefSeq; NP_001278035.1; NM_001291106.1. [Q5SZQ8-2]
DR RefSeq; NP_001278036.1; NM_001291107.1. [Q5SZQ8-3]
DR RefSeq; NP_009116.3; NM_007185.6. [Q5SZQ8-1]
DR PDB; 2DNO; NMR; -; A=90-178.
DR PDBsum; 2DNO; -.
DR AlphaFoldDB; Q5SZQ8; -.
DR SMR; Q5SZQ8; -.
DR BioGRID; 116359; 12.
DR IntAct; Q5SZQ8; 8.
DR MINT; Q5SZQ8; -.
DR STRING; 9606.ENSP00000290583; -.
DR iPTMnet; Q5SZQ8; -.
DR PhosphoSitePlus; Q5SZQ8; -.
DR BioMuta; CELF3; -.
DR DMDM; 74756184; -.
DR MassIVE; Q5SZQ8; -.
DR PaxDb; Q5SZQ8; -.
DR PeptideAtlas; Q5SZQ8; -.
DR PRIDE; Q5SZQ8; -.
DR ProteomicsDB; 64095; -.
DR ProteomicsDB; 64096; -. [Q5SZQ8-1]
DR ProteomicsDB; 64097; -. [Q5SZQ8-2]
DR ProteomicsDB; 64098; -. [Q5SZQ8-3]
DR Antibodypedia; 20334; 98 antibodies from 22 providers.
DR DNASU; 11189; -.
DR Ensembl; ENST00000290583.9; ENSP00000290583.4; ENSG00000159409.15. [Q5SZQ8-1]
DR Ensembl; ENST00000290585.8; ENSP00000290585.4; ENSG00000159409.15. [Q5SZQ8-4]
DR GeneID; 11189; -.
DR KEGG; hsa:11189; -.
DR MANE-Select; ENST00000290583.9; ENSP00000290583.4; NM_007185.7; NP_009116.3.
DR UCSC; uc001eys.3; human. [Q5SZQ8-1]
DR CTD; 11189; -.
DR DisGeNET; 11189; -.
DR GeneCards; CELF3; -.
DR HGNC; HGNC:11967; CELF3.
DR HPA; ENSG00000159409; Tissue enhanced (brain, pituitary gland).
DR MIM; 612678; gene.
DR neXtProt; NX_Q5SZQ8; -.
DR OpenTargets; ENSG00000159409; -.
DR PharmGKB; PA36654; -.
DR VEuPathDB; HostDB:ENSG00000159409; -.
DR eggNOG; KOG0146; Eukaryota.
DR GeneTree; ENSGT00940000154716; -.
DR HOGENOM; CLU_015367_0_1_1; -.
DR InParanoid; Q5SZQ8; -.
DR OMA; NYPAYNA; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; Q5SZQ8; -.
DR TreeFam; TF314924; -.
DR PathwayCommons; Q5SZQ8; -.
DR SignaLink; Q5SZQ8; -.
DR BioGRID-ORCS; 11189; 14 hits in 1067 CRISPR screens.
DR ChiTaRS; CELF3; human.
DR EvolutionaryTrace; Q5SZQ8; -.
DR GenomeRNAi; 11189; -.
DR Pharos; Q5SZQ8; Tbio.
DR PRO; PR:Q5SZQ8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5SZQ8; protein.
DR Bgee; ENSG00000159409; Expressed in cortical plate and 137 other tissues.
DR ExpressionAtlas; Q5SZQ8; baseline and differential.
DR Genevisible; Q5SZQ8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0097322; F:7SK snRNA binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0036002; F:pre-mRNA binding; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0098781; P:ncRNA transcription; IEA:Ensembl.
DR GO; GO:0030575; P:nuclear body organization; IEA:Ensembl.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd12632; RRM1_CELF3_4_5_6; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034648; CELF3/4/5/6_RRM1.
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 SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..465
FT /note="CUGBP Elav-like family member 3"
FT /id="PRO_0000295198"
FT DOMAIN 7..88
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 95..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 380..458
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 346..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026824"
FT VAR_SEQ 258..307
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046642"
FT VAR_SEQ 330
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026825"
FT CONFLICT 149
FT /note="Q -> K (in Ref. 5; AAH52491)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> T (in Ref. 5; AAH52491)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="P -> Q (in Ref. 5; AAH52491)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> V (in Ref. 1; AAK07474 and 2; AAN73884)"
FT /evidence="ECO:0000305"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2DNO"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2DNO"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2DNO"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:2DNO"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:2DNO"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2DNO"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2DNO"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2DNO"
SQ SEQUENCE 465 AA; 50548 MW; 59B74F120090C15F CRC64;
MKEPDAIKLF VGQIPRHLEE KDLKPIFEQF GRIFELTVIK DKYTGLHKGC AFLTYCARDS
ALKAQSALHE QKTLPGMNRP IQVKPADSES RGEDRKLFVG MLGKQQTDED VRKMFEPFGT
IDECTVLRGP DGTSKGCAFV KFQTHAEAQA AINTLHSSRT LPGASSSLVV KFADTEKERG
LRRMQQVATQ LGMFSPIALQ FGAYSAYTQA LMQQQAALVA AHSAYLSPMA TMAAVQMQHM
AAINANGLIA TPITPSSGTS TPPAIAATPV SAIPAALGVN GYSPVPTQPT GQPAPDALYP
NGVHPYPAQS PAAPVDPLQQ AYAGMQHYTA AYPAAYSLVA PAFPQPPALV AQQPPPPPQQ
QQQQQQQQQQ QQQREGPDGC NIFIYHLPQE FTDSEILQMF VPFGHVISAK VFVDRATNQS
KCFGFVSFDN PASAQAAIQA MNGFQIGMKR LKVQLKRPKD ANRPY
