RBM24_HUMAN
ID RBM24_HUMAN Reviewed; 236 AA.
AC Q9BX46; E9PAY4; Q6QDA4; Q8N9D3; Q96NI3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA-binding protein 24 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 24 {ECO:0000303|PubMed:20977548};
DE AltName: Full=RNA-binding region-containing protein 6;
GN Name=RBM24 {ECO:0000312|HGNC:HGNC:21539}; Synonyms=RNPC6;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Li H., Zhong G., Zhou G., Wang C., Shen C., Ke R., Li M., Xiao W., Lin L.,
RA Yang S.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex;
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 [5]
RP INDUCTION.
RX PubMed=19658189; DOI=10.1002/stem.166;
RA Xu X.Q., Soo S.Y., Sun W., Zweigerdt R.;
RT "Global expression profile of highly enriched cardiomyocytes derived from
RT human embryonic stem cells.";
RL Stem Cells 27:2163-2174(2009).
RN [6]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=20977548; DOI=10.1111/j.1365-2443.2010.01446.x;
RA Jin D., Hidaka K., Shirai M., Morisaki T.;
RT "RNA-binding motif protein 24 regulates myogenin expression and promotes
RT myogenic differentiation.";
RL Genes Cells 15:1158-1167(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22345307; DOI=10.1093/cvr/cvs095;
RA Poon K.L., Tan K.T., Wei Y.Y., Ng C.P., Colman A., Korzh V., Xu X.Q.;
RT "RNA-binding protein RBM24 is required for sarcomere assembly and heart
RT contractility.";
RL Cardiovasc. Res. 94:418-427(2012).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=25313962; DOI=10.1016/j.devcel.2014.08.025;
RA Yang J., Hung L.H., Licht T., Kostin S., Looso M., Khrameeva E.,
RA Bindereif A., Schneider A., Braun T.;
RT "RBM24 is a major regulator of muscle-specific alternative splicing.";
RL Dev. Cell 31:87-99(2014).
RN [9]
RP FUNCTION, RNA-BINDING, INDUCTION, AND DOMAIN.
RX PubMed=24356969; DOI=10.1074/jbc.m113.524413;
RA Jiang Y., Zhang M., Qian Y., Xu E., Zhang J., Chen X.;
RT "Rbm24, an RNA-binding protein and a target of p53, regulates p21
RT expression via mRNA stability.";
RL J. Biol. Chem. 289:3164-3175(2014).
RN [10]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=24375645; DOI=10.1158/1541-7786.mcr-13-0526;
RA Xu E., Zhang J., Zhang M., Jiang Y., Cho S.J., Chen X.;
RT "RNA-binding protein RBM24 regulates p63 expression via mRNA stability.";
RL Mol. Cancer Res. 12:359-369(2014).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=26990106; DOI=10.1002/stem.2366;
RA Zhang T., Lin Y., Liu J., Zhang Z.G., Fu W., Guo L.Y., Pan L., Kong X.,
RA Zhang M.K., Lu Y.H., Huang Z.R., Xie Q., Li W.H., Xu X.Q.;
RT "Rbm24 regulates alternative splicing switch in embryonic stem cell cardiac
RT lineage differentiation.";
RL Stem Cells 34:1776-1789(2016).
RN [12]
RP FUNCTION, INTERACTION WITH EIF4E, RNA-BINDING, MUTAGENESIS OF SER-181, AND
RP DOMAIN.
RX PubMed=29358667; DOI=10.1038/s41418-017-0029-8;
RA Zhang M., Zhang Y., Xu E., Mohibi S., de Anda D.M., Jiang Y., Zhang J.,
RA Chen X.;
RT "Rbm24, a target of p53, is necessary for proper expression of p53 and
RT heart development.";
RL Cell Death Differ. 25:1118-1130(2018).
RN [13]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=29104163; DOI=10.1016/j.biocel.2017.11.002;
RA Lin Y., Tan K.T., Liu J., Kong X., Huang Z., Xu X.Q.;
RT "Global profiling of Rbm24 bound RNAs uncovers a multi-tasking RNA binding
RT protein.";
RL Int. J. Biochem. Cell Biol. 94:10-21(2018).
RN [14]
RP INTERACTION WITH HCV SERINE PROTEASE/HELICASE NS3 AND MATURE CORE PROTEIN
RP (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=29380205; DOI=10.1007/s13238-018-0507-x;
RA Cao H., Zhao K., Yao Y., Guo J., Gao X., Yang Q., Guo M., Zhu W., Wang Y.,
RA Wu C., Chen J., Zhou Y., Hu X., Lu M., Chen X., Pei R.;
RT "RNA binding protein 24 regulates the translation and replication of
RT hepatitis C virus.";
RL Protein Cell 9:930-944(2018).
CC -!- FUNCTION: Multifunctional RNA-binding protein involved in the
CC regulation of pre-mRNA splicing, mRNA stability and mRNA translation
CC important for cell fate decision and differentiation (PubMed:20977548,
CC PubMed:24375645, PubMed:29358667, PubMed:29104163). Plays a major role
CC in pre-mRNA alternative splicing regulation (PubMed:26990106,
CC PubMed:29104163). Mediates preferentially muscle-specific exon
CC inclusion in numerous mRNAs important for striated cardiac and skeletal
CC muscle cell differentiation (PubMed:29104163). Binds to intronic
CC splicing enhancer (ISE) composed of stretches of GU-rich motifs
CC localized in flanking intron of exon that will be included by
CC alternative splicing (By similarity). Involved in embryonic stem cell
CC (ESC) transition to cardiac cell differentiation by promoting pre-mRNA
CC alternative splicing events of several pluripotency and/or
CC differentiation genes (PubMed:26990106). Plays a role in the regulation
CC of mRNA stability (PubMed:20977548, PubMed:24356969, PubMed:24375645,
CC PubMed:29104163). Binds to 3'-untranslated region (UTR) AU-rich
CC elements in target transcripts, such as CDKN1A and MYOG, leading to
CC maintain their stabilities (PubMed:20977548, PubMed:24356969). Involved
CC in myogenic differentiation by regulating MYOG levels
CC (PubMed:20977548). Binds to multiple regions in the mRNA 3'-UTR of TP63
CC isoform 2, hence inducing its destabilization (PubMed:24375645).
CC Promotes also the destabilization of the CHRM2 mRNA via its binding to
CC a region in the coding sequence (PubMed:29104163). Plays a role in the
CC regulation of mRNA translation (PubMed:29358667). Mediates repression
CC of p53/TP53 mRNA translation through its binding to U-rich element in
CC the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and
CC translation initiation (PubMed:29358667). Binds to a huge amount of
CC mRNAs (PubMed:29104163). Required for embryonic heart development,
CC sarcomer and M-band formation in striated muscles (By similarity).
CC Together with RBM20, promotes the expression of short isoforms of
CC PDLIM5/ENH in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:D3Z4I3, ECO:0000250|UniProtKB:M0R7T6,
CC ECO:0000269|PubMed:20977548, ECO:0000269|PubMed:24356969,
CC ECO:0000269|PubMed:24375645, ECO:0000269|PubMed:26990106,
CC ECO:0000269|PubMed:29104163, ECO:0000269|PubMed:29358667}.
CC -!- FUNCTION: (Microbial infection) Promotes hepatitis C virus (HCV)
CC replication over translation through the inhibition of viral protein
CC expression. Decreases viral translation by linking viral 5'- and 3'-
CC UTRs, blocking 80S ribosome assembly on the viral IRES and enhancing
CC the interaction of the mature core protein and 5'-UTR.
CC {ECO:0000269|PubMed:29380205}.
CC -!- SUBUNIT: Interacts with EIF4E; this interaction prevents EIF4E from
CC binding to p53/TP53 mRNA and inhibits the assembly of translation
CC initiation complex (PubMed:29358667). {ECO:0000269|PubMed:29358667}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV mature core protein;
CC this interaction, which enhances the interaction of Core with 5'-UTR
CC may favor viral replication over translation.
CC {ECO:0000269|PubMed:29380205}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV Serine
CC protease/helicase NS3. {ECO:0000269|PubMed:29380205}.
CC -!- INTERACTION:
CC Q9BX46-2; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-12224445, EBI-12809220;
CC Q9BX46-2; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12224445, EBI-724310;
CC Q9BX46-2; Q16633: POU2AF1; NbExp=3; IntAct=EBI-12224445, EBI-943588;
CC Q9BX46-2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-12224445, EBI-740343;
CC Q9BX46-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12224445, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm
CC {ECO:0000250|UniProtKB:D3Z4I3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BX46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BX46-2; Sequence=VSP_022526;
CC Name=3;
CC IsoId=Q9BX46-5; Sequence=VSP_046775;
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult heart and skeletal
CC muscles (PubMed:22345307, PubMed:25313962).
CC {ECO:0000269|PubMed:22345307, ECO:0000269|PubMed:25313962}.
CC -!- INDUCTION: By p53/TP53 following DNA damage (at protein level)
CC (PubMed:24356969). Up-regulated during embryonic stem cell (ESC)
CC differentiation into cardiomyocytes (PubMed:19658189, PubMed:26990106).
CC {ECO:0000269|PubMed:19658189, ECO:0000269|PubMed:24356969,
CC ECO:0000269|PubMed:26990106}.
CC -!- DOMAIN: The RRM domain is necessary for mRNA stability and mRNA
CC translation regulation (PubMed:24356969, PubMed:29358667).
CC {ECO:0000269|PubMed:24356969, ECO:0000269|PubMed:29358667}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04474.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; AK055391; BAB70914.1; -; mRNA.
DR EMBL; AK095016; BAC04474.1; ALT_SEQ; mRNA.
DR EMBL; AY547318; AAS55633.1; -; mRNA.
DR EMBL; AL136305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104810; AAI04811.1; -; mRNA.
DR EMBL; BC104808; AAI04809.1; -; mRNA.
DR CCDS; CCDS4538.1; -. [Q9BX46-2]
DR CCDS; CCDS47378.1; -. [Q9BX46-1]
DR CCDS; CCDS47379.1; -. [Q9BX46-5]
DR RefSeq; NP_001137413.1; NM_001143941.1. [Q9BX46-5]
DR RefSeq; NP_001137414.1; NM_001143942.1. [Q9BX46-1]
DR RefSeq; NP_694565.1; NM_153020.2. [Q9BX46-2]
DR AlphaFoldDB; Q9BX46; -.
DR SMR; Q9BX46; -.
DR BioGRID; 128744; 44.
DR IntAct; Q9BX46; 27.
DR STRING; 9606.ENSP00000368341; -.
DR iPTMnet; Q9BX46; -.
DR PhosphoSitePlus; Q9BX46; -.
DR BioMuta; RBM24; -.
DR DMDM; 74761312; -.
DR EPD; Q9BX46; -.
DR jPOST; Q9BX46; -.
DR MassIVE; Q9BX46; -.
DR MaxQB; Q9BX46; -.
DR PaxDb; Q9BX46; -.
DR PeptideAtlas; Q9BX46; -.
DR PRIDE; Q9BX46; -.
DR Antibodypedia; 44354; 91 antibodies from 20 providers.
DR DNASU; 221662; -.
DR Ensembl; ENST00000318204.5; ENSP00000319551.5; ENSG00000112183.15. [Q9BX46-2]
DR Ensembl; ENST00000379052.10; ENSP00000368341.5; ENSG00000112183.15. [Q9BX46-1]
DR Ensembl; ENST00000425446.6; ENSP00000396898.2; ENSG00000112183.15. [Q9BX46-5]
DR GeneID; 221662; -.
DR KEGG; hsa:221662; -.
DR MANE-Select; ENST00000379052.10; ENSP00000368341.5; NM_001143942.2; NP_001137414.1.
DR UCSC; uc003nbz.5; human. [Q9BX46-1]
DR CTD; 221662; -.
DR DisGeNET; 221662; -.
DR GeneCards; RBM24; -.
DR HGNC; HGNC:21539; RBM24.
DR HPA; ENSG00000112183; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 617603; gene.
DR neXtProt; NX_Q9BX46; -.
DR OpenTargets; ENSG00000112183; -.
DR PharmGKB; PA134964569; -.
DR VEuPathDB; HostDB:ENSG00000112183; -.
DR eggNOG; KOG0149; Eukaryota.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000156245; -.
DR HOGENOM; CLU_065652_0_1_1; -.
DR InParanoid; Q9BX46; -.
DR OMA; IPAHYMY; -.
DR PhylomeDB; Q9BX46; -.
DR TreeFam; TF314235; -.
DR PathwayCommons; Q9BX46; -.
DR SignaLink; Q9BX46; -.
DR BioGRID-ORCS; 221662; 14 hits in 1075 CRISPR screens.
DR GenomeRNAi; 221662; -.
DR Pharos; Q9BX46; Tbio.
DR PRO; PR:Q9BX46; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BX46; protein.
DR Bgee; ENSG00000112183; Expressed in tibialis anterior and 155 other tissues.
DR ExpressionAtlas; Q9BX46; baseline and differential.
DR Genevisible; Q9BX46; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:1990715; F:mRNA CDS binding; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:UniProtKB.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:UniProtKB.
DR GO; GO:1902811; P:positive regulation of skeletal muscle fiber differentiation; ISS:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0010830; P:regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
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; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Differentiation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..236
FT /note="RNA-binding protein 24"
FT /id="PRO_0000273370"
FT DOMAIN 11..88
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 175..199
FT /note="Necessary for interaction with EIF4E"
FT /evidence="ECO:0000269|PubMed:29358667"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046775"
FT VAR_SEQ 1..56
FT /note="MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGEIEEAVVITDRQTGKSR
FT GYGF -> MYVCLCVSVAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022526"
FT MUTAGEN 181
FT /note="S->A: Decreases p53/TP53 expression."
FT /evidence="ECO:0000269|PubMed:29358667"
FT MUTAGEN 181
FT /note="S->D: Increases p53/TP53 expression."
FT /evidence="ECO:0000269|PubMed:29358667"
FT CONFLICT 144
FT /note="A -> D (in Ref. 1; BAC04474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 24776 MW; 1CFB5AEBD4E3AA24 CRC64;
MHTTQKDTTY TKIFVGGLPY HTTDASLRKY FEVFGEIEEA VVITDRQTGK SRGYGFVTMA
DRAAAERACK DPNPIIDGRK ANVNLAYLGA KPRIMQPGFA FGVQQLHPAL IQRPFGIPAH
YVYPQAFVQP GVVIPHVQPT AAAASTTPYI DYTGAAYAQY SAAAAAAAAA AAYDQYPYAA
SPAAAGYVTA GGYGYAVQQP ITAAAPGTAA AAAAAAAAAA AFGQYQPQQL QTDRMQ
