RBM23_HUMAN
ID RBM23_HUMAN Reviewed; 439 AA.
AC Q86U06; D3DS32; Q8ND16; Q8TB88; Q8WY40; Q9BUJ1; Q9NVV7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Probable RNA-binding protein 23 {ECO:0000303|PubMed:31693891};
DE AltName: Full=CAPER beta {ECO:0000303|PubMed:15694343};
DE Short=CAPERbeta {ECO:0000303|PubMed:15694343};
DE AltName: Full=RNA-binding motif protein 23;
DE AltName: Full=RNA-binding region-containing protein 4;
DE AltName: Full=Splicing factor SF2;
GN Name=RBM23 {ECO:0000303|PubMed:31693891, ECO:0000312|HGNC:HGNC:20155};
GN Synonyms=RNPC4; ORFNames=PP239;
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 2), AND VARIANT ALA-393 INS.
RA Yang J., Yu L., Zhou Y., Dai F.Y., Xin Y.R., Zhao S.Y.;
RT "Cloning and characterization of a new human cDNA homology to human
RT splicing factor (CC1.3) mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT ALA-393
RP INS.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ALA-393
RP INS.
RC TISSUE=Neuron;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-393
RP INS.
RC TISSUE=Muscle, and Placenta;
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 [9]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 169-PHE--LEU-173;
RP 266-TYR--LEU-270 AND 369-LEU--LEU-373.
RX PubMed=15694343; DOI=10.1016/j.molcel.2004.12.025;
RA Dowhan D.H., Hong E.P., Auboeuf D., Dennis A.P., Wilson M.M., Berget S.M.,
RA O'Malley B.W.;
RT "Steroid hormone receptor coactivation and alternative RNA splicing by
RT U2AF65-related proteins CAPERalpha and CAPERbeta.";
RL Mol. Cell 17:429-439(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP UBIQUITINATION.
RX PubMed=31693891; DOI=10.1016/j.celrep.2019.09.079;
RA Ting T.C., Goralski M., Klein K., Wang B., Kim J., Xie Y., Nijhawan D.;
RT "Aryl sulfonamides degrade RBM39 and RBM23 by recruitment to CRL4-DCAF15.";
RL Cell Rep. 29:1499-1510(2019).
RN [15]
RP UBIQUITINATION.
RX PubMed=31686031; DOI=10.1038/s41589-019-0378-3;
RA Faust T.B., Yoon H., Nowak R.P., Donovan K.A., Li Z., Cai Q.,
RA Eleuteri N.A., Zhang T., Gray N.S., Fischer E.S.;
RT "Structural complementarity facilitates E7820-mediated degradation of RBM39
RT by DCAF15.";
RL Nat. Chem. Biol. 16:7-14(2020).
RN [16]
RP UBIQUITINATION.
RX PubMed=31819272; DOI=10.1038/s41589-019-0411-6;
RA Bussiere D.E., Xie L., Srinivas H., Shu W., Burke A., Be C., Zhao J.,
RA Godbole A., King D., Karki R.G., Hornak V., Xu F., Cobb J., Carte N.,
RA Frank A.O., Frommlet A., Graff P., Knapp M., Fazal A., Okram B., Jiang S.,
RA Michellys P.Y., Beckwith R., Voshol H., Wiesmann C., Solomon J.M.,
RA Paulk J.;
RT "Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3
RT ligase complex.";
RL Nat. Chem. Biol. 16:15-23(2020).
RN [17]
RP STRUCTURE BY NMR OF 148-347.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domains in RNA binding motif protein
RT 23.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein that acts both as a transcription
CC coactivator and pre-mRNA splicing factor (PubMed:15694343). Regulates
CC steroid hormone receptor-mediated transcription, independently of the
CC pre-mRNA splicing factor activity (PubMed:15694343).
CC {ECO:0000269|PubMed:15694343}.
CC -!- INTERACTION:
CC Q86U06; O14503: BHLHE40; NbExp=3; IntAct=EBI-780319, EBI-711810;
CC Q86U06; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-780319, EBI-10175124;
CC Q86U06; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-780319, EBI-10178634;
CC Q86U06; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-780319, EBI-716006;
CC Q86U06; O14744: PRMT5; NbExp=3; IntAct=EBI-780319, EBI-351098;
CC Q86U06; P78362: SRPK2; NbExp=2; IntAct=EBI-780319, EBI-593303;
CC Q86U06; P14373: TRIM27; NbExp=3; IntAct=EBI-780319, EBI-719493;
CC Q86U06-2; O14503: BHLHE40; NbExp=3; IntAct=EBI-10258579, EBI-711810;
CC Q86U06-2; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-10258579, EBI-10178634;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86U06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86U06-2; Sequence=VSP_008312;
CC Name=3;
CC IsoId=Q86U06-3; Sequence=VSP_008314, VSP_008315;
CC Name=4;
CC IsoId=Q86U06-4; Sequence=VSP_008312, VSP_008313;
CC Name=5;
CC IsoId=Q86U06-5; Sequence=VSP_008311;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, liver, skeletal
CC muscle, heart and kidney (PubMed:15694343). Expressed at lower levels
CC in the colon, thymus, spleen, small intestine and lung
CC (PubMed:15694343). {ECO:0000269|PubMed:15694343}.
CC -!- PTM: Aryl sulfonamide anticancer drugs, such as indisulam (E7070) or
CC E7820, promote ubiquitination and subsequent degradation by the
CC DCX(DCAF15) complex (PubMed:31693891, PubMed:31686031,
CC PubMed:31819272). Aryl sulfonamide anticancer drugs change the
CC substrate specificity of DCAF15 by acting as a molecular glue that
CC promotes binding between DCAF15 and weak affinity interactor RBM23
CC (PubMed:31686031, PubMed:31819272). {ECO:0000269|PubMed:31686031,
CC ECO:0000269|PubMed:31693891, ECO:0000269|PubMed:31819272}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF087905; AAP97203.1; -; mRNA.
DR EMBL; AF275678; AAG24388.1; -; mRNA.
DR EMBL; AK001344; BAA91638.1; -; mRNA.
DR EMBL; AL834198; CAD38887.1; -; mRNA.
DR EMBL; BX161440; CAD61910.1; -; mRNA.
DR EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66223.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66229.1; -; Genomic_DNA.
DR EMBL; BC002566; AAH02566.1; -; mRNA.
DR EMBL; BC024208; AAH24208.1; -; mRNA.
DR CCDS; CCDS41919.1; -. [Q86U06-4]
DR CCDS; CCDS41920.1; -. [Q86U06-2]
DR CCDS; CCDS41921.1; -. [Q86U06-1]
DR RefSeq; NP_001070819.1; NM_001077351.1. [Q86U06-1]
DR RefSeq; NP_001070820.1; NM_001077352.1. [Q86U06-4]
DR RefSeq; NP_001294973.1; NM_001308044.1.
DR RefSeq; NP_060577.3; NM_018107.4. [Q86U06-2]
DR RefSeq; XP_016876896.1; XM_017021407.1.
DR RefSeq; XP_016876902.1; XM_017021413.1.
DR PDB; 2CQ4; NMR; -; A=148-248.
DR PDB; 2DNZ; NMR; -; A=265-346.
DR PDBsum; 2CQ4; -.
DR PDBsum; 2DNZ; -.
DR AlphaFoldDB; Q86U06; -.
DR SMR; Q86U06; -.
DR BioGRID; 120450; 91.
DR IntAct; Q86U06; 38.
DR MINT; Q86U06; -.
DR STRING; 9606.ENSP00000352956; -.
DR GlyGen; Q86U06; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86U06; -.
DR PhosphoSitePlus; Q86U06; -.
DR SwissPalm; Q86U06; -.
DR BioMuta; RBM23; -.
DR DMDM; 34925229; -.
DR EPD; Q86U06; -.
DR jPOST; Q86U06; -.
DR MassIVE; Q86U06; -.
DR MaxQB; Q86U06; -.
DR PaxDb; Q86U06; -.
DR PeptideAtlas; Q86U06; -.
DR PRIDE; Q86U06; -.
DR ProteomicsDB; 69751; -. [Q86U06-1]
DR ProteomicsDB; 69752; -. [Q86U06-2]
DR ProteomicsDB; 69753; -. [Q86U06-3]
DR ProteomicsDB; 69754; -. [Q86U06-4]
DR ProteomicsDB; 69755; -. [Q86U06-5]
DR Antibodypedia; 114; 77 antibodies from 17 providers.
DR DNASU; 55147; -.
DR Ensembl; ENST00000346528.9; ENSP00000339220.5; ENSG00000100461.18. [Q86U06-4]
DR Ensembl; ENST00000359890.8; ENSP00000352956.3; ENSG00000100461.18. [Q86U06-1]
DR Ensembl; ENST00000399922.6; ENSP00000382806.2; ENSG00000100461.18. [Q86U06-2]
DR GeneID; 55147; -.
DR KEGG; hsa:55147; -.
DR MANE-Select; ENST00000359890.8; ENSP00000352956.3; NM_001077351.2; NP_001070819.1.
DR UCSC; uc001whg.4; human. [Q86U06-1]
DR CTD; 55147; -.
DR DisGeNET; 55147; -.
DR GeneCards; RBM23; -.
DR HGNC; HGNC:20155; RBM23.
DR HPA; ENSG00000100461; Low tissue specificity.
DR neXtProt; NX_Q86U06; -.
DR OpenTargets; ENSG00000100461; -.
DR PharmGKB; PA134974852; -.
DR VEuPathDB; HostDB:ENSG00000100461; -.
DR eggNOG; KOG0147; Eukaryota.
DR GeneTree; ENSGT00940000162546; -.
DR HOGENOM; CLU_020551_2_0_1; -.
DR InParanoid; Q86U06; -.
DR OMA; KSPHYRE; -.
DR OrthoDB; 873705at2759; -.
DR PhylomeDB; Q86U06; -.
DR TreeFam; TF320448; -.
DR PathwayCommons; Q86U06; -.
DR SignaLink; Q86U06; -.
DR BioGRID-ORCS; 55147; 34 hits in 1083 CRISPR screens.
DR ChiTaRS; RBM23; human.
DR EvolutionaryTrace; Q86U06; -.
DR GeneWiki; RBM23; -.
DR GenomeRNAi; 55147; -.
DR Pharos; Q86U06; Tbio.
DR PRO; PR:Q86U06; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86U06; protein.
DR Bgee; ENSG00000100461; Expressed in calcaneal tendon and 200 other tissues.
DR ExpressionAtlas; Q86U06; baseline and differential.
DR Genevisible; Q86U06; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029123; RBM39_linker.
DR InterPro; IPR006509; RBM39_SF.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF15519; RBM39linker; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01622; SF-CC1; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..439
FT /note="Probable RNA-binding protein 23"
FT /id="PRO_0000081783"
FT DOMAIN 166..243
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 263..341
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 13..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..104
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..100
FT /note="MASDDFDIVIEAMLEAPYKKEEDEQQRKEVKKDYPSNTTSSTSNSGNETSGS
FT STIGETSKKKRSRSHNKSRDRKRSRSRDRDRYRRRNSRSRSPGRQCRH -> MSNKGKK
FT LKRIILAIPPAAPATVAMRPVEAAPSGRQARRRGVGAIIKAGIESAVVVEIGIGIDGEI
FT VGAEVQVGSVVT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_008311"
FT VAR_SEQ 60..76
FT /note="KKKRSRSHNKSRDRKRS -> N (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_008312"
FT VAR_SEQ 135..152
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008313"
FT VAR_SEQ 311..319
FT /note="FSDSECARR -> LHPPPLGTV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008314"
FT VAR_SEQ 320..439
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008315"
FT VARIANT 184
FT /note="D -> N (in dbSNP:rs34246954)"
FT /id="VAR_052221"
FT VARIANT 393
FT /note="A -> AA"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15498874,
FT ECO:0000269|Ref.1"
FT /id="VAR_016841"
FT VARIANT 428
FT /note="F -> L (in dbSNP:rs1127066)"
FT /id="VAR_052222"
FT MUTAGEN 169..173
FT /note="FCMQL->ACMQA: In M1; abolished ability to regulate
FT steroid hormone receptor-mediated transcription, without
FT affecting the pre-mRNA splicing factor activity."
FT /evidence="ECO:0000269|PubMed:15694343"
FT MUTAGEN 266..270
FT /note="YVGSL->AVGSA: In M2; reduced pre-mRNA splicing
FT factor activity without affecting steroid hormone receptor-
FT mediated transcription."
FT /evidence="ECO:0000269|PubMed:15694343"
FT MUTAGEN 369..373
FT /note="LMAKL->AMAKA: In M3; reduced pre-mRNA splicing
FT factor activity without affecting steroid hormone receptor-
FT mediated transcription."
FT /evidence="ECO:0000269|PubMed:15694343"
FT CONFLICT 132
FT /note="A -> T (in Ref. 3; AAG24388)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..330
FT /note="LEQLNGFELA -> CGTVEWGLSLL (in Ref. 1; AAP97203)"
FT /evidence="ECO:0000305"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2CQ4"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:2CQ4"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2CQ4"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2CQ4"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:2CQ4"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:2CQ4"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2DNZ"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:2DNZ"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2DNZ"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:2DNZ"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:2DNZ"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:2DNZ"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:2DNZ"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:2DNZ"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:2DNZ"
SQ SEQUENCE 439 AA; 48731 MW; CFF3E56F7EA12D0B CRC64;
MASDDFDIVI EAMLEAPYKK EEDEQQRKEV KKDYPSNTTS STSNSGNETS GSSTIGETSK
KKRSRSHNKS RDRKRSRSRD RDRYRRRNSR SRSPGRQCRH RSRSWDRRHG SESRSRDHRR
EDRVHYRSPP LATGYRYGHS KSPHFREKSP VREPVDNLSP EERDARTVFC MQLAARIRPR
DLEDFFSAVG KVRDVRIISD RNSRRSKGIA YVEFCEIQSV PLAIGLTGQR LLGVPIIVQA
SQAEKNRLAA MANNLQKGNG GPMRLYVGSL HFNITEDMLR GIFEPFGKID NIVLMKDSDT
GRSKGYGFIT FSDSECARRA LEQLNGFELA GRPMRVGHVT ERLDGGTDIT FPDGDQELDL
GSAGGRFQLM AKLAEGAGIQ LPSTAAAAAA AAAQAAALQL NGAVPLGALN PAALTALSPA
LNLASQCFQL SSLFTPQTM
