RBM25_HUMAN
ID RBM25_HUMAN Reviewed; 843 AA.
AC P49756; A0PJL9; B2RNA8; B3KT03; Q2TA72; Q5XJ17; Q6P665; Q9H6A1; Q9UEQ5;
AC Q9UIE9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=RNA-binding protein 25;
DE AltName: Full=Arg/Glu/Asp-rich protein of 120 kDa;
DE Short=RED120;
DE AltName: Full=Protein S164;
DE AltName: Full=RNA-binding motif protein 25;
DE AltName: Full=RNA-binding region-containing protein 7;
GN Name=RBM25; Synonyms=RNPC7;
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 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-430 (ISOFORM 1).
RC TISSUE=Amygdala, and Kidney epithelium;
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 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Cerebellum, Fetal brain, Prostate, and Uterus;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-843.
RA Rowen L., Madan A., Qin S., Abbasi N., Dors M., Ratcliffe A., Madan A.,
RA Dickhoff R., Shaffer T., James R., Lasky S., Hood L.;
RT "Complete sequence of the gene for presenilin 1.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 146-155; 209-216 AND 672-685, PHOSPHORYLATION AT
RP SER-677, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 146-155 AND 247-261, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH APEX1; DDX39B; NCBP1; RBM8; RNPS1 AND SRRM1.
RX PubMed=17560998; DOI=10.1016/j.febslet.2007.05.066;
RA Fortes P., Longman D., McCracken S., Ip J.Y., Poot R., Mattaj I.W.,
RA Caceres J.F., Blencowe B.J.;
RT "Identification and characterization of RED120: a conserved PWI domain
RT protein with links to splicing and 3'-end formation.";
RL FEBS Lett. 581:3087-3097(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 571-843.
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M.,
RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F.,
RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L.,
RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W.,
RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D.,
RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [9]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [10]
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-683, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [13]
RP FUNCTION, INTERACTION WITH LUC7L3, AND SUBCELLULAR LOCATION.
RX PubMed=18663000; DOI=10.1128/mcb.00560-08;
RA Zhou A., Ou A.C., Cho A., Benz E.J. Jr., Huang S.C.;
RT "Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site
RT selection.";
RL Mol. Cell. Biol. 28:5924-5936(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583; SER-677; SER-683 AND
RP SER-703, AND IDENTIFICATION BY 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).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP FUNCTION.
RX PubMed=21859973; DOI=10.1161/circulationaha.111.044495;
RA Gao G., Xie A., Huang S.C., Zhou A., Zhang J., Herman A.M.,
RA Ghassemzadeh S., Jeong E.M., Kasturirangan S., Raicu M., Sobieski M.A. II,
RA Bhat G., Tatooles A., Benz E.J. Jr., Kamp T.J., Dudley S.C. Jr.;
RT "Role of RBM25/LUC7L3 in abnormal cardiac sodium channel splicing
RT regulation in human heart failure.";
RL Circulation 124:1124-1131(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-683 AND SER-703, AND
RP IDENTIFICATION BY 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-229; SER-583;
RP SER-677; SER-683 AND SER-703, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-578, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-273 AND LYS-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-261; LYS-273; LYS-430; LYS-578;
RP LYS-671; LYS-688; LYS-697 AND LYS-722, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 734-843, PWI DOMAIN, AND
RP MUTAGENESIS OF 734-LYS--LYS-736; 777-LYS-LYS-778; LYS-825 AND ARG-828.
RX PubMed=23190262; DOI=10.1042/bj20121382;
RA Gong D., Yang F., Li F., Qian D., Wu M., Shao Z., Wu M., Wu J., Shi Y.;
RT "Crystal structure and functional characterization of the human RBM25 PWI
RT domain and its flanking basic region.";
RL Biochem. J. 450:85-94(2013).
CC -!- FUNCTION: RNA-binding protein that acts as a regulator of alternative
CC pre-mRNA splicing. Involved in apoptotic cell death through the
CC regulation of the apoptotic factor BCL2L1 isoform expression. Modulates
CC the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1
CC isoform L mRNA expression. When overexpressed, stimulates proapoptotic
CC BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its
CC depletion caused the accumulation of antiapoptotic BCL2L1 isoform L.
CC Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA
CC sequence. Its association with LUC7L3 promotes U1 snRNP binding to a
CC weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic
CC splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of
CC the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and
CC truncated splice form of SCN5A in heart failure.
CC {ECO:0000269|PubMed:18663000, ECO:0000269|PubMed:21859973}.
CC -!- SUBUNIT: Interacts with LUC7L3 and SRRM1. Specifically associates with
CC functional splicing complexes, including Sm proteins and U1, U2, U4, U5
CC and U6 snRNAs. Associates with exon junction complex (EJC) proteins,
CC including APEX1, DDX39B, NCBP1, RBM8A and RNPS1. Interaction with NCBP1
CC is RNA-dependent. {ECO:0000269|PubMed:17560998,
CC ECO:0000269|PubMed:18663000}.
CC -!- INTERACTION:
CC P49756; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2211856, EBI-618309;
CC P49756; A7MD48: SRRM4; NbExp=3; IntAct=EBI-2211856, EBI-3867173;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Note=Colocalizes
CC predominantly, with SFRS2 and LUC7L3 splicing factors, in nuclear
CC speckles. Cytoplasmic localization is faint.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P49756-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49756-2; Sequence=VSP_036792, VSP_036793;
CC Name=3;
CC IsoId=P49756-3; Sequence=VSP_036791, VSP_036794;
CC Name=4;
CC IsoId=P49756-4; Sequence=VSP_039881, VSP_039882;
CC -!- DOMAIN: The PWI domain binds nucleic acids with significant help from
CC its N-terminal flanking basic region. It has an equal preference for
CC binding to single- or double-stranded species, and it contributes to
CC RBM25 role in modulation of alternative splicing, maybe by mediating
CC RNA-dependent association with LUC7L3.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62440.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH62440.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH83496.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG52915.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK026107; BAB15362.1; -; mRNA.
DR EMBL; AK094697; BAG52915.1; ALT_SEQ; mRNA.
DR EMBL; AL442663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004858; AAF19255.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81087.1; -; Genomic_DNA.
DR EMBL; BC062440; AAH62440.1; ALT_SEQ; mRNA.
DR EMBL; BC083496; AAH83496.1; ALT_INIT; mRNA.
DR EMBL; BC111066; AAI11067.1; -; mRNA.
DR EMBL; BC113389; AAI13390.1; -; mRNA.
DR EMBL; BC113391; AAI13392.1; -; mRNA.
DR EMBL; BC136775; AAI36776.1; -; mRNA.
DR EMBL; BC136776; AAI36777.1; -; mRNA.
DR EMBL; BC144407; AAI44408.1; -; mRNA.
DR EMBL; AF109907; AAC97961.1; -; Genomic_DNA.
DR EMBL; L40392; AAC41999.1; -; mRNA.
DR CCDS; CCDS32113.1; -. [P49756-1]
DR RefSeq; NP_067062.1; NM_021239.2. [P49756-1]
DR RefSeq; XP_011535346.1; XM_011537044.2. [P49756-1]
DR RefSeq; XP_011535347.1; XM_011537045.2.
DR PDB; 3V53; X-ray; 2.90 A; A/B/C/D/E=734-843.
DR PDBsum; 3V53; -.
DR AlphaFoldDB; P49756; -.
DR SMR; P49756; -.
DR BioGRID; 121843; 236.
DR CORUM; P49756; -.
DR IntAct; P49756; 55.
DR MINT; P49756; -.
DR STRING; 9606.ENSP00000261973; -.
DR GlyGen; P49756; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49756; -.
DR MetOSite; P49756; -.
DR PhosphoSitePlus; P49756; -.
DR SwissPalm; P49756; -.
DR BioMuta; RBM25; -.
DR DMDM; 226693631; -.
DR EPD; P49756; -.
DR jPOST; P49756; -.
DR MassIVE; P49756; -.
DR MaxQB; P49756; -.
DR PaxDb; P49756; -.
DR PeptideAtlas; P49756; -.
DR PRIDE; P49756; -.
DR ProteomicsDB; 56071; -. [P49756-1]
DR ProteomicsDB; 56072; -. [P49756-2]
DR ProteomicsDB; 56073; -. [P49756-3]
DR ProteomicsDB; 56074; -. [P49756-4]
DR Antibodypedia; 158; 71 antibodies from 17 providers.
DR DNASU; 58517; -.
DR Ensembl; ENST00000261973.12; ENSP00000261973.7; ENSG00000119707.14. [P49756-1]
DR Ensembl; ENST00000525321.5; ENSP00000436868.1; ENSG00000119707.14. [P49756-3]
DR Ensembl; ENST00000526754.5; ENSP00000436225.1; ENSG00000119707.14. [P49756-2]
DR Ensembl; ENST00000527432.5; ENSP00000431150.1; ENSG00000119707.14. [P49756-1]
DR Ensembl; ENST00000528081.5; ENSP00000434444.1; ENSG00000119707.14. [P49756-4]
DR GeneID; 58517; -.
DR KEGG; hsa:58517; -.
DR MANE-Select; ENST00000261973.12; ENSP00000261973.7; NM_021239.3; NP_067062.1.
DR UCSC; uc001xnn.5; human. [P49756-1]
DR CTD; 58517; -.
DR DisGeNET; 58517; -.
DR GeneCards; RBM25; -.
DR HGNC; HGNC:23244; RBM25.
DR HPA; ENSG00000119707; Low tissue specificity.
DR MIM; 612427; gene.
DR neXtProt; NX_P49756; -.
DR OpenTargets; ENSG00000119707; -.
DR PharmGKB; PA134912024; -.
DR VEuPathDB; HostDB:ENSG00000119707; -.
DR eggNOG; KOG2217; Eukaryota.
DR eggNOG; KOG2253; Eukaryota.
DR GeneTree; ENSGT00730000111019; -.
DR HOGENOM; CLU_009855_0_0_1; -.
DR InParanoid; P49756; -.
DR OMA; DYKEQEC; -.
DR OrthoDB; 885027at2759; -.
DR PhylomeDB; P49756; -.
DR TreeFam; TF320185; -.
DR PathwayCommons; P49756; -.
DR SignaLink; P49756; -.
DR BioGRID-ORCS; 58517; 779 hits in 1091 CRISPR screens.
DR ChiTaRS; RBM25; human.
DR GeneWiki; RBM25; -.
DR GenomeRNAi; 58517; -.
DR Pharos; P49756; Tbio.
DR PRO; PR:P49756; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49756; protein.
DR Bgee; ENSG00000119707; Expressed in tendon of biceps brachii and 207 other tissues.
DR ExpressionAtlas; P49756; baseline and differential.
DR Genevisible; P49756; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12446; RRM_RBM25; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034268; RBM25_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00311; PWI; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51025; PWI; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..843
FT /note="RNA-binding protein 25"
FT /id="PRO_0000081784"
FT DOMAIN 87..164
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 750..843
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..644
FT /note="Necessary for nuclear speckle localization"
FT REGION 498..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:B2RY56"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 671
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 722
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 109..164
FT /note="KCGLVLSWKRVQGASGKLQAFGFCEYKEPESTLRALRLLHDLQIGEKKLLVK
FT VDAK -> PSDSVSTRSQNLPSVHSDYYMTCKLERKSYSLKLMQRQRHSWMNGKQRRKL
FT LMGLG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039881"
FT VAR_SEQ 165..843
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039882"
FT VAR_SEQ 290..300
FT /note="KLEEEKGKKEK -> VVFLSFHLIPI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036791"
FT VAR_SEQ 290..294
FT /note="KLEEE -> RSYGD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036792"
FT VAR_SEQ 295..843
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036793"
FT VAR_SEQ 301..843
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036794"
FT MUTAGEN 734..736
FT /note="KRK->AAA: Reduced DNA/RNA binding."
FT /evidence="ECO:0000269|PubMed:23190262"
FT MUTAGEN 777..778
FT /note="KK->AA: Reduced DNA/RNA binding."
FT /evidence="ECO:0000269|PubMed:23190262"
FT MUTAGEN 825
FT /note="K->A: Reduced DNA/RNA binding; when associated with
FT A-828."
FT /evidence="ECO:0000269|PubMed:23190262"
FT MUTAGEN 828
FT /note="R->A: Reduced DNA/RNA binding; when associated with
FT A-825."
FT /evidence="ECO:0000269|PubMed:23190262"
FT CONFLICT 428
FT /note="D -> K (in Ref. 1; BAB15362)"
FT /evidence="ECO:0000305"
FT CONFLICT 571..574
FT /note="RRRQ -> EAQE (in Ref. 8; AAC41999)"
FT /evidence="ECO:0000305"
FT HELIX 739..744
FT /evidence="ECO:0007829|PDB:3V53"
FT HELIX 749..754
FT /evidence="ECO:0007829|PDB:3V53"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:3V53"
FT HELIX 764..769
FT /evidence="ECO:0007829|PDB:3V53"
FT HELIX 771..782
FT /evidence="ECO:0007829|PDB:3V53"
FT HELIX 789..799
FT /evidence="ECO:0007829|PDB:3V53"
FT HELIX 804..815
FT /evidence="ECO:0007829|PDB:3V53"
FT HELIX 818..839
FT /evidence="ECO:0007829|PDB:3V53"
SQ SEQUENCE 843 AA; 100185 MW; 80534590147A342A CRC64;
MSFPPHLNRP PMGIPALPPG IPPPQFPGFP PPVPPGTPMI PVPMSIMAPA PTVLVPTVSM
VGKHLGARKD HPGLKAKEND ENCGPTTTVF VGNISEKASD MLIRQLLAKC GLVLSWKRVQ
GASGKLQAFG FCEYKEPEST LRALRLLHDL QIGEKKLLVK VDAKTKAQLD EWKAKKKASN
GNARPETVTN DDEEALDEET KRRDQMIKGA IEVLIREYSS ELNAPSQESD SHPRKKKKEK
KEDIFRRFPV APLIPYPLIT KEDINAIEME EDKRDLISRE ISKFRDTHKK LEEEKGKKEK
ERQEIEKERR ERERERERER ERRERERERE REREREKEKE RERERERDRD RDRTKERDRD
RDRERDRDRD RERSSDRNKD RSRSREKSRD RERERERERE RERERERERE RERERERERE
REREREKDKK RDREEDEEDA YERRKLERKL REKEAAYQER LKNWEIRERK KTREYEKEAE
REEERRREMA KEAKRLKEFL EDYDDDRDDP KYYRGSALQK RLRDREKEME ADERDRKREK
EELEEIRQRL LAEGHPDPDA ELQRMEQEAE RRRQPQIKQE PESEEEEEEK QEKEEKREEP
MEEEEEPEQK PCLKPTLRPI SSAPSVSSAS GNATPNTPGD ESPCGIIIPH ENSPDQQQPE
EHRPKIGLSL KLGASNSPGQ PNSVKRKKLP VDSVFNKFED EDSDDVPRKR KLVPLDYGED
DKNATKGTVN TEEKRKHIKS LIEKIPTAKP ELFAYPLDWS IVDSILMERR IRPWINKKII
EYIGEEEATL VDFVCSKVMA HSSPQSILDD VAMVLDEEAE VFIVKMWRLL IYETEAKKIG
LVK
