RBM5_HUMAN
ID RBM5_HUMAN Reviewed; 815 AA.
AC P52756; B2RA45; B4DM16; B4DMF9; B4DZ63; Q93021; Q9BU14; Q9HDA6; Q9UKY8;
AC Q9UL24;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=RNA-binding protein 5;
DE AltName: Full=Protein G15;
DE AltName: Full=Putative tumor suppressor LUCA15;
DE AltName: Full=RNA-binding motif protein 5;
DE AltName: Full=Renal carcinoma antigen NY-REN-9;
GN Name=RBM5; ORFNames=H37, LUCA15;
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).
RA Bader S., Latif F., Duh F.-M., Wei M., Kashuba V., Sekido Y., Lee C.,
RA Koonin E., Zabarofsky E., Klein G., Minna J.D., Lerman M.I.;
RT "A putative tumor suppressor gene LUCA15 on 3p21.3 encodes two RNA
RT recognizing motifs and is related to the Drosophila tumor suppressor gene
RT Sxl.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10486216; DOI=10.1006/geno.1999.5878;
RA Timmer T., Terpstra P., van den Berg A., Veldhuis P.M.J.F., Ter Elst A.,
RA van der Veen A.Y., Kok K., Naylor S.L., Buys C.H.C.M.;
RT "An evolutionary rearrangement of the Xp11.3-11.23 region in 3p21.3, a
RT region frequently deleted in a variety of cancers.";
RL Genomics 60:238-240(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT "Identification of differentially expressed genes associated with HER-2/neu
RT overexpression in human breast cancer cells.";
RL Nucleic Acids Res. 27:4008-4017(1999).
RN [4]
RP SEQUENCE REVISION TO 61.
RC TISSUE=Testis;
RA Oh J.J., Wong S.G., Slamon D.J.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND FUNCTION.
RX PubMed=10949932; DOI=10.1038/sj.onc.1203720;
RA Sutherland L.C., Edwards S.E., Cable H.C., Poirier G.G., Miller B.A.,
RA Cooper C.S., Williams G.T.;
RT "LUCA-15-encoded sequence variants regulate CD95-mediated apoptosis.";
RL Oncogene 19:3774-3781(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Placenta;
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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-815.
RA Bentley D., Maggi L.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [10]
RP FUNCTION.
RX PubMed=12207175; DOI=10.1023/a:1020083008017;
RA Mourtada-Maarabouni M., Sutherland L.C., Williams G.T.;
RT "Candidate tumour suppressor LUCA-15 can regulate multiple apoptotic
RT pathways.";
RL Apoptosis 7:421-432(2002).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORM 5), AND FUNCTION.
RX PubMed=12581154; DOI=10.1046/j.1365-2443.2003.00619.x;
RA Mourtada-Maarabouni M., Sutherland L.C., Meredith J.M., Williams G.T.;
RT "Simultaneous acceleration of the cell cycle and suppression of apoptosis
RT by splice variant delta-6 of the candidate tumour suppressor LUCA-
RT 15/RBM5.";
RL Genes Cells 8:109-119(2003).
RN [12]
RP FUNCTION.
RX PubMed=15192330; DOI=10.1023/b:appt.0000031455.79352.57;
RA Rintala-Maki N.D., Sutherland L.C.;
RT "LUCA-15/RBM5, a putative tumour suppressor, enhances multiple receptor-
RT initiated death signals.";
RL Apoptosis 9:475-484(2004).
RN [13]
RP FUNCTION.
RX PubMed=16585163; DOI=10.1158/0008-5472.can-05-1667;
RA Oh J.J., Razfar A., Delgado I., Reed R.A., Malkina A., Boctor B.,
RA Slamon D.J.;
RT "3p21.3 tumor suppressor gene H37/Luca15/RBM5 inhibits growth of human lung
RT cancer cells through cell cycle arrest and apoptosis.";
RL Cancer Res. 66:3419-3427(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP A COMPLEX.
RX PubMed=17332742; DOI=10.1038/sj.emboj.7601631;
RA Behzadnia N., Golas M.M., Hartmuth K., Sander B., Kastner B., Deckert J.,
RA Dube P., Will C.L., Urlaub H., Stark H., Luehrmann R.;
RT "Composition and three-dimensional EM structure of double affinity-
RT purified, human prespliceosomal A complexes.";
RL EMBO J. 26:1737-1748(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP FUNCTION, INTERACTION WITH ACIN1; PRPF8; SFRS3; SNRPB; SNRPN; SNRNP70;
RP SNRNP200 AND U2AF2, AND SUBCELLULAR LOCATION.
RX PubMed=18851835; DOI=10.1016/j.molcel.2008.08.008;
RA Bonnal S., Martinez C., Foerch P., Bachi A., Wilm M., Valcarcel J.;
RT "RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon
RT definition.";
RL Mol. Cell 32:81-95(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-624, AND
RP IDENTIFICATION BY 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 [20]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=18840686; DOI=10.1073/pnas.0805569105;
RA Fushimi K., Ray P., Kar A., Wang L., Sutherland L.C., Wu J.Y.;
RT "Up-regulation of the proapoptotic caspase 2 splicing isoform by a
RT candidate tumor suppressor, RBM5.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15708-15713(2008).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-624, AND
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-59; SER-69; SER-72;
RP SER-78 AND SER-624, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-624, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Component of the spliceosome A complex. Regulates alternative
CC splicing of a number of mRNAs. May modulate splice site pairing after
CC recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of
CC the intron. May both positively and negatively regulate apoptosis by
CC regulating the alternative splicing of several genes involved in this
CC process, including FAS and CASP2/caspase-2. In the case of FAS,
CC promotes exclusion of exon 6 thereby producing a soluble form of FAS
CC that inhibits apoptosis. In the case of CASP2/caspase-2, promotes
CC exclusion of exon 9 thereby producing a catalytically active form of
CC CASP2/Caspase-2 that induces apoptosis. {ECO:0000269|PubMed:10949932,
CC ECO:0000269|PubMed:12207175, ECO:0000269|PubMed:12581154,
CC ECO:0000269|PubMed:15192330, ECO:0000269|PubMed:16585163,
CC ECO:0000269|PubMed:18840686, ECO:0000269|PubMed:18851835}.
CC -!- SUBUNIT: Component of the spliceosome A complex (also known as the
CC prespliceosome). Appears to dissociate from the spliceosome upon
CC formation of the spliceosome B complex (also known as the precatalytic
CC spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound.
CC Interacts with U2AF2; this interaction is direct. Also interacts with
CC ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these
CC interactions may be indirect. {ECO:0000269|PubMed:17332742,
CC ECO:0000269|PubMed:18851835}.
CC -!- INTERACTION:
CC P52756; P02649: APOE; NbExp=3; IntAct=EBI-714003, EBI-1222467;
CC P52756; P27797: CALR; NbExp=3; IntAct=EBI-714003, EBI-1049597;
CC P52756; O43143: DHX15; NbExp=15; IntAct=EBI-714003, EBI-1237044;
CC P52756; P36957: DLST; NbExp=3; IntAct=EBI-714003, EBI-351007;
CC P52756; P42858: HTT; NbExp=6; IntAct=EBI-714003, EBI-466029;
CC P52756; Q92876: KLK6; NbExp=3; IntAct=EBI-714003, EBI-2432309;
CC P52756; P50221: MEOX1; NbExp=4; IntAct=EBI-714003, EBI-2864512;
CC P52756; Q6FHY5: MEOX2; NbExp=6; IntAct=EBI-714003, EBI-16439278;
CC P52756; O95822-2: MLYCD; NbExp=4; IntAct=EBI-714003, EBI-13315321;
CC P52756; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-714003, EBI-1055945;
CC P52756; Q9UMS4: PRPF19; NbExp=8; IntAct=EBI-714003, EBI-395746;
CC P52756; P37173: TGFBR2; NbExp=3; IntAct=EBI-714003, EBI-296151;
CC P52756; P26368: U2AF2; NbExp=2; IntAct=EBI-714003, EBI-742339;
CC P52756; O15042: U2SURP; NbExp=2; IntAct=EBI-714003, EBI-310697;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18851835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P52756-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52756-2; Sequence=VSP_037432, VSP_037434;
CC Name=3;
CC IsoId=P52756-3; Sequence=VSP_037429, VSP_037430;
CC Name=4;
CC IsoId=P52756-4; Sequence=VSP_037433;
CC Name=5; Synonyms=delta-6;
CC IsoId=P52756-5; Sequence=VSP_037431, VSP_037435;
CC -!- TISSUE SPECIFICITY: Isoform 5 is widely expressed in normal tissues and
CC is expressed at increased levels in T-leukemic cell lines.
CC -!- SIMILARITY: Belongs to the RBM5/RBM10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG59728.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAG59871.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAG63975.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBM5ID42069ch3p21.html";
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; U23946; AAA99715.1; -; mRNA.
DR EMBL; AF091263; AAD04159.1; -; mRNA.
DR EMBL; AF103802; AAF02422.2; -; mRNA.
DR EMBL; AF107493; AAF99551.1; -; mRNA.
DR EMBL; AK297249; BAG59728.1; ALT_SEQ; mRNA.
DR EMBL; AK297445; BAG59871.1; ALT_SEQ; mRNA.
DR EMBL; AK302766; BAG63975.1; ALT_SEQ; mRNA.
DR EMBL; AK314032; BAG36742.1; -; mRNA.
DR EMBL; CH471055; EAW65040.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65041.1; -; Genomic_DNA.
DR EMBL; U73168; AAB42216.1; -; Genomic_DNA.
DR CCDS; CCDS2810.1; -. [P52756-1]
DR RefSeq; NP_005769.1; NM_005778.3. [P52756-1]
DR RefSeq; XP_016860992.1; XM_017005503.1. [P52756-1]
DR PDB; 2LK0; NMR; -; A=181-210.
DR PDB; 2LK1; NMR; -; A=181-210.
DR PDB; 2LKZ; NMR; -; A=231-316.
DR PDB; 5MF9; NMR; -; A=451-511.
DR PDB; 5MFY; NMR; -; A=451-511.
DR PDBsum; 2LK0; -.
DR PDBsum; 2LK1; -.
DR PDBsum; 2LKZ; -.
DR PDBsum; 5MF9; -.
DR PDBsum; 5MFY; -.
DR AlphaFoldDB; P52756; -.
DR BMRB; P52756; -.
DR SMR; P52756; -.
DR BioGRID; 115480; 163.
DR DIP; DIP-47277N; -.
DR IntAct; P52756; 61.
DR MINT; P52756; -.
DR STRING; 9606.ENSP00000343054; -.
DR GlyGen; P52756; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52756; -.
DR PhosphoSitePlus; P52756; -.
DR BioMuta; RBM5; -.
DR DMDM; 13124794; -.
DR EPD; P52756; -.
DR jPOST; P52756; -.
DR MassIVE; P52756; -.
DR MaxQB; P52756; -.
DR PaxDb; P52756; -.
DR PeptideAtlas; P52756; -.
DR PRIDE; P52756; -.
DR ProteomicsDB; 56524; -. [P52756-1]
DR ProteomicsDB; 56525; -. [P52756-2]
DR ProteomicsDB; 56526; -. [P52756-3]
DR ProteomicsDB; 56527; -. [P52756-4]
DR ProteomicsDB; 56528; -. [P52756-5]
DR Antibodypedia; 1962; 258 antibodies from 30 providers.
DR DNASU; 10181; -.
DR Ensembl; ENST00000347869.8; ENSP00000343054.3; ENSG00000003756.17. [P52756-1]
DR Ensembl; ENST00000469838.5; ENSP00000419534.1; ENSG00000003756.17. [P52756-2]
DR GeneID; 10181; -.
DR KEGG; hsa:10181; -.
DR MANE-Select; ENST00000347869.8; ENSP00000343054.3; NM_005778.4; NP_005769.1.
DR UCSC; uc003cyf.4; human. [P52756-1]
DR CTD; 10181; -.
DR DisGeNET; 10181; -.
DR GeneCards; RBM5; -.
DR HGNC; HGNC:9902; RBM5.
DR HPA; ENSG00000003756; Low tissue specificity.
DR MIM; 606884; gene.
DR neXtProt; NX_P52756; -.
DR OpenTargets; ENSG00000003756; -.
DR PharmGKB; PA34267; -.
DR VEuPathDB; HostDB:ENSG00000003756; -.
DR eggNOG; KOG0154; Eukaryota.
DR GeneTree; ENSGT00940000156617; -.
DR HOGENOM; CLU_010527_0_0_1; -.
DR InParanoid; P52756; -.
DR OMA; TIMGVIR; -.
DR PhylomeDB; P52756; -.
DR TreeFam; TF315789; -.
DR PathwayCommons; P52756; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P52756; -.
DR BioGRID-ORCS; 10181; 78 hits in 1088 CRISPR screens.
DR ChiTaRS; RBM5; human.
DR GeneWiki; RBM5; -.
DR GenomeRNAi; 10181; -.
DR Pharos; P52756; Tbio.
DR PRO; PR:P52756; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P52756; protein.
DR Bgee; ENSG00000003756; Expressed in right uterine tube and 199 other tissues.
DR ExpressionAtlas; P52756; baseline and differential.
DR Genevisible; P52756; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; TAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:UniProtKB.
DR CDD; cd12752; RRM1_RBM5; 1.
DR CDD; cd12755; RRM2_RBM5; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033094; RBM5.
DR InterPro; IPR034991; RBM5_RRM1.
DR InterPro; IPR034993; RBM5_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF21; PTHR13948:SF21; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..815
FT /note="RNA-binding protein 5"
FT /id="PRO_0000081759"
FT DOMAIN 98..178
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 231..315
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 743..789
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 181..210
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 647..677
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..809
FT /note="Required for interaction with U2AF2"
FT /evidence="ECO:0000269|PubMed:18851835"
FT REGION 411..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..535
FT /note="Sufficient for interaction with ACIN1, PRPF8, SFRS3,
FT SNRPB, SNRPN, SNRNP70 and SNRNP200"
FT /evidence="ECO:0000269|PubMed:18851835"
FT REGION 507..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 65..126
FT /note="ERRNSDRSEDGYHSDGDYGEHDYRHDISDERESKTIMLRGLPITITESDIRE
FT MMESFEGPQP -> YSRNDGVLRRPSACGCEADEEENRCKPWFRLRGVLSLARCYQLDG
FT SQSEKVGDSRKAHCNAL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037429"
FT VAR_SEQ 127..815
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037430"
FT VAR_SEQ 137..150
FT /note="GVSRGFAFVEFYHL -> EKVGDSRKAHCNAL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037431"
FT VAR_SEQ 138..143
FT /note="VSRGFA -> ESLLSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10949932"
FT /id="VSP_037432"
FT VAR_SEQ 142..815
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037433"
FT VAR_SEQ 144..815
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10949932"
FT /id="VSP_037434"
FT VAR_SEQ 151..815
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037435"
FT VARIANT 163
FT /note="K -> N (in dbSNP:rs56783610)"
FT /id="VAR_061831"
FT CONFLICT 53..54
FT /note="DY -> GS (in Ref. 1; AAA99715)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="G -> V (in Ref. 1; AAA99715)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="Missing (in Ref. 8; AAB42216)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="G -> A (in Ref. 8; AAB42216)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="T -> I (in Ref. 1; AAA99715)"
FT /evidence="ECO:0000305"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2LK0"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2LK0"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2LK0"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2LK0"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2LKZ"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:2LKZ"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2LKZ"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2LKZ"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2LKZ"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:2LKZ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2LKZ"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:2LKZ"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:2LKZ"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2LKZ"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:2LKZ"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:5MF9"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5MF9"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:5MF9"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:5MF9"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:5MF9"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:5MF9"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:5MF9"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5MF9"
FT TURN 490..493
FT /evidence="ECO:0007829|PDB:5MF9"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:5MF9"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:5MF9"
SQ SEQUENCE 815 AA; 92154 MW; AA79962D13405479 CRC64;
MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP
ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES
FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP
KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESVQSVDYYC DTIILRNIAP
HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP
LKIDGKTIGV DFAKSARKDL VLSDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGSVDYSY
LQPGQDGYAQ YAQYSQDYQQ FYQQQAGGLE SDASSASGTA VTTTSAAVVS QSPQLYNQTS
NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY
DPNSQYYYNS LTQQYLYWDG EKETYVPAAE SSSHQQSGLP PAKEGKEKKE KPKSKTAQQI
AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLIP
ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNKD
ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP
KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK
GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME
