RBPMS_HUMAN
ID RBPMS_HUMAN Reviewed; 196 AA.
AC Q93062; D3DSU9; Q92516; Q92517; Q92518; Q96J26;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=RNA-binding protein with multiple splicing;
DE Short=RBP-MS;
DE AltName: Full=Heart and RRM expressed sequence;
DE Short=Hermes;
GN Name=RBPMS; Synonyms=HERMES;
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] (ISOFORMS A; B; C; D AND E).
RC TISSUE=Lip;
RX PubMed=8855282; DOI=10.1073/pnas.93.20.10913;
RA Shimamoto A., Kitao S., Ichikawa K., Suzuki N., Yamabe Y., Imamura O.,
RA Tokutake Y., Satoh M., Matsumoto T., Kuromitsu J., Kataoka H., Sugawara K.,
RA Sugawara M., Sugimoto M., Goto M., Furuichi Y.;
RT "A unique human gene that spans over 230 kb in the human chromosome 8p11-12
RT and codes multiple family proteins sharing RNA-binding motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10913-10917(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=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 [4]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [5]
RP FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND TGFBR1, SUBCELLULAR
RP LOCATION, AND RNA-BINDING.
RX PubMed=17099224; DOI=10.1093/nar/gkl914;
RA Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H.,
RA Ye Q.;
RT "Potentiation of Smad-mediated transcriptional activation by the RNA-
RT binding protein RBPMS.";
RL Nucleic Acids Res. 34:6314-6326(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8] {ECO:0007744|PDB:5CYJ, ECO:0007744|PDB:5DET}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 14-111 OF APOPROTEIN AND IN
RP COMPLEX WITH RNA, FUNCTION IN RNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF PHE-27; 36-LYS--ARG-38; PHE-65; GLU-97; LYS-100 AND
RP 103-THR-LYS-104.
RX PubMed=26347403; DOI=10.1017/s0033583515000207;
RA Teplova M., Farazi T.A., Tuschl T., Patel D.J.;
RT "Structural basis underlying CAC RNA recognition by the RRM domain of
RT dimeric RNA-binding protein RBPMS.";
RL Q. Rev. Biophys. 2015:1-11(2015).
CC -!- FUNCTION: Acts as a coactivator of transcriptional activity. Required
CC to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2,
CC SMAD3 and SMAD4 to increase transcriptional activity. Increases
CC phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif,
CC possibly through recruitment of TGFBR1. Promotes the nuclear
CC accumulation of SMAD2, SMAD3 and SMAD4 proteins (PubMed:26347403).
CC Binds to poly(A) RNA (PubMed:17099224, PubMed:26347403).
CC {ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:26347403}.
CC -!- SUBUNIT: Homodimer; each protein chain binds one RNA molecule via the
CC external surface of the homodimer (PubMed:26347403). Interacts with
CC SMAD2, SMAD3 and SMAD4; the interactions are direct (PubMed:17099224).
CC {ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:26347403}.
CC -!- INTERACTION:
CC Q93062; Q13444: ADAM15; NbExp=3; IntAct=EBI-740322, EBI-77818;
CC Q93062; Q9Y4X0: AMMECR1; NbExp=4; IntAct=EBI-740322, EBI-8583355;
CC Q93062; P54253: ATXN1; NbExp=6; IntAct=EBI-740322, EBI-930964;
CC Q93062; Q8N9N5: BANP; NbExp=3; IntAct=EBI-740322, EBI-744695;
CC Q93062; Q9BXC9: BBS2; NbExp=3; IntAct=EBI-740322, EBI-748297;
CC Q93062; A8KA13: BCL6B; NbExp=3; IntAct=EBI-740322, EBI-10174813;
CC Q93062; O14503: BHLHE40; NbExp=3; IntAct=EBI-740322, EBI-711810;
CC Q93062; Q8N9W6: BOLL; NbExp=3; IntAct=EBI-740322, EBI-998198;
CC Q93062; Q6NUJ2: C11orf87; NbExp=3; IntAct=EBI-740322, EBI-6660291;
CC Q93062; Q6P1W5: C1orf94; NbExp=4; IntAct=EBI-740322, EBI-946029;
CC Q93062; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-740322, EBI-7317823;
CC Q93062; Q13554: CAMK2B; NbExp=3; IntAct=EBI-740322, EBI-1058722;
CC Q93062; P51959: CCNG1; NbExp=3; IntAct=EBI-740322, EBI-3905829;
CC Q93062; O75909: CCNK; NbExp=4; IntAct=EBI-740322, EBI-739806;
CC Q93062; Q9UJX2: CDC23; NbExp=4; IntAct=EBI-740322, EBI-396137;
CC Q93062; Q96SW2: CRBN; NbExp=3; IntAct=EBI-740322, EBI-2510250;
CC Q93062; Q02930-3: CREB5; NbExp=3; IntAct=EBI-740322, EBI-10192698;
CC Q93062; P05813: CRYBA1; NbExp=3; IntAct=EBI-740322, EBI-7043337;
CC Q93062; P07498: CSN3; NbExp=4; IntAct=EBI-740322, EBI-2602175;
CC Q93062; Q15038: DAZAP2; NbExp=6; IntAct=EBI-740322, EBI-724310;
CC Q93062; Q5TAQ9: DCAF8; NbExp=3; IntAct=EBI-740322, EBI-740686;
CC Q93062; A2VCK2: DCDC2B; NbExp=3; IntAct=EBI-740322, EBI-10173222;
CC Q93062; Q9BTE1: DCTN5; NbExp=3; IntAct=EBI-740322, EBI-747324;
CC Q93062; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-740322, EBI-9679045;
CC Q93062; Q7L591: DOK3; NbExp=3; IntAct=EBI-740322, EBI-2834978;
CC Q93062; Q6PKX4: DOK6; NbExp=3; IntAct=EBI-740322, EBI-2880244;
CC Q93062; O14531: DPYSL4; NbExp=3; IntAct=EBI-740322, EBI-719542;
CC Q93062; Q86UW9: DTX2; NbExp=7; IntAct=EBI-740322, EBI-740376;
CC Q93062; O95967: EFEMP2; NbExp=3; IntAct=EBI-740322, EBI-743414;
CC Q93062; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-740322, EBI-741626;
CC Q93062; Q92567: FAM168A; NbExp=5; IntAct=EBI-740322, EBI-7957930;
CC Q93062; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-740322, EBI-10244131;
CC Q93062; Q96D16: FBXL18; NbExp=3; IntAct=EBI-740322, EBI-744419;
CC Q93062; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-740322, EBI-744935;
CC Q93062; Q99958: FOXC2; NbExp=3; IntAct=EBI-740322, EBI-3956892;
CC Q93062; Q9BZS1: FOXP3; NbExp=6; IntAct=EBI-740322, EBI-983719;
CC Q93062; O75603: GCM2; NbExp=5; IntAct=EBI-740322, EBI-10188645;
CC Q93062; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-740322, EBI-748515;
CC Q93062; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-740322, EBI-5666657;
CC Q93062; Q13227: GPS2; NbExp=3; IntAct=EBI-740322, EBI-713355;
CC Q93062; Q13588: GRAP; NbExp=3; IntAct=EBI-740322, EBI-2847510;
CC Q93062; Q14687: GSE1; NbExp=3; IntAct=EBI-740322, EBI-372619;
CC Q93062; B4DNA4: hCG_20425; NbExp=3; IntAct=EBI-740322, EBI-7399002;
CC Q93062; Q9UBP5: HEY2; NbExp=3; IntAct=EBI-740322, EBI-750630;
CC Q93062; Q9NQ87: HEYL; NbExp=4; IntAct=EBI-740322, EBI-751092;
CC Q93062; Q8WVV9: HNRNPLL; NbExp=3; IntAct=EBI-740322, EBI-535849;
CC Q93062; P49639: HOXA1; NbExp=3; IntAct=EBI-740322, EBI-740785;
CC Q93062; P01344: IGF2; NbExp=3; IntAct=EBI-740322, EBI-7178764;
CC Q93062; Q9NXX0: ILF3; NbExp=3; IntAct=EBI-740322, EBI-743980;
CC Q93062; Q0VD86: INCA1; NbExp=3; IntAct=EBI-740322, EBI-6509505;
CC Q93062; Q9NRY2: INIP; NbExp=4; IntAct=EBI-740322, EBI-2881520;
CC Q93062; Q9UHH9: IP6K2; NbExp=3; IntAct=EBI-740322, EBI-747509;
CC Q93062; Q7L273: KCTD9; NbExp=3; IntAct=EBI-740322, EBI-4397613;
CC Q93062; Q96HR4: KIAA1305; NbExp=3; IntAct=EBI-740322, EBI-10288524;
CC Q93062; Q99706: KIR2DL4; NbExp=3; IntAct=EBI-740322, EBI-10294579;
CC Q93062; P52292: KPNA2; NbExp=3; IntAct=EBI-740322, EBI-349938;
CC Q93062; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-740322, EBI-10176379;
CC Q93062; Q3LI72: KRTAP19-5; NbExp=4; IntAct=EBI-740322, EBI-1048945;
CC Q93062; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-740322, EBI-10241353;
CC Q93062; A1A580: KRTAP23-1; NbExp=3; IntAct=EBI-740322, EBI-10171734;
CC Q93062; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-740322, EBI-10261141;
CC Q93062; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-740322, EBI-9088829;
CC Q93062; Q8N8I6: LINC00482; NbExp=3; IntAct=EBI-740322, EBI-10267998;
CC Q93062; Q9Y4M8: LINC00588; NbExp=3; IntAct=EBI-740322, EBI-10039207;
CC Q93062; P61968: LMO4; NbExp=3; IntAct=EBI-740322, EBI-2798728;
CC Q93062; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-740322, EBI-2341787;
CC Q93062; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-740322, EBI-716006;
CC Q93062; B1AHB0: MCM5; NbExp=3; IntAct=EBI-740322, EBI-10175425;
CC Q93062; Q9NPC6: MYOZ2; NbExp=3; IntAct=EBI-740322, EBI-746712;
CC Q93062; Q6XQN6: NAPRT; NbExp=3; IntAct=EBI-740322, EBI-10254872;
CC Q93062; Q6XQN6-2: NAPRT; NbExp=3; IntAct=EBI-740322, EBI-10254820;
CC Q93062; Q14511: NEDD9; NbExp=3; IntAct=EBI-740322, EBI-2108053;
CC Q93062; Q6NSM0: NR1D2; NbExp=4; IntAct=EBI-740322, EBI-10250949;
CC Q93062; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-740322, EBI-741158;
CC Q93062; P32242: OTX1; NbExp=4; IntAct=EBI-740322, EBI-740446;
CC Q93062; J3QSH9: PER1; NbExp=3; IntAct=EBI-740322, EBI-10178671;
CC Q93062; Q6IN51: PER1; NbExp=3; IntAct=EBI-740322, EBI-10250187;
CC Q93062; O43189: PHF1; NbExp=4; IntAct=EBI-740322, EBI-530034;
CC Q93062; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-740322, EBI-357318;
CC Q93062; Q13526: PIN1; NbExp=4; IntAct=EBI-740322, EBI-714158;
CC Q93062; P78337: PITX1; NbExp=6; IntAct=EBI-740322, EBI-748265;
CC Q93062; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-740322, EBI-1389308;
CC Q93062; Q96HA1: POM121; NbExp=4; IntAct=EBI-740322, EBI-739990;
CC Q93062; P09565: PP9974; NbExp=3; IntAct=EBI-740322, EBI-10196507;
CC Q93062; Q13131: PRKAA1; NbExp=3; IntAct=EBI-740322, EBI-1181405;
CC Q93062; P54646: PRKAA2; NbExp=3; IntAct=EBI-740322, EBI-1383852;
CC Q93062; P86479: PRR20C; NbExp=3; IntAct=EBI-740322, EBI-10172814;
CC Q93062; Q96PU8: QKI; NbExp=5; IntAct=EBI-740322, EBI-945792;
CC Q93062; Q9Y2K5-2: R3HDM2; NbExp=3; IntAct=EBI-740322, EBI-10326419;
CC Q93062; Q9NWB1: RBFOX1; NbExp=3; IntAct=EBI-740322, EBI-945906;
CC Q93062; Q96NR8: RDH12; NbExp=3; IntAct=EBI-740322, EBI-3916363;
CC Q93062; O94955: RHOBTB3; NbExp=4; IntAct=EBI-740322, EBI-2367123;
CC Q93062; Q9BQY4: RHOXF2; NbExp=6; IntAct=EBI-740322, EBI-372094;
CC Q93062; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-740322, EBI-10226430;
CC Q93062; A1L4F5: ROR2; NbExp=3; IntAct=EBI-740322, EBI-10172778;
CC Q93062; Q14D33: RTP5; NbExp=3; IntAct=EBI-740322, EBI-10217913;
CC Q93062; Q9BVN2: RUSC1; NbExp=4; IntAct=EBI-740322, EBI-6257312;
CC Q93062; Q86WG5: SBF2; NbExp=3; IntAct=EBI-740322, EBI-2683289;
CC Q93062; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-740322, EBI-9089805;
CC Q93062; Q08AM8: SH3RF2; NbExp=3; IntAct=EBI-740322, EBI-10225873;
CC Q93062; O00241-2: SIRPB1; NbExp=3; IntAct=EBI-740322, EBI-10179231;
CC Q93062; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-740322, EBI-10269322;
CC Q93062; Q53HV7: SMUG1; NbExp=2; IntAct=EBI-740322, EBI-749970;
CC Q93062; P14678-2: SNRPB; NbExp=3; IntAct=EBI-740322, EBI-372475;
CC Q93062; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-740322, EBI-10246938;
CC Q93062; Q5T0L3: SPATA46; NbExp=3; IntAct=EBI-740322, EBI-750105;
CC Q93062; Q6RVD6: SPATA8; NbExp=4; IntAct=EBI-740322, EBI-8635958;
CC Q93062; Q9UQ90: SPG7; NbExp=3; IntAct=EBI-740322, EBI-717201;
CC Q93062; Q96SI9: STRBP; NbExp=4; IntAct=EBI-740322, EBI-740355;
CC Q93062; O95947: TBX6; NbExp=3; IntAct=EBI-740322, EBI-2824328;
CC Q93062; Q6PIY7: TENT2; NbExp=3; IntAct=EBI-740322, EBI-2802204;
CC Q93062; Q96LM6: TEX37; NbExp=4; IntAct=EBI-740322, EBI-743976;
CC Q93062; Q92734: TFG; NbExp=3; IntAct=EBI-740322, EBI-357061;
CC Q93062; P35590: TIE1; NbExp=3; IntAct=EBI-740322, EBI-2256865;
CC Q93062; Q9GZM7-3: TINAGL1; NbExp=3; IntAct=EBI-740322, EBI-10303636;
CC Q93062; Q08117: TLE5; NbExp=3; IntAct=EBI-740322, EBI-717810;
CC Q93062; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-740322, EBI-10226570;
CC Q93062; Q6FIE9: TOLLIP; NbExp=3; IntAct=EBI-740322, EBI-10249783;
CC Q93062; Q9H0E2: TOLLIP; NbExp=4; IntAct=EBI-740322, EBI-74615;
CC Q93062; Q9H496: TOR1AIP2; NbExp=3; IntAct=EBI-740322, EBI-2510146;
CC Q93062; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-740322, EBI-7844656;
CC Q93062; O75896: TUSC2; NbExp=4; IntAct=EBI-740322, EBI-1052725;
CC Q93062; O95231: VENTX; NbExp=4; IntAct=EBI-740322, EBI-10191303;
CC Q93062; Q6RSH7: VHLL; NbExp=3; IntAct=EBI-740322, EBI-10254232;
CC Q93062; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-740322, EBI-2559305;
CC Q93062; Q96KV7: WDR90; NbExp=3; IntAct=EBI-740322, EBI-9478492;
CC Q93062; A0A0C4DGF1: ZBTB32; NbExp=5; IntAct=EBI-740322, EBI-10188476;
CC Q93062; Q96K80: ZC3H10; NbExp=4; IntAct=EBI-740322, EBI-742550;
CC Q93062; Q66K41: ZNF385C; NbExp=3; IntAct=EBI-740322, EBI-8651919;
CC Q93062; Q96MN9: ZNF488; NbExp=4; IntAct=EBI-740322, EBI-948288;
CC Q93062; Q9P0T4: ZNF581; NbExp=4; IntAct=EBI-740322, EBI-745520;
CC Q93062; B2R550; NbExp=3; IntAct=EBI-740322, EBI-10175488;
CC Q93062; Q96EJ4; NbExp=3; IntAct=EBI-740322, EBI-750454;
CC Q93062; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-740322, EBI-3957603;
CC Q93062-3; A0A0S2Z645: ABCF3; NbExp=3; IntAct=EBI-740343, EBI-16432404;
CC Q93062-3; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-740343, EBI-12224467;
CC Q93062-3; A0A0S2Z596: ANKMY1; NbExp=3; IntAct=EBI-740343, EBI-16433724;
CC Q93062-3; Q03989: ARID5A; NbExp=3; IntAct=EBI-740343, EBI-948603;
CC Q93062-3; P54253: ATXN1; NbExp=6; IntAct=EBI-740343, EBI-930964;
CC Q93062-3; P54252: ATXN3; NbExp=3; IntAct=EBI-740343, EBI-946046;
CC Q93062-3; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-740343, EBI-12809220;
CC Q93062-3; Q6NUJ2: C11orf87; NbExp=3; IntAct=EBI-740343, EBI-6660291;
CC Q93062-3; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-740343, EBI-11976299;
CC Q93062-3; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-740343, EBI-12155483;
CC Q93062-3; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-740343, EBI-1383687;
CC Q93062-3; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-740343, EBI-744556;
CC Q93062-3; Q16740: CLPP; NbExp=3; IntAct=EBI-740343, EBI-1056029;
CC Q93062-3; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-740343, EBI-741032;
CC Q93062-3; P27658: COL8A1; NbExp=3; IntAct=EBI-740343, EBI-747133;
CC Q93062-3; Q02930-3: CREB5; NbExp=3; IntAct=EBI-740343, EBI-10192698;
CC Q93062-3; Q15038: DAZAP2; NbExp=7; IntAct=EBI-740343, EBI-724310;
CC Q93062-3; A8MTA8-2: FAM166B; NbExp=6; IntAct=EBI-740343, EBI-12160437;
CC Q93062-3; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-740343, EBI-11978259;
CC Q93062-3; Q9BZS1: FOXP3; NbExp=3; IntAct=EBI-740343, EBI-983719;
CC Q93062-3; P23769: GATA2; NbExp=3; IntAct=EBI-740343, EBI-2806671;
CC Q93062-3; O75603: GCM2; NbExp=3; IntAct=EBI-740343, EBI-10188645;
CC Q93062-3; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-740343, EBI-7251368;
CC Q93062-3; P08631-2: HCK; NbExp=3; IntAct=EBI-740343, EBI-9834454;
CC Q93062-3; P42858: HTT; NbExp=3; IntAct=EBI-740343, EBI-466029;
CC Q93062-3; Q0VD86: INCA1; NbExp=3; IntAct=EBI-740343, EBI-6509505;
CC Q93062-3; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-740343, EBI-9478422;
CC Q93062-3; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-740343, EBI-1052037;
CC Q93062-3; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-740343, EBI-10210845;
CC Q93062-3; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-740343, EBI-10176396;
CC Q93062-3; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-740343, EBI-10241252;
CC Q93062-3; Q3LI76: KRTAP15-1; NbExp=6; IntAct=EBI-740343, EBI-11992140;
CC Q93062-3; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-740343, EBI-12811111;
CC Q93062-3; Q7Z4W3: KRTAP19-3; NbExp=3; IntAct=EBI-740343, EBI-12020132;
CC Q93062-3; Q3LI72: KRTAP19-5; NbExp=6; IntAct=EBI-740343, EBI-1048945;
CC Q93062-3; Q3SYF9: KRTAP19-7; NbExp=6; IntAct=EBI-740343, EBI-10241353;
CC Q93062-3; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-740343, EBI-3957672;
CC Q93062-3; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-740343, EBI-9996449;
CC Q93062-3; Q14847-2: LASP1; NbExp=8; IntAct=EBI-740343, EBI-9088686;
CC Q93062-3; P55197-2: MLLT10; NbExp=3; IntAct=EBI-740343, EBI-12853322;
CC Q93062-3; P28360: MSX1; NbExp=3; IntAct=EBI-740343, EBI-3919342;
CC Q93062-3; A7E2Y1-2: MYH7B; NbExp=3; IntAct=EBI-740343, EBI-12813813;
CC Q93062-3; P52952: NKX2-5; NbExp=3; IntAct=EBI-740343, EBI-936601;
CC Q93062-3; Q9HBE1-4: PATZ1; NbExp=6; IntAct=EBI-740343, EBI-11022007;
CC Q93062-3; O43189: PHF1; NbExp=3; IntAct=EBI-740343, EBI-530034;
CC Q93062-3; P78337: PITX1; NbExp=4; IntAct=EBI-740343, EBI-748265;
CC Q93062-3; Q99697-2: PITX2; NbExp=3; IntAct=EBI-740343, EBI-12138495;
CC Q93062-3; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-740343, EBI-769257;
CC Q93062-3; Q7Z3K3: POGZ; NbExp=5; IntAct=EBI-740343, EBI-1389308;
CC Q93062-3; Q12837: POU4F2; NbExp=3; IntAct=EBI-740343, EBI-17236143;
CC Q93062-3; P78424: POU6F2; NbExp=3; IntAct=EBI-740343, EBI-12029004;
CC Q93062-3; O43741: PRKAB2; NbExp=3; IntAct=EBI-740343, EBI-1053424;
CC Q93062-3; P86480: PRR20D; NbExp=3; IntAct=EBI-740343, EBI-12754095;
CC Q93062-3; P0CG20: PRR35; NbExp=3; IntAct=EBI-740343, EBI-11986293;
CC Q93062-3; A0A024R0L9: PSG11; NbExp=3; IntAct=EBI-740343, EBI-10696468;
CC Q93062-3; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-740343, EBI-948156;
CC Q93062-3; Q9NWB1-5: RBFOX1; NbExp=4; IntAct=EBI-740343, EBI-12123390;
CC Q93062-3; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-740343, EBI-11963050;
CC Q93062-3; Q9BX46-2: RBM24; NbExp=3; IntAct=EBI-740343, EBI-12224445;
CC Q93062-3; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-740343, EBI-11987469;
CC Q93062-3; Q96NR8: RDH12; NbExp=3; IntAct=EBI-740343, EBI-3916363;
CC Q93062-3; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-740343, EBI-372094;
CC Q93062-3; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-740343, EBI-366570;
CC Q93062-3; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-740343, EBI-6257312;
CC Q93062-3; Q6ZT89-3: SLC25A48; NbExp=3; IntAct=EBI-740343, EBI-12065614;
CC Q93062-3; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-740343, EBI-12061577;
CC Q93062-3; Q53HV7-2: SMUG1; NbExp=6; IntAct=EBI-740343, EBI-12275818;
CC Q93062-3; P09234: SNRPC; NbExp=3; IntAct=EBI-740343, EBI-766589;
CC Q93062-3; A0A0S2Z5K8: STRBP; NbExp=3; IntAct=EBI-740343, EBI-16433759;
CC Q93062-3; Q96SI9: STRBP; NbExp=3; IntAct=EBI-740343, EBI-740355;
CC Q93062-3; O95947: TBX6; NbExp=4; IntAct=EBI-740343, EBI-2824328;
CC Q93062-3; Q15560: TCEA2; NbExp=3; IntAct=EBI-740343, EBI-710310;
CC Q93062-3; Q96M29: TEKT5; NbExp=3; IntAct=EBI-740343, EBI-10239812;
CC Q93062-3; Q96LM6: TEX37; NbExp=3; IntAct=EBI-740343, EBI-743976;
CC Q93062-3; Q08117-2: TLE5; NbExp=5; IntAct=EBI-740343, EBI-11741437;
CC Q93062-3; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-740343, EBI-12038591;
CC Q93062-3; Q86WV8: TSC1; NbExp=3; IntAct=EBI-740343, EBI-12806590;
CC Q93062-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-740343, EBI-10241197;
CC Q93062-3; Q8N831: TSPYL6; NbExp=3; IntAct=EBI-740343, EBI-12023322;
CC Q93062-3; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-740343, EBI-2514383;
CC Q93062-3; Q14119: VEZF1; NbExp=3; IntAct=EBI-740343, EBI-11980193;
CC Q93062-3; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-740343, EBI-11957216;
CC Q93062-3; Q6RSH7: VHLL; NbExp=3; IntAct=EBI-740343, EBI-10254232;
CC Q93062-3; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-740343, EBI-2559305;
CC Q93062-3; A0A0C4DGF1: ZBTB32; NbExp=7; IntAct=EBI-740343, EBI-10188476;
CC Q93062-3; Q15915: ZIC1; NbExp=3; IntAct=EBI-740343, EBI-11963196;
CC Q93062-3; Q9P0T4: ZNF581; NbExp=8; IntAct=EBI-740343, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17099224}. Cytoplasm
CC {ECO:0000269|PubMed:17099224}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:26347403}. Note=Translocates into cytoplasmic
CC stress granules that probably correspond to P-bodies in response to
CC oxidative stress. {ECO:0000269|PubMed:26347403}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=Q93062-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q93062-2; Sequence=VSP_005813;
CC Name=C;
CC IsoId=Q93062-3; Sequence=VSP_005814;
CC Name=D;
CC IsoId=Q93062-4; Sequence=VSP_005815;
CC Name=E;
CC IsoId=Q93062-5; Sequence=VSP_005816;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, at various levels depending
CC on the isoform and the tissue.
CC -!- DOMAIN: The RRM domain is necessary for interaction with SMAD4. Both
CC the RRM domain and the C-terminus are required for TGFB1/Smad-mediated
CC transactivation activity.
CC -!- MISCELLANEOUS: [Isoform A]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
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DR EMBL; D84110; BAA12228.1; -; mRNA.
DR EMBL; D84107; BAA12225.1; -; mRNA.
DR EMBL; D84108; BAA12226.1; -; mRNA.
DR EMBL; D84109; BAA12227.1; -; mRNA.
DR EMBL; D84111; BAA12229.1; -; mRNA.
DR EMBL; CH471080; EAW63451.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63453.1; -; Genomic_DNA.
DR EMBL; BC003608; AAH03608.1; -; mRNA.
DR CCDS; CCDS34875.1; -. [Q93062-2]
DR CCDS; CCDS34876.1; -. [Q93062-3]
DR CCDS; CCDS6077.1; -. [Q93062-1]
DR PIR; JC6127; JC6127.
DR RefSeq; NP_001008710.1; NM_001008710.2. [Q93062-1]
DR RefSeq; NP_001008711.1; NM_001008711.2. [Q93062-2]
DR RefSeq; NP_001008712.1; NM_001008712.2. [Q93062-3]
DR RefSeq; NP_006858.1; NM_006867.3. [Q93062-1]
DR RefSeq; XP_016868475.1; XM_017012986.1. [Q93062-1]
DR PDB; 5CYJ; X-ray; 1.79 A; A/B=14-111.
DR PDB; 5DET; X-ray; 1.95 A; A/B=14-111.
DR PDBsum; 5CYJ; -.
DR PDBsum; 5DET; -.
DR AlphaFoldDB; Q93062; -.
DR BMRB; Q93062; -.
DR SMR; Q93062; -.
DR BioGRID; 116220; 360.
DR IntAct; Q93062; 281.
DR MINT; Q93062; -.
DR STRING; 9606.ENSP00000340176; -.
DR MoonDB; Q93062; Predicted.
DR GlyGen; Q93062; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q93062; -.
DR PhosphoSitePlus; Q93062; -.
DR BioMuta; RBPMS; -.
DR DMDM; 13124469; -.
DR EPD; Q93062; -.
DR jPOST; Q93062; -.
DR MassIVE; Q93062; -.
DR MaxQB; Q93062; -.
DR PaxDb; Q93062; -.
DR PeptideAtlas; Q93062; -.
DR PRIDE; Q93062; -.
DR ProteomicsDB; 75691; -. [Q93062-1]
DR ProteomicsDB; 75692; -. [Q93062-2]
DR ProteomicsDB; 75693; -. [Q93062-3]
DR ProteomicsDB; 75694; -. [Q93062-4]
DR ProteomicsDB; 75695; -. [Q93062-5]
DR Antibodypedia; 23209; 471 antibodies from 30 providers.
DR DNASU; 11030; -.
DR Ensembl; ENST00000287771.9; ENSP00000287771.5; ENSG00000157110.16. [Q93062-2]
DR Ensembl; ENST00000320203.8; ENSP00000318102.4; ENSG00000157110.16. [Q93062-1]
DR Ensembl; ENST00000339877.8; ENSP00000340176.4; ENSG00000157110.16. [Q93062-3]
DR Ensembl; ENST00000397323.9; ENSP00000380486.4; ENSG00000157110.16. [Q93062-1]
DR GeneID; 11030; -.
DR KEGG; hsa:11030; -.
DR MANE-Select; ENST00000397323.9; ENSP00000380486.4; NM_001008710.3; NP_001008710.1.
DR UCSC; uc003xib.5; human. [Q93062-1]
DR CTD; 11030; -.
DR DisGeNET; 11030; -.
DR GeneCards; RBPMS; -.
DR HGNC; HGNC:19097; RBPMS.
DR HPA; ENSG00000157110; Low tissue specificity.
DR MIM; 601558; gene.
DR neXtProt; NX_Q93062; -.
DR OpenTargets; ENSG00000157110; -.
DR PharmGKB; PA134985584; -.
DR VEuPathDB; HostDB:ENSG00000157110; -.
DR eggNOG; KOG1457; Eukaryota.
DR GeneTree; ENSGT00940000159617; -.
DR HOGENOM; CLU_099973_1_1_1; -.
DR InParanoid; Q93062; -.
DR OMA; FIAREPX; -.
DR OrthoDB; 1368991at2759; -.
DR PhylomeDB; Q93062; -.
DR TreeFam; TF351070; -.
DR PathwayCommons; Q93062; -.
DR SignaLink; Q93062; -.
DR SIGNOR; Q93062; -.
DR BioGRID-ORCS; 11030; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; RBPMS; human.
DR GeneWiki; RBPMS; -.
DR GenomeRNAi; 11030; -.
DR Pharos; Q93062; Tbio.
DR PRO; PR:Q93062; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q93062; protein.
DR Bgee; ENSG00000157110; Expressed in popliteal artery and 196 other tissues.
DR ExpressionAtlas; Q93062; baseline and differential.
DR Genevisible; Q93062; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
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 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..196
FT /note="RNA-binding protein with multiple splicing"
FT /id="PRO_0000081793"
FT DOMAIN 24..101
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 98..105
FT /note="Interaction with RNA"
FT /evidence="ECO:0000269|PubMed:26347403"
FT SITE 27
FT /note="Interaction with RNA"
FT /evidence="ECO:0000269|PubMed:26347403"
FT SITE 61
FT /note="Interaction with RNA"
FT /evidence="ECO:0000269|PubMed:26347403"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVB0"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 133..196
FT /note="YELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQMRWLPPSE
FT ATSQGWKSRQFC -> LGGANEHGERQ (in isoform D)"
FT /evidence="ECO:0000303|PubMed:8855282"
FT /id="VSP_005815"
FT VAR_SEQ 133..176
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:8855282"
FT /id="VSP_005816"
FT VAR_SEQ 177..196
FT /note="MRWLPPSEATSQGWKSRQFC -> LCEGQTVRRSHPLSAPSPDSASLAWFPV
FT (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8855282"
FT /id="VSP_005813"
FT VAR_SEQ 177..196
FT /note="MRWLPPSEATSQGWKSRQFC -> CFSPEAKPNTPVFCPLLQQIRFVSGNVF
FT VTYQPTADQQRELPC (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8855282"
FT /id="VSP_005814"
FT MUTAGEN 27
FT /note="F->A: Abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:26347403"
FT MUTAGEN 36..38
FT /note="KPR->EPE: Impairs dimerization and RNA binding."
FT /evidence="ECO:0000269|PubMed:26347403"
FT MUTAGEN 65
FT /note="F->A: Abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:26347403"
FT MUTAGEN 97
FT /note="E->A: Abolishes RNA binding; when associated with A-
FT 100."
FT /evidence="ECO:0000269|PubMed:26347403"
FT MUTAGEN 100
FT /note="K->A: Abolishes RNA binding; when associated with A-
FT 97."
FT /evidence="ECO:0000269|PubMed:26347403"
FT MUTAGEN 100
FT /note="K->E: Abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:26347403"
FT MUTAGEN 103..104
FT /note="TK->AA: Abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:26347403"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5CYJ"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:5CYJ"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5CYJ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5CYJ"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:5CYJ"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:5CYJ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5CYJ"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5CYJ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5CYJ"
SQ SEQUENCE 196 AA; 21802 MW; 05DD964E62F8F88C CRC64;
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY EGSLIKLTSK
QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK ANTKMAKNKL VGTPNPSTPL
PNTVPQFIAR EPYELTVPAL YPSSPEVWAP YPLYPAELAP ALPPPAFTYP ASLHAQMRWL
PPSEATSQGW KSRQFC
