RBPMS_MOUSE
ID RBPMS_MOUSE Reviewed; 197 AA.
AC Q9WVB0; Q78HG1; Q9CPU5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 146.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10096065; DOI=10.1016/s0925-4773(98)00195-6;
RA Gerber W.V., Yatskievych T.A., Antin P.B., Correia K.M., Conlon R.A.,
RA Krieg P.A.;
RT "The RNA-binding protein gene, hermes, is expressed at high levels in the
RT developing heart.";
RL Mech. Dev. 80:77-86(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Binds to poly(A) RNA.
CC {ECO:0000250|UniProtKB:Q93062}.
CC -!- SUBUNIT: Homodimer; each protein chain binds one RNA molecule via the
CC external surface of the homodimer. Interacts with SMAD2, SMAD3 and
CC SMAD4; the interactions are direct. {ECO:0000250|UniProtKB:Q93062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93062}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q93062}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q93062}. Note=Translocates into cytoplasmic
CC stress granules that probably correspond to P-bodies in response to
CC oxidative stress. {ECO:0000250|UniProtKB:Q93062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVB0-2; Sequence=VSP_045747;
CC -!- TISSUE SPECIFICITY: mRNA expressed in developing heart, with
CC significantly higher expression in the atria relative to the
CC ventricles. {ECO:0000269|PubMed:10096065}.
CC -!- DEVELOPMENTAL STAGE: mRNA already detected at 9.5 dpc.
CC {ECO:0000269|PubMed:10096065}.
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 (By similarity). {ECO:0000250}.
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DR EMBL; AF148511; AAD39515.1; -; mRNA.
DR EMBL; AK012265; BAB28128.1; -; mRNA.
DR EMBL; AK012586; BAB28336.1; -; mRNA.
DR EMBL; AK041118; BAC30827.1; -; mRNA.
DR EMBL; AC123616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030397; AAH30397.1; -; mRNA.
DR CCDS; CCDS40317.1; -. [Q9WVB0-1]
DR CCDS; CCDS40318.1; -. [Q9WVB0-2]
DR RefSeq; NP_001036139.1; NM_001042674.2. [Q9WVB0-1]
DR RefSeq; NP_001036140.1; NM_001042675.2. [Q9WVB0-2]
DR RefSeq; NP_062707.1; NM_019733.3. [Q9WVB0-1]
DR AlphaFoldDB; Q9WVB0; -.
DR BMRB; Q9WVB0; -.
DR SMR; Q9WVB0; -.
DR BioGRID; 202831; 3.
DR STRING; 10090.ENSMUSP00000033995; -.
DR iPTMnet; Q9WVB0; -.
DR PhosphoSitePlus; Q9WVB0; -.
DR MaxQB; Q9WVB0; -.
DR PaxDb; Q9WVB0; -.
DR PRIDE; Q9WVB0; -.
DR ProteomicsDB; 255160; -. [Q9WVB0-1]
DR ProteomicsDB; 255161; -. [Q9WVB0-2]
DR Antibodypedia; 23209; 471 antibodies from 30 providers.
DR DNASU; 19663; -.
DR Ensembl; ENSMUST00000033995; ENSMUSP00000033995; ENSMUSG00000031586. [Q9WVB0-2]
DR Ensembl; ENSMUST00000053251; ENSMUSP00000055813; ENSMUSG00000031586. [Q9WVB0-1]
DR Ensembl; ENSMUST00000182987; ENSMUSP00000138483; ENSMUSG00000031586. [Q9WVB0-1]
DR Ensembl; ENSMUST00000191473; ENSMUSP00000140387; ENSMUSG00000031586. [Q9WVB0-1]
DR GeneID; 19663; -.
DR KEGG; mmu:19663; -.
DR UCSC; uc009lkk.2; mouse. [Q9WVB0-1]
DR UCSC; uc009lkn.3; mouse. [Q9WVB0-2]
DR CTD; 11030; -.
DR MGI; MGI:1334446; Rbpms.
DR VEuPathDB; HostDB:ENSMUSG00000031586; -.
DR eggNOG; KOG1457; Eukaryota.
DR GeneTree; ENSGT00940000159617; -.
DR InParanoid; Q9WVB0; -.
DR OMA; FIAREPX; -.
DR OrthoDB; 1368991at2759; -.
DR TreeFam; TF351070; -.
DR BioGRID-ORCS; 19663; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Rbpms; mouse.
DR PRO; PR:Q9WVB0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9WVB0; protein.
DR Bgee; ENSMUSG00000031586; Expressed in ascending aorta and 242 other tissues.
DR ExpressionAtlas; Q9WVB0; baseline and differential.
DR Genevisible; Q9WVB0; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
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 Acetylation; Activator; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..197
FT /note="RNA-binding protein with multiple splicing"
FT /id="PRO_0000081794"
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:0000250|UniProtKB:Q93062"
FT SITE 27
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:Q93062"
FT SITE 61
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:Q93062"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q93062"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q93062"
FT VAR_SEQ 178..197
FT /note="MRWIPPSEATSQGWKSRQFC -> CFSPEAKPNTPVFCPLLQQIRFVSGNVF
FT VTYQPTADQQRELPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_045747"
FT CONFLICT 96
FT /note="L -> I (in Ref. 1; AAD39515)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..128
FT /note="QFI -> HSV (in Ref. 1; AAD39515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 21816 MW; 03457D84F803CC78 CRC64;
MNGGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY EGSLIKLTSK
QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK ANTKMAKNKL VGTPNPSTPL
PNTVPQFIAR EPYELTVPAL YPSSPEVWAP YPLYPAELAP ALPPPAAFTY PASLHAQMRW
IPPSEATSQG WKSRQFC
