RBM38_MOUSE
ID RBM38_MOUSE Reviewed; 237 AA.
AC Q62176; Q5U418; Q922Z2;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA-binding protein 38;
DE AltName: Full=RNA-binding motif protein 38;
DE AltName: Full=RNA-binding region-containing protein 1;
DE AltName: Full=ssDNA-binding protein SEB4;
GN Name=Rbm38; Synonyms=Rnpc1, Seb4, Seb4l;
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].
RA Ruehlmann A., Gupta A., Terhorst C.;
RT "A novel murine RRM-type protein and its human homolog.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Placenta, and Spleen;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [6]
RP FUNCTION, RNA-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=19817877; DOI=10.1111/j.1365-2443.2009.01347.x;
RA Miyamoto S., Hidaka K., Jin D., Morisaki T.;
RT "RNA-binding proteins Rbm38 and Rbm24 regulate myogenic differentiation via
RT p21-dependent and -independent regulatory pathways.";
RL Genes Cells 14:1241-1252(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: RNA-binding protein that specifically bind the 3'-UTR of
CC CDKN1A transcripts, leading to maintain the stability of CDKN1A
CC transcripts, thereby acting as a mediator of the p53/TP53 family to
CC regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor
CC transcriptionally regulated by the p53/TP53 family to induce cell cycle
CC arrest. Has the ability to induce cell cycle arrest in G1 and maintain
CC the stability of CDKN1A transcripts induced by p53/TP53. Also acts as a
CC mRNA splicing factor. Specifically regulates the expression of FGFR2-
CC IIIb, an epithelial cell-specific isoform of FGFR2 (By similarity).
CC Plays a role in myogenic differentiation. {ECO:0000250,
CC ECO:0000269|PubMed:19817877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle tissues.
CC {ECO:0000269|PubMed:19817877}.
CC -!- SIMILARITY: Belongs to the RBM38 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-22 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X75316; CAA53065.1; -; mRNA.
DR EMBL; AK146026; BAE26841.1; -; mRNA.
DR EMBL; AK162141; BAE36749.1; -; mRNA.
DR EMBL; AK172625; BAE43103.1; -; mRNA.
DR EMBL; AL928599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06620.1; -; Genomic_DNA.
DR EMBL; BC085307; AAH85307.1; -; mRNA.
DR CCDS; CCDS17139.1; -.
DR PIR; S38384; S38384.
DR RefSeq; NP_062420.2; NM_019547.2.
DR AlphaFoldDB; Q62176; -.
DR SMR; Q62176; -.
DR BioGRID; 207830; 33.
DR STRING; 10090.ENSMUSP00000133816; -.
DR iPTMnet; Q62176; -.
DR PhosphoSitePlus; Q62176; -.
DR EPD; Q62176; -.
DR MaxQB; Q62176; -.
DR PaxDb; Q62176; -.
DR PRIDE; Q62176; -.
DR ProteomicsDB; 255039; -.
DR Antibodypedia; 28985; 137 antibodies from 21 providers.
DR DNASU; 56190; -.
DR Ensembl; ENSMUST00000029014; ENSMUSP00000029014; ENSMUSG00000027510.
DR Ensembl; ENSMUST00000173393; ENSMUSP00000133816; ENSMUSG00000027510.
DR GeneID; 56190; -.
DR KEGG; mmu:56190; -.
DR UCSC; uc008odh.1; mouse.
DR CTD; 55544; -.
DR MGI; MGI:1889294; Rbm38.
DR VEuPathDB; HostDB:ENSMUSG00000027510; -.
DR eggNOG; KOG0149; Eukaryota.
DR GeneTree; ENSGT00940000158489; -.
DR HOGENOM; CLU_065652_0_1_1; -.
DR InParanoid; Q62176; -.
DR OMA; HLQPERM; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; Q62176; -.
DR TreeFam; TF314235; -.
DR BioGRID-ORCS; 56190; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rbm38; mouse.
DR PRO; PR:Q62176; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q62176; protein.
DR Bgee; ENSMUSG00000027510; Expressed in hindlimb stylopod muscle and 174 other tissues.
DR ExpressionAtlas; Q62176; baseline and differential.
DR Genevisible; Q62176; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IMP:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:MGI.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0010830; P:regulation of myotube differentiation; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Cell cycle; Cytoplasm; Differentiation; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..237
FT /note="RNA-binding protein 38"
FT /id="PRO_0000081813"
FT DOMAIN 32..109
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 26
FT /note="Q -> R (in Ref. 1; CAA53065)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="A -> G (in Ref. 1; CAA53065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 25364 MW; 73D7DF81A56A22EE CRC64;
MLLQPACSPS VFPRPSAAPS AMHGSQKDTT FTKIFVGGLP YHTTDASLRK YFEGFGDIEE
AVVITDRQTG KSRGYGFVTM ADRAAADRAC KDPNPIIDGR KANVNLAYLG AKPRSLQTGF
AVGVQQLHPT LIQRTYGLTP HYIYPPAIVQ PSVVIPATPV PSLSSPYLEY TPASPAYAQY
PPATYDQYPY AASPAAATSF VGYGYPAAVP QALSAAAPAG TTFVQYQAPQ LQPDRMQ
