RBM11_MOUSE
ID RBM11_MOUSE Reviewed; 238 AA.
AC Q80YT9; D3Z0X9; Q8BYK1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Splicing regulator RBM11;
DE AltName: Full=RNA-binding motif protein 11;
GN Name=Rbm11;
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 [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 [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-238.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [5]
RP TISSUE SPECIFICITY, RNA-BINDING, AND DEVELOPMENTAL STAGE.
RX PubMed=21984414; DOI=10.1093/nar/gkr819;
RA Pedrotti S., Busa R., Compagnucci C., Sette C.;
RT "The RNA recognition motif protein RBM11 is a novel tissue-specific
RT splicing regulator.";
RL Nucleic Acids Res. 40:1021-1032(2012).
CC -!- FUNCTION: Tissue-specific splicing factor with potential implication in
CC the regulation of alternative splicing during neuron and germ cell
CC differentiation. Antagonizes SRSF1-mediated BCL-X splicing. May affect
CC the choice of alternative 5' splice sites by binding to specific
CC sequences in exons and antagonizing the SR protein SRSF1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus
CC speckle {ECO:0000250}. Note=Enriched in SRSF2-containing splicing
CC speckles; shuttles between nucleoplasm and speckles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Selectively expressed in brain, cerebellum and
CC testis, and to a lower extent in kidney. {ECO:0000269|PubMed:21984414}.
CC -!- DEVELOPMENTAL STAGE: Peaks perinatally in brain and cerebellum, and at
CC puberty in testis, in concomitance with differentiation events
CC occurring in neurons and germ cells. {ECO:0000269|PubMed:21984414}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK98269.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC166995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK98269.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC050779; AAH50779.1; -; mRNA.
DR EMBL; AK039297; BAC30309.1; -; mRNA.
DR CCDS; CCDS37377.1; -.
DR RefSeq; NP_938044.1; NM_198302.2.
DR AlphaFoldDB; Q80YT9; -.
DR SMR; Q80YT9; -.
DR STRING; 10090.ENSMUSP00000109887; -.
DR PhosphoSitePlus; Q80YT9; -.
DR PaxDb; Q80YT9; -.
DR PRIDE; Q80YT9; -.
DR ProteomicsDB; 254997; -.
DR Antibodypedia; 22166; 138 antibodies from 21 providers.
DR DNASU; 224344; -.
DR Ensembl; ENSMUST00000046378; ENSMUSP00000038956; ENSMUSG00000032940.
DR Ensembl; ENSMUST00000114253; ENSMUSP00000109891; ENSMUSG00000032940.
DR GeneID; 224344; -.
DR KEGG; mmu:224344; -.
DR UCSC; uc007zro.1; mouse.
DR CTD; 54033; -.
DR MGI; MGI:2447622; Rbm11.
DR VEuPathDB; HostDB:ENSMUSG00000032940; -.
DR eggNOG; ENOG502RYIT; Eukaryota.
DR GeneTree; ENSGT00870000136493; -.
DR HOGENOM; CLU_1165534_0_0_1; -.
DR InParanoid; Q80YT9; -.
DR OMA; MQFSPIN; -.
DR OrthoDB; 1298240at2759; -.
DR BioGRID-ORCS; 224344; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Rbm11; mouse.
DR PRO; PR:Q80YT9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q80YT9; protein.
DR Bgee; ENSMUSG00000032940; Expressed in lumbar dorsal root ganglion and 73 other tissues.
DR ExpressionAtlas; Q80YT9; baseline and differential.
DR Genevisible; Q80YT9; MM.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12593; RRM_RBM11; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034501; RBM11_RRM.
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 Developmental protein; Differentiation; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..238
FT /note="Splicing regulator RBM11"
FT /id="PRO_0000416116"
FT DOMAIN 10..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 172..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..237
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 197..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 26945 MW; 70A402DC4194E194 CRC64;
MFPAQEEADR TVFVGNLEAR VREEILYELF LQAGPLTKVT LCKDRDGKPK SFGFVCFKHP
ESVSYAIALL NGIRLYGRPI NVQYRFGSSR SSEPANQSFE SCAKINSHSF RNDEMAGRPS
FPVPFFPITS AALPQEYFFF QKMPWYAHSP VLQPPFCEMP APLPNSVPGS CALNHSPGPE
AGPSSYEWTH QPPSDPDLYP RNKRKRQRPD SDSDSSSEDK RGNEGSQKCR KCKKKKRY
