RBM25_MOUSE
ID RBM25_MOUSE Reviewed; 838 AA.
AC B2RY56; Q3TPH6; Q3U976; Q3UQU7; Q6NWW2; Q8BVT8; Q91XE6; Q9CT27; Q9CT49;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=RNA-binding protein 25;
DE AltName: Full=RNA-binding motif protein 25;
GN Name=Rbm25;
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 MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryonic eye, Embryonic spinal ganglion, Macrophage, and
RC Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Embryonic germ cell;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; SER-672 AND SER-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; SER-678 AND SER-698, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: RNA-binding protein that acts as a regulator of alternative
CC pre-mRNA splicing. Involved in apoptotic cell death through the
CC regulation of the apoptotic factor BCL2L1 isoform expression. Modulates
CC the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1
CC isoform L mRNA expression. When overexpressed, stimulates proapoptotic
CC BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its
CC depletion caused the accumulation of antiapoptotic BCL2L1 isoform L.
CC Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA
CC sequence. Its association with LUC7L3 promotes U1 snRNP binding to a
CC weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic
CC splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of
CC the BCL2L1 pre-mRNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LUC7L3 and SRRM1 (By similarity). Specifically
CC associates with functional splicing complexes, including Sm proteins
CC and U1, U2, U4, U5 and U6 snRNAs (By similarity). Associates with exon
CC junction complex (EJC) proteins, including APEX1, DDX39B, NCBP1, RBM8A
CC and RNPS1. Interaction with NCBP1 is RNA-dependent (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00627}. Cytoplasm {ECO:0000250}. Note=Colocalizes
CC predominantly, with SFRS2 and LUC7L3 splicing factors, in nuclear
CC speckles. Cytoplasmic localization is faint (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The PWI domain binds nucleic acids with significant help from
CC its N-terminal flanking basic region. It has an equal preference for
CC binding to single- or double-stranded species, and it contributes to
CC RBM25 role in modulation of alternative splicing, maybe by mediating
CC RNA-dependent association with LUC7L3 (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10792.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH10792.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAH66150.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH67400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI58105.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAB27451.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE24941.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AK011184; BAB27451.2; ALT_INIT; mRNA.
DR EMBL; AK011403; BAB27595.3; -; mRNA.
DR EMBL; AK076553; BAC36389.1; -; mRNA.
DR EMBL; AK142132; BAE24941.1; ALT_INIT; mRNA.
DR EMBL; AK151910; BAE30791.1; -; mRNA.
DR EMBL; AK164367; BAE37760.1; -; mRNA.
DR EMBL; BC158104; AAI58105.1; ALT_SEQ; mRNA.
DR EMBL; BC010792; AAH10792.1; ALT_SEQ; mRNA.
DR EMBL; BC066150; AAH66150.1; ALT_INIT; mRNA.
DR EMBL; BC067400; AAH67400.1; ALT_INIT; mRNA.
DR CCDS; CCDS49107.1; -.
DR RefSeq; NP_081625.3; NM_027349.3.
DR RefSeq; XP_006516230.1; XM_006516167.3.
DR RefSeq; XP_006516231.1; XM_006516168.3.
DR RefSeq; XP_006516232.1; XM_006516169.3.
DR RefSeq; XP_017170651.1; XM_017315162.1.
DR AlphaFoldDB; B2RY56; -.
DR SMR; B2RY56; -.
DR BioGRID; 211893; 19.
DR IntAct; B2RY56; 3.
DR MINT; B2RY56; -.
DR STRING; 10090.ENSMUSP00000048470; -.
DR iPTMnet; B2RY56; -.
DR PhosphoSitePlus; B2RY56; -.
DR EPD; B2RY56; -.
DR jPOST; B2RY56; -.
DR MaxQB; B2RY56; -.
DR PaxDb; B2RY56; -.
DR PeptideAtlas; B2RY56; -.
DR PRIDE; B2RY56; -.
DR ProteomicsDB; 253181; -.
DR Antibodypedia; 158; 71 antibodies from 17 providers.
DR DNASU; 67039; -.
DR Ensembl; ENSMUST00000048155; ENSMUSP00000048470; ENSMUSG00000010608.
DR GeneID; 67039; -.
DR KEGG; mmu:67039; -.
DR UCSC; uc007odj.1; mouse.
DR CTD; 58517; -.
DR MGI; MGI:1914289; Rbm25.
DR VEuPathDB; HostDB:ENSMUSG00000010608; -.
DR eggNOG; KOG2253; Eukaryota.
DR GeneTree; ENSGT00730000111019; -.
DR HOGENOM; CLU_009855_0_0_1; -.
DR InParanoid; B2RY56; -.
DR OMA; DYKEQEC; -.
DR OrthoDB; 885027at2759; -.
DR PhylomeDB; B2RY56; -.
DR TreeFam; TF320185; -.
DR BioGRID-ORCS; 67039; 31 hits in 73 CRISPR screens.
DR ChiTaRS; Rbm25; mouse.
DR PRO; PR:B2RY56; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; B2RY56; protein.
DR Bgee; ENSMUSG00000010608; Expressed in undifferentiated genital tubercle and 257 other tissues.
DR ExpressionAtlas; B2RY56; baseline and differential.
DR Genevisible; B2RY56; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12446; RRM_RBM25; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034268; RBM25_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00311; PWI; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51025; PWI; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cytoplasm; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..838
FT /note="RNA-binding protein 25"
FT /id="PRO_0000368187"
FT DOMAIN 87..164
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 745..838
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..639
FT /note="Necessary for nuclear speckle localization"
FT /evidence="ECO:0000250"
FT REGION 493..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..601
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 683
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 692
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CROSSLNK 717
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49756"
FT CONFLICT 487
FT /note="E -> G (in Ref. 1; BAB27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="S -> F (in Ref. 2; AAH66150/AAH67400)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="A -> D (in Ref. 1; BAB27451)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="K -> R (in Ref. 1; BAB27451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 99552 MW; FD5D178EBDF12E23 CRC64;
MSFPPHLNRP PMGIPALPPG IPPPQFPGFP PPVPPGTPMI PVPMSIMAPA PTVLVPTVSM
VGKHLGARKD HPGLKLKEND ENCGPTTTVF VGNISEKASD MLIRQLLAKC GLVLSWKRVQ
GASGKLQAFG FCEYKEPEST LRALRLLHDL QIGEKKLLVK VDAKTKAQLD EWKAKKKANG
NARPETVTND DEEALDEETK RRDQMIKGAI EVLIREYSSE LNAPSQESDS HPRKKKKEKK
EDIFRRFPVA PLIPYPLITK EDINAIEMEE DKRDLISREI SKFRDTHKKL EEEKGKKEKE
RQEIEKERRE RERERERERE RRERERERER EREREKEKER ERERERDRDR DRTKERDRDR
ERDRDRDRER SSDRNKDRSR SREKSRDRER ERERERERER ERERERERER ERERERERER
EKDKKRDREE DEEDAYERRK LERKLREKEA AYQERLKNWE IRERKKTREY EKEAEREEER
RREMAKEAKR LKEFLEDYDD DRDDPKYYRG SALQKRLRDR EKEMEADERD RKREKEELEE
IRQRLLAEGH PDPDAELQRM EQEAERRRQP QIKQEPESEE EEEEKQEKEE KREEPVEEEE
EPEQKPCLKP TLRPISSAPS VSSASGNATP NTPGDESPCG IIIPHENSPD QQQPEEHRPK
IGLSLKLGAS NSPGQPNSVK RKKLPVDSVF NKFEDEDSDD VPRKRKLVPL DYGEDDKNAT
KGTVNTEEKR KHIKSLIEKI PTAKPELFAY PLDWSIVDSI LMERRIRPWI NKKIIEYIGE
EEATLVDFVC SKVMAHSSPQ SILDDVAMVL DEEAEVFIVK MWRLLIYETE AKKIGLVK
