RBMX2_MOUSE
ID RBMX2_MOUSE Reviewed; 326 AA.
AC Q8R0F5; A2AF74; Q3TI42;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RNA-binding motif protein, X-linked 2;
GN Name=Rbmx2;
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;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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: Involved in pre-mRNA splicing as component of the activated
CC spliceosome. {ECO:0000250|UniProtKB:Q9Y388}.
CC -!- SUBUNIT: Part of the activated spliceosome B/catalytic step 1
CC spliceosome, one of the forms of the spliceosome which has a well-
CC formed active site but still cannot catalyze the branching reaction and
CC is composed of at least 52 proteins, the U2, U5 and U6 snRNAs and the
CC pre-mRNA. {ECO:0000250|UniProtKB:Q9Y388}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y388}.
CC -!- SIMILARITY: Belongs to the IST3 family. {ECO:0000305}.
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DR EMBL; AK076115; BAC36195.1; -; mRNA.
DR EMBL; AK168018; BAE40004.1; -; mRNA.
DR EMBL; AL672042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026976; AAH26976.1; -; mRNA.
DR CCDS; CCDS30114.1; -.
DR RefSeq; NP_775552.1; NM_173376.3.
DR AlphaFoldDB; Q8R0F5; -.
DR SMR; Q8R0F5; -.
DR BioGRID; 229035; 2.
DR IntAct; Q8R0F5; 2.
DR STRING; 10090.ENSMUSP00000033433; -.
DR iPTMnet; Q8R0F5; -.
DR PhosphoSitePlus; Q8R0F5; -.
DR EPD; Q8R0F5; -.
DR MaxQB; Q8R0F5; -.
DR PaxDb; Q8R0F5; -.
DR PeptideAtlas; Q8R0F5; -.
DR PRIDE; Q8R0F5; -.
DR ProteomicsDB; 300273; -.
DR Antibodypedia; 6828; 122 antibodies from 22 providers.
DR DNASU; 209003; -.
DR Ensembl; ENSMUST00000033433; ENSMUSP00000033433; ENSMUSG00000031107.
DR GeneID; 209003; -.
DR KEGG; mmu:209003; -.
DR UCSC; uc009tct.1; mouse.
DR CTD; 51634; -.
DR MGI; MGI:1919414; Rbmx2.
DR VEuPathDB; HostDB:ENSMUSG00000031107; -.
DR eggNOG; KOG0126; Eukaryota.
DR GeneTree; ENSGT00890000139472; -.
DR HOGENOM; CLU_045495_1_0_1; -.
DR InParanoid; Q8R0F5; -.
DR OMA; ISPEGSW; -.
DR OrthoDB; 1484811at2759; -.
DR PhylomeDB; Q8R0F5; -.
DR TreeFam; TF313727; -.
DR BioGRID-ORCS; 209003; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Rbmx2; mouse.
DR PRO; PR:Q8R0F5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8R0F5; protein.
DR Bgee; ENSMUSG00000031107; Expressed in morula and 64 other tissues.
DR Genevisible; Q8R0F5; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR CDD; cd12411; RRM_ist3_like; 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; IPR000504; RRM_dom.
DR InterPro; IPR045844; RRM_Ist3-like.
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 Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spliceosome; Ubl conjugation.
FT CHAIN 1..326
FT /note="RNA-binding motif protein, X-linked 2"
FT /id="PRO_0000081898"
FT DOMAIN 36..114
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 117..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..313
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y388"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y388"
SQ SEQUENCE 326 AA; 37536 MW; EC702B0E79404CD5 CRC64;
MNPLTKVKLI NELNEREVQL GVAEKVSWHS EYKHSAWIFV GGLPYELTEG DIICVFSQYG
EIVNINLVRD KKTGKSKGFC FLCYEDQRST VLAVDNFNGI KIKGRTIRVD HVSNYRAPQE
SEDVDDVTRE LQEKGCGVKT PPSSPPEVSE DEDAKLTKKH KKDKKEKKKR KKEKTEGQAQ
AEQPSCSRSA TVKEKKDERA SRKHSSKTSE RAQKSEHRES KKSHSGSPDG RSSYHARAED
PECKARKEKP KHEHKSASRR EAEEKSRERE RGRSSGTHSG RHRGHSDGRS HRSRSRSRSP
DKSHRHKKYR HSRERDSYHG SDRRHH
