RMXL1_MOUSE
ID RMXL1_MOUSE Reviewed; 388 AA.
AC Q91VM5; O35479;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=RNA binding motif protein, X-linked-like-1;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G-like 1;
DE AltName: Full=RNA binding motif protein, X chromosome retrogene;
GN Name=Rbmxl1; Synonyms=Rbmxrt;
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].
RX PubMed=9457683; DOI=10.1007/s003359900712;
RA Delbridge M.L., Ma K., Subbarao M.N., Cooke H.J., Bhasin S., Graves J.A.M.;
RT "Evolution of mammalian HNRPG and its relationship with the putative
RT azoospermia factor RBM.";
RL Mamm. Genome 9:168-170(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 MRNA].
RC STRAIN=129, and C57BL/6J; TISSUE=Brain, 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).
CC -!- FUNCTION: RNA-binding protein which may be involved in pre-mRNA
CC splicing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AF031568; AAB86639.1; -; mRNA.
DR EMBL; AK041927; BAC31099.1; -; mRNA.
DR EMBL; BC011441; AAH11441.1; -; mRNA.
DR EMBL; BC089350; AAH89350.1; -; mRNA.
DR CCDS; CCDS22430.1; -.
DR RefSeq; NP_001239018.1; NM_001252089.1.
DR RefSeq; NP_033059.2; NM_009033.2.
DR RefSeq; XP_006530838.1; XM_006530775.2.
DR RefSeq; XP_006530839.1; XM_006530776.2.
DR AlphaFoldDB; Q91VM5; -.
DR SMR; Q91VM5; -.
DR BioGRID; 202825; 11.
DR IntAct; Q91VM5; 6.
DR MINT; Q91VM5; -.
DR STRING; 10090.ENSMUSP00000048153; -.
DR iPTMnet; Q91VM5; -.
DR PhosphoSitePlus; Q91VM5; -.
DR EPD; Q91VM5; -.
DR jPOST; Q91VM5; -.
DR MaxQB; Q91VM5; -.
DR PaxDb; Q91VM5; -.
DR PeptideAtlas; Q91VM5; -.
DR PRIDE; Q91VM5; -.
DR ProteomicsDB; 300524; -.
DR DNASU; 19656; -.
DR Ensembl; ENSMUST00000049245; ENSMUSP00000048153; ENSMUSG00000037070.
DR Ensembl; ENSMUST00000211719; ENSMUSP00000147384; ENSMUSG00000037070.
DR GeneID; 19656; -.
DR KEGG; mmu:19656; -.
DR UCSC; uc009mhz.1; mouse.
DR CTD; 494115; -.
DR MGI; MGI:1343045; Rbmxl1.
DR VEuPathDB; HostDB:ENSMUSG00000037070; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000153425; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; Q91VM5; -.
DR OMA; DAQQWNG; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; Q91VM5; -.
DR TreeFam; TF331833; -.
DR BioGRID-ORCS; 19656; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Rbmxl1; mouse.
DR PRO; PR:Q91VM5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91VM5; protein.
DR Bgee; ENSMUSG00000037070; Expressed in ventricular zone and 74 other tissues.
DR Genevisible; Q91VM5; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044530; C:supraspliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; 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; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..388
FT /note="RNA binding motif protein, X-linked-like-1"
FT /id="PRO_0000408006"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 59..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E39"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96E39"
FT CONFLICT 38
FT /note="L -> I (in Ref. 1; AAB86639)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="F -> L (in Ref. 1; AAB86639)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="S -> F (in Ref. 1; AAB86639)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="A -> T (in Ref. 1; AAB86639)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="S -> C (in Ref. 1; AAB86639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42162 MW; F4532F545E431A59 CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGSGGTRGPP
SRGGYMDDGG YSMNFNMSSS RGPLPVKRGP PPRSGGPPPK RSTPSGPVRS SSGMGGRTPV
SRGRDSYGGP PRREPLPSRR DVYLSPRDDG YSTKDSYSSR DYPSSRDTRD YAPPPRDYTY
RDYSHSSSRD DYPSRGYGDR DGYGRDRDYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS
YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM ERGYPPPRDS
YSSSSRGAPR GGGRGGSRSD RGGGRSRY
