RMXL1_HUMAN
ID RMXL1_HUMAN Reviewed; 390 AA.
AC Q96E39;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=RNA binding motif protein, X-linked-like-1;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G-like 1;
GN Name=RBMXL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP RETROGENE.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: RNA-binding protein which may be involved in pre-mRNA
CC splicing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: According to some authors, RBMXL1 is a RBMX retrogene on
CC chromosome X which is likely to be functional.
CC {ECO:0000305|PubMed:16201836}.
CC -!- CAUTION: The first non-coding exon of RBMXL1 is in common with that of
CC CCBL2. {ECO:0000305}.
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DR EMBL; AL832554; CAI46148.1; -; mRNA.
DR EMBL; AL139416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73155.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73156.1; -; Genomic_DNA.
DR EMBL; BC012942; AAH12942.1; -; mRNA.
DR CCDS; CCDS716.1; -.
DR RefSeq; NP_001156008.1; NM_001162536.2.
DR RefSeq; NP_062556.2; NM_019610.5.
DR AlphaFoldDB; Q96E39; -.
DR SMR; Q96E39; -.
DR BioGRID; 138936; 150.
DR IntAct; Q96E39; 33.
DR MINT; Q96E39; -.
DR STRING; 9606.ENSP00000446099; -.
DR GlyGen; Q96E39; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96E39; -.
DR PhosphoSitePlus; Q96E39; -.
DR SwissPalm; Q96E39; -.
DR BioMuta; RBMXL1; -.
DR DMDM; 74760797; -.
DR EPD; Q96E39; -.
DR jPOST; Q96E39; -.
DR MassIVE; Q96E39; -.
DR MaxQB; Q96E39; -.
DR PaxDb; Q96E39; -.
DR PeptideAtlas; Q96E39; -.
DR PRIDE; Q96E39; -.
DR ProteomicsDB; 76370; -.
DR Antibodypedia; 67132; 76 antibodies from 12 providers.
DR DNASU; 494115; -.
DR Ensembl; ENST00000321792.5; ENSP00000318415.5; ENSG00000213516.10.
DR Ensembl; ENST00000399794.6; ENSP00000446099.1; ENSG00000213516.10.
DR Ensembl; ENST00000652648.1; ENSP00000498248.1; ENSG00000213516.10.
DR GeneID; 494115; -.
DR KEGG; hsa:494115; -.
DR MANE-Select; ENST00000652648.1; ENSP00000498248.1; NM_001162536.3; NP_001156008.1.
DR UCSC; uc001dms.4; human.
DR CTD; 494115; -.
DR DisGeNET; 494115; -.
DR GeneCards; RBMXL1; -.
DR HGNC; HGNC:25073; RBMXL1.
DR HPA; ENSG00000213516; Low tissue specificity.
DR neXtProt; NX_Q96E39; -.
DR OpenTargets; ENSG00000213516; -.
DR PharmGKB; PA165752300; -.
DR VEuPathDB; HostDB:ENSG00000213516; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000153425; -.
DR HOGENOM; CLU_042286_0_0_1; -.
DR InParanoid; Q96E39; -.
DR OMA; PYESHAY; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; Q96E39; -.
DR TreeFam; TF331833; -.
DR PathwayCommons; Q96E39; -.
DR SignaLink; Q96E39; -.
DR BioGRID-ORCS; 494115; 586 hits in 999 CRISPR screens.
DR GenomeRNAi; 494115; -.
DR Pharos; Q96E39; Tdark.
DR PRO; PR:Q96E39; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96E39; protein.
DR Bgee; ENSG00000213516; Expressed in cauda epididymis and 181 other tissues.
DR ExpressionAtlas; Q96E39; baseline and differential.
DR Genevisible; Q96E39; HS.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..390
FT /note="RNA binding motif protein, X-linked-like-1"
FT /id="PRO_0000408005"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 62..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
SQ SEQUENCE 390 AA; 42142 MW; E8D74676C3AE6420 CRC64;
MVEADRPGKL FIGGLNTETN EKALETVFGK YGRIVEVLLI KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE RGRHGPPPPP RSRGPPRGFG AGRGGSGGTR
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP SPKRSAPSGL VRSSSGMGGR
APLSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY GDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPLTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSCDR VGRQERGLPP SVERGYPSSR
DSYSSSSRGA PRGAGPGGSR SDRGGGRSRY
