RBMX_MACFA
ID RBMX_MACFA Reviewed; 391 AA.
AC Q4R7F0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=RNA-binding motif protein, X chromosome;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
DE Short=hnRNP G;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
GN Name=RBMX; Synonyms=HNRPG, RBMXP1; ORFNames=QtsA-15489;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that plays several role in the regulation
CC of pre- and post-transcriptional processes. Implicated in tissue-
CC specific regulation of gene transcription and alternative splicing of
CC several pre-mRNAs. Binds to and stimulates transcription from the tumor
CC suppressor TXNIP gene promoter; may thus be involved in tumor
CC suppression. When associated with SAFB, binds to and stimulates
CC transcription from the SREBF1 promoter. Associates with nascent mRNAs
CC transcribed by RNA polymerase II. Component of the supraspliceosome
CC complex that regulates pre-mRNA alternative splice site selection. Can
CC either activate or suppress exon inclusion; acts additively with TRA2B
CC to promote exon 7 inclusion of the survival motor neuron SMN. Represses
CC the splicing of MAPT/Tau exon 10. Binds preferentially to single-
CC stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-
CC stranded conformation; probably binds RNA as a homodimer. Binds non-
CC specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1
CC trafficking pathways; promotes both the IL-1-beta-mediated inducible
CC proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1
CC exosome-like vesicles to the extracellular compartment (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer. Found in the supraspliceosome complex.
CC Identified in the spliceosome C complex. Forms a complex with ILF2,
CC ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2,
CC KHDRBS3, SAFB/SAFB1, TRA2B and YTHDC1. Interacts with ERAP1; the
CC interaction is RNA-independent (By similarity). Interacts with
CC PPIA/CYPA (By similarity). {ECO:0000250|UniProtKB:P38159,
CC ECO:0000250|UniProtKB:Q9WV02}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC ribonucleosomes. Localizes in numerous small granules in the nucleus
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for splice
CC site selection, indicating that its splicing activity does not require
CC direct binding to RNA. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: Arg-185 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
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DR EMBL; AB168869; BAE00972.1; -; mRNA.
DR RefSeq; NP_001270702.1; NM_001283773.1.
DR RefSeq; XP_015299206.1; XM_015443720.1.
DR RefSeq; XP_015299207.1; XM_015443721.1.
DR AlphaFoldDB; Q4R7F0; -.
DR BMRB; Q4R7F0; -.
DR SMR; Q4R7F0; -.
DR STRING; 9541.XP_005594764.1; -.
DR Ensembl; ENSMFAT00000069585; ENSMFAP00000019037; ENSMFAG00000032479.
DR GeneID; 101864797; -.
DR KEGG; mcf:101864797; -.
DR CTD; 27316; -.
DR VEuPathDB; HostDB:ENSMFAG00000032479; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000153425; -.
DR OMA; AKYHEGF; -.
DR OrthoDB; 1248417at2759; -.
DR Proteomes; UP000233100; Chromosome X.
DR Bgee; ENSMFAG00000032479; Expressed in thymus and 13 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0044530; C:supraspliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS: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; ISS: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; ISS: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 Acetylation; Activator; Glycoprotein; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..391
FT /note="RNA-binding motif protein, X chromosome"
FT /id="PRO_0000413018"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CHAIN 2..391
FT /note="RNA-binding motif protein, X chromosome, N-
FT terminally processed"
FT /id="PRO_0000413019"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 61..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..236
FT /note="Necessary for the association to nascent RNAPII
FT transcripts and nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 333..391
FT /note="Necessary for RNA-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Pro residues"
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 308..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein G; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 2
FT /note="N-acetylvaline; in Heterogeneous nuclear
FT ribonucleoprotein G, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 125
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 164
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
SQ SEQUENCE 391 AA; 42318 MW; 8C3FEB9BFC566403 CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGRGGSGGTR
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR
APVSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQDRGLP PSMERGYPPP
RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y
