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Protein

RNA-binding motif protein, X chromosome

Gene

RBMX

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding motif protein, X chromosome
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein G
Short name:
hnRNP G
Cleaved into the following chain:
Gene namesi
Name:RBMX
Synonyms:HNRPG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

  • Nucleus

  • Note: Component of ribonucleosomes. Localizes in numerous small granules in the nucleus (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396RNA-binding motif protein, X chromosomePRO_0000240607Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 396395RNA-binding motif protein, X chromosome, N-terminally processedPRO_0000367118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternateBy similarity
Modified residuei2 – 21N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processedBy similarity
Modified residuei30 – 301N6-acetyllysineBy similarity
Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei91 – 911PhosphoserineBy similarity
Modified residuei185 – 1851Omega-N-methylated arginineBy similarity
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei355 – 3551PhosphoserineBy similarity

Post-translational modificationi

O-glycosylated.By similarity
Arg-185 is dimethylated, probably to asymmetric dimethylarginine.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ29RT0.
PRIDEiQ29RT0.

Interactioni

Subunit structurei

Homomultimer. Found in the supraspliceosome complex. Identified in the spliceosome C complex. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2, KHDRBS3, SAFB/SAFB1, TRA2B and YTHDC1. Interacts with ERAP1; the interaction is RNA-independent (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000056096.

Structurei

3D structure databases

ProteinModelPortaliQ29RT0.
SMRiQ29RT0. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 8679RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 23651Necessary for the association to nascent RNAPII transcripts and nuclear localizationBy similarityAdd
BLAST
Regioni336 – 39661Necessary for RNA-bindingBy similarityAdd
BLAST

Domaini

The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA.By similarity

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiQ29RT0.
KOiK12885.
OMAiLSMERGC.
OrthoDBiEOG780RPD.
TreeFamiTF331833.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q29RT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEADRPGKL FIGGLNLETD EKSLEATFGK YGRISEVLLM KDRETNKSRG
60 70 80 90 100
FAFITFESPA DAKAAVRDMN GKSLDGKAIK VAQATKPAFE SGRRGPPLSR
110 120 130 140 150
SRGRSRGLRG ARGGGPRRPP SRGGPADDGG YAGDFDLRPS RAPLPMKRGP
160 170 180 190 200
PPPRRAGPPP KRAAPSGPAR SGSGGGMRGR APAARGRDGY EGPPRRDPPP
210 220 230 240 250
PRRDPYLGSR EGGYSPRDGY SSRDYSSARD ARDFAPSPRE YTYRDYGHSS
260 270 280 290 300
ARDECPSRGY GDRDGYGGRD RDYADHPSGG SYRDPFESYG DPRSAAPARG
310 320 330 340 350
PPPSYGGGGG RYEEYRGCSP DAYGGGRDGY AGGRSERYSG GRDRVGRADR
360 370 380 390
GLPQSVERGC PPPRESYSRS GRKVPRGGGR LGSRSERGGG GGRSRY
Length:396
Mass (Da):42,369
Last modified:April 4, 2006 - v1
Checksum:i2A81CE93A59F8118
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114040 mRNA. Translation: AAI14041.1.
RefSeqiNP_001040075.1. NM_001046610.1.
UniGeneiBt.59490.

Genome annotation databases

EnsembliENSBTAT00000066112; ENSBTAP00000056096; ENSBTAG00000047652.
GeneIDi617969.
KEGGibta:617969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114040 mRNA. Translation: AAI14041.1.
RefSeqiNP_001040075.1. NM_001046610.1.
UniGeneiBt.59490.

3D structure databases

ProteinModelPortaliQ29RT0.
SMRiQ29RT0. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000056096.

Proteomic databases

PaxDbiQ29RT0.
PRIDEiQ29RT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000066112; ENSBTAP00000056096; ENSBTAG00000047652.
GeneIDi617969.
KEGGibta:617969.

Organism-specific databases

CTDi27288.

Phylogenomic databases

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiQ29RT0.
KOiK12885.
OMAiLSMERGC.
OrthoDBiEOG780RPD.
TreeFamiTF331833.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Testis.

Entry informationi

Entry nameiRBMX_BOVIN
AccessioniPrimary (citable) accession number: Q29RT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: April 4, 2006
Last modified: July 6, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.