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Protein

RNA-binding motif protein, X chromosome

Gene

RBMX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.7 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • mRNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • single-stranded RNA binding Source: Ensembl

GO - Biological processi

  • cellular response to interleukin-1 Source: UniProtKB
  • gene expression Source: Reactome
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • mRNA splice site selection Source: Ensembl
  • mRNA splicing, via spliceosome Source: UniProtKB
  • negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147274-MONOMER.
ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding motif protein, X chromosome
Alternative name(s):
Glycoprotein p43
Heterogeneous nuclear ribonucleoprotein G
Short name:
hnRNP G
Cleaved into the following chain:
Gene namesi
Name:RBMX
Synonyms:HNRPG, RBMXP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9910. RBMX.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear euchromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • supraspliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, 11 (MRXS11)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXS11 patients manifest moderate intellectual disability and craniofacial dysmorphism.
See also OMIM:300238

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22K → A: Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter. 2 Publications1

Keywords - Diseasei

Mental retardation, Tumor suppressor

Organism-specific databases

DisGeNETi27316.
MIMi300238. phenotype.
OpenTargetsiENSG00000147274.
PharmGKBiPA34277.

Polymorphism and mutation databases

BioMutaiRBMX.
DMDMi23503093.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000818541 – 391RNA-binding motif protein, X chromosomeAdd BLAST391
Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00003045822 – 391RNA-binding motif protein, X chromosome, N-terminally processedAdd BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate1 Publication1
Modified residuei2N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed1 Publication1
Modified residuei30N6-acetyllysineCombined sources1
Cross-linki80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei88PhosphoserineCombined sources1
Modified residuei91PhosphoserineCombined sources1
Modified residuei125Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei125Omega-N-methylarginine; alternateBy similarity1
Modified residuei144Omega-N-methylarginineBy similarity1
Modified residuei164Omega-N-methylarginineBy similarity1
Modified residuei165PhosphoserineCombined sources1
Modified residuei172Omega-N-methylarginineBy similarity1
Modified residuei174PhosphoserineCombined sources1
Modified residuei261PhosphoserineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Modified residuei329PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei352PhosphoserineCombined sources1

Post-translational modificationi

O-glycosylated.1 Publication
Arg-185 is dimethylated, probably to asymmetric dimethylarginine.
Cleavage of initiator Met is partial. If Met-1 is not removed, it is acetylated. If it is removed, Val-2 is acetylated.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiP38159.
MaxQBiP38159.
PaxDbiP38159.
PeptideAtlasiP38159.
PRIDEiP38159.
TopDownProteomicsiP38159-1. [P38159-1]

2D gel databases

SWISS-2DPAGEP38159.

PTM databases

iPTMnetiP38159.
PhosphoSitePlusiP38159.
SwissPalmiP38159.

Expressioni

Tissue specificityi

Expressed strongly in oral keratinocytes, but only weakly detected in oral squamous cell carcinomas (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000147274.
CleanExiHS_RBMX.
ExpressionAtlasiP38159. baseline and differential.
GenevisibleiP38159. HS.

Organism-specific databases

HPAiHPA057707.

Interactioni

Subunit structurei

Homomultimer. Interacts with SAFB/SAFB1 (By similarity). Found in the supraspliceosome complex. Identified in the spliceosome C complex. Interacts with KHDRBS3. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the interaction is RNA-independent.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-743526,EBI-743526
APOBEC3CQ9NRW35EBI-743526,EBI-1044593
CIRBPQ140114EBI-743526,EBI-538850
CLK3P497613EBI-743526,EBI-745579
HNRNPKP619786EBI-743526,EBI-304185
HNRNPKP61978-24EBI-743526,EBI-7060731
HNRPKQ6IBN15EBI-743526,EBI-3440248
KHDRBS2Q5VWX111EBI-743526,EBI-742808
KHDRBS3O755253EBI-743526,EBI-722504
LNX1Q8TBB13EBI-743526,EBI-739832
MAGOHBQ96A723EBI-743526,EBI-746778
NABP1Q96AH03EBI-743526,EBI-2889252
PRR3P795225EBI-743526,EBI-2803328
RBM3P981795EBI-743526,EBI-2949699
RBMY1A1P0DJD33EBI-743526,EBI-8638511
RBMY1A1P0DJD3-24EBI-743526,EBI-11994018
RBMY1JQ154157EBI-743526,EBI-8642021
ROBO3Q96HH03EBI-743526,EBI-10288358
SNRPAP090123EBI-743526,EBI-607085
Srek1Q9JKL73EBI-743526,EBI-6452221From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi118134. 154 interactors.
DIPiDIP-34447N.
IntActiP38159. 84 interactors.
MINTiMINT-5000999.
STRINGi9606.ENSP00000359645.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Helixi21 – 28Combined sources8
Turni29 – 31Combined sources3
Beta strandi34 – 39Combined sources6
Turni43 – 45Combined sources3
Beta strandi50 – 58Combined sources9
Helixi61 – 66Combined sources6
Beta strandi67 – 74Combined sources8
Beta strandi80 – 83Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MB0NMR-B1-95[»]
2MKSNMR-A1-90[»]
ProteinModelPortaliP38159.
SMRiP38159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 86RRMPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni186 – 236Necessary for the association to nascent RNAPII transcripts and nuclear localizationAdd BLAST51
Regioni333 – 391Necessary for RNA-bindingAdd BLAST59

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.
InParanoidiP38159.
KOiK12885.
OMAiRDYSYRE.
OrthoDBiEOG091G13K0.
PhylomeDBiP38159.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P38159-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG
60 70 80 90 100
FAFVTFESPA DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP
110 120 130 140 150
RSRGPPRGLR GGRGGSGGTR GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK
160 170 180 190 200
RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR APVSRGRDSY GGPPRREPLP
210 220 230 240 250
SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD YTYRDYGHSS
260 270 280 290 300
SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP
310 320 330 340 350
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP
360 370 380 390
PSMERGYPPP RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y
Length:391
Mass (Da):42,332
Last modified:September 19, 2002 - v3
Checksum:i904FEB9BFC573546
GO
Isoform 2 (identifier: P38159-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-57: Missing.

Show »
Length:378
Mass (Da):40,846
Checksum:i032DD488FA08CE19
GO
Isoform 3 (identifier: P38159-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-196: SLDGKAIKVE...RDSYGGPPRR → LLYHVEEIVM...YGRGVLIDSQ
     197-391: Missing.

Note: No experimental confirmation available.
Show »
Length:196
Mass (Da):22,172
Checksum:i7FB2ABEE20A3D582
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti259G → E in CAA80599 (PubMed:7692398).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04220345 – 57Missing in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_04365073 – 196SLDGK…GPPRR → LLYHVEEIVMEVHLEGNRCP LVEMFICPQEMMGILLKTAI QAEITQVLVILEIMHHHHEI ILTVIMVIPVHVMTIHQEDI AIEMDMVVIVTIQIIQVEVP TEIHMRVMVGDFAHYGRGVL IDSQ in isoform 3. 1 PublicationAdd BLAST124
Alternative sequenceiVSP_043651197 – 391Missing in isoform 3. 1 PublicationAdd BLAST195

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23064 mRNA. Translation: CAA80599.1.
AF266723
, AF266720, AF266721, AF266722 Genomic DNA. Translation: AAK58567.1.
AY464692 mRNA. Translation: AAR28036.1.
AK096015 mRNA. Translation: BAC04674.1.
AK304868 mRNA. Translation: BAG65606.1.
AL683813 Genomic DNA. Translation: CAI39448.1.
CH471150 Genomic DNA. Translation: EAW88453.1.
CH471150 Genomic DNA. Translation: EAW88454.1.
CH471150 Genomic DNA. Translation: EAW88455.1.
CH471150 Genomic DNA. Translation: EAW88457.1.
BC006550 mRNA. Translation: AAH06550.1.
BC007435 mRNA. Translation: AAH07435.1.
CCDSiCCDS14661.1. [P38159-1]
CCDS55510.1. [P38159-3]
RefSeqiNP_001158275.1. NM_001164803.1. [P38159-3]
NP_002130.2. NM_002139.3. [P38159-1]
UniGeneiHs.380118.
Hs.710162.

Genome annotation databases

EnsembliENST00000320676; ENSP00000359645; ENSG00000147274. [P38159-1]
ENST00000431446; ENSP00000411989; ENSG00000147274. [P38159-3]
GeneIDi27316.
KEGGihsa:27316.
UCSCiuc004fae.4. human. [P38159-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23064 mRNA. Translation: CAA80599.1.
AF266723
, AF266720, AF266721, AF266722 Genomic DNA. Translation: AAK58567.1.
AY464692 mRNA. Translation: AAR28036.1.
AK096015 mRNA. Translation: BAC04674.1.
AK304868 mRNA. Translation: BAG65606.1.
AL683813 Genomic DNA. Translation: CAI39448.1.
CH471150 Genomic DNA. Translation: EAW88453.1.
CH471150 Genomic DNA. Translation: EAW88454.1.
CH471150 Genomic DNA. Translation: EAW88455.1.
CH471150 Genomic DNA. Translation: EAW88457.1.
BC006550 mRNA. Translation: AAH06550.1.
BC007435 mRNA. Translation: AAH07435.1.
CCDSiCCDS14661.1. [P38159-1]
CCDS55510.1. [P38159-3]
RefSeqiNP_001158275.1. NM_001164803.1. [P38159-3]
NP_002130.2. NM_002139.3. [P38159-1]
UniGeneiHs.380118.
Hs.710162.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MB0NMR-B1-95[»]
2MKSNMR-A1-90[»]
ProteinModelPortaliP38159.
SMRiP38159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118134. 154 interactors.
DIPiDIP-34447N.
IntActiP38159. 84 interactors.
MINTiMINT-5000999.
STRINGi9606.ENSP00000359645.

PTM databases

iPTMnetiP38159.
PhosphoSitePlusiP38159.
SwissPalmiP38159.

Polymorphism and mutation databases

BioMutaiRBMX.
DMDMi23503093.

2D gel databases

SWISS-2DPAGEP38159.

Proteomic databases

EPDiP38159.
MaxQBiP38159.
PaxDbiP38159.
PeptideAtlasiP38159.
PRIDEiP38159.
TopDownProteomicsiP38159-1. [P38159-1]

Protocols and materials databases

DNASUi27316.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320676; ENSP00000359645; ENSG00000147274. [P38159-1]
ENST00000431446; ENSP00000411989; ENSG00000147274. [P38159-3]
GeneIDi27316.
KEGGihsa:27316.
UCSCiuc004fae.4. human. [P38159-1]

Organism-specific databases

CTDi27316.
DisGeNETi27316.
GeneCardsiRBMX.
HGNCiHGNC:9910. RBMX.
HPAiHPA057707.
MIMi300199. gene.
300238. phenotype.
neXtProtiNX_P38159.
OpenTargetsiENSG00000147274.
PharmGKBiPA34277.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiP38159.
KOiK12885.
OMAiRDYSYRE.
OrthoDBiEOG091G13K0.
PhylomeDBiP38159.
TreeFamiTF331833.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147274-MONOMER.
ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.

Miscellaneous databases

ChiTaRSiRBMX. human.
GeneWikiiRBMX.
GenomeRNAii27316.
PROiP38159.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147274.
CleanExiHS_RBMX.
ExpressionAtlasiP38159. baseline and differential.
GenevisibleiP38159. HS.

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...

Entry informationi

Entry nameiRBMX_HUMAN
AccessioniPrimary (citable) accession number: P38159
Secondary accession number(s): B4E3U4
, D3DWH0, E9PG86, Q5JQ67, Q8N8Y7, Q969R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: September 19, 2002
Last modified: November 30, 2016
This is version 188 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.