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UniProtKB - P38159 (RBMX_HUMAN)

Entry version 215 (16 Oct 2019)
Sequence version 3 (19 Sep 2002)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Repressor, Ribonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing, Transcription

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
RNA-binding motif protein, X chromosome, N-terminally processed
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RBMX
Synonyms:HNRPG, RBMXP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9910 RBMX

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		300199 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P38159

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Spliceosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi22K → A: Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter. 2 Publications1

Keywords - Diseasei

Mental retardation, Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		27316

MalaCards human disease database

More...MalaCardsi		RBMX
MIMi300238 phenotype

Open Targets

More...OpenTargetsi		ENSG00000147274

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34277

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P38159

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RBMX

Domain mapping of disease mutations (DMDM)

More...DMDMi		23503093

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000818541 – 391RNA-binding motif protein, X chromosomeAdd BLAST391
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00003045822 – 391RNA-binding motif protein, X chromosome, N-terminally processedAdd BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate1 Publication1
Modified residuei2N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei30N6-acetyllysineCombined sources1
Cross-linki80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei88PhosphoserineCombined sources1
Modified residuei91PhosphoserineCombined sources1
Modified residuei125Omega-N-methylarginineBy 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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P38159

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P38159

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P38159

MaxQB - The MaxQuant DataBase

More...MaxQBi		P38159

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P38159

PeptideAtlas

More...PeptideAtlasi		P38159

PRoteomics IDEntifications database

More...PRIDEi		P38159

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55284 [P38159-1]
55285 [P38159-2]
55286 [P38159-3]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P38159-1 [P38159-1]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P38159

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P38159

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P38159

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P38159

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000147274 Expressed in 204 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P38159 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P38159 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA057707

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		118134, 190 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P38159

Database of interacting proteins

More...DIPi		DIP-34447N

Protein interaction database and analysis system

More...IntActi		P38159, 127 interactors

Molecular INTeraction database

More...MINTi		P38159

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000359645

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P38159

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 86RRMPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni186 – 236Necessary for the association to nascent RNAPII transcripts and nuclear localizationAdd BLAST51
Regioni333 – 391Necessary for RNA-bindingAdd BLAST59

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IHG3 Eukaryota
ENOG4111GI6 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153425

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000276235

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P38159

KEGG Orthology (KO)

More...KOi		K12885

Identification of Orthologs from Complete Genome Data

More...OMAi		AKYHEGF

Database of Orthologous Groups

More...OrthoDBi		1248417at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P38159

TreeFam database of animal gene trees

More...TreeFami		TF331833

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.70.330, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR012604 RBM1CTR
IPR000504 RRM_dom
IPR003954 RRM_dom_euk

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08081 RBM1CTR, 1 hit
PF00076 RRM_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00360 RRM, 1 hit
SM00361 RRM_1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50102 RRM, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y6E7H0Y6E7_HUMAN
RNA-binding motif protein, X chromo...
RBMX
292Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BT71H3BT71_HUMAN
RNA-binding motif protein, X chromo...
RBMX
296Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BUY5H3BUY5_HUMAN
RNA-binding motif protein, X chromo...
RBMX
263Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BR27H3BR27_HUMAN
RNA-binding motif protein, X chromo...
RBMX
78Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BNC1H3BNC1_HUMAN
RNA-binding motif protein, X chromo...
RBMX
37Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti259G → E in CAA80599 (PubMed:7692398).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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 No translation available.
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS14661.1 [P38159-1]
CCDS55510.1 [P38159-3]

NCBI Reference Sequences

More...RefSeqi		NP_001158275.1, NM_001164803.1 [P38159-3]
NP_002130.2, NM_002139.3 [P38159-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000320676; ENSP00000359645; ENSG00000147274 [P38159-1]
ENST00000431446; ENSP00000411989; ENSG00000147274 [P38159-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		27316

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:27316

UCSC genome browser

More...UCSCi		uc004fae.4 human [P38159-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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 No translation available.
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MB0NMR-B1-95[»]
2MKSNMR-A1-90[»]
SMRiP38159
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi118134, 190 interactors
CORUMiP38159
DIPiDIP-34447N
IntActiP38159, 127 interactors
MINTiP38159
STRINGi9606.ENSP00000359645

PTM databases

iPTMnetiP38159
PhosphoSitePlusiP38159
SwissPalmiP38159

Polymorphism and mutation databases

BioMutaiRBMX
DMDMi23503093

2D gel databases

SWISS-2DPAGEiP38159

Proteomic databases

EPDiP38159
jPOSTiP38159
MassIVEiP38159
MaxQBiP38159
PaxDbiP38159
PeptideAtlasiP38159
PRIDEiP38159
ProteomicsDBi55284 [P38159-1]
55285 [P38159-2]
55286 [P38159-3]
TopDownProteomicsiP38159-1 [P38159-1]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P38159

The DNASU plasmid repository

More...DNASUi		27316

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		27316
DisGeNETi27316

GeneCards: human genes, protein and diseases

More...GeneCardsi		RBMX
HGNCiHGNC:9910 RBMX
HPAiHPA057707
MalaCardsiRBMX
MIMi300199 gene
300238 phenotype
neXtProtiNX_P38159
OpenTargetsiENSG00000147274
PharmGKBiPA34277

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IHG3 Eukaryota
ENOG4111GI6 LUCA
GeneTreeiENSGT00940000153425
HOGENOMiHOG000276235
InParanoidiP38159
KOiK12885
OMAiAKYHEGF
OrthoDBi1248417at2759
PhylomeDBiP38159
TreeFamiTF331833

Enzyme and pathway databases

ReactomeiR-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RBMX human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RBMX

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		27316
PharosiP38159

Protein Ontology

More...PROi		PR:P38159

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000147274 Expressed in 204 organ(s), highest expression level in kidney
ExpressionAtlasiP38159 baseline and differential
GenevisibleiP38159 HS

Family and domain databases

Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR012604 RBM1CTR
IPR000504 RRM_dom
IPR003954 RRM_dom_euk
PfamiView protein in Pfam
PF08081 RBM1CTR, 1 hit
PF00076 RRM_1, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SM00361 RRM_1, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRBMX_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38159
Secondary accession number(s): B4E3U4
, D3DWH0, E9PG86, Q5JQ67, Q8N8Y7, Q969R3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: September 19, 2002
Last modified: October 16, 2019
This is version 215 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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