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Protein

RNA-binding protein with serine-rich domain 1

Gene

RNPS1

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

Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions.10 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

  • mRNA 3'-UTR binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

<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 functionRNA-binding
Biological processmRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.18.1.1 the nuclear mrna exporter (mrna-e) family

<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 protein with serine-rich domain 1
Alternative name(s):
SR-related protein LDC2
<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:RNPS1
Synonyms:LDC2
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000205937.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:10080 RNPS1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606447 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15287

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

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>Mutagenesisi53S → A: Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. 1 Publication1
Mutagenesisi53S → E: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. 1 Publication1
Mutagenesisi171N → R: Impairs interaction with SAP18. 1 Publication1
Mutagenesisi205Y → A: Abolishes exon-skipping. 1 Publication1
Mutagenesisi207Y → A: Abolishes exon-skipping. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
10921

Open Targets

More...
OpenTargetsi
ENSG00000205937

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA34453

Polymorphism and mutation databases

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74754492

<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_00000818161 – 305RNA-binding protein with serine-rich domain 1Add BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<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 residuei53Phosphoserine; by CK21 Publication1
Modified residuei155PhosphoserineCombined sources1
Modified residuei157PhosphoserineCombined sources1
Modified residuei161PhosphothreonineCombined sources1
Modified residuei218N6-acetyllysineCombined 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

Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q15287

MaxQB - The MaxQuant DataBase

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MaxQBi
Q15287

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

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PaxDbi
Q15287

PeptideAtlas

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PeptideAtlasi
Q15287

PRoteomics IDEntifications database

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PRIDEi
Q15287

ProteomicsDB human proteome resource

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ProteomicsDBi
60514
60515 [Q15287-2]
60516 [Q15287-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q15287

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

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PhosphoSitePlusi
Q15287

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q15287

<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

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000205937 Expressed in 203 organ(s), highest expression level in cerebellar hemisphere

CleanEx database of gene expression profiles

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CleanExi
HS_RNPS1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15287 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15287 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA044014

<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

Found in mRNA splicing-dependent exon junction complexes (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. Component of the active spliceosome. Associates with polysomes. Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10.14 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
116125, 199 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q15287

Database of interacting proteins

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DIPi
DIP-32943N

Protein interaction database and analysis system

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IntActi
Q15287, 103 interactors

Molecular INTeraction database

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MINTi
Q15287

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000301730

<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

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q15287

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

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SMRi
Q15287

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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>Domaini161 – 240RRMPROSITE-ProRule annotationAdd BLAST80

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>Regioni1 – 220Necessary for interaction with the cleaved p110 isoform of CDC2L1Add BLAST220
Regioni1 – 161Necessary for interaction with SRP54, nuclear localization and exon-skipping1 PublicationAdd BLAST161
Regioni69 – 121Necessary for interactions with UPF2 and UPF3B and UPF2-dependent NMDAdd BLAST53
Regioni156 – 242Necessary for interaction with PNN and exon-skippingAdd BLAST87
Regioni159 – 244Interaction with SAP18 and ACIN11 PublicationAdd BLAST86
Regioni238 – 305Necessary for interaction with TRA2B, nuclear localization and exon-skipping1 PublicationAdd BLAST68

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi7 – 64Lys-richAdd BLAST58
Compositional biasi67 – 141Ser-richAdd BLAST75
Compositional biasi128 – 154Arg-richAdd BLAST27
Compositional biasi241 – 298Arg/Pro-richAdd BLAST58

<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 required for the formation of the ASAP complex.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the splicing factor SR family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4209 Eukaryota
ENOG4111PFV LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00730000111029

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053138

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15287

KEGG Orthology (KO)

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KOi
K14325

Identification of Orthologs from Complete Genome Data

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OMAi
PNFGRGV

Database of Orthologous Groups

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OrthoDBi
EOG091G14LV

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15287

TreeFam database of animal gene trees

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TreeFami
TF314165

Family and domain databases

Conserved Domains Database

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CDDi
cd12365 RRM_RNPS1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.330, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR034201 RNPS1_RRM
IPR000504 RRM_dom

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00360 RRM, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

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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>.<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.

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 14 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q15287-1) [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
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK
60 70 80 90 100
ESSEKDRGRD KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS
110 120 130 140 150
SASSRSGSSS TSRSSSSSSS SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE
160 170 180 190 200
RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI FSTYGKIKMI DMPVERMHPH
210 220 230 240 250
LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA PWPRPPPRRF
260 270 280 290 300
SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS

SNSSR
Length:305
Mass (Da):34,208
Last modified:November 1, 1996 - v1
<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:i930C9D36C2486144
GO
Isoform 2 (identifier: Q15287-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-24: Missing.

Show »
Length:282
Mass (Da):31,709
Checksum:iD3F7AAD16B6309F4
GO
Isoform 3 (identifier: Q15287-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-24: Missing.
     69-82: Missing.

Show »
Length:268
Mass (Da):30,354
Checksum:i9058DEEC9B433103
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 14 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BMM9H3BMM9_HUMAN
RNA-binding protein with serine-ric...
RNPS1
284Annotation 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>
H3BTC0H3BTC0_HUMAN
RNA-binding protein with serine-ric...
RNPS1
302Annotation 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>
H3BTR6H3BTR6_HUMAN
RNA-binding protein with serine-ric...
RNPS1
127Annotation 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>
H3BUL0H3BUL0_HUMAN
RNA-binding protein with serine-ric...
RNPS1
169Annotation 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>
H3BUG0H3BUG0_HUMAN
RNA-binding protein with serine-ric...
RNPS1
139Annotation 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>
H3BP82H3BP82_HUMAN
RNA-binding protein with serine-ric...
RNPS1
98Annotation 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>
H3BTY0H3BTY0_HUMAN
RNA-binding protein with serine-ric...
RNPS1
150Annotation 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>
H3BNI3H3BNI3_HUMAN
RNA-binding protein with serine-ric...
RNPS1
85Annotation 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>
H3BMS0H3BMS0_HUMAN
RNA-binding protein with serine-ric...
RNPS1
257Annotation 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>
H3BPG5H3BPG5_HUMAN
RNA binding protein S1, serine-rich...
RNPS1 hCG_1989969
128Annotation 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>
There are more potential isoformsShow all

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 conflicti32K → E in BAG56859 (PubMed:14702039).Curated1
Sequence conflicti66R → G in AAC39791 (PubMed:9580558).Curated1
Sequence conflicti249R → G in BAG56859 (PubMed:14702039).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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0162432 – 24Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST23
Alternative sequenceiVSP_03760169 – 82Missing in isoform 3. 1 PublicationAdd BLAST14

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L37368 mRNA Translation: AAA92859.1
AF015608 mRNA Translation: AAC39791.1
AF274003 mRNA Translation: AAL56665.1
AK289955 mRNA Translation: BAF82644.1
AK293343 mRNA Translation: BAG56859.1
AK303100 mRNA Translation: BAG64209.1
AK316132 mRNA Translation: BAH14503.1
AC009065 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85516.1
BC001659 mRNA Translation: AAH01659.1
BC001838 mRNA Translation: AAH01838.1
BC108316 mRNA Translation: AAI08317.1
AF247662 mRNA Translation: AAF72519.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10465.1 [Q15287-1]
CCDS66907.1 [Q15287-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4525

NCBI Reference Sequences

More...
RefSeqi
NP_001273554.1, NM_001286625.1 [Q15287-1]
NP_001273555.1, NM_001286626.1 [Q15287-2]
NP_001273556.1, NM_001286627.1
NP_006702.1, NM_006711.4 [Q15287-1]
NP_542161.1, NM_080594.3 [Q15287-1]
XP_005255105.1, XM_005255048.1 [Q15287-1]
XP_005255106.1, XM_005255049.3 [Q15287-1]
XP_016878363.1, XM_017022874.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.355643
Hs.507343
Hs.733012

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000301730; ENSP00000301730; ENSG00000205937 [Q15287-1]
ENST00000320225; ENSP00000315859; ENSG00000205937 [Q15287-1]
ENST00000397086; ENSP00000380275; ENSG00000205937 [Q15287-1]
ENST00000565678; ENSP00000457723; ENSG00000205937 [Q15287-1]
ENST00000566458; ENSP00000456352; ENSG00000205937 [Q15287-2]
ENST00000568631; ENSP00000457820; ENSG00000205937 [Q15287-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
10921

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10921

UCSC genome browser

More...
UCSCi
uc002cpt.5 human [Q15287-1]

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
L37368 mRNA Translation: AAA92859.1
AF015608 mRNA Translation: AAC39791.1
AF274003 mRNA Translation: AAL56665.1
AK289955 mRNA Translation: BAF82644.1
AK293343 mRNA Translation: BAG56859.1
AK303100 mRNA Translation: BAG64209.1
AK316132 mRNA Translation: BAH14503.1
AC009065 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85516.1
BC001659 mRNA Translation: AAH01659.1
BC001838 mRNA Translation: AAH01838.1
BC108316 mRNA Translation: AAI08317.1
AF247662 mRNA Translation: AAF72519.1
CCDSiCCDS10465.1 [Q15287-1]
CCDS66907.1 [Q15287-2]
PIRiJC4525
RefSeqiNP_001273554.1, NM_001286625.1 [Q15287-1]
NP_001273555.1, NM_001286626.1 [Q15287-2]
NP_001273556.1, NM_001286627.1
NP_006702.1, NM_006711.4 [Q15287-1]
NP_542161.1, NM_080594.3 [Q15287-1]
XP_005255105.1, XM_005255048.1 [Q15287-1]
XP_005255106.1, XM_005255049.3 [Q15287-1]
XP_016878363.1, XM_017022874.1
UniGeneiHs.355643
Hs.507343
Hs.733012

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
4A8XX-ray1.90A159-244[»]
ProteinModelPortaliQ15287
SMRiQ15287
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116125, 199 interactors
CORUMiQ15287
DIPiDIP-32943N
IntActiQ15287, 103 interactors
MINTiQ15287
STRINGi9606.ENSP00000301730

Protein family/group databases

TCDBi3.A.18.1.1 the nuclear mrna exporter (mrna-e) family

PTM databases

iPTMnetiQ15287
PhosphoSitePlusiQ15287
SwissPalmiQ15287

Polymorphism and mutation databases

DMDMi74754492

Proteomic databases

EPDiQ15287
MaxQBiQ15287
PaxDbiQ15287
PeptideAtlasiQ15287
PRIDEiQ15287
ProteomicsDBi60514
60515 [Q15287-2]
60516 [Q15287-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10921
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301730; ENSP00000301730; ENSG00000205937 [Q15287-1]
ENST00000320225; ENSP00000315859; ENSG00000205937 [Q15287-1]
ENST00000397086; ENSP00000380275; ENSG00000205937 [Q15287-1]
ENST00000565678; ENSP00000457723; ENSG00000205937 [Q15287-1]
ENST00000566458; ENSP00000456352; ENSG00000205937 [Q15287-2]
ENST00000568631; ENSP00000457820; ENSG00000205937 [Q15287-1]
GeneIDi10921
KEGGihsa:10921
UCSCiuc002cpt.5 human [Q15287-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10921
DisGeNETi10921
EuPathDBiHostDB:ENSG00000205937.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RNPS1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0031789
HGNCiHGNC:10080 RNPS1
HPAiHPA044014
MIMi606447 gene
neXtProtiNX_Q15287
OpenTargetsiENSG00000205937
PharmGKBiPA34453

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4209 Eukaryota
ENOG4111PFV LUCA
GeneTreeiENSGT00730000111029
HOVERGENiHBG053138
InParanoidiQ15287
KOiK14325
OMAiPNFGRGV
OrthoDBiEOG091G14LV
PhylomeDBiQ15287
TreeFamiTF314165

Enzyme and pathway databases

ReactomeiR-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

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

More...
ChiTaRSi
RNPS1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RNPS1

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

More...
GenomeRNAii
10921

Protein Ontology

More...
PROi
PR:Q15287

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000205937 Expressed in 203 organ(s), highest expression level in cerebellar hemisphere
CleanExiHS_RNPS1
ExpressionAtlasiQ15287 baseline and differential
GenevisibleiQ15287 HS

Family and domain databases

CDDicd12365 RRM_RNPS1, 1 hit
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR034201 RNPS1_RRM
IPR000504 RRM_dom
PfamiView protein in Pfam
PF00076 RRM_1, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiRNPS1_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: Q15287
Secondary accession number(s): A8K1P0
, B4DDU8, B4DZU7, B7ZA17, O75308, Q32P25, Q8WY42, Q9NYG3
<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: November 22, 2005
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 186 of the entry and version 1 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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