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UniProtKB - Q15287 (RNPS1_HUMAN)

Entry version 201 (02 Dec 2020)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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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

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

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q15287

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		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-73856, RNA Polymerase II Transcription Termination
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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000205937.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:10080, RNPS1

Online Mendelian Inheritance in Man (OMIM)

More...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 & Seán O’Donoghue; 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%5Fand%5Fbiotech%5Fsection">'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

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q15287, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RNPS1

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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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

More...EPDi		Q15287

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q15287

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q15287

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q15287

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

More...PaxDbi		Q15287

PeptideAtlas

More...PeptideAtlasi		Q15287

PRoteomics IDEntifications database

More...PRIDEi		Q15287

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		60514 [Q15287-1]
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.

More...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

More...Bgeei		ENSG00000205937, Expressed in cortical plate and 215 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q15287, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q15287, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000205937, Low tissue specificity

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		116125, 244 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q15287

Database of interacting proteins

More...DIPi		DIP-32943N

Protein interaction database and analysis system

More...IntActi		Q15287, 132 interactors

Molecular INTeraction database

More...MINTi		Q15287

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000457723

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q15287, protein

<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

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

More...SMRi		Q15287

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%5Fand%5Fdomains%5Fsection">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

More...eggNOGi		KOG4209, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00730000111029

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q15287

Identification of Orthologs from Complete Genome Data

More...OMAi		PNFGRGV

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q15287

TreeFam database of animal gene trees

More...TreeFami		TF314165

Family and domain databases

Conserved Domains Database

More...CDDi		cd12365, RRM_RNPS1, 1 hit

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
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

More...SMARTi		View protein in SMART
SM00360, RRM, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 <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
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:2 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:2 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:2 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>
H3BV80H3BV80_HUMAN
RNA-binding protein with serine-ric...
RNPS1
211Annotation score:

Annotation score:2 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 with serine-ric...
RNPS1 hCG_1989969
128Annotation score:

Annotation score:2 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>
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>
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>
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>
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.<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

More...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

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

More...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

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[»]
SMRiQ15287
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi116125, 244 interactors
CORUMiQ15287
DIPiDIP-32943N
IntActiQ15287, 132 interactors
MINTiQ15287
STRINGi9606.ENSP00000457723

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

BioMutaiRNPS1
DMDMi74754492

Proteomic databases

EPDiQ15287
jPOSTiQ15287
MassIVEiQ15287
MaxQBiQ15287
PaxDbiQ15287
PeptideAtlasiQ15287
PRIDEiQ15287
ProteomicsDBi60514 [Q15287-1]
60515 [Q15287-2]
60516 [Q15287-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		23681, 70 antibodies

The DNASU plasmid repository

More...DNASUi		10921

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
HGNCiHGNC:10080, RNPS1
HPAiENSG00000205937, Low tissue specificity
MIMi606447, gene
neXtProtiNX_Q15287
OpenTargetsiENSG00000205937
PharmGKBiPA34453

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4209, Eukaryota
GeneTreeiENSGT00730000111029
InParanoidiQ15287
OMAiPNFGRGV
PhylomeDBiQ15287
TreeFamiTF314165

Enzyme and pathway databases

PathwayCommonsiQ15287
ReactomeiR-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-73856, RNA Polymerase II Transcription Termination
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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		10921, 691 hits in 854 CRISPR screens

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
PharosiQ15287, Tbio

Protein Ontology

More...PROi		PR:Q15287
RNActiQ15287, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000205937, Expressed in cortical plate and 215 other tissues
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...

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 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%5Fand%5Fisoforms">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 2, 2020
This is version 201 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, Reference proteome

Documents

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