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UniProtKB - P08865 (RSSA_HUMAN)

Protein

40S ribosomal protein SA

Gene

RPSA

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

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA.UniRule annotation2 Publications
(Microbial infection) Acts as a receptor for the Adeno-associated viruses 2,3,8 and 9.1 Publication
(Microbial infection) Acts as a receptor for the Dengue virus.1 Publication
(Microbial infection) Acts as a receptor for the Sindbis virus.1 Publication
(Microbial infection) Acts as a receptor for the Venezuelan equine encephalitis virus.1 Publication
(Microbial infection) Acts as a receptor for the pathogenic prion protein.2 Publications
(Microbial infection) Acts as a receptor for bacteria.1 Publication

Miscellaneous

This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage.
It is thought that in vertebrates 37/67 kDa laminin receptor acquired a dual function during evolution. It developed from the ribosomal protein SA, playing an essential role in the protein biosynthesis lacking any laminin binding activity, to a cell surface receptor with laminin binding activity.

<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

  • laminin binding Source: UniProtKB-UniRule
  • laminin receptor activity Source: UniProtKB-UniRule
  • ribosome binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central
  • virus receptor activity Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionHost cell receptor for virus entry, Receptor, Ribonucleoprotein, Ribosomal protein
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-156902 Peptide chain elongation
R-HSA-1799339 SRP-dependent cotranslational protein targeting to membrane
R-HSA-192823 Viral mRNA Translation
R-HSA-2408557 Selenocysteine synthesis
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-HSA-72649 Translation initiation complex formation
R-HSA-72689 Formation of a pool of free 40S subunits
R-HSA-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-HSA-72702 Ribosomal scanning and start codon recognition
R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-HSA-72764 Eukaryotic Translation Termination
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

<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:
40S ribosomal protein SAUniRule annotation
Alternative name(s):
37 kDa laminin receptor precursorUniRule annotation
Short name:
37LRPUniRule annotation
37/67 kDa laminin receptorUniRule annotation
Short name:
LRP/LRUniRule annotation
67 kDa laminin receptorUniRule annotation
Short name:
67LRUniRule annotation
Colon carcinoma laminin-binding protein
Laminin receptor 1UniRule annotation
Short name:
LamRUniRule annotation
Laminin-binding protein precursor p40UniRule annotation
Short name:
LBP/p40UniRule annotation
Multidrug resistance-associated protein MGr1-Ag
NEM/1CHD4
Small ribosomal subunit protein uS21 Publication
<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:RPSAUniRule annotation
Synonyms:LAMBR, LAMR1
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000168028.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:6502 RPSA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		150370 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P08865

<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

Cell membrane, Cytoplasm, Membrane, 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

<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

Asplenia, isolated congenital (ICAS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare primary immunodeficiency and life-threatening condition, often presenting with pneumococcal sepsis. Most affected individuals die of severe bacterial infections in early childhood. Isolated asplenia is distinct from asplenia associated with other complex visceral defects, notably heterotaxy syndromes such as Ivemark syndrome.
See also OMIM:271400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07509254T → N in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514762EnsemblClinVar.1
Natural variantiVAR_07509358L → F in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514763EnsemblClinVar.1
Natural variantiVAR_075094180R → G in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514760EnsemblClinVar.1
Natural variantiVAR_075095180R → W in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514760EnsemblClinVar.1
Natural variantiVAR_075097186R → C in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514761EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		3921

MalaCards human disease database

More...MalaCardsi		RPSA
MIMi271400 phenotype

Open Targets

More...OpenTargetsi		ENSG00000168028

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		101351 Familial isolated congenital asplenia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30287

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL6119

Drug and drug target database

More...DrugBanki		DB04985 PCK3145

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RPSA

Domain mapping of disease mutations (DMDM)

More...DMDMi		125969

<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 <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 methionineiRemovedUniRule annotationCombined sources1 Publication
<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_00001343582 – 29540S ribosomal protein SAAdd BLAST294

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 residuei2N-acetylserineUniRule annotationCombined sources1 Publication1
Modified residuei43PhosphoserineCombined sources1
Modified residuei52N6-acetyllysineCombined sources1
Modified residuei89N6-acetyllysine; alternateBy similarity1
<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-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei97PhosphothreonineCombined 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

Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association (PubMed:9581863).UniRule annotation1 Publication
Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei115 – 116Cleavage; by ST3; site 1UniRule annotation2
Sitei133 – 134Cleavage; by ST3; site 2UniRule annotation2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P08865

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08865

MaxQB - The MaxQuant DataBase

More...MaxQBi		P08865

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

More...PaxDbi		P08865

PeptideAtlas

More...PeptideAtlasi		P08865

PRoteomics IDEntifications database

More...PRIDEi		P08865

ProteomicsDB human proteome resource

More...ProteomicsDBi		52170

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P08865

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08865

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

More...PhosphoSitePlusi		P08865

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P08865

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000168028 Expressed in 88 organ(s), highest expression level in right uterine tube

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P08865 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P08865 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB009561

<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

Monomer (37LRP) and homodimer (67LR). Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts with RPS21. Interacts with several laminins including at least LAMB1. Interacts with MDK (By similarity). The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B.UniRule annotation10 Publications
(Microbial infection) 67LR interacts with capsid protein of Adeno-associated virus 2,3,8 and 9.1 Publication
(Microbial infection) 67LR interacts with envelope protein of dengue virus.1 Publication
(Microbial infection) 6s7LR interacts with E2 glycoprotein of Sindbis and Venezuelan equine encephalitis virus (PubMed:8764073, PubMed:1385835).2 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110115, 236 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P08865

Database of interacting proteins

More...DIPi		DIP-32878N

Protein interaction database and analysis system

More...IntActi		P08865, 49 interactors

Molecular INTeraction database

More...MINTi		P08865

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000346067

<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

1295
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
3BCHX-ray2.15A2-220[»]
4UG0electron microscopy-SA1-295[»]
4V6Xelectron microscopy5.00AA1-295[»]
5A2Qelectron microscopy3.90A1-295[»]
5AJ0electron microscopy3.50BA1-295[»]
5FLXelectron microscopy3.90A1-295[»]
5LKSelectron microscopy3.60SA1-295[»]
5OA3electron microscopy4.30A1-295[»]
5T2Celectron microscopy3.60Ao1-295[»]
5VYCX-ray6.00A1/A2/A3/A4/A5/A61-295[»]
6EK0electron microscopy2.90SA1-295[»]
6FECelectron microscopy6.30f2-209[»]
6G18electron microscopy3.60A1-295[»]
6G4Selectron microscopy4.00A1-295[»]
6G51electron microscopy4.10A1-295[»]
6G53electron microscopy4.50A1-295[»]
6G5Helectron microscopy3.60A1-295[»]
6G5Ielectron microscopy3.50A1-295[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P08865

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

More...SMRi		P08865

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08865

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati230 – 232[DE]-W-[ST] 13
Repeati247 – 249[DE]-W-[ST] 23
Repeati266 – 268[DE]-W-[ST] 33
Repeati275 – 277[DE]-W-[ST] 43
Repeati293 – 295[DE]-W-[ST] 53

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>Regioni54 – 113Interaction with PPP1R16B1 PublicationAdd BLAST60
Regioni161 – 180Laminin-bindingAdd BLAST20
Regioni205 – 229Laminin-bindingAdd BLAST25
Regioni242 – 295Laminin-bindingAdd BLAST54

<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 universal ribosomal protein uS2 family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0830 Eukaryota
COG0052 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153327

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG054466

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08865

KEGG Orthology (KO)

More...KOi		K02998

Database of Orthologous Groups

More...OrthoDBi		1129610at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08865

TreeFam database of animal gene trees

More...TreeFami		TF300100

Family and domain databases

Conserved Domains Database

More...CDDi		cd01425 RPS2, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_03015 Ribosomal_S2_euk, 1 hit
MF_03016 Ribosomal_S2_laminin_receptor, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027504 40S_ribosomal_SA
IPR032281 40S_SA_C
IPR001865 Ribosomal_S2
IPR018130 Ribosomal_S2_CS
IPR027498 Ribosomal_S2_euk
IPR005707 Ribosomal_S2_euk/arc
IPR023591 Ribosomal_S2_flav_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR11489 PTHR11489, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16122 40S_SA_C, 1 hit
PF00318 Ribosomal_S2, 2 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00395 RIBOSOMALS2

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52313 SSF52313, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01012 uS2_euk_arch, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00962 RIBOSOMAL_S2_1, 1 hit
PS00963 RIBOSOMAL_S2_2, 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>Sequence (1+)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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P08865-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN 
        60         70         80         90        100
LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA 
       110        120        130        140        150
GRFTPGTFTN QIQAAFREPR LLVVTDPRAD HQPLTEASYV NLPTIALCNT 
       160        170        180        190        200
DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR EVLRMRGTIS REHPWEVMPD 
       210        220        230        240        250
LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA TQPEVADWSE 
       260        270        280        290 
GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTDWS
Length:295
Mass (Da):32,854
Last modified:January 23, 2007 - v4
<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:iC68DDB16B759E79E
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0C4DG17A0A0C4DG17_HUMAN
40S ribosomal protein SA
RPSA hCG_1997894
300Annotation 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>
C9J9K3C9J9K3_HUMAN
40S ribosomal protein SA
RPSA
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>
F8WD59F8WD59_HUMAN
40S ribosomal protein SA
RPSA
116Annotation 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 conflicti60L → V in CAA43469 (Ref. 9) Curated1
Sequence conflicti84Q → QVCGTV in CAA33112 (PubMed:2543954).Curated1
Sequence conflicti115A → T in AAH50688 (PubMed:15489334).Curated1
Sequence conflicti135T → S in AAH70263 (PubMed:15489334).Curated1
Sequence conflicti211E → G in AAB22299 (PubMed:1534510).Curated1
Sequence conflicti214E → G in AAH66941 (PubMed:15489334).Curated1
Sequence conflicti228Q → L in AAB22299 (PubMed:1534510).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07509254T → N in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514762EnsemblClinVar.1
Natural variantiVAR_07509358L → F in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514763EnsemblClinVar.1
Natural variantiVAR_025522117R → W1 PublicationCorresponds to variant dbSNP:rs17856150Ensembl.1
Natural variantiVAR_075094180R → G in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514760EnsemblClinVar.1
Natural variantiVAR_075095180R → W in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514760EnsemblClinVar.1
Natural variantiVAR_075096185M → V1 PublicationCorresponds to variant dbSNP:rs1214087389Ensembl.1
Natural variantiVAR_075097186R → C in ICAS; reduced protein levels. 1 PublicationCorresponds to variant dbSNP:rs397514761EnsemblClinVar.1
Natural variantiVAR_075098257V → G1 PublicationCorresponds to variant dbSNP:rs369708612Ensembl.1
Natural variantiVAR_075099278A → T1 PublicationCorresponds to variant dbSNP:rs143085301Ensembl.1

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
J03799 mRNA Translation: AAA36161.1
X15005 mRNA Translation: CAA33112.1
S37431 mRNA Translation: AAB22299.1
U43901 Genomic DNA Translation: AAC50652.1
AF503367 mRNA Translation: AAM33304.1
BT007219 mRNA Translation: AAP35883.1
BC005391 mRNA Translation: AAH05391.1
BC008867 mRNA Translation: AAH08867.1
BC010418 mRNA Translation: AAH10418.1
BC013827 mRNA Translation: AAH13827.1
BC034537 mRNA Translation: AAH34537.1
BC050688 mRNA Translation: AAH50688.1
BC053370 mRNA Translation: AAH53370.1
BC062714 mRNA Translation: AAH62714.1
BC066941 mRNA Translation: AAH66941.1
BC068062 mRNA Translation: AAH68062.1
BC070263 mRNA Translation: AAH70263.1
BC071693 mRNA Translation: AAH71693.1
BC071968 mRNA Translation: AAH71968.1
BC071969 mRNA Translation: AAH71969.1
BC071970 mRNA Translation: AAH71970.1
BC073863 mRNA Translation: AAH73863.1
BC107567 mRNA Translation: AAI07568.1
X61156 mRNA Translation: CAA43469.1
U36484 Genomic DNA Translation: AAC50313.1
M14199 mRNA Translation: AAA36165.1
AB007146 Genomic DNA Translation: BAA25812.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2686.1

Protein sequence database of the Protein Information Resource

More...PIRi		A31233

NCBI Reference Sequences

More...RefSeqi		NP_001291217.1, NM_001304288.1
NP_002286.2, NM_002295.5

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.449909

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000301821; ENSP00000346067; ENSG00000168028

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3921

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3921

UCSC genome browser

More...UCSCi		uc003cjp.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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
J03799 mRNA Translation: AAA36161.1
X15005 mRNA Translation: CAA33112.1
S37431 mRNA Translation: AAB22299.1
U43901 Genomic DNA Translation: AAC50652.1
AF503367 mRNA Translation: AAM33304.1
BT007219 mRNA Translation: AAP35883.1
BC005391 mRNA Translation: AAH05391.1
BC008867 mRNA Translation: AAH08867.1
BC010418 mRNA Translation: AAH10418.1
BC013827 mRNA Translation: AAH13827.1
BC034537 mRNA Translation: AAH34537.1
BC050688 mRNA Translation: AAH50688.1
BC053370 mRNA Translation: AAH53370.1
BC062714 mRNA Translation: AAH62714.1
BC066941 mRNA Translation: AAH66941.1
BC068062 mRNA Translation: AAH68062.1
BC070263 mRNA Translation: AAH70263.1
BC071693 mRNA Translation: AAH71693.1
BC071968 mRNA Translation: AAH71968.1
BC071969 mRNA Translation: AAH71969.1
BC071970 mRNA Translation: AAH71970.1
BC073863 mRNA Translation: AAH73863.1
BC107567 mRNA Translation: AAI07568.1
X61156 mRNA Translation: CAA43469.1
U36484 Genomic DNA Translation: AAC50313.1
M14199 mRNA Translation: AAA36165.1
AB007146 Genomic DNA Translation: BAA25812.1
CCDSiCCDS2686.1
PIRiA31233
RefSeqiNP_001291217.1, NM_001304288.1
NP_002286.2, NM_002295.5
UniGeneiHs.449909

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BCHX-ray2.15A2-220[»]
4UG0electron microscopy-SA1-295[»]
4V6Xelectron microscopy5.00AA1-295[»]
5A2Qelectron microscopy3.90A1-295[»]
5AJ0electron microscopy3.50BA1-295[»]
5FLXelectron microscopy3.90A1-295[»]
5LKSelectron microscopy3.60SA1-295[»]
5OA3electron microscopy4.30A1-295[»]
5T2Celectron microscopy3.60Ao1-295[»]
5VYCX-ray6.00A1/A2/A3/A4/A5/A61-295[»]
6EK0electron microscopy2.90SA1-295[»]
6FECelectron microscopy6.30f2-209[»]
6G18electron microscopy3.60A1-295[»]
6G4Selectron microscopy4.00A1-295[»]
6G51electron microscopy4.10A1-295[»]
6G53electron microscopy4.50A1-295[»]
6G5Helectron microscopy3.60A1-295[»]
6G5Ielectron microscopy3.50A1-295[»]
ProteinModelPortaliP08865
SMRiP08865
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110115, 236 interactors
CORUMiP08865
DIPiDIP-32878N
IntActiP08865, 49 interactors
MINTiP08865
STRINGi9606.ENSP00000346067

Chemistry databases

ChEMBLiCHEMBL6119
DrugBankiDB04985 PCK3145

PTM databases

iPTMnetiP08865
PhosphoSitePlusiP08865
SwissPalmiP08865

Polymorphism and mutation databases

BioMutaiRPSA
DMDMi125969

Proteomic databases

EPDiP08865
jPOSTiP08865
MaxQBiP08865
PaxDbiP08865
PeptideAtlasiP08865
PRIDEiP08865
ProteomicsDBi52170
TopDownProteomicsiP08865

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3921
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301821; ENSP00000346067; ENSG00000168028
GeneIDi3921
KEGGihsa:3921
UCSCiuc003cjp.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3921
DisGeNETi3921
EuPathDBiHostDB:ENSG00000168028.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		RPSA
HGNCiHGNC:6502 RPSA
HPAiCAB009561
MalaCardsiRPSA
MIMi150370 gene
271400 phenotype
neXtProtiNX_P08865
OpenTargetsiENSG00000168028
Orphaneti101351 Familial isolated congenital asplenia
PharmGKBiPA30287

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0830 Eukaryota
COG0052 LUCA
GeneTreeiENSGT00940000153327
HOVERGENiHBG054466
InParanoidiP08865
KOiK02998
OrthoDBi1129610at2759
PhylomeDBiP08865
TreeFamiTF300100

Enzyme and pathway databases

ReactomeiR-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-156902 Peptide chain elongation
R-HSA-1799339 SRP-dependent cotranslational protein targeting to membrane
R-HSA-192823 Viral mRNA Translation
R-HSA-2408557 Selenocysteine synthesis
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-HSA-72649 Translation initiation complex formation
R-HSA-72689 Formation of a pool of free 40S subunits
R-HSA-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-HSA-72702 Ribosomal scanning and start codon recognition
R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-HSA-72764 Eukaryotic Translation Termination
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
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		RPSA human
EvolutionaryTraceiP08865

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Ribosomal_protein_SA

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

More...GenomeRNAii		3921

Protein Ontology

More...PROi		PR:P08865

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000168028 Expressed in 88 organ(s), highest expression level in right uterine tube
ExpressionAtlasiP08865 baseline and differential
GenevisibleiP08865 HS

Family and domain databases

CDDicd01425 RPS2, 1 hit
HAMAPiMF_03015 Ribosomal_S2_euk, 1 hit
MF_03016 Ribosomal_S2_laminin_receptor, 1 hit
InterProiView protein in InterPro
IPR027504 40S_ribosomal_SA
IPR032281 40S_SA_C
IPR001865 Ribosomal_S2
IPR018130 Ribosomal_S2_CS
IPR027498 Ribosomal_S2_euk
IPR005707 Ribosomal_S2_euk/arc
IPR023591 Ribosomal_S2_flav_dom_sf
PANTHERiPTHR11489 PTHR11489, 1 hit
PfamiView protein in Pfam
PF16122 40S_SA_C, 1 hit
PF00318 Ribosomal_S2, 2 hits
PRINTSiPR00395 RIBOSOMALS2
SUPFAMiSSF52313 SSF52313, 1 hit
TIGRFAMsiTIGR01012 uS2_euk_arch, 1 hit
PROSITEiView protein in PROSITE
PS00962 RIBOSOMAL_S2_1, 1 hit
PS00963 RIBOSOMAL_S2_2, 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 nameiRSSA_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: P08865
Secondary accession number(s): P11085
, P12030, Q16471, Q6IPD1, Q6IPD2, Q6NSD1, Q6NXQ8, Q86VC0
<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 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 214 of the entry and version 4 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
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