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Protein

40S ribosomal protein SA

Gene

RPSA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

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)

Names & Taxonomyi

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
Gene namesi
Name:RPSAUniRule annotation
Synonyms:LAMBR, LAMR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000168028.13
HGNCiHGNC:6502 RPSA
MIMi150370 gene
neXtProtiNX_P08865

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

Pathology & Biotechi

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
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

DisGeNETi3921
MalaCardsiRPSA
MIMi271400 phenotype
OpenTargetsiENSG00000168028
Orphaneti101351 Familial isolated congenital asplenia
PharmGKBiPA30287

Chemistry databases

ChEMBLiCHEMBL6119
DrugBankiDB04985 PCK3145

Polymorphism and mutation databases

BioMutaiRPSA
DMDMi125969

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotationCombined sources1 Publication
ChainiPRO_00001343582 – 29540S ribosomal protein SAAdd BLAST294

Amino acid modifications

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

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
Sitei115 – 116Cleavage; by ST3; site 1UniRule annotation2
Sitei133 – 134Cleavage; by ST3; site 2UniRule annotation2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP08865
MaxQBiP08865
PaxDbiP08865
PeptideAtlasiP08865
PRIDEiP08865
TopDownProteomicsiP08865

PTM databases

iPTMnetiP08865
PhosphoSitePlusiP08865
SwissPalmiP08865

Expressioni

Gene expression databases

BgeeiENSG00000168028
ExpressionAtlasiP08865 baseline and differential
GenevisibleiP08865 HS

Organism-specific databases

HPAiCAB009561

Interactioni

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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi110115, 227 interactors
CORUMiP08865
DIPiDIP-32878N
IntActiP08865, 45 interactors
MINTiP08865
STRINGi9606.ENSP00000346067

Structurei

Secondary structure

1295
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 21Combined sources10
Turni22 – 24Combined sources3
Helixi32 – 37Combined sources6
Beta strandi38 – 41Combined sources4
Beta strandi47 – 49Combined sources3
Helixi51 – 66Combined sources16
Helixi71 – 73Combined sources3
Beta strandi74 – 78Combined sources5
Helixi81 – 94Combined sources14
Beta strandi97 – 101Combined sources5
Turni105 – 109Combined sources5
Beta strandi120 – 125Combined sources6
Turni127 – 130Combined sources4
Helixi131 – 139Combined sources9
Beta strandi144 – 148Combined sources5
Beta strandi158 – 163Combined sources6
Helixi168 – 185Combined sources18
Beta strandi191 – 193Combined sources3
Helixi199 – 202Combined sources4

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[»]
ProteinModelPortaliP08865
SMRiP08865
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08865

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni54 – 113Interaction with PPP1R16B1 PublicationAdd BLAST60
Regioni161 – 180Laminin-bindingAdd BLAST20
Regioni205 – 229Laminin-bindingAdd BLAST25
Regioni242 – 295Laminin-bindingAdd BLAST54

Sequence similaritiesi

Belongs to the universal ribosomal protein uS2 family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0830 Eukaryota
COG0052 LUCA
GeneTreeiENSGT00390000015036
HOVERGENiHBG054466
InParanoidiP08865
KOiK02998
PhylomeDBiP08865
TreeFamiTF300100

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

Sequencei

Sequence statusi: Complete.

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

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
Checksum:iC68DDB16B759E79E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 Publication1
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:
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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRSSA_HUMAN
AccessioniPrimary (citable) accession number: P08865
Secondary accession number(s): P11085
, P12030, Q16471, Q6IPD1, Q6IPD2, Q6NSD1, Q6NXQ8, Q86VC0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 207 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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