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Protein

40S ribosomal protein SA

Gene

RPSA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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, dengue virus, Sindbis virus and Venezuelan equine encephalitis virus (PubMed:1385835, PubMed:15507651, PubMed:16973587). Also acts as a receptor for pathogenic prion protein and bacteria (PubMed:9396609, PubMed:11689427, PubMed:15516338).6 Publications

GO - Molecular functioni

  • laminin receptor activity Source: UniProtKB-HAMAP
  • poly(A) RNA binding Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168028-MONOMER.
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-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
Gene namesi
Name:RPSAUniRule annotation
Synonyms:LAMBR, LAMR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6502. RPSA.

Subcellular locationi

  • Cell membrane
  • Cytoplasm
  • Nucleus UniRule annotation

  • Note: 67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus (By similarity). Colocalizes with PPP1R16B in the cell membrane.UniRule annotation

GO - Cellular componenti

  • 90S preribosome Source: GO_Central
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

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 rs397514762dbSNPEnsembl.1
Natural variantiVAR_07509358L → F in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514763dbSNPEnsembl.1
Natural variantiVAR_075094180R → G in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514760dbSNPEnsembl.1
Natural variantiVAR_075095180R → W in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514760dbSNPEnsembl.1
Natural variantiVAR_075097186R → C in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514761dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3921.
MalaCardsiRPSA.
MIMi271400. phenotype.
OpenTargetsiENSG00000168028.
Orphaneti101351. Familial isolated congenital asplenia.
PharmGKBiPA30287.

Chemistry databases

ChEMBLiCHEMBL6119.

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-acetyllysineBy similarity1
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, Phosphoprotein

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

WithEntry#Exp.IntActNotes
KARSQ150465EBI-354112,EBI-356367
TINF2Q9BSI42EBI-354112,EBI-717399

Protein-protein interaction databases

BioGridi110115. 218 interactors.
DIPiDIP-32878N.
IntActiP08865. 41 interactors.
MINTiMINT-1402850.
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[»]
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 ribosomal protein S2P 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.
InterProiIPR027504. 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.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

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 rs397514762dbSNPEnsembl.1
Natural variantiVAR_07509358L → F in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514763dbSNPEnsembl.1
Natural variantiVAR_025522117R → W.1 PublicationCorresponds to variant rs17856150dbSNPEnsembl.1
Natural variantiVAR_075094180R → G in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514760dbSNPEnsembl.1
Natural variantiVAR_075095180R → W in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514760dbSNPEnsembl.1
Natural variantiVAR_075096185M → V.1 Publication1
Natural variantiVAR_075097186R → C in ICAS; reduced protein levels. 1 PublicationCorresponds to variant rs397514761dbSNPEnsembl.1
Natural variantiVAR_075098257V → G.1 PublicationCorresponds to variant rs369708612dbSNPEnsembl.1
Natural variantiVAR_075099278A → T.1 PublicationCorresponds to variant rs143085301dbSNPEnsembl.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

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

Protein-protein interaction databases

BioGridi110115. 218 interactors.
DIPiDIP-32878N.
IntActiP08865. 41 interactors.
MINTiMINT-1402850.
STRINGi9606.ENSP00000346067.

Chemistry databases

ChEMBLiCHEMBL6119.

PTM databases

iPTMnetiP08865.
PhosphoSitePlusiP08865.
SwissPalmiP08865.

Polymorphism and mutation databases

BioMutaiRPSA.
DMDMi125969.

Proteomic databases

EPDiP08865.
MaxQBiP08865.
PaxDbiP08865.
PeptideAtlasiP08865.
PRIDEiP08865.
TopDownProteomicsiP08865.

Protocols and materials databases

DNASUi3921.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3921.
DisGeNETi3921.
GeneCardsiRPSA.
HGNCiHGNC:6502. RPSA.
HPAiCAB009561.
MalaCardsiRPSA.
MIMi150370. gene.
271400. phenotype.
neXtProtiNX_P08865.
OpenTargetsiENSG00000168028.
Orphaneti101351. Familial isolated congenital asplenia.
PharmGKBiPA30287.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOVERGENiHBG054466.
InParanoidiP08865.
KOiK02998.
PhylomeDBiP08865.
TreeFamiTF300100.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168028-MONOMER.
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-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

ChiTaRSiRPSA. human.
EvolutionaryTraceiP08865.
GeneWikiiRibosomal_protein_SA.
GenomeRNAii3921.
PROiP08865.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168028.
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.
InterProiIPR027504. 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.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRSSA_HUMAN
AccessioniPrimary (citable) accession number: P08865
Secondary accession number(s): P11085
, P12030, Q16471, Q6IPD1, Q6IPD2, Q6NSD1, Q6NXQ8, Q86VC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 193 of the entry and version 4 of the sequence. [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

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.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.