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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

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-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
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541T → N in ICAS; reduced protein levels. 1 Publication
VAR_075092
Natural varianti58 – 581L → F in ICAS; reduced protein levels. 1 Publication
VAR_075093
Natural varianti180 – 1801R → G in ICAS; reduced protein levels. 1 Publication
VAR_075094
Natural varianti180 – 1801R → W in ICAS; reduced protein levels. 1 Publication
VAR_075095
Natural varianti186 – 1861R → C in ICAS; reduced protein levels. 1 Publication
VAR_075097

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL6119.

Polymorphism and mutation databases

BioMutaiRPSA.
DMDMi125969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotationCombined sources1 Publication
Chaini2 – 29529440S ribosomal protein SAPRO_0000134358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotationCombined sources1 Publication
Modified residuei52 – 521N6-acetyllysineCombined sources
Modified residuei89 – 891N6-acetyllysineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei115 – 1162Cleavage; by ST3; site 1UniRule annotation
Sitei133 – 1342Cleavage; by ST3; site 2UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP08865.
MaxQBiP08865.
PaxDbiP08865.
PRIDEiP08865.
TopDownProteomicsiP08865.

PTM databases

iPTMnetiP08865.
PhosphoSiteiP08865.
SwissPalmiP08865.

Expressioni

Gene expression databases

BgeeiP08865.
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. 216 interactions.
DIPiDIP-32878N.
IntActiP08865. 41 interactions.
MINTiMINT-1402850.
STRINGi9606.ENSP00000346067.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2110Combined sources
Turni22 – 243Combined sources
Helixi32 – 376Combined sources
Beta strandi38 – 414Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 6616Combined sources
Helixi71 – 733Combined sources
Beta strandi74 – 785Combined sources
Helixi81 – 9414Combined sources
Beta strandi97 – 1015Combined sources
Turni105 – 1095Combined sources
Beta strandi120 – 1256Combined sources
Turni127 – 1304Combined sources
Helixi131 – 1399Combined sources
Beta strandi144 – 1485Combined sources
Beta strandi158 – 1636Combined sources
Helixi168 – 18518Combined sources
Beta strandi191 – 1933Combined sources
Helixi199 – 2024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 9-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08865.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati230 – 2323[DE]-W-[ST] 1
Repeati247 – 2493[DE]-W-[ST] 2
Repeati266 – 2683[DE]-W-[ST] 3
Repeati275 – 2773[DE]-W-[ST] 4
Repeati293 – 2953[DE]-W-[ST] 5

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 11360Interaction with PPP1R16BAdd
BLAST
Regioni161 – 18020Laminin-bindingAdd
BLAST
Regioni205 – 22925Laminin-bindingAdd
BLAST
Regioni242 – 29554Laminin-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOVERGENiHBG054466.
InParanoidiP08865.
KOiK02998.
OrthoDBiEOG73NG4F.
PhylomeDBiP08865.
TreeFamiTF300100.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601L → V in CAA43469 (Ref. 9) Curated
Sequence conflicti84 – 841Q → QVCGTV in CAA33112 (PubMed:2543954).Curated
Sequence conflicti115 – 1151A → T in AAH50688 (PubMed:15489334).Curated
Sequence conflicti135 – 1351T → S in AAH70263 (PubMed:15489334).Curated
Sequence conflicti211 – 2111E → G in AAB22299 (PubMed:1534510).Curated
Sequence conflicti214 – 2141E → G in AAH66941 (PubMed:15489334).Curated
Sequence conflicti228 – 2281Q → L in AAB22299 (PubMed:1534510).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541T → N in ICAS; reduced protein levels. 1 Publication
VAR_075092
Natural varianti58 – 581L → F in ICAS; reduced protein levels. 1 Publication
VAR_075093
Natural varianti117 – 1171R → W.1 Publication
Corresponds to variant rs17856150 [ dbSNP | Ensembl ].
VAR_025522
Natural varianti180 – 1801R → G in ICAS; reduced protein levels. 1 Publication
VAR_075094
Natural varianti180 – 1801R → W in ICAS; reduced protein levels. 1 Publication
VAR_075095
Natural varianti185 – 1851M → V.1 Publication
VAR_075096
Natural varianti186 – 1861R → C in ICAS; reduced protein levels. 1 Publication
VAR_075097
Natural varianti257 – 2571V → G.1 Publication
VAR_075098
Natural varianti278 – 2781A → T.1 Publication
VAR_075099

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
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. Positions 9-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110115. 216 interactions.
DIPiDIP-32878N.
IntActiP08865. 41 interactions.
MINTiMINT-1402850.
STRINGi9606.ENSP00000346067.

Chemistry

ChEMBLiCHEMBL6119.

PTM databases

iPTMnetiP08865.
PhosphoSiteiP08865.
SwissPalmiP08865.

Polymorphism and mutation databases

BioMutaiRPSA.
DMDMi125969.

Proteomic databases

EPDiP08865.
MaxQBiP08865.
PaxDbiP08865.
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.
GeneCardsiRPSA.
HGNCiHGNC:6502. RPSA.
HPAiCAB009561.
MalaCardsiRPSA.
MIMi150370. gene.
271400. phenotype.
neXtProtiNX_P08865.
Orphaneti101351. Familial isolated congenital asplenia.
PharmGKBiPA30287.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOVERGENiHBG054466.
InParanoidiP08865.
KOiK02998.
OrthoDBiEOG73NG4F.
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-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.
NextBioi15405.
PROiP08865.
SOURCEiSearch...

Gene expression databases

BgeeiP08865.
ExpressionAtlasiP08865. baseline and differential.
GenevisibleiP08865. HS.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein."
    Yow H., Wong J.M., Chen H.S., Lee C., Steele G.D. Jr., Chen L.B.
    Proc. Natl. Acad. Sci. U.S.A. 85:6394-6398(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characteristics of a multicopy gene family predominantly consisting of processed pseudogenes."
    van den Ouweland A.M.W., van Duijnhoven H.L.P., Deichmann K.A., van Groningen J.J.M., de Leij L., van de Ven W.J.M.
    Nucleic Acids Res. 17:3829-3843(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung."
    Satoh K., Narumi K., Sakai T., Abe T., Kikuchi T., Matsushima K., Sindoh S., Motomiya M.
    Cancer Lett. 62:199-203(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  4. "Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3."
    Jackers P., Minoletti F., Belotti D., Clausse N., Sozzi G., Sobel M.E., Castronovo V.
    Oncogene 13:495-503(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Multidrug resistance associated protein MGr1-Ag is identical to human 67-KDa laminin receptor precursor."
    Shi Y., Zhai H., Wang X., Wu H., Ning X., Han Y., Zhang D., Xiao B., Wu K., Fan D.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-117.
    Tissue: Bone marrow, Brain, Cervix, Hippocampus, Liver, Lung, Lymph, Placenta, Prostate, Skin and Urinary bladder.
  8. Bienvenut W.V., Potts A., Barblan J., Quadroni M.
    Submitted (JUL-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  9. "Determination and analysis of the primary sequence of human laminin-binding protein."
    Siyanova E.Y., Lukashev V.A., Blinov V.M., Troyanovskii S.M.
    Dokl. Biochem. 313:227-231(1990)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-295.
  10. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
    Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
    Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-26 AND 90-99.
  11. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 43-52; 64-80; 103-117; 129-155 AND 192-205, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  12. "The gene for human E2 small nucleolar RNA resides in an intron of a laminin-binding protein gene."
    Selvamurugan N., Eliceiri G.L.
    Genomics 30:400-401(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-209.
    Tissue: Blood.
  13. "Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin."
    Wewer U.M., Liotta L.A., Jaye M., Ricca G.A., Drohan W.N., Claysmith A.P., Rao C.N., Wirth P., Coligan J.E., Albrechtsen R., Mudryj M., Sobel M.E.
    Proc. Natl. Acad. Sci. U.S.A. 83:7137-7141(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-295, PROTEIN SEQUENCE OF 177-184.
  14. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-295.
  15. Cited for: FUNCTION, INTERACTION WITH LAMININ-1.
  16. "Functional domains of the 67-kDa laminin receptor precursor."
    Castronovo V., Taraboletti G., Sobel M.E.
    J. Biol. Chem. 266:20440-20446(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS, INTERACTION WITH LAMININ-1.
  17. "High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells."
    Wang K.-S., Kuhn R.J., Strauss E.G., Ou S., Strauss J.H.
    J. Virol. 66:4992-5001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SINDBIS VIRUS E2 ENVELOPE GLYCOPROTEIN.
  18. "Interaction between the 67 kilodalton metastasis-associated laminin receptor and laminin."
    Cioce V., Margulies I.M.K., Sobel M.E., Castronovo V.
    Kidney Int. 43:30-37(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAMININ-1.
  19. "A putative receptor for Venezuelan equine encephalitis virus from mosquito cells."
    Ludwig G.V., Kondig J.P., Smith J.F.
    J. Virol. 70:5592-5599(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH VENEZUELAN EQUINE ENCEPHALITIS VIRUS E2 GLYCOPROTEIN.
  20. "The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells."
    Rieger R., Edenhofer F., Lasmezas C.I., Weiss S.
    Nat. Med. 3:1383-1388(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRNP.
  21. Cited for: ACYLATION.
  22. "The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution."
    Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V., Sobel M.E., Colnaghi M.I., Menard S.
    Mol. Biol. Evol. 15:1017-1025(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAMININ-5.
  23. "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system."
    Sato M., Saeki Y., Tanaka K., Kaneda Y.
    Biochem. Biophys. Res. Commun. 256:385-390(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS21.
  24. "Phage display mapping for peptide 11 sensitive sequences binding to laminin-1."
    Kazmin D.A., Hoyt T.R., Taubner L., Teintze M., Starkey J.R.
    J. Mol. Biol. 298:431-445(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAMB1.
  25. "The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein."
    Gauczynski S., Peyrin J.-M., Haik S., Leucht C., Hundt C., Rieger R., Krasemann S., Deslys J.-P., Dormont D., Lasmezas C.I., Weiss S.
    EMBO J. 20:5863-5875(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION-BINDING, SUBCELLULAR LOCATION, SUBUNIT.
  26. "Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor."
    Thepparit C., Smith D.R.
    J. Virol. 78:12647-12656(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH DENGUE VIRUS ENVELOPE PROTEIN E.
  27. "The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1 phosphorylation."
    Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.
    Biochem. Biophys. Res. Commun. 338:1327-1334(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PPP1R16B AND PPP1CA.
  28. "67-kDa laminin receptor promotes internalization of cytotoxic necrotizing factor 1-expressing Escherichia coli K1 into human brain microvascular endothelial cells."
    Kim K.J., Chung J.W., Kim K.S.
    J. Biol. Chem. 280:1360-1368(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION).
  29. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9."
    Akache B., Grimm D., Pandey K., Yant S.R., Xu H., Kay M.A.
    J. Virol. 80:9831-9836(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH ADENO-ASSOCIATED VIRUS CAPSID PROTEINS.
  31. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. Cited for: INVOLVEMENT IN ICAS, VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 AND CYS-186, CHARACTERIZATION OF VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 AND CYS-186, VARIANTS VAL-185; GLY-257 AND THR-278.
  36. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  37. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "Crystal structure of the human laminin receptor precursor."
    Jamieson K.V., Wu J., Hubbard S.R., Meruelo D.
    J. Biol. Chem. 283:3002-3005(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 9-205.

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: April 13, 2016
This is version 188 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.