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P08865

- RSSA_HUMAN

UniProt

P08865 - RSSA_HUMAN

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Protein
40S ribosomal protein SA
Gene
RPSA, LAMBR, LAMR1
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei115 – 1162Cleavage; by ST3; site 1 By similarity
Sitei133 – 1342Cleavage; by ST3; site 2 By similarity

GO - Molecular functioni

  1. laminin receptor activity Source: UniProtKB-HAMAP
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. ribosome binding Source: UniProtKB
  5. structural constituent of ribosome Source: RefGenome

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  3. cell adhesion Source: ProtInc
  4. cellular protein metabolic process Source: Reactome
  5. endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: RefGenome
  6. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: RefGenome
  7. gene expression Source: Reactome
  8. mRNA metabolic process Source: Reactome
  9. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  10. rRNA export from nucleus Source: RefGenome
  11. ribosomal small subunit assembly Source: RefGenome
  12. translation Source: UniProtKB
  13. translational elongation Source: Reactome
  14. translational initiation Source: Reactome
  15. translational termination Source: Reactome
  16. viral life cycle Source: Reactome
  17. viral process Source: Reactome
  18. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor, Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein SA
Alternative name(s):
37 kDa laminin receptor precursor
Short name:
37LRP
37/67 kDa laminin receptor
Short name:
LRP/LR
67 kDa laminin receptor
Short name:
67LR
Colon carcinoma laminin-binding protein
Laminin receptor 1
Short name:
LamR
Laminin-binding protein precursor p40
Short name:
LBP/p40
Multidrug resistance-associated protein MGr1-Ag
NEM/1CHD4
Gene namesi
Name:RPSA
Synonyms:LAMBR, LAMR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6502. RPSA.

Subcellular locationi

Cell membrane. Cytoplasm. Nucleus By similarity
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.2 Publications

GO - Cellular componenti

  1. 90S preribosome Source: RefGenome
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. cytosolic small ribosomal subunit Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti101351. Familial isolated congenital asplenia.
PharmGKBiPA30287.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 29529440S ribosomal protein SAUniRule annotation
PRO_0000134358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei89 – 891N6-acetyllysine By similarity
Modified residuei139 – 1391PhosphotyrosineUniRule annotation
Modified residuei241 – 2411PhosphothreonineUniRule annotation

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 (1 Publication).UniRule annotation
Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP08865.
PaxDbiP08865.
PRIDEiP08865.

PTM databases

PhosphoSiteiP08865.

Expressioni

Gene expression databases

BgeeiP08865.
GenevestigatoriP08865.

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. Interacts with PRNP. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B.9 Publications

Protein-protein interaction databases

BioGridi110115. 157 interactions.
DIPiDIP-32878N.
IntActiP08865. 25 interactions.
MINTiMINT-1402850.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BCHX-ray2.15A2-220[»]
3J3Aelectron microscopy5.00A1-295[»]
ProteinModelPortaliP08865.
SMRiP08865. Positions 9-205.

Miscellaneous databases

EvolutionaryTraceiP08865.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 11360Interaction with PPP1R16BUniRule annotation
Add
BLAST
Regioni161 – 18020Laminin-bindingUniRule annotation
Add
BLAST
Regioni205 – 22925Laminin-bindingUniRule annotation
Add
BLAST
Regioni242 – 29554Laminin-bindingUniRule annotation
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0052.
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.
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.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. Sa_S2_E_A. 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

MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN    50
LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA 100
GRFTPGTFTN QIQAAFREPR LLVVTDPRAD HQPLTEASYV NLPTIALCNT 150
DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR EVLRMRGTIS REHPWEVMPD 200
LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA TQPEVADWSE 250
GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTDWS 295
Length:295
Mass (Da):32,854
Last modified:January 23, 2007 - v4
Checksum:iC68DDB16B759E79E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171R → W.1 Publication
Corresponds to variant rs17856150 [ dbSNP | Ensembl ].
VAR_025522

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601L → V in CAA43469. 1 Publication
Sequence conflicti84 – 841Q → QVCGTV in CAA33112. 1 Publication
Sequence conflicti115 – 1151A → T in AAH50688. 1 Publication
Sequence conflicti135 – 1351T → S in AAH70263. 1 Publication
Sequence conflicti211 – 2111E → G in AAB22299. 1 Publication
Sequence conflicti214 – 2141E → G in AAH66941. 1 Publication
Sequence conflicti228 – 2281Q → L in AAB22299. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001012321.1. NM_001012321.1.
NP_002286.2. NM_002295.4.
UniGeneiHs.449909.

Genome annotation databases

EnsembliENST00000301821; ENSP00000346067; ENSG00000168028.
ENST00000443003; ENSP00000389351; ENSG00000168028.
GeneIDi3921.
KEGGihsa:3921.
UCSCiuc003cjp.3. human.

Polymorphism databases

DMDMi125969.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2686.1.
PIRi A31233.
RefSeqi NP_001012321.1. NM_001012321.1.
NP_002286.2. NM_002295.4.
UniGenei Hs.449909.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BCH X-ray 2.15 A 2-220 [» ]
3J3A electron microscopy 5.00 A 1-295 [» ]
ProteinModelPortali P08865.
SMRi P08865. Positions 9-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110115. 157 interactions.
DIPi DIP-32878N.
IntActi P08865. 25 interactions.
MINTi MINT-1402850.

Chemistry

ChEMBLi CHEMBL6119.

PTM databases

PhosphoSitei P08865.

Polymorphism databases

DMDMi 125969.

Proteomic databases

MaxQBi P08865.
PaxDbi P08865.
PRIDEi P08865.

Protocols and materials databases

DNASUi 3921.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301821 ; ENSP00000346067 ; ENSG00000168028 .
ENST00000443003 ; ENSP00000389351 ; ENSG00000168028 .
GeneIDi 3921.
KEGGi hsa:3921.
UCSCi uc003cjp.3. human.

Organism-specific databases

CTDi 3921.
GeneCardsi GC03P039448.
HGNCi HGNC:6502. RPSA.
HPAi CAB009561.
MIMi 150370. gene.
neXtProti NX_P08865.
Orphaneti 101351. Familial isolated congenital asplenia.
PharmGKBi PA30287.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0052.
HOVERGENi HBG054466.
InParanoidi P08865.
KOi K02998.
OrthoDBi EOG73NG4F.
PhylomeDBi P08865.
TreeFami TF300100.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSi RPSA. human.
EvolutionaryTracei P08865.
GeneWikii Ribosomal_protein_SA.
GenomeRNAii 3921.
NextBioi 15405.
PROi P08865.
SOURCEi Search...

Gene expression databases

Bgeei P08865.
Genevestigatori P08865.

Family and domain databases

HAMAPi MF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
InterProi IPR027504. 40S_ribosomal_SA.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view ]
PANTHERi PTHR11489. PTHR11489. 1 hit.
Pfami PF00318. Ribosomal_S2. 1 hit.
[Graphical view ]
PRINTSi PR00395. RIBOSOMALS2.
SUPFAMi SSF52313. SSF52313. 1 hit.
TIGRFAMsi TIGR01012. Sa_S2_E_A. 1 hit.
PROSITEi PS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 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. "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.
  18. "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.
  19. Cited for: ACYLATION.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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 AS A RECEPTOR FOR BACTERIA.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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: September 3, 2014
This is version 170 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

External Data

Dasty 3

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