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P08865

- RSSA_HUMAN

UniProt

P08865 - RSSA_HUMAN

Protein

40S ribosomal protein SA

Gene

RPSA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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 PublicationsUniRule annotation

    Sites

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

    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. cell adhesion Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. 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
    4. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: RefGenome
    5. gene expression Source: Reactome
    6. mRNA metabolic process Source: Reactome
    7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    8. ribosomal small subunit assembly Source: RefGenome
    9. RNA metabolic process Source: Reactome
    10. rRNA export from nucleus Source: RefGenome
    11. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    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

    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 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
    ProteomesiUP000005640: 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

    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. membrane Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    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 PublicationUniRule annotation
    Chaini2 – 29529440S ribosomal protein SAPRO_0000134358Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 PublicationUniRule annotation
    Modified residuei89 – 891N6-acetyllysineBy similarity
    Modified residuei139 – 1391Phosphotyrosine1 Publication
    Modified residuei241 – 2411Phosphothreonine1 Publication

    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).1 PublicationUniRule annotation
    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

    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 PublicationsUniRule annotation

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi110115. 157 interactions.
    DIPiDIP-32878N.
    IntActiP08865. 27 interactions.
    MINTiMINT-1402850.

    Structurei

    Secondary structure

    1
    295
    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.
    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601L → V in CAA43469. 1 PublicationCurated
    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 varianti117 – 1171R → W.1 Publication
    Corresponds to variant rs17856150 [ dbSNP | Ensembl ].
    VAR_025522

    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. 27 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

    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: October 1, 2014
    This is version 171 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