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P08865 (RSSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RPSA
Synonyms:LAMBR, LAMR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.24 Ref.25

Subunit structure

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. Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Subcellular location

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. Ref.23 Ref.24

Post-translational modification

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 (Ref.19). HAMAP-Rule MF_03016

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. HAMAP-Rule MF_03016

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.

Sequence similarities

Belongs to the ribosomal protein S2P family.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionReceptor
Ribonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cell adhesion

Non-traceable author statement PubMed 2970671. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

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)

Inferred from Biological aspect of Ancestor. Source: RefGenome

endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from Biological aspect of Ancestor. Source: RefGenome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

rRNA export from nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

ribosomal small subunit assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

translation

Inferred by curator Ref.10. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_component90S preribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay Ref.24. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay Ref.10. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Traceable author statement PubMed 16130169. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.24. Source: UniProtKB

   Molecular_functionlaminin receptor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.24. Source: UniProtKB

ribosome binding

Inferred from physical interaction Ref.21. Source: UniProtKB

structural constituent of ribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 29529440S ribosomal protein SA HAMAP-Rule MF_03016
PRO_0000134358

Regions

Repeat230 – 2323[DE]-W-[ST] 1 HAMAP-Rule MF_03016
Repeat247 – 2493[DE]-W-[ST] 2 HAMAP-Rule MF_03016
Repeat266 – 2683[DE]-W-[ST] 3 HAMAP-Rule MF_03016
Repeat275 – 2773[DE]-W-[ST] 4 HAMAP-Rule MF_03016
Repeat293 – 2953[DE]-W-[ST] 5 HAMAP-Rule MF_03016
Region54 – 11360Interaction with PPP1R16B HAMAP-Rule MF_03016
Region161 – 18020Laminin-binding HAMAP-Rule MF_03016
Region205 – 22925Laminin-binding HAMAP-Rule MF_03016
Region242 – 29554Laminin-binding HAMAP-Rule MF_03016

Sites

Site115 – 1162Cleavage; by ST3; site 1 By similarity
Site133 – 1342Cleavage; by ST3; site 2 By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue891N6-acetyllysine By similarity
Modified residue1391Phosphotyrosine HAMAP-Rule MF_03016
Modified residue2411Phosphothreonine HAMAP-Rule MF_03016

Natural variations

Natural variant1171R → W. Ref.7
Corresponds to variant rs17856150 [ dbSNP | Ensembl ].
VAR_025522

Experimental info

Sequence conflict601L → V in CAA43469. Ref.9
Sequence conflict841Q → QVCGTV in CAA33112. Ref.2
Sequence conflict1151A → T in AAH50688. Ref.7
Sequence conflict1351T → S in AAH70263. Ref.7
Sequence conflict2111E → G in AAB22299. Ref.3
Sequence conflict2141E → G in AAH66941. Ref.7
Sequence conflict2281Q → L in AAB22299. Ref.3

Secondary structure

................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08865 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C68DDB16B759E79E

FASTA29532,854
        10         20         30         40         50         60 
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL 

        70         80         90        100        110        120 
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR 

       130        140        150        160        170        180 
LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR 

       190        200        210        220        230        240 
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA 

       250        260        270        280        290 
TQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTDWS 

« Hide

References

« Hide 'large scale' references
[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]"Laminin receptor on human breast carcinoma cells."
Terranova V.P., Rao C.N., Kalebic T., Margulies I.M., Liotta L.A.
Proc. Natl. Acad. Sci. U.S.A. 80:444-448(1983) [PubMed] [Europe PMC] [Abstract]
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]"Formation of the 67-kDa laminin receptor by acylation of the precursor."
Buto S., Tagliabue E., Ardini E., Magnifico A., Ghirelli C., van den Brule F., Castronovo V., Colnaghi M.I., Sobel M.E., Menard S.
J. Cell. Biochem. 69:244-251(1998) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2686.1.
PIRA31233.
RefSeqNP_001012321.1. NM_001012321.1.
NP_002286.2. NM_002295.4.
UniGeneHs.449909.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BCHX-ray2.15A2-220[»]
3J3Aelectron microscopy5.00A1-295[»]
ProteinModelPortalP08865.
SMRP08865. Positions 9-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110115. 156 interactions.
DIPDIP-32878N.
IntActP08865. 25 interactions.
MINTMINT-1402850.

Chemistry

ChEMBLCHEMBL6119.

PTM databases

PhosphoSiteP08865.

Polymorphism databases

DMDM125969.

Proteomic databases

MaxQBP08865.
PaxDbP08865.
PRIDEP08865.

Protocols and materials databases

DNASU3921.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301821; ENSP00000346067; ENSG00000168028.
ENST00000443003; ENSP00000389351; ENSG00000168028.
GeneID3921.
KEGGhsa:3921.
UCSCuc003cjp.3. human.

Organism-specific databases

CTD3921.
GeneCardsGC03P039448.
HGNCHGNC:6502. RPSA.
HPACAB009561.
MIM150370. gene.
neXtProtNX_P08865.
Orphanet101351. Familial isolated congenital asplenia.
PharmGKBPA30287.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0052.
HOVERGENHBG054466.
InParanoidP08865.
KOK02998.
OrthoDBEOG73NG4F.
PhylomeDBP08865.
TreeFamTF300100.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP08865.
GenevestigatorP08865.

Family and domain databases

HAMAPMF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
InterProIPR027504. 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]
PANTHERPTHR11489. PTHR11489. 1 hit.
PfamPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSPR00395. RIBOSOMALS2.
SUPFAMSSF52313. SSF52313. 1 hit.
TIGRFAMsTIGR01012. Sa_S2_E_A. 1 hit.
PROSITEPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPSA. human.
EvolutionaryTraceP08865.
GeneWikiRibosomal_protein_SA.
GenomeRNAi3921.
NextBio15405.
PROP08865.
SOURCESearch...

Entry information

Entry nameRSSA_HUMAN
AccessionPrimary (citable) accession number: P08865
Secondary accession number(s): P11085 expand/collapse secondary AC list , P12030, Q16471, Q6IPD1, Q6IPD2, Q6NSD1, Q6NXQ8, Q86VC0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 169 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM