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P62753

- RS6_HUMAN

UniProt

P62753 - RS6_HUMAN

Protein

40S ribosomal protein S6

Gene

RPS6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. glucose homeostasis Source: UniProtKB
    4. insulin receptor signaling pathway Source: Reactome
    5. mRNA metabolic process Source: Reactome
    6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    7. positive regulation of apoptotic process Source: UniProtKB
    8. ribosomal small subunit biogenesis Source: UniProtKB
    9. RNA metabolic process Source: Reactome
    10. rRNA processing Source: UniProtKB
    11. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    12. TOR signaling Source: UniProtKB
    13. translation Source: UniProtKB
    14. translational elongation Source: Reactome
    15. translational initiation Source: Reactome
    16. translational termination Source: Reactome
    17. viral life cycle Source: Reactome
    18. viral process Source: Reactome
    19. viral transcription Source: Reactome

    Keywords - Molecular functioni

    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_6772. S6K1 signalling.
    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.
    SignaLinkiP62753.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    40S ribosomal protein S6
    Alternative name(s):
    Phosphoprotein NP33
    Gene namesi
    Name:RPS6
    ORF Names:OK/SW-cl.2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:10429. RPS6.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: ParkinsonsUK-UCL
    2. cytoplasm Source: HPA
    3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    4. cytosol Source: Reactome
    5. cytosolic small ribosomal subunit Source: UniProtKB
    6. dendrite Source: ParkinsonsUK-UCL
    7. membrane Source: UniProtKB
    8. nucleolus Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. ribonucleoprotein complex Source: MGI
    11. small ribosomal subunit Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi235 – 2362SS → AA: Abolishes phosphorylation by PASK. 1 Publication

    Organism-specific databases

    PharmGKBiPA34844.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24924940S ribosomal protein S6PRO_0000137312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111N6-acetyllysine1 Publication
    Modified residuei235 – 2351Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK4 Publications
    Modified residuei236 – 2361Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK5 Publications
    Modified residuei240 – 2401Phosphoserine3 Publications
    Modified residuei242 – 2421Phosphoserine1 Publication
    Modified residuei244 – 2441Phosphoserine1 Publication
    Modified residuei247 – 2471Phosphoserine1 Publication

    Post-translational modificationi

    Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes. The phosphorylation is stimulated by growth factors, tumor promoting agents, and mitogens. It is dephosphorylated at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the preinitiation complex.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62753.
    PaxDbiP62753.
    PRIDEiP62753.

    PTM databases

    PhosphoSiteiP62753.

    Expressioni

    Gene expression databases

    ArrayExpressiP62753.
    BgeeiP62753.
    CleanExiHS_RPS6.
    GenevestigatoriP62753.

    Organism-specific databases

    HPAiCAB004027.
    HPA031153.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCBP1Q091613EBI-356625,EBI-464743
    PASKQ96RG23EBI-356625,EBI-1042651

    Protein-protein interaction databases

    BioGridi112108. 165 interactions.
    DIPiDIP-31507N.
    IntActiP62753. 40 interactions.
    MINTiMINT-1162101.
    STRINGi9606.ENSP00000369757.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00G1-249[»]
    ProteinModelPortaliP62753.
    SMRiP62753. Positions 1-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S6e family.Curated

    Phylogenomic databases

    eggNOGiCOG2125.
    HOGENOMiHOG000190952.
    HOVERGENiHBG011441.
    InParanoidiP62753.
    KOiK02991.
    OMAiCQKLFEV.
    OrthoDBiEOG7Z0JXB.
    PhylomeDBiP62753.
    TreeFamiTF300035.

    Family and domain databases

    InterProiIPR014401. Ribosomal_S6_euk.
    IPR001377. Ribosomal_S6e.
    IPR018282. Ribosomal_S6e_CS.
    [Graphical view]
    PANTHERiPTHR11502. PTHR11502. 1 hit.
    PfamiPF01092. Ribosomal_S6e. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002129. Ribosom_S6_euk. 1 hit.
    PROSITEiPS00578. RIBOSOMAL_S6E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P62753-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV    50
    RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC 100
    IVDANLSVLN LVIVKKGEKD IPGLTDTTVP RRLGPKRASR IRKLFNLSKE 150
    DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV TPRVLQHKRR RIALKKQRTK 200
    KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS TSKSESSQK 249
    Length:249
    Mass (Da):28,681
    Last modified:August 1, 1988 - v1
    Checksum:iA61E435884E636AE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231K → T in AAA60288. (PubMed:2840355)Curated
    Sequence conflicti144 – 1441L → R in AAA60288. (PubMed:2840355)Curated
    Sequence conflicti155 – 1562QY → EC in AAA60287. (PubMed:3279029)Curated
    Sequence conflicti168 – 1681K → R in AAA60287. (PubMed:3279029)Curated
    Sequence conflicti196 – 1961K → Q in AAA60288. (PubMed:2840355)Curated
    Sequence conflicti219 – 2191E → Q in AAA60287. (PubMed:3279029)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211K → R.1 Publication
    Corresponds to variant rs17852447 [ dbSNP | Ensembl ].
    VAR_025314

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20020 mRNA. Translation: AAA60288.1.
    J03537 mRNA. Translation: AAA60287.1.
    X67309 Genomic DNA. Translation: CAA47719.1.
    M77232 Genomic DNA. Translation: AAA60289.1.
    AB062123 mRNA. Translation: BAB93455.1.
    BC000524 mRNA. Translation: AAH00524.1.
    BC009427 mRNA. Translation: AAH09427.2.
    BC027620 mRNA. Translation: AAH27620.1.
    BC071907 mRNA. Translation: AAH71907.1.
    BC071908 mRNA. Translation: AAH71908.1.
    BC094826 mRNA. Translation: AAH94826.1.
    CCDSiCCDS6492.1.
    PIRiJC1394. R3HU6.
    RefSeqiNP_001001.2. NM_001010.2.
    UniGeneiHs.408073.

    Genome annotation databases

    EnsembliENST00000380394; ENSP00000369757; ENSG00000137154.
    GeneIDi6194.
    KEGGihsa:6194.
    UCSCiuc003znv.1. human.

    Polymorphism databases

    DMDMi51338632.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20020 mRNA. Translation: AAA60288.1 .
    J03537 mRNA. Translation: AAA60287.1 .
    X67309 Genomic DNA. Translation: CAA47719.1 .
    M77232 Genomic DNA. Translation: AAA60289.1 .
    AB062123 mRNA. Translation: BAB93455.1 .
    BC000524 mRNA. Translation: AAH00524.1 .
    BC009427 mRNA. Translation: AAH09427.2 .
    BC027620 mRNA. Translation: AAH27620.1 .
    BC071907 mRNA. Translation: AAH71907.1 .
    BC071908 mRNA. Translation: AAH71908.1 .
    BC094826 mRNA. Translation: AAH94826.1 .
    CCDSi CCDS6492.1.
    PIRi JC1394. R3HU6.
    RefSeqi NP_001001.2. NM_001010.2.
    UniGenei Hs.408073.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3A electron microscopy 5.00 G 1-249 [» ]
    ProteinModelPortali P62753.
    SMRi P62753. Positions 1-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112108. 165 interactions.
    DIPi DIP-31507N.
    IntActi P62753. 40 interactions.
    MINTi MINT-1162101.
    STRINGi 9606.ENSP00000369757.

    PTM databases

    PhosphoSitei P62753.

    Polymorphism databases

    DMDMi 51338632.

    Proteomic databases

    MaxQBi P62753.
    PaxDbi P62753.
    PRIDEi P62753.

    Protocols and materials databases

    DNASUi 6194.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380394 ; ENSP00000369757 ; ENSG00000137154 .
    GeneIDi 6194.
    KEGGi hsa:6194.
    UCSCi uc003znv.1. human.

    Organism-specific databases

    CTDi 6194.
    GeneCardsi GC09M019366.
    HGNCi HGNC:10429. RPS6.
    HPAi CAB004027.
    HPA031153.
    MIMi 180460. gene.
    neXtProti NX_P62753.
    PharmGKBi PA34844.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2125.
    HOGENOMi HOG000190952.
    HOVERGENi HBG011441.
    InParanoidi P62753.
    KOi K02991.
    OMAi CQKLFEV.
    OrthoDBi EOG7Z0JXB.
    PhylomeDBi P62753.
    TreeFami TF300035.

    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_6772. S6K1 signalling.
    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.
    SignaLinki P62753.

    Miscellaneous databases

    ChiTaRSi RPS6. human.
    GenomeRNAii 6194.
    NextBioi 24053.
    PROi P62753.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62753.
    Bgeei P62753.
    CleanExi HS_RPS6.
    Genevestigatori P62753.

    Family and domain databases

    InterProi IPR014401. Ribosomal_S6_euk.
    IPR001377. Ribosomal_S6e.
    IPR018282. Ribosomal_S6e_CS.
    [Graphical view ]
    PANTHERi PTHR11502. PTHR11502. 1 hit.
    Pfami PF01092. Ribosomal_S6e. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002129. Ribosom_S6_euk. 1 hit.
    PROSITEi PS00578. RIBOSOMAL_S6E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of cloned cDNAs that code for human ribosomal protein S6."
      Lott J.B., Mackie G.A.
      Gene 65:31-39(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The primary structure of the human ribosomal protein S6 derived from a cloned cDNA."
      Heinze H., Arnold H.H., Fischer D., Kruppa J.
      J. Biol. Chem. 263:4139-4144(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The organization of the intron-containing human S6 ribosomal protein (rpS6) gene and determination of its location at chromosome 9p21."
      Antoine M., Fried M.
      Hum. Mol. Genet. 1:565-570(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The human ribosomal protein S6 gene: isolation, primary structure and location in chromosome 9."
      Pata I., Hoth S., Kruppa J., Metspalu A.
      Gene 121:387-392(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon adenocarcinoma.
    6. "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 ARG-221.
      Tissue: Colon, Muscle, Pancreas, Skin and Testis.
    7. "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 1-15.
      Tissue: Placenta.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
      Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
      J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-235 AND SER-236.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240; SER-244 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling."
      Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O., Hupp T.
      J. Biol. Chem. 284:334-344(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
    13. "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-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN."
      Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P., Wenger R.H.
      FEBS J. 278:1757-1768(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-235 AND SER-236, MUTAGENESIS OF 235-SER-SER-236.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRS6_HUMAN
    AccessioniPrimary (citable) accession number: P62753
    Secondary accession number(s): P08227
    , P10660, Q4VBY7, Q8N6Z7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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