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P18124

- RL7_HUMAN

UniProt

P18124 - RL7_HUMAN

Protein

60S ribosomal protein L7

Gene

RPL7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. mRNA binding Source: MGI
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: MGI
    6. RNA binding Source: ProtInc
    7. structural constituent of ribosome Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. ribosomal large subunit biogenesis Source: UniProtKB
    6. RNA metabolic process Source: Reactome
    7. rRNA processing Source: UniProtKB
    8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    9. translation Source: UniProtKB
    10. translational elongation Source: Reactome
    11. translational initiation Source: Reactome
    12. translational termination Source: Reactome
    13. viral life cycle Source: Reactome
    14. viral process Source: Reactome
    15. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    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_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S ribosomal protein L7
    Gene namesi
    Name:RPL7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:10363. RPL7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProt
    6. ribonucleoprotein complex Source: MGI

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34759.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24824860S ribosomal protein L7PRO_0000104633Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei124 – 1241N6-acetyllysine1 Publication
    Modified residuei127 – 1271N6-succinyllysineBy similarity
    Modified residuei139 – 1391Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP18124.
    PaxDbiP18124.
    PRIDEiP18124.

    2D gel databases

    SWISS-2DPAGEP18124.

    PTM databases

    PhosphoSiteiP18124.

    Expressioni

    Gene expression databases

    ArrayExpressiP18124.
    BgeeiP18124.
    CleanExiHS_RPL7.
    GenevestigatoriP18124.

    Organism-specific databases

    HPAiHPA058373.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IPO5O004104EBI-350806,EBI-356424
    NEDD8Q158432EBI-350806,EBI-716247

    Protein-protein interaction databases

    BioGridi112049. 132 interactions.
    IntActiP18124. 29 interactions.
    MINTiMINT-1152474.
    STRINGi9606.ENSP00000339795.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00F1-248[»]
    ProteinModelPortaliP18124.
    SMRiP18124. Positions 20-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati7 – 18121Add
    BLAST
    Repeati19 – 30122Add
    BLAST
    Repeati31 – 42123Add
    BLAST
    Repeati43 – 54124Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 54484 X 12 AA tandem repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein L30P family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1841.
    HOGENOMiHOG000170917.
    HOVERGENiHBG003280.
    KOiK02937.
    OMAiKATQQML.
    OrthoDBiEOG7K9K3X.
    PhylomeDBiP18124.
    TreeFamiTF300740.

    Family and domain databases

    Gene3Di3.30.1390.20. 2 hits.
    InterProiIPR018038. Ribosomal_L30_CS.
    IPR016082. Ribosomal_L30_ferredoxin-like.
    IPR012988. Ribosomal_L30_N.
    IPR005998. Ribosomal_L7_euk.
    [Graphical view]
    PfamiPF00327. Ribosomal_L30. 1 hit.
    PF08079. Ribosomal_L30_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF55129. SSF55129. 1 hit.
    TIGRFAMsiTIGR01310. L7. 1 hit.
    PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P18124-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGVEEKKKE VPAVPETLKK KRRNFAELKI KRLRKKFAQK MLRKARRKLI    50
    YEKAKHYHKE YRQMYRTEIR MARMARKAGN FYVPAEPKLA FVIRIRGING 100
    VSPKVRKVLQ LLRLRQIFNG TFVKLNKASI NMLRIVEPYI AWGYPNLKSV 150
    NELIYKRGYG KINKKRIALT DNALIARSLG KYGIICMEDL IHEIYTVGKR 200
    FKEANNFLWP FKLSSPRGGM KKKTTHFVEG GDAGNREDQI NRLIRRMN 248
    Length:248
    Mass (Da):29,226
    Last modified:November 1, 1990 - v1
    Checksum:i070EB4C904E6795A
    GO

    Sequence cautioni

    The sequence CAA41026.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481K → E in CAG33054. 1 PublicationCurated
    Sequence conflicti157 – 1571R → L in CAA41026. (PubMed:8441630)Curated
    Sequence conflicti157 – 1571R → L in CAA41027. (PubMed:8441630)Curated
    Sequence conflicti160 – 1601G → A in CAA41026. (PubMed:8441630)Curated
    Sequence conflicti166 – 1661R → Q in CAA41026. (PubMed:8441630)Curated
    Sequence conflicti173 – 1731A → S in AAA03081. (PubMed:8360149)Curated
    Sequence conflicti192 – 1921H → R in CAG33054. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57958 mRNA. Translation: CAA41026.1. Different initiation.
    X57959 mRNA. Translation: CAA41027.1.
    L16558 mRNA. Translation: AAA03081.1.
    X52967 mRNA. Translation: CAA37139.1.
    CR456773 mRNA. Translation: CAG33054.1.
    AK291119 mRNA. Translation: BAF83808.1.
    AK313365 mRNA. Translation: BAG36165.1.
    BC006095 mRNA. Translation: AAH06095.1.
    BC008850 mRNA. Translation: AAH08850.1.
    BC009599 mRNA. Translation: AAH09599.1.
    BC071671 mRNA. Translation: AAH71671.1.
    BC071894 mRNA. Translation: AAH71894.1.
    BC071895 mRNA. Translation: AAH71895.1.
    BC087837 mRNA. Translation: AAH87837.1.
    CCDSiCCDS6212.1.
    PIRiS11709. R5HU7.
    RefSeqiNP_000962.2. NM_000971.3.
    UniGeneiHs.421257.
    Hs.571841.

    Genome annotation databases

    EnsembliENST00000352983; ENSP00000339795; ENSG00000147604.
    GeneIDi6129.
    KEGGihsa:6129.
    UCSCiuc003xzg.3. human.

    Polymorphism databases

    DMDMi133021.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57958 mRNA. Translation: CAA41026.1 . Different initiation.
    X57959 mRNA. Translation: CAA41027.1 .
    L16558 mRNA. Translation: AAA03081.1 .
    X52967 mRNA. Translation: CAA37139.1 .
    CR456773 mRNA. Translation: CAG33054.1 .
    AK291119 mRNA. Translation: BAF83808.1 .
    AK313365 mRNA. Translation: BAG36165.1 .
    BC006095 mRNA. Translation: AAH06095.1 .
    BC008850 mRNA. Translation: AAH08850.1 .
    BC009599 mRNA. Translation: AAH09599.1 .
    BC071671 mRNA. Translation: AAH71671.1 .
    BC071894 mRNA. Translation: AAH71894.1 .
    BC071895 mRNA. Translation: AAH71895.1 .
    BC087837 mRNA. Translation: AAH87837.1 .
    CCDSi CCDS6212.1.
    PIRi S11709. R5HU7.
    RefSeqi NP_000962.2. NM_000971.3.
    UniGenei Hs.421257.
    Hs.571841.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3B electron microscopy 5.00 F 1-248 [» ]
    ProteinModelPortali P18124.
    SMRi P18124. Positions 20-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112049. 132 interactions.
    IntActi P18124. 29 interactions.
    MINTi MINT-1152474.
    STRINGi 9606.ENSP00000339795.

    PTM databases

    PhosphoSitei P18124.

    Polymorphism databases

    DMDMi 133021.

    2D gel databases

    SWISS-2DPAGE P18124.

    Proteomic databases

    MaxQBi P18124.
    PaxDbi P18124.
    PRIDEi P18124.

    Protocols and materials databases

    DNASUi 6129.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352983 ; ENSP00000339795 ; ENSG00000147604 .
    GeneIDi 6129.
    KEGGi hsa:6129.
    UCSCi uc003xzg.3. human.

    Organism-specific databases

    CTDi 6129.
    GeneCardsi GC08M074202.
    H-InvDB HIX0058339.
    HGNCi HGNC:10363. RPL7.
    HPAi HPA058373.
    MIMi 604166. gene.
    neXtProti NX_P18124.
    PharmGKBi PA34759.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1841.
    HOGENOMi HOG000170917.
    HOVERGENi HBG003280.
    KOi K02937.
    OMAi KATQQML.
    OrthoDBi EOG7K9K3X.
    PhylomeDBi P18124.
    TreeFami TF300740.

    Enzyme and pathway databases

    Reactomei 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_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_9491. Viral mRNA Translation.

    Miscellaneous databases

    ChiTaRSi RPL7. human.
    GeneWikii RPL7.
    GenomeRNAii 6129.
    NextBioi 23805.
    PROi P18124.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18124.
    Bgeei P18124.
    CleanExi HS_RPL7.
    Genevestigatori P18124.

    Family and domain databases

    Gene3Di 3.30.1390.20. 2 hits.
    InterProi IPR018038. Ribosomal_L30_CS.
    IPR016082. Ribosomal_L30_ferredoxin-like.
    IPR012988. Ribosomal_L30_N.
    IPR005998. Ribosomal_L7_euk.
    [Graphical view ]
    Pfami PF00327. Ribosomal_L30. 1 hit.
    PF08079. Ribosomal_L30_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55129. SSF55129. 1 hit.
    TIGRFAMsi TIGR01310. L7. 1 hit.
    PROSITEi PS00634. RIBOSOMAL_L30. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural and functional properties of ribosomal protein L7 from humans and rodents."
      Hemmerich P., von Mikecz A., Neumann F., Soezen O., Wolff-Vorbeck G., Zoebelein R., Krawinkel U.
      Nucleic Acids Res. 21:223-231(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    2. "Identification of a transcript that is down-regulated in senescent human fibroblasts. Cloning, sequence analysis, and regulation of the human L7 ribosomal protein gene."
      Seshadri T., Uzman J.A., Oshima J., Campisi J.
      J. Biol. Chem. 268:18474-18480(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    3. Schneider R., Herzog H., Hfferer L., Schweiger M.
      Submitted (MAY-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thymus.
    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].
      Tissue: Bone marrow, Eye, Lung, Mammary gland, Muscle and Skin.
    7. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-7; 10-20; 48-53; 77-88; 107-113; 128-156; 167-177; 201-212 AND 224-242, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    8. "Human ribosomal protein L7 inhibits cell-free translation in reticulocyte lysates and affects the expression of nuclear proteins upon stable transfection into Jurkat T-lymphoma cells."
      Neumann F., Hemmerich P., von Mikecz A., Peter H.-H., Krawinkel U.
      Nucleic Acids Res. 23:195-202(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
      Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
      J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRL7_HUMAN
    AccessioniPrimary (citable) accession number: P18124
    Secondary accession number(s): A8K504
    , Q15289, Q3KQU0, Q5I0X1, Q6IBM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 156 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Ribosomal proteins
      Ribosomal proteins families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3