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P12724

- ECP_HUMAN

UniProt

P12724 - ECP_HUMAN

Protein

Eosinophil cationic protein

Gene

RNASE3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei42 – 421Proton acceptor
    Sitei60 – 601May be involved in LPS-binding
    Sitei62 – 621May be involved in LPS- and LTA-binding
    Active sitei155 – 1551Proton donor

    GO - Molecular functioni

    1. endoribonuclease activity, producing 3'-phosphomonoesters Source: InterPro
    2. nucleic acid binding Source: InterPro
    3. ribonuclease activity Source: ProtInc

    GO - Biological processi

    1. antibacterial humoral response Source: UniProt
    2. defense response to Gram-positive bacterium Source: UniProt
    3. innate immune response in mucosa Source: UniProt
    4. RNA catabolic process Source: ProtInc
    5. RNA phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Endonuclease, Hydrolase, Nuclease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eosinophil cationic protein (EC:3.1.27.-)
    Short name:
    ECP
    Alternative name(s):
    Ribonuclease 3
    Short name:
    RNase 3
    Gene namesi
    Name:RNASE3
    Synonyms:ECP, RNS3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:10046. RNASE3.

    Subcellular locationi

    Secreted
    Note: Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus.

    GO - Cellular componenti

    1. extracellular region Source: ProtInc
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401I → A: Loss of in vitro formation of amyloid-like aggregates. 1 Publication

    Organism-specific databases

    PharmGKBiPA34414.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27272 PublicationsAdd
    BLAST
    Chaini28 – 160133Eosinophil cationic proteinPRO_0000030862Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 110
    Modified residuei60 – 601Nitrated tyrosine1 Publication
    Disulfide bondi64 ↔ 123
    Disulfide bondi82 ↔ 138
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi89 ↔ 98
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Nitration

    Proteomic databases

    PaxDbiP12724.
    PRIDEiP12724.

    PTM databases

    PhosphoSiteiP12724.

    Expressioni

    Gene expression databases

    BgeeiP12724.
    CleanExiHS_RNASE3.
    GenevestigatoriP12724.

    Organism-specific databases

    HPAiHPA056183.

    Interactioni

    Subunit structurei

    Interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). In vitro interacts with and insert into lipid bilayers composed of dioleoyl phosphatidylcholine and dioleoyl phosphatidylglycerol. In vitro, tends to form amyloid-like aggregates at pH 3, but not at pH 5, nor 7.1 Publication

    Protein-protein interaction databases

    BioGridi111966. 1 interaction.
    STRINGi9606.ENSP00000302324.

    Structurei

    Secondary structure

    1
    160
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 323
    Helixi34 – 429
    Helixi50 – 534
    Helixi55 – 584
    Beta strandi61 – 633
    Beta strandi66 – 738
    Helixi75 – 817
    Turni93 – 953
    Beta strandi98 – 1003
    Beta strandi105 – 1139
    Helixi120 – 1223
    Beta strandi125 – 1328
    Beta strandi134 – 1407
    Turni143 – 1453
    Beta strandi150 – 15910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DYTX-ray1.75A/B28-160[»]
    1H1HX-ray2.00A28-160[»]
    1QMTX-ray2.40A28-160[»]
    2KB5NMR-A28-160[»]
    2LVZNMR-A28-160[»]
    4A2OX-ray1.69A/B28-160[»]
    4A2YX-ray1.70A/B28-160[»]
    ProteinModelPortaliP12724.
    SMRiP12724. Positions 28-160.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12724.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni28 – 7245Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarizationAdd
    BLAST
    Regioni65 – 695Substrate binding

    Sequence similaritiesi

    Belongs to the pancreatic ribonuclease family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG118739.
    HOGENOMiHOG000276882.
    HOVERGENiHBG008396.
    InParanoidiP12724.
    KOiK10787.
    OMAiNISRNCH.
    OrthoDBiEOG7KDFCP.
    PhylomeDBiP12724.
    TreeFamiTF333393.

    Family and domain databases

    Gene3Di3.10.130.10. 1 hit.
    InterProiIPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view]
    PANTHERiPTHR11437. PTHR11437. 1 hit.
    PfamiPF00074. RnaseA. 1 hit.
    [Graphical view]
    PRINTSiPR00794. RIBONUCLEASE.
    ProDomiPD000535. RNaseA. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00092. RNAse_Pc. 1 hit.
    [Graphical view]
    SUPFAMiSSF54076. SSF54076. 1 hit.
    PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12724-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVPKLFTSQI CLLLLLGLMG VEGSLHARPP QFTRAQWFAI QHISLNPPRC    50
    TIAMRAINNY RWRCKNQNTF LRTTFANVVN VCGNQSIRCP HNRTLNNCHR 100
    SRFRVPLLHC DLINPGAQNI SNCTYADRPG RRFYVVACDN RDPRDSPRYP 150
    VVPVHLDTTI 160
    Length:160
    Mass (Da):18,385
    Last modified:May 15, 2007 - v2
    Checksum:iD7BED24F67B23FA9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721R → C.1 Publication
    Corresponds to variant rs151169198 [ dbSNP | Ensembl ].
    VAR_014109
    Natural varianti124 – 1241T → R.7 Publications
    Corresponds to variant rs2073342 [ dbSNP | Ensembl ].
    VAR_013149
    Natural varianti130 – 1301G → R.
    Corresponds to variant rs12147890 [ dbSNP | Ensembl ].
    VAR_029017

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15161 mRNA. Translation: CAA33251.1.
    M28128 mRNA. Translation: AAA50283.1.
    X16545 Genomic DNA. Translation: CAA34545.1.
    X55990 Genomic DNA. Translation: CAA39462.1.
    AF294019 Genomic DNA. Translation: AAG31589.1.
    AF294020 Genomic DNA. Translation: AAG31590.1.
    AF294021 Genomic DNA. Translation: AAG31591.1.
    AF294022 Genomic DNA. Translation: AAG31592.1.
    AF294023 Genomic DNA. Translation: AAG31593.1.
    AF294024 Genomic DNA. Translation: AAG31594.1.
    AF294025 Genomic DNA. Translation: AAG31595.1.
    AF294026 Genomic DNA. Translation: AAG31596.1.
    AL133371 Genomic DNA. No translation available.
    BC096060 mRNA. Translation: AAH96060.1.
    BC096061 mRNA. Translation: AAH96061.1.
    BC096062 mRNA. Translation: AAH96062.1.
    AF441204 Genomic DNA. Translation: AAL35279.1.
    AF441205 Genomic DNA. Translation: AAL35280.1.
    AF441206 Genomic DNA. Translation: AAL35281.1.
    CCDSiCCDS9560.1.
    PIRiB35328. JL0106.
    RefSeqiNP_002926.2. NM_002935.2.
    UniGeneiHs.73839.

    Genome annotation databases

    EnsembliENST00000304639; ENSP00000302324; ENSG00000169397.
    GeneIDi6037.
    KEGGihsa:6037.
    UCSCiuc001vyj.3. human.

    Polymorphism databases

    DMDMi147744558.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15161 mRNA. Translation: CAA33251.1 .
    M28128 mRNA. Translation: AAA50283.1 .
    X16545 Genomic DNA. Translation: CAA34545.1 .
    X55990 Genomic DNA. Translation: CAA39462.1 .
    AF294019 Genomic DNA. Translation: AAG31589.1 .
    AF294020 Genomic DNA. Translation: AAG31590.1 .
    AF294021 Genomic DNA. Translation: AAG31591.1 .
    AF294022 Genomic DNA. Translation: AAG31592.1 .
    AF294023 Genomic DNA. Translation: AAG31593.1 .
    AF294024 Genomic DNA. Translation: AAG31594.1 .
    AF294025 Genomic DNA. Translation: AAG31595.1 .
    AF294026 Genomic DNA. Translation: AAG31596.1 .
    AL133371 Genomic DNA. No translation available.
    BC096060 mRNA. Translation: AAH96060.1 .
    BC096061 mRNA. Translation: AAH96061.1 .
    BC096062 mRNA. Translation: AAH96062.1 .
    AF441204 Genomic DNA. Translation: AAL35279.1 .
    AF441205 Genomic DNA. Translation: AAL35280.1 .
    AF441206 Genomic DNA. Translation: AAL35281.1 .
    CCDSi CCDS9560.1.
    PIRi B35328. JL0106.
    RefSeqi NP_002926.2. NM_002935.2.
    UniGenei Hs.73839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DYT X-ray 1.75 A/B 28-160 [» ]
    1H1H X-ray 2.00 A 28-160 [» ]
    1QMT X-ray 2.40 A 28-160 [» ]
    2KB5 NMR - A 28-160 [» ]
    2LVZ NMR - A 28-160 [» ]
    4A2O X-ray 1.69 A/B 28-160 [» ]
    4A2Y X-ray 1.70 A/B 28-160 [» ]
    ProteinModelPortali P12724.
    SMRi P12724. Positions 28-160.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111966. 1 interaction.
    STRINGi 9606.ENSP00000302324.

    Chemistry

    DrugBanki DB01411. Pranlukast.

    PTM databases

    PhosphoSitei P12724.

    Polymorphism databases

    DMDMi 147744558.

    Proteomic databases

    PaxDbi P12724.
    PRIDEi P12724.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304639 ; ENSP00000302324 ; ENSG00000169397 .
    GeneIDi 6037.
    KEGGi hsa:6037.
    UCSCi uc001vyj.3. human.

    Organism-specific databases

    CTDi 6037.
    GeneCardsi GC14P021359.
    H-InvDB HIX0037784.
    HGNCi HGNC:10046. RNASE3.
    HPAi HPA056183.
    MIMi 131398. gene.
    neXtProti NX_P12724.
    PharmGKBi PA34414.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG118739.
    HOGENOMi HOG000276882.
    HOVERGENi HBG008396.
    InParanoidi P12724.
    KOi K10787.
    OMAi NISRNCH.
    OrthoDBi EOG7KDFCP.
    PhylomeDBi P12724.
    TreeFami TF333393.

    Miscellaneous databases

    EvolutionaryTracei P12724.
    GeneWikii Eosinophil_cationic_protein.
    GenomeRNAii 6037.
    NextBioi 23529.
    PROi P12724.
    SOURCEi Search...

    Gene expression databases

    Bgeei P12724.
    CleanExi HS_RNASE3.
    Genevestigatori P12724.

    Family and domain databases

    Gene3Di 3.10.130.10. 1 hit.
    InterProi IPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view ]
    PANTHERi PTHR11437. PTHR11437. 1 hit.
    Pfami PF00074. RnaseA. 1 hit.
    [Graphical view ]
    PRINTSi PR00794. RIBONUCLEASE.
    ProDomi PD000535. RNaseA. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00092. RNAse_Pc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54076. SSF54076. 1 hit.
    PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity."
      Rosenberg H.F., Ackerman S.J., Tenen D.G.
      J. Exp. Med. 170:163-176(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-124.
      Tissue: Peripheral blood granulocyte.
    2. "Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily."
      Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T., Schad C.R., Pease L.R., Gleich G.J., Barker R.L.
      Genomics 7:535-546(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-124.
      Tissue: Fetal liver.
    3. "Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases."
      Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R., Gleich G.J.
      J. Immunol. 143:952-955(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-124.
    4. Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.
      Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-124.
      Tissue: Colon.
    5. "Sequence variation at two eosinophil-associated ribonuclease loci in humans."
      Zhang J., Rosenberg H.F.
      Genetics 156:1949-1958(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-124.
    6. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 ARG-124.
    8. "Identification of polymorphisms in the ECP gene. Relation to disease activity in Hodgkins lymphoma."
      Bystrom J., Molin D., Jonsson U.B., Enblad G., Sundstrom C., Hogbom E., Venge P.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-160, VARIANTS CYS-72 AND ARG-124.
    9. "Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease."
      Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J., McKean D.J.
      Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-87.
    10. Cited for: PROTEIN SEQUENCE OF 28-47, FUNCTION AS AN ANTIMICROBIAL PROTEIN.
    11. Cited for: NITRATION AT TYR-60.
    12. "Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment."
      Torrent M., de la Torre B.G., Nogues V.M., Andreu D., Boix E.
      Biochem. J. 421:425-434(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LPS; LTA AND LIPID BILAYERS.
    13. "Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region."
      Torrent M., Odorizzi F., Nogues M.V., Boix E.
      Biomacromolecules 11:1983-1990(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IN VITRO FORMATION OF AMYLOID-LIKE AGGREGATES, MUTAGENESIS OF ILE-40.
    14. "Crystal structure of eosinophil cationic protein at 2.4 A resolution."
      Boix E., Leonidas D.D., Nikolovski Z., Nogues M.V., Cuchillo C.M., Acharya K.R.
      Biochemistry 38:16794-16801(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-160.
    15. "Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution."
      Mallorqui-Fernandez G., Pous J., Peracaula R., Aymami J., Maeda T., Tada H., Yamada H., Seno M., de Llorens R., Gomis-Rueth F.-X., Coll M.
      J. Mol. Biol. 300:1297-1307(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 28-160.
    16. "The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site."
      Mohan C.G., Boix E., Evans H.R., Nikolovski Z., Nogues M.V., Cuchillo C.M., Acharya K.R.
      Biochemistry 41:12100-12106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-160.

    Entry informationi

    Entry nameiECP_HUMAN
    AccessioniPrimary (citable) accession number: P12724
    Secondary accession number(s): Q4VBC1
    , Q8WTP7, Q8WZ62, Q9GZN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3