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O00161

- SNP23_HUMAN

UniProt

O00161 - SNP23_HUMAN

Protein

Synaptosomal-associated protein 23

Gene

SNAP23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. exocytosis Source: Ensembl
    2. membrane fusion Source: ProtInc
    3. membrane organization Source: Reactome
    4. post-Golgi vesicle-mediated transport Source: Reactome
    5. protein transport Source: UniProtKB-KW
    6. vesicle targeting Source: ProtInc

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_19187. Clathrin derived vesicle budding.

    Protein family/group databases

    TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synaptosomal-associated protein 23
    Short name:
    SNAP-23
    Alternative name(s):
    Vesicle-membrane fusion protein SNAP-23
    Gene namesi
    Name:SNAP23
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11131. SNAP23.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Cell junctionsynapsesynaptosome
    Note: Mainly localized to the plasma membrane.

    GO - Cellular componenti

    1. azurophil granule Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. extracellular vesicular exosome Source: UniProt
    4. neuron projection Source: UniProtKB-SubCell
    5. nucleus Source: HPA
    6. plasma membrane Source: HPA
    7. specific granule Source: UniProtKB
    8. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35979.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Synaptosomal-associated protein 23PRO_0000213598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine7 Publications
    Modified residuei20 – 201PhosphoserineBy similarity
    Modified residuei23 – 231PhosphoserineBy similarity
    Modified residuei34 – 341Phosphoserine1 Publication
    Lipidationi79 – 791S-palmitoyl cysteine1 Publication
    Lipidationi80 – 801S-palmitoyl cysteine1 Publication
    Lipidationi83 – 831S-palmitoyl cysteine1 Publication
    Lipidationi85 – 851S-palmitoyl cysteine1 Publication
    Lipidationi87 – 871S-palmitoyl cysteine1 Publication
    Modified residuei110 – 1101Phosphoserine3 Publications
    Lipidationi112 – 1121S-palmitoyl cysteine1 Publication

    Keywords - PTMi

    Acetylation, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiO00161.
    PaxDbiO00161.
    PRIDEiO00161.

    2D gel databases

    OGPiO00161.

    PTM databases

    PhosphoSiteiO00161.

    Miscellaneous databases

    PMAP-CutDBO00161.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest levels where found in placenta.

    Gene expression databases

    ArrayExpressiO00161.
    BgeeiO00161.
    CleanExiHS_SNAP23.
    GenevestigatoriO00161.

    Organism-specific databases

    HPAiHPA001214.

    Interactioni

    Subunit structurei

    Homotetramer (via coiled-coil domain), also forms heterotetramers with STX4 and VAMP3. Binds simultaneously to SNAPIN and SYN4. Found in a complex with VAMP8 and STX4 in pancreas. Interacts with STX1A and STX12 By similarity. Binds tightly to multiple syntaxins and synaptobrevins/VAMPs. Found in a complex with VAMP8 and STX1A.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NAPAP549202EBI-745000,EBI-749652
    ZDHHC17Q8IUH54EBI-745000,EBI-524753

    Protein-protein interaction databases

    BioGridi114303. 49 interactions.
    IntActiO00161. 15 interactions.
    MINTiMINT-4999382.
    STRINGi9606.ENSP00000249647.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 7451

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NHLX-ray2.30A23-76[»]
    3ZUSX-ray2.95A/B/C/D150-211[»]
    ProteinModelPortaliO00161.
    SMRiO00161. Positions 23-76, 147-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00161.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 7663t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini146 – 20863t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili23 – 76541 PublicationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNAP-25 family.Curated
    Contains 2 t-SNARE coiled-coil homology domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG259235.
    HOGENOMiHOG000231599.
    HOVERGENiHBG056971.
    InParanoidiO00161.
    KOiK08508.
    OMAiCPCNRFS.
    PhylomeDBiO00161.
    TreeFamiTF315125.

    Family and domain databases

    InterProiIPR000928. SNAP-25.
    IPR000727. T_SNARE_dom.
    [Graphical view]
    PfamiPF00835. SNAP-25. 1 hit.
    PF05739. SNARE. 1 hit.
    [Graphical view]
    SMARTiSM00397. t_SNARE. 2 hits.
    [Graphical view]
    PROSITEiPS50192. T_SNARE. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform SNAP-23a (identifier: O00161-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE    50
    QLNRIEEGLD QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK 100
    TTWGDGGENS PCNVVSKQPG PVTNGQLQQP TTGAASGGYI KRITNDARED 150
    EMEENLTQVG SILGNLKDMA LNIGNEIDAQ NPQIKRITDK ADTNRDRIDI 200
    ANARAKKLID S 211
    Length:211
    Mass (Da):23,354
    Last modified:July 1, 1997 - v1
    Checksum:iAC378E9786C3A239
    GO
    Isoform SNAP-23b (identifier: O00161-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         89-89: R → S
         90-142: Missing.

    Show »
    Length:158
    Mass (Da):17,789
    Checksum:i985F775F40884E07
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351A → V in AAC50537. (PubMed:8663154)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei89 – 891R → S in isoform SNAP-23b. 1 PublicationVSP_006187
    Alternative sequencei90 – 14253Missing in isoform SNAP-23b. 1 PublicationVSP_006188Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U55936 mRNA. Translation: AAC50537.1.
    Y09567 mRNA. Translation: CAA70760.1.
    Y09568 mRNA. Translation: CAA70761.1.
    AJ011915 mRNA. Translation: CAA09864.1.
    AJ278972, AJ278973, AJ278974 Genomic DNA. Translation: CAC07504.1.
    BT006916 mRNA. Translation: AAP35562.1.
    CR457212 mRNA. Translation: CAG33493.1.
    BC000148 mRNA. Translation: AAH00148.1.
    BC003686 mRNA. Translation: AAH03686.1.
    BC022890 mRNA. Translation: AAH22890.1.
    CCDSiCCDS10087.1. [O00161-1]
    CCDS10088.1. [O00161-2]
    PIRiJC5296.
    JC5297.
    RefSeqiNP_003816.2. NM_003825.3. [O00161-1]
    NP_570710.1. NM_130798.2. [O00161-2]
    UniGeneiHs.511149.

    Genome annotation databases

    EnsembliENST00000249647; ENSP00000249647; ENSG00000092531. [O00161-1]
    ENST00000349777; ENSP00000207062; ENSG00000092531. [O00161-2]
    ENST00000397138; ENSP00000380327; ENSG00000092531. [O00161-2]
    GeneIDi8773.
    KEGGihsa:8773.
    UCSCiuc001zpz.2. human. [O00161-1]
    uc001zqa.2. human. [O00161-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U55936 mRNA. Translation: AAC50537.1 .
    Y09567 mRNA. Translation: CAA70760.1 .
    Y09568 mRNA. Translation: CAA70761.1 .
    AJ011915 mRNA. Translation: CAA09864.1 .
    AJ278972 , AJ278973 , AJ278974 Genomic DNA. Translation: CAC07504.1 .
    BT006916 mRNA. Translation: AAP35562.1 .
    CR457212 mRNA. Translation: CAG33493.1 .
    BC000148 mRNA. Translation: AAH00148.1 .
    BC003686 mRNA. Translation: AAH03686.1 .
    BC022890 mRNA. Translation: AAH22890.1 .
    CCDSi CCDS10087.1. [O00161-1 ]
    CCDS10088.1. [O00161-2 ]
    PIRi JC5296.
    JC5297.
    RefSeqi NP_003816.2. NM_003825.3. [O00161-1 ]
    NP_570710.1. NM_130798.2. [O00161-2 ]
    UniGenei Hs.511149.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NHL X-ray 2.30 A 23-76 [» ]
    3ZUS X-ray 2.95 A/B/C/D 150-211 [» ]
    ProteinModelPortali O00161.
    SMRi O00161. Positions 23-76, 147-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114303. 49 interactions.
    IntActi O00161. 15 interactions.
    MINTi MINT-4999382.
    STRINGi 9606.ENSP00000249647.

    Protein family/group databases

    TCDBi 1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

    PTM databases

    PhosphoSitei O00161.

    2D gel databases

    OGPi O00161.

    Proteomic databases

    MaxQBi O00161.
    PaxDbi O00161.
    PRIDEi O00161.

    Protocols and materials databases

    DNASUi 8773.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249647 ; ENSP00000249647 ; ENSG00000092531 . [O00161-1 ]
    ENST00000349777 ; ENSP00000207062 ; ENSG00000092531 . [O00161-2 ]
    ENST00000397138 ; ENSP00000380327 ; ENSG00000092531 . [O00161-2 ]
    GeneIDi 8773.
    KEGGi hsa:8773.
    UCSCi uc001zpz.2. human. [O00161-1 ]
    uc001zqa.2. human. [O00161-2 ]

    Organism-specific databases

    CTDi 8773.
    GeneCardsi GC15P042787.
    HGNCi HGNC:11131. SNAP23.
    HPAi HPA001214.
    MIMi 602534. gene.
    neXtProti NX_O00161.
    PharmGKBi PA35979.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259235.
    HOGENOMi HOG000231599.
    HOVERGENi HBG056971.
    InParanoidi O00161.
    KOi K08508.
    OMAi CPCNRFS.
    PhylomeDBi O00161.
    TreeFami TF315125.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_19187. Clathrin derived vesicle budding.

    Miscellaneous databases

    ChiTaRSi SNAP23. human.
    EvolutionaryTracei O00161.
    GeneWikii SNAP23.
    GenomeRNAii 8773.
    NextBioi 32894.
    PMAP-CutDB O00161.
    PROi O00161.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00161.
    Bgeei O00161.
    CleanExi HS_SNAP23.
    Genevestigatori O00161.

    Family and domain databases

    InterProi IPR000928. SNAP-25.
    IPR000727. T_SNARE_dom.
    [Graphical view ]
    Pfami PF00835. SNAP-25. 1 hit.
    PF05739. SNARE. 1 hit.
    [Graphical view ]
    SMARTi SM00397. t_SNARE. 2 hits.
    [Graphical view ]
    PROSITEi PS50192. T_SNARE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues."
      Ravichandran V., Chawla A., Roche P.A.
      J. Biol. Chem. 271:13300-13303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-23A).
      Tissue: B-cell.
    2. "Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells."
      Mollinedo F., Lazo P.A.
      Biochem. Biophys. Res. Commun. 231:808-812(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B).
      Tissue: Neutrophil.
    3. "Genomic organization, chromosomal localization, alternative splicing, and isoforms of human Synaptosome associated protein-23 gene implicated in vesicle-membrane fusion."
      Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J., Nabokina S.M., Mollinedo F., Estivill X.
      Hum. Genet. 108:211-215(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
    4. "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] (ISOFORM SNAP-23A).
    5. "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] (ISOFORM SNAP-23A).
    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] (ISOFORM SNAP-23A).
      Tissue: Cervix, Placenta and Testis.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12, ACETYLATION AT MET-1.
      Tissue: Platelet.
    8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    9. "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion."
      Polgar J., Chung S.H., Reed G.L.
      Blood 100:1081-1083(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Site-specific analysis of protein S-acylation by resin-assisted capture."
      Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J.
      J. Lipid Res. 52:393-398(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain."
      Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.
      J. Biol. Chem. 278:13462-13467(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiSNP23_HUMAN
    AccessioniPrimary (citable) accession number: O00161
    Secondary accession number(s): O00162, Q13602, Q6IAE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 153 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 15
      Human chromosome 15: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3