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P20160

- CAP7_HUMAN

UniProt

P20160 - CAP7_HUMAN

Protein

Azurocidin

Gene

AZU1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G.2 Publications

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB
    2. serine-type endopeptidase activity Source: InterPro
    3. toxic substance binding Source: UniProtKB

    GO - Biological processi

    1. cellular extravasation Source: UniProtKB
    2. defense response to Gram-negative bacterium Source: UniProtKB
    3. glial cell migration Source: UniProtKB
    4. induction of positive chemotaxis Source: UniProtKB
    5. inflammatory response Source: UniProtKB
    6. macrophage chemotaxis Source: UniProtKB
    7. microglial cell activation Source: UniProtKB
    8. monocyte activation Source: UniProtKB
    9. negative regulation of apoptotic process Source: UniProtKB
    10. positive regulation of cell adhesion Source: UniProtKB
    11. positive regulation of fractalkine biosynthetic process Source: UniProtKB
    12. positive regulation of interleukin-1 beta biosynthetic process Source: UniProtKB
    13. positive regulation of MHC class II biosynthetic process Source: UniProtKB
    14. positive regulation of phagocytosis Source: UniProtKB
    15. positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
    16. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    17. regulation of vascular permeability Source: UniProtKB

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Serine protease homolog

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    Heparin-binding

    Protein family/group databases

    MEROPSiS01.971.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Azurocidin
    Alternative name(s):
    Cationic antimicrobial protein CAP37
    Heparin-binding protein
    Short name:
    HBP
    Gene namesi
    Name:AZU1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:913. AZU1.

    Subcellular locationi

    Cytoplasmic granule
    Note: Cytoplasmic granules of neutrophils.

    GO - Cellular componenti

    1. azurophil granule Source: UniProtKB
    2. extracellular region Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521C → S: Loss of antibiotic activity.
    Mutagenesisi68 – 681C → S: Loss of antibiotic activity.

    Organism-specific databases

    PharmGKBiPA25206.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26269 PublicationsAdd
    BLAST
    Chaini27 – 248222AzurocidinPRO_0000027705Add
    BLAST
    Propeptidei249 – 2513PRO_0000027706

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 681 PublicationPROSITE-ProRule annotation
    Glycosylationi126 – 1261N-linked (GlcNAc...); partial2 Publications
    Glycosylationi140 – 1401N-linked (GlcNAc...)2 Publications
    Disulfide bondi149 ↔ 207
    Glycosylationi171 – 1711N-linked (GlcNAc...); partial2 Publications
    Disulfide bondi180 ↔ 186
    Disulfide bondi197 ↔ 222

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP20160.
    PRIDEiP20160.

    Expressioni

    Gene expression databases

    BgeeiP20160.
    CleanExiHS_AZU1.
    GenevestigatoriP20160.

    Organism-specific databases

    HPAiHPA055851.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi107043. 2 interactions.
    IntActiP20160. 2 interactions.
    MINTiMINT-4054423.
    STRINGi9606.ENSP00000233997.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 466
    Beta strandi49 – 5810
    Beta strandi61 – 644
    Helixi66 – 683
    Beta strandi76 – 827
    Turni91 – 933
    Beta strandi95 – 1039
    Turni109 – 1124
    Beta strandi117 – 1237
    Beta strandi148 – 1547
    Beta strandi157 – 1604
    Beta strandi168 – 1747
    Helixi177 – 1793
    Beta strandi184 – 1885
    Beta strandi190 – 1934
    Beta strandi204 – 2074
    Beta strandi210 – 2189
    Beta strandi227 – 2315
    Helixi232 – 2354
    Helixi236 – 2449

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A7SX-ray1.12A27-251[»]
    1AE5X-ray2.30A27-251[»]
    1FY1X-ray2.50A27-251[»]
    1FY3X-ray1.89A27-251[»]
    ProteinModelPortaliP20160.
    SMRiP20160. Positions 27-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20160.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 244218Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 7025Possesses antibiotic activityAdd
    BLAST
    Regioni52 – 8433HydrophobicAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP20160.
    OMAiWIDSVIN.
    OrthoDBiEOG73FQNK.
    PhylomeDBiP20160.
    TreeFamiTF335284.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P20160-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH    50
    FCGGALIHAR FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS 100
    SMSENGYDPQ QNLNDLMLLQ LDREANLTSS VTILPLPLQN ATVEAGTRCQ 150
    VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC RPNNVCTGVL TRRGGICNGD 200
    GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID GVLNNPGPGP 250
    A 251
    Length:251
    Mass (Da):26,886
    Last modified:October 1, 1993 - v3
    Checksum:i22F80D9EBE87DE60
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361R → H AA sequence (PubMed:2404977)Curated
    Sequence conflicti130 – 1301S → N AA sequence (PubMed:2026172)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti248 – 2481Missing in 50% of the molecules.
    VAR_006496

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96326 Genomic DNA. Translation: AAB59353.1.
    AC004799 Genomic DNA. No translation available.
    BC069495 mRNA. Translation: AAH69495.1.
    BC093931 mRNA. Translation: AAH93931.1.
    BC093933 mRNA. Translation: AAH93933.1.
    X58794 mRNA. Translation: CAA41601.1.
    CCDSiCCDS12044.1.
    PIRiA46268. TRHUAZ.
    RefSeqiNP_001691.1. NM_001700.3.
    UniGeneiHs.72885.

    Genome annotation databases

    EnsembliENST00000233997; ENSP00000233997; ENSG00000172232.
    GeneIDi566.
    KEGGihsa:566.
    UCSCiuc002lpz.1. human.

    Polymorphism databases

    DMDMi416746.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96326 Genomic DNA. Translation: AAB59353.1 .
    AC004799 Genomic DNA. No translation available.
    BC069495 mRNA. Translation: AAH69495.1 .
    BC093931 mRNA. Translation: AAH93931.1 .
    BC093933 mRNA. Translation: AAH93933.1 .
    X58794 mRNA. Translation: CAA41601.1 .
    CCDSi CCDS12044.1.
    PIRi A46268. TRHUAZ.
    RefSeqi NP_001691.1. NM_001700.3.
    UniGenei Hs.72885.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A7S X-ray 1.12 A 27-251 [» ]
    1AE5 X-ray 2.30 A 27-251 [» ]
    1FY1 X-ray 2.50 A 27-251 [» ]
    1FY3 X-ray 1.89 A 27-251 [» ]
    ProteinModelPortali P20160.
    SMRi P20160. Positions 27-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107043. 2 interactions.
    IntActi P20160. 2 interactions.
    MINTi MINT-4054423.
    STRINGi 9606.ENSP00000233997.

    Protein family/group databases

    MEROPSi S01.971.

    Polymorphism databases

    DMDMi 416746.

    Proteomic databases

    PaxDbi P20160.
    PRIDEi P20160.

    Protocols and materials databases

    DNASUi 566.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233997 ; ENSP00000233997 ; ENSG00000172232 .
    GeneIDi 566.
    KEGGi hsa:566.
    UCSCi uc002lpz.1. human.

    Organism-specific databases

    CTDi 566.
    GeneCardsi GC19P000825.
    HGNCi HGNC:913. AZU1.
    HPAi HPA055851.
    MIMi 162815. gene.
    neXtProti NX_P20160.
    PharmGKBi PA25206.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi P20160.
    OMAi WIDSVIN.
    OrthoDBi EOG73FQNK.
    PhylomeDBi P20160.
    TreeFami TF335284.

    Miscellaneous databases

    EvolutionaryTracei P20160.
    GeneWikii Azurocidin_1.
    GenomeRNAii 566.
    NextBioi 2309.
    PROi P20160.
    SOURCEi Search...

    Gene expression databases

    Bgeei P20160.
    CleanExi HS_AZU1.
    Genevestigatori P20160.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNA for the serine protease homolog CAP37/azurocidin, a microbicidal and chemotactic protein from human granulocytes."
      Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K., Guerra M.E., Larrick J.L.
      J. Immunol. 147:3210-3214(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter."
      Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.
      Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Complementary DNA sequence of human neutrophil azurocidin, an antibiotic with extensive homology to serine proteases."
      Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.
      Biochem. Biophys. Res. Commun. 177:688-695(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-251.
      Tissue: Neutrophil.
    6. "Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase."
      Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.
      FEBS Lett. 272:200-204(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-248.
    7. "Covalent structure of two novel neutrophile leucocyte-derived proteins of porcine and human origin. Neutrophile elastase homologues with strong monocyte and fibroblast chemotactic activities."
      Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J., Engels M., Wollmer A.
      Eur. J. Biochem. 197:535-547(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-248.
      Tissue: Neutrophil.
    8. "CAP37, a human neutrophil-derived chemotactic factor with monocyte specific activity."
      Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.
      J. Clin. Invest. 85:1468-1476(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-68.
      Tissue: Neutrophil.
    9. "CAP 37, a 37 kD human neutrophil granule cationic protein shares homology with inflammatory proteinases."
      Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J., Palings I., Larrick J.W.
      Life Sci. 46:189-196(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-67.
      Tissue: Neutrophil.
    10. "Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa."
      Wasiluk K.R., Skubitz K.M., Gray B.H.
      Infect. Immun. 59:4193-4200(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-48, FUNCTION.
      Tissue: Leukocyte.
    11. "PMN elastases: a comparison of the specificity of human isozymes and the enzyme from other species toward substrates and inhibitors."
      Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W., Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S., Walakovits L., Knight W.B.
      Arch. Biochem. Biophys. 286:284-292(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-47.
    12. Cited for: PROTEIN SEQUENCE OF 27-46.
    13. "Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase."
      Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.
      J. Biol. Chem. 265:2038-2041(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-46 AND 194-217.
    14. "Human neutrophil azurocidin synergizes with leukocyte elastase and cathepsin G in the killing of Capnocytophaga sputigena."
      Miyasaki K.T., Bodeau A.L.
      Infect. Immun. 60:4973-4975(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-46, FUNCTION.
    15. "Human neutrophil granule cationic protein CAP37 is a specific macrophage chemotaxin that shares homology with inflammatory proteinases."
      Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K., Larrick J.W.
      Adv. Exp. Med. Biol. 305:89-96(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Synthetic bactericidal peptide based on CAP37: a 37-kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes."
      Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.
      Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SYNTHESIS OF 46-70.
    17. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-140 AND ASN-171.
      Tissue: Liver.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structure of HBP, a multifunctional protein with a serine proteinase fold."
      Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C., Flodgaard H.J., Larsen I.K.
      Nat. Struct. Biol. 4:265-268(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    20. Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS).

    Entry informationi

    Entry nameiCAP7_HUMAN
    AccessioniPrimary (citable) accession number: P20160
    Secondary accession number(s): P80014
    , Q52LG4, Q9UCM1, Q9UCT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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 19
      Human chromosome 19: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3