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P16444

- DPEP1_HUMAN

UniProt

P16444 - DPEP1_HUMAN

Protein

Dipeptidase 1

Gene

DPEP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.

    Catalytic activityi

    Hydrolysis of dipeptides.PROSITE-ProRule annotation

    Cofactori

    Zinc.1 PublicationPROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by L-penicillamine.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi36 – 361Zinc 1; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi38 – 381Zinc 1; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi141 – 1411Zinc 1; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi141 – 1411Zinc 2; catalytic1 PublicationPROSITE-ProRule annotation
    Binding sitei168 – 1681Substrate
    Metal bindingi214 – 2141Zinc 2; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi235 – 2351Zinc 2; catalytic1 PublicationPROSITE-ProRule annotation
    Binding sitei246 – 2461Substrate
    Binding sitei304 – 3041Substrate

    GO - Molecular functioni

    1. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
    2. dipeptidyl-peptidase activity Source: InterPro
    3. GPI anchor binding Source: UniProtKB
    4. metallodipeptidase activity Source: UniProtKB
    5. metalloexopeptidase activity Source: UniProtKB
    6. modified amino acid binding Source: UniProtKB
    7. protein binding Source: IntAct
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. antibiotic metabolic process Source: UniProtKB
    2. arachidonic acid metabolic process Source: Reactome
    3. cellular lactam catabolic process Source: UniProtKB
    4. cellular response to calcium ion Source: UniProtKB
    5. cellular response to drug Source: UniProtKB
    6. cellular response to nitric oxide Source: UniProtKB
    7. glutathione metabolic process Source: UniProtKB
    8. homocysteine metabolic process Source: UniProtKB
    9. leukotriene metabolic process Source: Reactome
    10. negative regulation of apoptotic process Source: UniProtKB
    11. negative regulation of cell migration Source: UniProtKB
    12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    13. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00367-MONOMER.
    ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    SABIO-RKP16444.

    Protein family/group databases

    MEROPSiM19.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidase 1 (EC:3.4.13.19)
    Alternative name(s):
    Dehydropeptidase-I
    Microsomal dipeptidase
    Renal dipeptidase
    Short name:
    hRDP
    Gene namesi
    Name:DPEP1
    Synonyms:MDP, RDP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:3002. DPEP1.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. apical part of cell Source: UniProtKB
    3. apical plasma membrane Source: UniProtKB-SubCell
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProtKB
    6. microvillus membrane Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi141 – 1411E → D or C: Complete loss of activity.
    Mutagenesisi141 – 1411E → Q: Partial loss of activity.

    Organism-specific databases

    PharmGKBiPA144.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16163 PublicationsAdd
    BLAST
    Chaini17 – 385369Dipeptidase 1PRO_0000018652Add
    BLAST
    Propeptidei386 – 41126Removed in mature formPRO_0000018653Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)2 Publications
    Disulfide bondi87 ↔ 1701 PublicationPROSITE-ProRule annotation
    Disulfide bondi242 ↔ 2741 PublicationPROSITE-ProRule annotation
    Glycosylationi279 – 2791N-linked (GlcNAc...)1 Publication
    Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
    Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 – 377Interchain1 PublicationPROSITE-ProRule annotation
    Lipidationi385 – 3851GPI-anchor amidated serine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP16444.
    PaxDbiP16444.
    PRIDEiP16444.

    PTM databases

    PhosphoSiteiP16444.

    Expressioni

    Gene expression databases

    ArrayExpressiP16444.
    BgeeiP16444.
    CleanExiHS_DPEP1.
    GenevestigatoriP16444.

    Organism-specific databases

    HPAiHPA009426.
    HPA012783.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 PublicationPROSITE-ProRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KIAA1279Q96EK52EBI-749514,EBI-744150

    Protein-protein interaction databases

    BioGridi108134. 2 interactions.
    IntActiP16444. 1 interaction.
    MINTiMINT-5000950.
    STRINGi9606.ENSP00000261615.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 2710
    Beta strandi32 – 376
    Helixi39 – 479
    Helixi54 – 563
    Turni58 – 603
    Beta strandi63 – 653
    Helixi68 – 736
    Beta strandi76 – 838
    Helixi87 – 893
    Turni90 – 934
    Helixi94 – 11118
    Turni113 – 1153
    Beta strandi116 – 1183
    Helixi122 – 13110
    Beta strandi134 – 1418
    Helixi143 – 1464
    Helixi150 – 1589
    Beta strandi161 – 1666
    Beta strandi168 – 1703
    Beta strandi173 – 1753
    Helixi178 – 1803
    Turni181 – 1833
    Beta strandi188 – 1925
    Helixi194 – 20613
    Beta strandi209 – 2113
    Helixi217 – 22610
    Beta strandi232 – 2354
    Turni239 – 2413
    Helixi250 – 25910
    Beta strandi262 – 2654
    Helixi269 – 2724
    Beta strandi274 – 2763
    Helixi280 – 29415
    Helixi296 – 2983
    Beta strandi299 – 3013
    Turni305 – 3073
    Helixi321 – 33010
    Helixi335 – 3428
    Helixi344 – 35613
    Beta strandi359 – 3613
    Helixi370 – 3723
    Beta strandi375 – 3773
    Turni381 – 3833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ITQX-ray2.30A/B17-385[»]
    1ITUX-ray2.00A/B17-385[»]
    ProteinModelPortaliP16444.
    SMRiP16444. Positions 17-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16444.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2355.
    HOGENOMiHOG000072016.
    HOVERGENiHBG002339.
    InParanoidiP16444.
    KOiK01273.
    OMAiGHYATAM.
    PhylomeDBiP16444.
    TreeFamiTF324523.

    Family and domain databases

    InterProiIPR000180. Dipep_AS.
    IPR028536. Dpep1.
    IPR008257. Renal_dipep_fam.
    [Graphical view]
    PANTHERiPTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF17. PTHR10443:SF17. 1 hit.
    PfamiPF01244. Peptidase_M19. 1 hit.
    [Graphical view]
    PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16444-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWSGWWLWPL VAVCTADFFR DEAERIMRDS PVIDGHNDLP WQLLDMFNNR    50
    LQDERANLTT LAGTHTNIPK LRAGFVGGQF WSVYTPCDTQ NKDAVRRTLE 100
    QMDVVHRMCR MYPETFLYVT SSAGIRQAFR EGKVASLIGV EGGHSIDSSL 150
    GVLRALYQLG MRYLTLTHSC NTPWADNWLV DTGDSEPQSQ GLSPFGQRVV 200
    KELNRLGVLI DLAHVSVATM KATLQLSRAP VIFSHSSAYS VCASRRNVPD 250
    DVLRLVKQTD SLVMVNFYNN YISCTNKANL SQVADHLDHI KEVAGARAVG 300
    FGGDFDGVPR VPEGLEDVSK YPDLIAELLR RNWTEAEVKG ALADNLLRVF 350
    EAVEQASNLT QAPEEEPIPL DQLGGSCRTH YGYSSGASSL HRHWGLLLAS 400
    LAPLVLCLSL L 411
    Length:411
    Mass (Da):45,674
    Last modified:March 7, 2006 - v3
    Checksum:iC8C6474C3479D20D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91P → S(PubMed:8439558)Curated
    Sequence conflicti9 – 91P → S(PubMed:7764673)Curated
    Sequence conflicti102 – 1021M → R(PubMed:2303490)Curated
    Sequence conflicti125 – 1251I → R(PubMed:2303490)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti246 – 2461R → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036496
    Natural varianti351 – 3511E → K.
    Corresponds to variant rs1126464 [ dbSNP | Ensembl ].
    VAR_061375
    Natural varianti351 – 3511E → Q.
    Corresponds to variant rs1126464 [ dbSNP | Ensembl ].
    VAR_061376

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13137 Genomic DNA. Translation: BAA02430.1.
    J05257 mRNA. Translation: AAB59410.1.
    D13138 mRNA. Translation: BAA02431.1.
    S70330, S70329 Genomic DNA. Translation: AAC60630.2.
    CH471184 Genomic DNA. Translation: EAW66719.1.
    CH471184 Genomic DNA. Translation: EAW66720.1.
    BC017023 mRNA. Translation: AAH17023.1.
    BT006664 mRNA. Translation: AAP35310.1.
    CCDSiCCDS10982.1.
    PIRiS29848.
    RefSeqiNP_001121613.1. NM_001128141.2.
    NP_004404.1. NM_004413.3.
    XP_005256342.1. XM_005256285.2.
    XP_005256343.1. XM_005256286.1.
    UniGeneiHs.109.

    Genome annotation databases

    EnsembliENST00000261615; ENSP00000261615; ENSG00000015413.
    ENST00000393092; ENSP00000376807; ENSG00000015413.
    ENST00000421184; ENSP00000397313; ENSG00000015413.
    GeneIDi1800.
    KEGGihsa:1800.
    UCSCiuc002fnr.4. human.

    Polymorphism databases

    DMDMi92090943.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13137 Genomic DNA. Translation: BAA02430.1 .
    J05257 mRNA. Translation: AAB59410.1 .
    D13138 mRNA. Translation: BAA02431.1 .
    S70330 , S70329 Genomic DNA. Translation: AAC60630.2 .
    CH471184 Genomic DNA. Translation: EAW66719.1 .
    CH471184 Genomic DNA. Translation: EAW66720.1 .
    BC017023 mRNA. Translation: AAH17023.1 .
    BT006664 mRNA. Translation: AAP35310.1 .
    CCDSi CCDS10982.1.
    PIRi S29848.
    RefSeqi NP_001121613.1. NM_001128141.2.
    NP_004404.1. NM_004413.3.
    XP_005256342.1. XM_005256285.2.
    XP_005256343.1. XM_005256286.1.
    UniGenei Hs.109.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ITQ X-ray 2.30 A/B 17-385 [» ]
    1ITU X-ray 2.00 A/B 17-385 [» ]
    ProteinModelPortali P16444.
    SMRi P16444. Positions 17-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108134. 2 interactions.
    IntActi P16444. 1 interaction.
    MINTi MINT-5000950.
    STRINGi 9606.ENSP00000261615.

    Chemistry

    BindingDBi P16444.
    ChEMBLi CHEMBL1989.
    DrugBanki DB01597. Cilastatin.

    Protein family/group databases

    MEROPSi M19.001.

    PTM databases

    PhosphoSitei P16444.

    Polymorphism databases

    DMDMi 92090943.

    Proteomic databases

    MaxQBi P16444.
    PaxDbi P16444.
    PRIDEi P16444.

    Protocols and materials databases

    DNASUi 1800.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261615 ; ENSP00000261615 ; ENSG00000015413 .
    ENST00000393092 ; ENSP00000376807 ; ENSG00000015413 .
    ENST00000421184 ; ENSP00000397313 ; ENSG00000015413 .
    GeneIDi 1800.
    KEGGi hsa:1800.
    UCSCi uc002fnr.4. human.

    Organism-specific databases

    CTDi 1800.
    GeneCardsi GC16P089679.
    HGNCi HGNC:3002. DPEP1.
    HPAi HPA009426.
    HPA012783.
    MIMi 179780. gene.
    neXtProti NX_P16444.
    PharmGKBi PA144.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2355.
    HOGENOMi HOG000072016.
    HOVERGENi HBG002339.
    InParanoidi P16444.
    KOi K01273.
    OMAi GHYATAM.
    PhylomeDBi P16444.
    TreeFami TF324523.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00367-MONOMER.
    Reactomei REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    SABIO-RK P16444.

    Miscellaneous databases

    EvolutionaryTracei P16444.
    GeneWikii Dipeptidase_1.
    GenomeRNAii 1800.
    NextBioi 7331.
    PROi P16444.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16444.
    Bgeei P16444.
    CleanExi HS_DPEP1.
    Genevestigatori P16444.

    Family and domain databases

    InterProi IPR000180. Dipep_AS.
    IPR028536. Dpep1.
    IPR008257. Renal_dipep_fam.
    [Graphical view ]
    PANTHERi PTHR10443. PTHR10443. 1 hit.
    PTHR10443:SF17. PTHR10443:SF17. 1 hit.
    Pfami PF01244. Peptidase_M19. 1 hit.
    [Graphical view ]
    PROSITEi PS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and structural analysis of genomic DNA for human renal dipeptidase."
      Satoh S., Kusunoki C., Konta Y., Niwa M., Kohsaka M.
      Biochim. Biophys. Acta 1172:181-183(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    2. "Primary structure of human microsomal dipeptidase deduced from molecular cloning."
      Adachi H., Tawaragi Y., Inuzuka C., Kubota I., Tsujimoto M., Nishihara T., Nakazato H.
      J. Biol. Chem. 265:3992-3995(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Gene structural analysis and expression of human renal dipeptidase."
      Satoh S., Ohtsuka K., Keida Y., Kusunoki C., Konta Y., Niwa M., Kohsaka M.
      Biotechnol. Prog. 10:134-140(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Colon.
    7. "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme."
      Hooper N.M., Keen J.N., Turner A.J.
      Biochem. J. 265:429-433(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-56; 111-121 AND 298-310.
    8. "Purification and characterization of human microsomal dipeptidase."
      Adachi H., Kubota I., Okamura N., Iwata H., Tsujimoto M., Nakazato H., Nishihara T., Noguchi T.
      J. Biochem. 105:957-961(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-39.
    9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-31.
    10. "Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form."
      Adachi H., Katayama T., Inuzuka C., Oikawa S., Tsujimoto M., Nakazato H.
      J. Biol. Chem. 265:15341-15345(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR AT SER-385.
    11. "Importance of Glu-125 in the catalytic activity of human renal dipeptidase."
      Adachi H., Katayama T., Nakazato H., Tsujimoto M.
      Biochim. Biophys. Acta 1163:42-48(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION BY CHEMICAL MODIFICATION.
    12. "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-57 AND ASN-279.
      Tissue: Liver.
    13. "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis."
      Nitanai Y., Satow Y., Adachi H., Tsujimoto M.
      J. Mol. Biol. 321:177-184(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-385 IN COMPLEX WITH ZINC AND CILASTATIN, SUBUNIT, COFACTOR, DISULFIDE BONDS, GLYCOSYLATION AT ASN-57 AND ASN-332.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-246.

    Entry informationi

    Entry nameiDPEP1_HUMAN
    AccessioniPrimary (citable) accession number: P16444
    Secondary accession number(s): D3DX80, Q96AK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 161 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 16
      Human chromosome 16: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3