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P48052

- CBPA2_HUMAN

UniProt

P48052 - CBPA2_HUMAN

Protein

Carboxypeptidase A2

Gene

CPA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi179 – 1791Zinc; catalytic
    Metal bindingi182 – 1821Zinc; catalytic
    Binding sitei237 – 2371SubstrateBy similarity
    Metal bindingi306 – 3061Zinc; catalytic
    Active sitei380 – 3801Nucleophile

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB
    2. metallocarboxypeptidase activity Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. protein catabolic process in the vacuole Source: ProtInc

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP48052.

    Protein family/group databases

    MEROPSiM14.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase A2 (EC:3.4.17.15)
    Gene namesi
    Name:CPA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2297. CPA2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26817.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 11496Activation peptide1 PublicationPRO_0000004353Add
    BLAST
    Chaini115 – 419305Carboxypeptidase A2PRO_0000004354Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi248 ↔ 271
    Disulfide bondi320 ↔ 354

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP48052.
    PRIDEiP48052.

    PTM databases

    PhosphoSiteiP48052.

    Expressioni

    Gene expression databases

    ArrayExpressiP48052.
    BgeeiP48052.
    CleanExiHS_CPA2.
    GenevestigatoriP48052.

    Organism-specific databases

    HPAiHPA020342.
    HPA021317.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-125621.
    STRINGi9606.ENSP00000222481.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 305
    Helixi35 – 4612
    Helixi48 – 503
    Beta strandi53 – 564
    Beta strandi65 – 695
    Helixi71 – 733
    Helixi74 – 8310
    Beta strandi88 – 936
    Helixi95 – 11218
    Turni113 – 1153
    Beta strandi120 – 1223
    Helixi126 – 13914
    Turni141 – 1433
    Beta strandi144 – 1518
    Beta strandi157 – 1637
    Beta strandi166 – 1683
    Beta strandi171 – 1755
    Helixi183 – 19917
    Turni200 – 2023
    Helixi204 – 2129
    Beta strandi214 – 2196
    Helixi223 – 2319
    Helixi253 – 2553
    Beta strandi257 – 2604
    Beta strandi263 – 2675
    Helixi284 – 29613
    Beta strandi299 – 3068
    Beta strandi311 – 3155
    Beta strandi317 – 3193
    Helixi326 – 34116
    Turni342 – 3443
    Beta strandi349 – 3524
    Helixi353 – 3564
    Helixi364 – 3718
    Beta strandi375 – 3806
    Beta strandi384 – 3874
    Helixi393 – 3953
    Helixi396 – 41621

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYEX-ray1.80A19-419[»]
    1DTDX-ray1.65A118-419[»]
    1O6XNMR-A19-96[»]
    ProteinModelPortaliP48052.
    SMRiP48052. Positions 19-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48052.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni179 – 1824Substrate bindingBy similarity
    Regioni254 – 2552Substrate bindingBy similarity
    Regioni307 – 3082Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOVERGENiHBG050815.
    InParanoidiP48052.
    KOiK01298.
    OMAiKAIMEHV.
    OrthoDBiEOG7RZ5Q9.
    PhylomeDBiP48052.
    TreeFamiTF317197.

    Family and domain databases

    Gene3Di3.30.70.340. 1 hit.
    InterProiIPR000834. Peptidase_M14.
    IPR003146. Prot_inh_M14A.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PfamiPF00246. Peptidase_M14. 1 hit.
    PF02244. Propep_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF54897. SSF54897. 1 hit.
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P48052-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMRLILFFG ALFGHIYCLE TFVGDQVLEI VPSNEEQIKN LLQLEAQEHL    50
    QLDFWKSPTT PGETAHVRVP FVNVQAVKVF LESQGIAYSI MIEDVQVLLD 100
    KENEEMLFNR RRERSGNFNF GAYHTLEEIS QEMDNLVAEH PGLVSKVNIG 150
    SSFENRPMNV LKFSTGGDKP AIWLDAGIHA REWVTQATAL WTANKIVSDY 200
    GKDPSITSIL DALDIFLLPV TNPDGYVFSQ TKNRMWRKTR SKVSGSLCVG 250
    VDPNRNWDAG FGGPGASSNP CSDSYHGPSA NSEVEVKSIV DFIKSHGKVK 300
    AFITLHSYSQ LLMFPYGYKC TKLDDFDELS EVAQKAAQSL RSLHGTKYKV 350
    GPICSVIYQA SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPARQILPTA 400
    EETWLGLKAI MEHVRDHPY 419
    Length:419
    Mass (Da):47,030
    Last modified:April 20, 2010 - v3
    Checksum:i00269F2AE50CA38D
    GO

    Sequence cautioni

    The sequence AAA74425.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH07009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH14571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH15140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAL24092.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191L → S AA sequence (PubMed:2920728)Curated
    Sequence conflicti39 – 391K → N AA sequence (PubMed:2920728)Curated
    Sequence conflicti304 – 3041T → I in AAA74425. (PubMed:7896805)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821E → G.2 Publications
    Corresponds to variant rs17850135 [ dbSNP | Ensembl ].
    VAR_031204

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC024085 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24092.1. Sequence problems.
    BC007009 mRNA. Translation: AAH07009.1. Different initiation.
    BC014571 mRNA. Translation: AAH14571.1. Different initiation.
    BC015140 mRNA. Translation: AAH15140.1. Different initiation.
    U19977 mRNA. Translation: AAA74425.1. Different initiation.
    BT007403 mRNA. Translation: AAP36067.1.
    CCDSiCCDS5817.2.
    PIRiA56171.
    RefSeqiNP_001860.2. NM_001869.2.
    UniGeneiHs.490038.

    Genome annotation databases

    EnsembliENST00000222481; ENSP00000222481; ENSG00000158516.
    GeneIDi1358.
    KEGGihsa:1358.
    UCSCiuc003vpq.3. human.

    Polymorphism databases

    DMDMi294862522.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC024085 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24092.1 . Sequence problems.
    BC007009 mRNA. Translation: AAH07009.1 . Different initiation.
    BC014571 mRNA. Translation: AAH14571.1 . Different initiation.
    BC015140 mRNA. Translation: AAH15140.1 . Different initiation.
    U19977 mRNA. Translation: AAA74425.1 . Different initiation.
    BT007403 mRNA. Translation: AAP36067.1 .
    CCDSi CCDS5817.2.
    PIRi A56171.
    RefSeqi NP_001860.2. NM_001869.2.
    UniGenei Hs.490038.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYE X-ray 1.80 A 19-419 [» ]
    1DTD X-ray 1.65 A 118-419 [» ]
    1O6X NMR - A 19-96 [» ]
    ProteinModelPortali P48052.
    SMRi P48052. Positions 19-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-125621.
    STRINGi 9606.ENSP00000222481.

    Chemistry

    BindingDBi P48052.

    Protein family/group databases

    MEROPSi M14.002.

    PTM databases

    PhosphoSitei P48052.

    Polymorphism databases

    DMDMi 294862522.

    Proteomic databases

    PaxDbi P48052.
    PRIDEi P48052.

    Protocols and materials databases

    DNASUi 1358.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222481 ; ENSP00000222481 ; ENSG00000158516 .
    GeneIDi 1358.
    KEGGi hsa:1358.
    UCSCi uc003vpq.3. human.

    Organism-specific databases

    CTDi 1358.
    GeneCardsi GC07P129906.
    HGNCi HGNC:2297. CPA2.
    HPAi HPA020342.
    HPA021317.
    MIMi 600688. gene.
    neXtProti NX_P48052.
    PharmGKBi PA26817.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    HOVERGENi HBG050815.
    InParanoidi P48052.
    KOi K01298.
    OMAi KAIMEHV.
    OrthoDBi EOG7RZ5Q9.
    PhylomeDBi P48052.
    TreeFami TF317197.

    Enzyme and pathway databases

    SABIO-RK P48052.

    Miscellaneous databases

    EvolutionaryTracei P48052.
    GeneWikii Carboxypeptidase_A2.
    GenomeRNAii 1358.
    NextBioi 5501.
    PROi P48052.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48052.
    Bgeei P48052.
    CleanExi HS_CPA2.
    Genevestigatori P48052.

    Family and domain databases

    Gene3Di 3.30.70.340. 1 hit.
    InterProi IPR000834. Peptidase_M14.
    IPR003146. Prot_inh_M14A.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    Pfami PF00246. Peptidase_M14. 1 hit.
    PF02244. Propep_M14. 1 hit.
    [Graphical view ]
    PRINTSi PR00765. CRBOXYPTASEA.
    SMARTi SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54897. SSF54897. 1 hit.
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 GLY-82.
      Tissue: Brain and Pancreas.
    4. "The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model."
      Catasus L., Vendrell J., Aviles F.X., Carreira S., Puigserver A., Billeter M.
      J. Biol. Chem. 270:6651-6657(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-419, 3D-STRUCTURE MODELING.
      Tissue: Pancreas.
    5. "Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2."
      Laethem R.M., Blumenkopf T.A., Cory M., Elwell L., Moxham C.P., Ray P.H., Walton L.M., Smith G.K.
      Arch. Biochem. Biophys. 332:8-18(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-419, CHARACTERIZATION.
    6. "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] OF 3-419, VARIANT GLY-82.
    7. "Purification and properties of five different forms of human procarboxypeptidases."
      Pascual R., Burgos F.J., Salva M., Soriano F., Mendez E., Aviles F.X.
      Eur. J. Biochem. 179:609-616(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-45, CHARACTERIZATION.
    8. "Separation of human pancreatic carboxypeptidase A isoenzymes by high performance liquid chromatography."
      Linder D., Linder M., Schade H., Sziegoleit A.
      Biomed. Chromatogr. 7:143-145(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 115-144.
      Tissue: Pancreas.
    9. "The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen."
      Garcia-Saez I., Reverter D., Vendrell J., Aviles F.X., Coll M.
      EMBO J. 16:6906-6913(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    10. "Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2."
      Reverter D., Garcia-Saez I., Catasus L., Vendrell J., Coll M., Aviles F.X.
      FEBS Lett. 420:7-10(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-419.
    11. "Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2."
      Reverter D., Fernandez-Catalan C., Baumgartner R., Pfander R., Huber R., Bode W., Vendrell J., Holak T.A., Aviles F.X.
      Nat. Struct. Biol. 7:322-328(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 118-419.
    12. "A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins."
      Dantas G., Kuhlman B., Callender D., Wong M., Baker D.
      J. Mol. Biol. 332:449-460(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    13. "NMR solution structure of the activation domain of human procarboxypeptidase A2."
      Jimenez M.A., Villegas V., Santoro J., Serrano L., Vendrell J., Aviles F.X., Rico M.
      Protein Sci. 12:296-305(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 19-96.

    Entry informationi

    Entry nameiCBPA2_HUMAN
    AccessioniPrimary (citable) accession number: P48052
    Secondary accession number(s): A4D1M4
    , C9JIK1, Q53XS1, Q96A12, Q96QN3, Q9UCF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 150 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 7
      Human chromosome 7: 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