Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P48147

- PPCE_HUMAN

UniProt

P48147 - PPCE_HUMAN

Protein

Prolyl endopeptidase

Gene

PREP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.

    Catalytic activityi

    Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei554 – 5541Charge relay systemPROSITE-ProRule annotation
    Active sitei641 – 6411Charge relay systemPROSITE-ProRule annotation
    Active sitei680 – 6801Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: ProtInc
    2. serine-type exopeptidase activity Source: InterPro
    3. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS09.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolyl endopeptidase (EC:3.4.21.26)
    Short name:
    PE
    Alternative name(s):
    Post-proline cleaving enzyme
    Gene namesi
    Name:PREP
    Synonyms:PEP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9358. PREP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. membrane Source: UniProtKB
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33730.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 710710Prolyl endopeptidasePRO_0000122401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei157 – 1571N6-acetyllysine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48147.
    PaxDbiP48147.
    PRIDEiP48147.

    PTM databases

    PhosphoSiteiP48147.

    Miscellaneous databases

    PMAP-CutDBQ8N6D4.

    Expressioni

    Gene expression databases

    BgeeiP48147.
    CleanExiHS_PREP.
    GenevestigatoriP48147.

    Organism-specific databases

    HPAiCAB025414.
    HPA031388.
    HPA031389.
    HPA031390.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GAPDHP044065EBI-1049962,EBI-354056

    Protein-protein interaction databases

    BioGridi111541. 6 interactions.
    IntActiP48147. 1 interaction.
    MINTiMINT-5004282.
    STRINGi9606.ENSP00000358106.

    Structurei

    Secondary structure

    1
    710
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 194
    Beta strandi22 – 254
    Helixi29 – 324
    Helixi37 – 5519
    Helixi59 – 7012
    Beta strandi80 – 823
    Beta strandi85 – 917
    Beta strandi99 – 1057
    Beta strandi111 – 1144
    Helixi116 – 1194
    Beta strandi121 – 1233
    Beta strandi125 – 1328
    Beta strandi136 – 14510
    Beta strandi151 – 1577
    Turni158 – 1614
    Beta strandi162 – 17110
    Beta strandi176 – 1783
    Beta strandi182 – 1898
    Beta strandi198 – 2003
    Beta strandi209 – 2146
    Helixi219 – 2213
    Beta strandi223 – 2264
    Beta strandi235 – 2406
    Beta strandi246 – 25712
    Beta strandi260 – 2656
    Helixi266 – 2683
    Beta strandi270 – 2734
    Beta strandi280 – 2834
    Beta strandi285 – 2884
    Beta strandi290 – 2967
    Beta strandi299 – 3046
    Beta strandi312 – 3176
    Helixi323 – 3253
    Beta strandi327 – 3304
    Beta strandi337 – 3448
    Turni345 – 3473
    Beta strandi348 – 3558
    Beta strandi358 – 3658
    Turni366 – 3683
    Beta strandi371 – 3755
    Beta strandi379 – 3868
    Beta strandi392 – 3998
    Beta strandi401 – 4033
    Beta strandi406 – 4116
    Beta strandi414 – 4163
    Beta strandi420 – 4234
    Helixi432 – 4343
    Beta strandi435 – 4439
    Beta strandi449 – 4579
    Beta strandi468 – 4714
    Helixi486 – 49510
    Beta strandi498 – 5025
    Helixi511 – 5166
    Helixi520 – 5234
    Helixi524 – 53916
    Helixi545 – 5473
    Beta strandi548 – 5536
    Helixi555 – 56612
    Helixi568 – 5703
    Beta strandi572 – 5787
    Turni583 – 5853
    Helixi586 – 5883
    Helixi592 – 5954
    Helixi596 – 5994
    Helixi605 – 61410
    Helixi616 – 6183
    Beta strandi632 – 6387
    Helixi647 – 65913
    Turni660 – 6623
    Beta strandi670 – 6778
    Helixi686 – 70419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DDUX-ray1.56A2-710[»]
    ProteinModelPortaliP48147.
    SMRiP48147. Positions 2-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48147.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Curated

    Phylogenomic databases

    eggNOGiCOG1505.
    HOGENOMiHOG000238967.
    HOVERGENiHBG007251.
    InParanoidiP48147.
    KOiK01322.
    OMAiDYQTIQI.
    OrthoDBiEOG78PV88.
    PhylomeDBiP48147.
    TreeFamiTF300655.

    Family and domain databases

    Gene3Di2.130.10.120. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR023302. Pept_S9A_N.
    IPR001375. Peptidase_S9.
    IPR002470. Peptidase_S9A.
    [Graphical view]
    PANTHERiPTHR11757. PTHR11757. 1 hit.
    PfamiPF00326. Peptidase_S9. 1 hit.
    PF02897. Peptidase_S9_N. 1 hit.
    [Graphical view]
    PRINTSiPR00862. PROLIGOPTASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48147-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSLQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT    50
    VPFLEQCPIR GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL 100
    YVQDSLEGEA RVFLDPNILS DDGTVALRGY AFSEDGEYFA YGLSASGSDW 150
    VTIKFMKVDG AKELPDVLER VKFSCMAWTH DGKGMFYNSY PQQDGKSDGT 200
    ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL SDDGRYVLLS 250
    IREGCDPVNR LWYCDLQQES SGIAGILKWV KLIDNFEGEY DYVTNEGTVF 300
    TFKTNRQSPN YRVINIDFRD PEESKWKVLV PEHEKDVLEW IACVRSNFLV 350
    LCYLHDVKNI LQLHDLTTGA LLKTFPLDVG SIVGYSGQKK DTEIFYQFTS 400
    FLSPGIIYHC DLTKEELEPR VFREVTVKGI DASDYQTVQI FYPSKDGTKI 450
    PMFIVHKKGI KLDGSHPAFL YGYGGFNISI TPNYSVSRLI FVRHMGGILA 500
    VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE GYTSPKRLTI 550
    NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG 600
    CSDSKQHFEW LVKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL 650
    KFIATLQYIV GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI 700
    ARCLNVDWIP 710
    Length:710
    Mass (Da):80,700
    Last modified:November 25, 2008 - v2
    Checksum:i139072B990820B90
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41L → F in CAA52605. (PubMed:7959018)Curated
    Sequence conflicti4 – 41L → F in BAA04661. (PubMed:8089089)Curated
    Sequence conflicti16 – 161V → I in BAA04661. (PubMed:8089089)Curated
    Sequence conflicti245 – 2451R → C in BAA04661. (PubMed:8089089)Curated
    Sequence conflicti298 – 2981T → A in BAA04661. (PubMed:8089089)Curated
    Sequence conflicti319 – 3191R → W in CAA52605. (PubMed:7959018)Curated
    Sequence conflicti440 – 4401I → L in BAA04661. (PubMed:8089089)Curated
    Sequence conflicti459 – 4591G → S in BAA04661. (PubMed:8089089)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti351 – 3511L → V.
    Corresponds to variant rs12192054 [ dbSNP | Ensembl ].
    VAR_047790
    Natural varianti706 – 7061V → I.1 Publication
    Corresponds to variant rs1051484 [ dbSNP | Ensembl ].
    VAR_047791

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74496 mRNA. Translation: CAA52605.1.
    D21102 mRNA. Translation: BAA04661.1.
    AY660966 mRNA. Translation: AAV70495.1.
    AL590871, AL133406, AL139191 Genomic DNA. Translation: CAH72545.1.
    AL139191, AL133406, AL590871 Genomic DNA. Translation: CAI21416.1.
    AL133406, AL139191, AL590871 Genomic DNA. Translation: CAI42689.1.
    CH471051 Genomic DNA. Translation: EAW48426.1.
    BC030636 mRNA. Translation: AAH30636.1.
    CCDSiCCDS5053.1.
    PIRiI38134.
    JC2257.
    RefSeqiNP_002717.3. NM_002726.4.
    UniGeneiHs.436564.

    Genome annotation databases

    EnsembliENST00000369110; ENSP00000358106; ENSG00000085377.
    GeneIDi5550.
    KEGGihsa:5550.
    UCSCiuc003prc.3. human.

    Polymorphism databases

    DMDMi215273868.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74496 mRNA. Translation: CAA52605.1 .
    D21102 mRNA. Translation: BAA04661.1 .
    AY660966 mRNA. Translation: AAV70495.1 .
    AL590871 , AL133406 , AL139191 Genomic DNA. Translation: CAH72545.1 .
    AL139191 , AL133406 , AL590871 Genomic DNA. Translation: CAI21416.1 .
    AL133406 , AL139191 , AL590871 Genomic DNA. Translation: CAI42689.1 .
    CH471051 Genomic DNA. Translation: EAW48426.1 .
    BC030636 mRNA. Translation: AAH30636.1 .
    CCDSi CCDS5053.1.
    PIRi I38134.
    JC2257.
    RefSeqi NP_002717.3. NM_002726.4.
    UniGenei Hs.436564.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DDU X-ray 1.56 A 2-710 [» ]
    ProteinModelPortali P48147.
    SMRi P48147. Positions 2-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111541. 6 interactions.
    IntActi P48147. 1 interaction.
    MINTi MINT-5004282.
    STRINGi 9606.ENSP00000358106.

    Chemistry

    BindingDBi P48147.
    ChEMBLi CHEMBL3202.
    DrugBanki DB00107. Oxytocin.
    GuidetoPHARMACOLOGYi 2395.

    Protein family/group databases

    MEROPSi S09.001.

    PTM databases

    PhosphoSitei P48147.

    Polymorphism databases

    DMDMi 215273868.

    Proteomic databases

    MaxQBi P48147.
    PaxDbi P48147.
    PRIDEi P48147.

    Protocols and materials databases

    DNASUi 5550.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369110 ; ENSP00000358106 ; ENSG00000085377 .
    GeneIDi 5550.
    KEGGi hsa:5550.
    UCSCi uc003prc.3. human.

    Organism-specific databases

    CTDi 5550.
    GeneCardsi GC06M105725.
    HGNCi HGNC:9358. PREP.
    HPAi CAB025414.
    HPA031388.
    HPA031389.
    HPA031390.
    MIMi 600400. gene.
    neXtProti NX_P48147.
    PharmGKBi PA33730.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1505.
    HOGENOMi HOG000238967.
    HOVERGENi HBG007251.
    InParanoidi P48147.
    KOi K01322.
    OMAi DYQTIQI.
    OrthoDBi EOG78PV88.
    PhylomeDBi P48147.
    TreeFami TF300655.

    Miscellaneous databases

    EvolutionaryTracei P48147.
    GeneWikii Prolyl_endopeptidase.
    GenomeRNAii 5550.
    NextBioi 21508.
    PMAP-CutDB Q8N6D4.
    PROi P48147.
    SOURCEi Search...

    Gene expression databases

    Bgeei P48147.
    CleanExi HS_PREP.
    Genevestigatori P48147.

    Family and domain databases

    Gene3Di 2.130.10.120. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR023302. Pept_S9A_N.
    IPR001375. Peptidase_S9.
    IPR002470. Peptidase_S9A.
    [Graphical view ]
    PANTHERi PTHR11757. PTHR11757. 1 hit.
    Pfami PF00326. Peptidase_S9. 1 hit.
    PF02897. Peptidase_S9_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00862. PROLIGOPTASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase."
      Vanhoof G., Goossens F., Hendriks L., De Meester I., Hendriks D., Vriend G., van Broeckhoven C., Scharpe S.
      Gene 149:363-366(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    2. "Molecular cloning and characterization of prolyl endopeptidase from human T cells."
      Shirasawa Y., Osawa T., Hirashima A.
      J. Biochem. 115:724-729(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-706.
    3. "cDNA cloning and recombinant expression of human brain prolyl oligopeptidase."
      Tarrago T., Giralt E.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Skin.
    7. "The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family."
      Goossens F., De Meester I., Vanhoof G., Hendriks D., Vriend G., Scharpe S.
      Eur. J. Biochem. 233:432-441(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 136-149, SUBUNIT, CHARACTERIZATION.
      Tissue: Lymphocyte.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP)."
      Haffner C.D., Diaz C.J., Miller A.B., Reid R.A., Madauss K.P., Hassell A., Hanlon M.H., Porter D.J., Becherer J.D., Carter L.H.
      Bioorg. Med. Chem. Lett. 18:4360-4363(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 2-710 IN COMPLEX WITH INHIBITOR.

    Entry informationi

    Entry nameiPPCE_HUMAN
    AccessioniPrimary (citable) accession number: P48147
    Secondary accession number(s): Q8N6D4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 136 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 6
      Human chromosome 6: 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