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Q9UBR2

- CATZ_HUMAN

UniProt

Q9UBR2 - CATZ_HUMAN

Protein

Cathepsin Z

Gene

CTSZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity.

    Catalytic activityi

    Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei92 – 921
    Active sitei241 – 2411
    Active sitei261 – 2611

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. angiotensin maturation Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. epithelial tube branching involved in lung morphogenesis Source: Ensembl
    4. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.18.1. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    REACT_19287. Lysosome Vesicle Biogenesis.

    Protein family/group databases

    MEROPSiC01.013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin Z (EC:3.4.18.1)
    Alternative name(s):
    Cathepsin P
    Cathepsin X
    Gene namesi
    Name:CTSZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:2547. CTSZ.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: LIFEdb
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular membrane-bounded organelle Source: HPA
    5. lysosome Source: UniProtKB-SubCell
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27043.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 6138Activation peptidePRO_0000026285Add
    BLAST
    Chaini62 – 303242Cathepsin ZPRO_0000026286Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi89 ↔ 132
    Disulfide bondi126 ↔ 164
    Disulfide bondi154 ↔ 170
    Disulfide bondi173 ↔ 179
    Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
    Disulfide bondi214 ↔ 296
    Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9UBR2.
    PaxDbiQ9UBR2.
    PeptideAtlasiQ9UBR2.
    PRIDEiQ9UBR2.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ9UBR2.
    CleanExiHS_CTSZ.
    GenevestigatoriQ9UBR2.

    Organism-specific databases

    HPAiCAB025114.
    HPA049876.

    Interactioni

    Protein-protein interaction databases

    BioGridi107902. 3 interactions.
    IntActiQ9UBR2. 1 interaction.
    MINTiMINT-3079312.
    STRINGi9606.ENSP00000217131.

    Structurei

    Secondary structure

    1
    303
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 423
    Helixi59 – 613
    Beta strandi85 – 873
    Helixi92 – 10817
    Turni109 – 1113
    Helixi120 – 1267
    Beta strandi127 – 1315
    Beta strandi133 – 1353
    Helixi137 – 14610
    Beta strandi149 – 1513
    Helixi152 – 1543
    Helixi166 – 1694
    Beta strandi170 – 1756
    Beta strandi178 – 1814
    Beta strandi190 – 1967
    Helixi199 – 20911
    Beta strandi212 – 2165
    Helixi220 – 2234
    Beta strandi227 – 2304
    Beta strandi241 – 25111
    Beta strandi254 – 2607
    Beta strandi272 – 2765
    Helixi280 – 2834
    Helixi285 – 2873
    Turni290 – 2934
    Beta strandi296 – 3016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DEUX-ray1.70A/B27-303[»]
    1EF7X-ray2.67A/B62-303[»]
    ProteinModelPortaliQ9UBR2.
    SMRiQ9UBR2. Positions 29-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBR2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000264454.
    HOVERGENiHBG004456.
    InParanoidiQ9UBR2.
    KOiK08568.
    OMAiQCGTCTE.
    OrthoDBiEOG751NFZ.
    PhylomeDBiQ9UBR2.
    TreeFamiTF313225.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UBR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARRGPGWRP LLLLVLLAGA AQGGLYFRRG QTCYRPLRGD GLAPLGRSTY    50
    PRPHEYLSPA DLPKSWDWRN VDGVNYASIT RNQHIPQYCG SCWAHASTSA 100
    MADRINIKRK GAWPSTLLSV QNVIDCGNAG SCEGGNDLSV WDYAHQHGIP 150
    DETCNNYQAK DQECDKFNQC GTCNEFKECH AIRNYTLWRV GDYGSLSGRE 200
    KMMAEIYANG PISCGIMATE RLANYTGGIY AEYQDTTYIN HVVSVAGWGI 250
    SDGTEYWIVR NSWGEPWGER GWLRIVTSTY KDGKGARYNL AIEEHCTFGD 300
    PIV 303
    Length:303
    Mass (Da):33,868
    Last modified:May 1, 2000 - v1
    Checksum:i6274FD1974D0EBDC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481S → T in AAC39839. (PubMed:9642240)Curated
    Sequence conflicti150 – 1501P → S in AAC61477. (PubMed:9738465)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361P → S.1 Publication
    VAR_010254
    Natural varianti129 – 1291A → R Requires 2 nucleotide substitutions. 1 Publication
    VAR_010255
    Natural varianti286 – 2861A → T.
    Corresponds to variant rs34069356 [ dbSNP | Ensembl ].
    VAR_033719

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073890 mRNA. Translation: AAC61477.1.
    AF032906 mRNA. Translation: AAC39839.1.
    AF136273 mRNA. Translation: AAF13145.1.
    AF136276, AF136274, AF136275 Genomic DNA. Translation: AAF13148.1.
    AK314931 mRNA. Translation: BAG37437.1.
    AL109840 Genomic DNA. Translation: CAC09370.1.
    CH471077 Genomic DNA. Translation: EAW75448.1.
    BC042168 mRNA. Translation: AAH42168.1.
    AF009923 mRNA. Translation: AAC63141.1.
    CCDSiCCDS13474.1.
    RefSeqiNP_001327.2. NM_001336.3.
    UniGeneiHs.252549.

    Genome annotation databases

    EnsembliENST00000217131; ENSP00000217131; ENSG00000101160.
    GeneIDi1522.
    KEGGihsa:1522.
    UCSCiuc002yai.2. human.

    Polymorphism databases

    DMDMi12643324.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073890 mRNA. Translation: AAC61477.1 .
    AF032906 mRNA. Translation: AAC39839.1 .
    AF136273 mRNA. Translation: AAF13145.1 .
    AF136276 , AF136274 , AF136275 Genomic DNA. Translation: AAF13148.1 .
    AK314931 mRNA. Translation: BAG37437.1 .
    AL109840 Genomic DNA. Translation: CAC09370.1 .
    CH471077 Genomic DNA. Translation: EAW75448.1 .
    BC042168 mRNA. Translation: AAH42168.1 .
    AF009923 mRNA. Translation: AAC63141.1 .
    CCDSi CCDS13474.1.
    RefSeqi NP_001327.2. NM_001336.3.
    UniGenei Hs.252549.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DEU X-ray 1.70 A/B 27-303 [» ]
    1EF7 X-ray 2.67 A/B 62-303 [» ]
    ProteinModelPortali Q9UBR2.
    SMRi Q9UBR2. Positions 29-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107902. 3 interactions.
    IntActi Q9UBR2. 1 interaction.
    MINTi MINT-3079312.
    STRINGi 9606.ENSP00000217131.

    Chemistry

    BindingDBi Q9UBR2.
    ChEMBLi CHEMBL4160.

    Protein family/group databases

    MEROPSi C01.013.

    Polymorphism databases

    DMDMi 12643324.

    Proteomic databases

    MaxQBi Q9UBR2.
    PaxDbi Q9UBR2.
    PeptideAtlasi Q9UBR2.
    PRIDEi Q9UBR2.

    Protocols and materials databases

    DNASUi 1522.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217131 ; ENSP00000217131 ; ENSG00000101160 .
    GeneIDi 1522.
    KEGGi hsa:1522.
    UCSCi uc002yai.2. human.

    Organism-specific databases

    CTDi 1522.
    GeneCardsi GC20M057570.
    HGNCi HGNC:2547. CTSZ.
    HPAi CAB025114.
    HPA049876.
    MIMi 603169. gene.
    neXtProti NX_Q9UBR2.
    PharmGKBi PA27043.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000264454.
    HOVERGENi HBG004456.
    InParanoidi Q9UBR2.
    KOi K08568.
    OMAi QCGTCTE.
    OrthoDBi EOG751NFZ.
    PhylomeDBi Q9UBR2.
    TreeFami TF313225.

    Enzyme and pathway databases

    BRENDAi 3.4.18.1. 2681.
    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    REACT_19287. Lysosome Vesicle Biogenesis.

    Miscellaneous databases

    ChiTaRSi CTSZ. human.
    EvolutionaryTracei Q9UBR2.
    GeneWikii Cathepsin_Z.
    GenomeRNAii 1522.
    NextBioi 6299.
    PROi Q9UBR2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UBR2.
    CleanExi HS_CTSZ.
    Genevestigatori Q9UBR2.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions."
      Naegler D.K., Menard R.
      FEBS Lett. 434:135-139(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-36 AND ARG-129.
      Tissue: Ovary.
    2. "Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location."
      Santamaria I., Velasco G., Pendas A.M., Fueyo A., Lopez-Otin C.
      J. Biol. Chem. 273:16816-16823(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Prostate.
    3. "Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization."
      Deussing J., von Olshausen I., Peters C.
      Biochim. Biophys. Acta 1491:93-106(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Blood and Colon tumor.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Pancreas.
    8. "Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family."
      Pungercar J., Ivanovski G.
      Pflugers Arch. 439:R116-R118(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 11-303.
      Tissue: Ileum.
    9. "Human cathepsin X: a cysteine protease with unique carboxypeptidase activity."
      Naegler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Menard R.
      Biochemistry 38:12648-12654(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.
    10. "Tissue expression and immunolocalization of a novel human cathepsin P."
      Pungercar J., Viyjak A., Ivanovski G., Krizaj I.
      Pflugers Arch. 439:R119-R121(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "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-184.
      Tissue: Liver.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease."
      Guncar G., Klemencic I., Turk B., Turk V., Karaoglanovic-Carmona A., Juliano L., Turk D.
      Structure 8:305-313(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS).

    Entry informationi

    Entry nameiCATZ_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBR2
    Secondary accession number(s): B2RC40
    , O75331, Q9UQV5, Q9UQV6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 139 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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