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)

P42785

- PCP_HUMAN

UniProt

P42785 - PCP_HUMAN

Protein

Lysosomal Pro-X carboxypeptidase

Gene

PRCP

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 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

    Catalytic activityi

    Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei179 – 1791Charge relay system1 Publication
    Active sitei430 – 4301Charge relay system1 Publication
    Active sitei455 – 4551Charge relay system1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. serine-type carboxypeptidase activity Source: Reactome

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, intrinsic pathway Source: Reactome

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Protease

    Enzyme and pathway databases

    ReactomeiREACT_326. Intrinsic Pathway.

    Protein family/group databases

    MEROPSiS28.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosomal Pro-X carboxypeptidase (EC:3.4.16.2)
    Alternative name(s):
    Angiotensinase C
    Lysosomal carboxypeptidase C
    Proline carboxypeptidase
    Prolylcarboxypeptidase
    Short name:
    PRCP
    Gene namesi
    Name:PRCP
    Synonyms:PCP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9344. PRCP.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. lysosome Source: UniProtKB-SubCell
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33705.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 4524PRO_0000027308Add
    BLAST
    Chaini46 – 496451Lysosomal Pro-X carboxypeptidasePRO_0000027309Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
    Disulfide bondi215 ↔ 3721 Publication
    Disulfide bondi233 ↔ 3101 Publication
    Disulfide bondi264 ↔ 3431 Publication
    Glycosylationi317 – 3171N-linked (GlcNAc...)2 Publications
    Glycosylationi336 – 3361N-linked (GlcNAc...)1 Publication
    Glycosylationi345 – 3451N-linked (GlcNAc...)1 Publication
    Disulfide bondi364 ↔ 3941 Publication
    Glycosylationi415 – 4151N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP42785.
    PaxDbiP42785.
    PRIDEiP42785.

    PTM databases

    PhosphoSiteiP42785.

    Expressioni

    Tissue specificityi

    Highest levels in placenta, lung and liver. Also present in heart, brain, pancreas and kidney.

    Gene expression databases

    ArrayExpressiP42785.
    BgeeiP42785.
    CleanExiHS_PRCP.
    GenevestigatoriP42785.

    Organism-specific databases

    HPAiHPA017065.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GPR37L1O608832EBI-2803892,EBI-2927498

    Protein-protein interaction databases

    BioGridi111538. 12 interactions.
    IntActiP42785. 4 interactions.
    MINTiMINT-3015634.
    STRINGi9606.ENSP00000377055.

    Structurei

    Secondary structure

    1
    496
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi49 – 579
    Beta strandi67 – 759
    Turni81 – 833
    Beta strandi85 – 906
    Helixi96 – 1027
    Helixi104 – 11310
    Beta strandi115 – 1206
    Helixi132 – 1365
    Turni139 – 1413
    Helixi147 – 16418
    Helixi168 – 1703
    Beta strandi173 – 1786
    Helixi180 – 19112
    Turni193 – 1953
    Beta strandi197 – 2026
    Helixi217 – 22711
    Helixi233 – 24715
    Helixi251 – 26010
    Beta strandi263 – 2653
    Helixi272 – 28817
    Beta strandi295 – 3017
    Helixi305 – 3128
    Helixi320 – 33617
    Beta strandi342 – 3443
    Helixi354 – 36512
    Beta strandi375 – 3806
    Helixi387 – 39812
    Helixi406 – 4116
    Beta strandi422 – 4298
    Helixi431 – 4355
    Beta strandi441 – 45010
    Helixi457 – 4593
    Helixi468 – 48922

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N2ZX-ray2.79B46-491[»]
    ProteinModelPortaliP42785.
    SMRiP42785. Positions 46-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42785.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni194 – 334141SKS domainAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S28 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG290141.
    HOGENOMiHOG000238311.
    HOVERGENiHBG005526.
    KOiK01285.
    OMAiRSWKAIN.
    OrthoDBiEOG78WKRN.
    PhylomeDBiP42785.
    TreeFamiTF314414.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR008758. Peptidase_S28.
    [Graphical view]
    PANTHERiPTHR11010. PTHR11010. 1 hit.
    PfamiPF05577. Peptidase_S28. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42785-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGRRALLLLL LSFLAPWATI ALRPALRALG SLHLPTNPTS LPAVAKNYSV    50
    LYFQQKVDHF GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC 100
    NNTGFMWDVA EELKAMLVFA EHRYYGESLP FGDNSFKDSR HLNFLTSEQA 150
    LADFAELIKH LKRTIPGAEN QPVIAIGGSY GGMLAAWFRM KYPHMVVGAL 200
    AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIHRS WDAINRLSNT 250
    GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP 300
    LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA 350
    TSSLGTLGWS YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV 400
    RPRPSWITTM YGGKNISSHT NIVFSNGELD PWSGGGVTKD ITDTLVAVTI 450
    SEGAHHLDLR TKNALDPMSV LLARSLEVRH MKNWIRDFYD SAGKQH 496
    Length:496
    Mass (Da):55,800
    Last modified:November 1, 1995 - v1
    Checksum:iFC5DD570D3D3AB4F
    GO
    Isoform 2 (identifier: P42785-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         56-56: K → KALAAGQLHICIIQLNHYKTPL

    Note: No experimental confirmation available.

    Show »
    Length:517
    Mass (Da):58,100
    Checksum:iA2490258A57E6F23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041G → E in BAG52417. (PubMed:14702039)Curated
    Sequence conflicti248 – 2481S → L in BAG52417. (PubMed:14702039)Curated
    Sequence conflicti304 – 3041W → R in BAG52417. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121E → D.1 Publication
    Corresponds to variant rs2298668 [ dbSNP | Ensembl ].
    VAR_020464
    Natural varianti444 – 4441T → S.
    Corresponds to variant rs2228312 [ dbSNP | Ensembl ].
    VAR_029329

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei56 – 561K → KALAAGQLHICIIQLNHYKT PL in isoform 2. 1 PublicationVSP_045799

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13977 mRNA. Translation: AAA99891.1.
    AK091786 mRNA. Translation: BAG52417.1.
    AK312919 mRNA. Translation: BAG35764.1.
    AB451270 mRNA. Translation: BAG70084.1.
    AB451397 mRNA. Translation: BAG70211.1.
    AP000893 Genomic DNA. No translation available.
    AP001646 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW75074.1.
    CH471076 Genomic DNA. Translation: EAW75075.1.
    BC001500 mRNA. Translation: AAH01500.1.
    CCDSiCCDS41695.1. [P42785-2]
    CCDS8262.1. [P42785-1]
    PIRiA47352.
    RefSeqiNP_005031.1. NM_005040.2. [P42785-1]
    NP_955450.2. NM_199418.2. [P42785-2]
    UniGeneiHs.523936.

    Genome annotation databases

    EnsembliENST00000313010; ENSP00000317362; ENSG00000137509. [P42785-1]
    ENST00000393399; ENSP00000377055; ENSG00000137509. [P42785-2]
    GeneIDi5547.
    KEGGihsa:5547.
    UCSCiuc001ozr.3. human.
    uc001ozs.3. human. [P42785-1]

    Polymorphism databases

    DMDMi1172047.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13977 mRNA. Translation: AAA99891.1 .
    AK091786 mRNA. Translation: BAG52417.1 .
    AK312919 mRNA. Translation: BAG35764.1 .
    AB451270 mRNA. Translation: BAG70084.1 .
    AB451397 mRNA. Translation: BAG70211.1 .
    AP000893 Genomic DNA. No translation available.
    AP001646 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW75074.1 .
    CH471076 Genomic DNA. Translation: EAW75075.1 .
    BC001500 mRNA. Translation: AAH01500.1 .
    CCDSi CCDS41695.1. [P42785-2 ]
    CCDS8262.1. [P42785-1 ]
    PIRi A47352.
    RefSeqi NP_005031.1. NM_005040.2. [P42785-1 ]
    NP_955450.2. NM_199418.2. [P42785-2 ]
    UniGenei Hs.523936.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3N2Z X-ray 2.79 B 46-491 [» ]
    ProteinModelPortali P42785.
    SMRi P42785. Positions 46-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111538. 12 interactions.
    IntActi P42785. 4 interactions.
    MINTi MINT-3015634.
    STRINGi 9606.ENSP00000377055.

    Chemistry

    BindingDBi P42785.
    ChEMBLi CHEMBL2335.

    Protein family/group databases

    MEROPSi S28.001.

    PTM databases

    PhosphoSitei P42785.

    Polymorphism databases

    DMDMi 1172047.

    Proteomic databases

    MaxQBi P42785.
    PaxDbi P42785.
    PRIDEi P42785.

    Protocols and materials databases

    DNASUi 5547.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313010 ; ENSP00000317362 ; ENSG00000137509 . [P42785-1 ]
    ENST00000393399 ; ENSP00000377055 ; ENSG00000137509 . [P42785-2 ]
    GeneIDi 5547.
    KEGGi hsa:5547.
    UCSCi uc001ozr.3. human.
    uc001ozs.3. human. [P42785-1 ]

    Organism-specific databases

    CTDi 5547.
    GeneCardsi GC11M082535.
    HGNCi HGNC:9344. PRCP.
    HPAi HPA017065.
    MIMi 176785. gene.
    neXtProti NX_P42785.
    PharmGKBi PA33705.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290141.
    HOGENOMi HOG000238311.
    HOVERGENi HBG005526.
    KOi K01285.
    OMAi RSWKAIN.
    OrthoDBi EOG78WKRN.
    PhylomeDBi P42785.
    TreeFami TF314414.

    Enzyme and pathway databases

    Reactomei REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi PRCP. human.
    EvolutionaryTracei P42785.
    GeneWikii PRCP.
    GenomeRNAii 5547.
    NextBioi 21494.
    PROi P42785.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42785.
    Bgeei P42785.
    CleanExi HS_PRCP.
    Genevestigatori P42785.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR008758. Peptidase_S28.
    [Graphical view ]
    PANTHERi PTHR11010. PTHR11010. 1 hit.
    Pfami PF05577. Peptidase_S28. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families."
      Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
      J. Biol. Chem. 268:16631-16638(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Kidney.
    2. Erratum
      Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
      J. Biol. Chem. 268:26032-26032(1993)
    3. "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] (ISOFORMS 1 AND 2), VARIANT ASP-112.
      Tissue: Kidney and Lung.
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. 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] (ISOFORM 1).
      Tissue: Brain.
    8. "Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney."
      Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., Erdos E.G.
      J. Biol. Chem. 253:5927-5931(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Kidney.
    9. "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-317 AND ASN-415.
      Tissue: Liver.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase."
      Soisson S.M., Patel S.B., Abeywickrema P.D., Byrne N.J., Diehl R.E., Hall D.L., Ford R.E., Reid J.C., Rickert K.W., Shipman J.M., Sharma S., Lumb K.J.
      BMC Struct. Biol. 10:16-16(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 46-491, SUBUNIT, DISULFIDE BONDS, ACTIVE SITE, GLYCOSYLATION AT ASN-101; ASN-317; ASN-336; ASN-345 AND ASN-415.

    Entry informationi

    Entry nameiPCP_HUMAN
    AccessioniPrimary (citable) accession number: P42785
    Secondary accession number(s): A8MU24
    , B2R7B7, B3KRK5, B5BU34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 136 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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