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Q99538

- LGMN_HUMAN

UniProt

Q99538 - LGMN_HUMAN

Protein

Legumain

Gene

LGMN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation By similarity. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.By similarity1 Publication

    Catalytic activityi

    Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.1 Publication

    pH dependencei

    Optimum pH is 5.5 for the free enzyme, and pH 6 in the presence of bound integrins.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei148 – 14811 Publication
    Active sitei189 – 1891Nucleophile1 Publication
    Sitei323 – 3242Cleavage; by autolysis

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. peptidase activity Source: MGI

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. innate immune response Source: Reactome
    3. negative regulation of ERBB signaling pathway Source: UniProtKB
    4. negative regulation of multicellular organism growth Source: Ensembl
    5. negative regulation of neuron apoptotic process Source: MGI
    6. proteolysis Source: UniProtKB
    7. proteolysis involved in cellular protein catabolic process Source: UniProtKB
    8. receptor catabolic process Source: UniProtKB
    9. renal system process Source: UniProtKB
    10. response to acid chemical Source: Ensembl
    11. small molecule metabolic process Source: Reactome
    12. steroid metabolic process Source: Reactome
    13. toll-like receptor signaling pathway Source: Reactome
    14. vitamin D metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.34. 2681.
    ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
    REACT_121399. MHC class II antigen presentation.
    REACT_13523. Vitamin D (calciferol) metabolism.
    SABIO-RKQ99538.

    Protein family/group databases

    MEROPSiC13.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Legumain (EC:3.4.22.34)
    Alternative name(s):
    Asparaginyl endopeptidase
    Protease, cysteine 1
    Gene namesi
    Name:LGMN
    Synonyms:PRSC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9472. LGMN.

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. late endosome Source: Ensembl
    3. lysosomal lumen Source: Reactome
    4. lysosome Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi190 – 1901E → K: Increases catalytic activity at pH 5.5. 1 Publication
    Mutagenesisi323 – 3231N → D, Q or S: Loss of autoactivation.

    Organism-specific databases

    PharmGKBiPA30354.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 323306LegumainPRO_0000026502Add
    BLAST
    Propeptidei324 – 433110PRO_0000026503Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi91 – 911N-linked (GlcNAc...)2 Publications
    Glycosylationi167 – 1671N-linked (GlcNAc...)2 Publications
    Glycosylationi263 – 2631N-linked (GlcNAc...)1 Publication
    Glycosylationi272 – 2721N-linked (GlcNAc...)1 Publication
    Disulfide bondi378 ↔ 412By similarity
    Disulfide bondi390 ↔ 429By similarity

    Post-translational modificationi

    Glycosylated.2 Publications
    Activated by autocatalytic processing at pH 4.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ99538.
    PaxDbiQ99538.
    PRIDEiQ99538.

    PTM databases

    PhosphoSiteiQ99538.

    Miscellaneous databases

    PMAP-CutDBQ99538.

    Expressioni

    Tissue specificityi

    Ubiquitous. Particularly abundant in kidney, heart and placenta.

    Gene expression databases

    ArrayExpressiQ99538.
    BgeeiQ99538.
    CleanExiHS_LGMN.
    GenevestigatoriQ99538.

    Organism-specific databases

    HPAiHPA000799.
    HPA001426.

    Interactioni

    Subunit structurei

    Homodimer before autocatalytic removal of the propeptide By similarity. Monomer after autocatalytic processing. May interact with integrins.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi111624. 11 interactions.
    IntActiQ99538. 4 interactions.
    MINTiMINT-4537529.
    STRINGi9606.ENSP00000334052.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 358
    Helixi40 – 423
    Helixi43 – 5816
    Helixi63 – 653
    Beta strandi66 – 694
    Beta strandi87 – 893
    Helixi105 – 1073
    Helixi110 – 1189
    Helixi122 – 1243
    Beta strandi140 – 1478
    Beta strandi153 – 1553
    Beta strandi157 – 1626
    Helixi163 – 17513
    Beta strandi180 – 1889
    Helixi191 – 1944
    Turni195 – 1973
    Beta strandi202 – 2109
    Beta strandi217 – 2226
    Turni223 – 2264
    Beta strandi227 – 2315
    Helixi232 – 24312
    Turni246 – 2483
    Helixi251 – 26111
    Beta strandi268 – 2714
    Helixi273 – 2775
    Helixi281 – 2844

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AW9X-ray2.20A26-309[»]
    4AWAX-ray2.50A26-309[»]
    4AWBX-ray2.70A/B26-309[»]
    4FGUX-ray3.90A/B18-433[»]
    ProteinModelPortaliQ99538.
    SMRiQ99538. Positions 28-433.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    In the zymogen form, the uncleaved propeptide blocks access to the active site.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5206.
    HOGENOMiHOG000236335.
    HOVERGENiHBG031304.
    InParanoidiQ99538.
    KOiK01369.
    OMAiKVMQFQG.
    PhylomeDBiQ99538.
    TreeFamiTF313403.

    Family and domain databases

    InterProiIPR001096. Peptidase_C13.
    [Graphical view]
    PANTHERiPTHR12000. PTHR12000. 1 hit.
    PfamiPF01650. Peptidase_C13. 1 hit.
    [Graphical view]
    PIRSFiPIRSF019663. Legumain. 1 hit.
    PRINTSiPR00776. HEMOGLOBNASE.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99538-1) [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

    MVWKVAVFLS VALGIGAVPI DDPEDGGKHW VVIVAGSNGW YNYRHQADAC    50
    HAYQIIHRNG IPDEQIVVMM YDDIAYSEDN PTPGIVINRP NGTDVYQGVP 100
    KDYTGEDVTP QNFLAVLRGD AEAVKGIGSG KVLKSGPQDH VFIYFTDHGS 150
    TGILVFPNED LHVKDLNETI HYMYKHKMYR KMVFYIEACE SGSMMNHLPD 200
    NINVYATTAA NPRESSYACY YDEKRSTYLG DWYSVNWMED SDVEDLTKET 250
    LHKQYHLVKS HTNTSHVMQY GNKTISTMKV MQFQGMKRKA SSPVPLPPVT 300
    HLDLTPSPDV PLTIMKRKLM NTNDLEESRQ LTEEIQRHLD ARHLIEKSVR 350
    KIVSLLAASE AEVEQLLSER APLTGHSCYP EALLHFRTHC FNWHSPTYEY 400
    ALRHLYVLVN LCEKPYPLHR IKLSMDHVCL GHY 433
    Length:433
    Mass (Da):49,411
    Last modified:May 1, 1997 - v1
    Checksum:i081AD2D0D584E72A
    GO
    Isoform 2 (identifier: Q99538-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         341-397: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:376
    Mass (Da):42,948
    Checksum:i582E0D702B640C1F
    GO
    Isoform 3 (identifier: Q99538-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         341-372: ARHLIEKSVRKIVSLLAASEAEVEQLLSERAP → DKIVHGPRVPWSLLKSCLLEAFPSVSAPPTVC
         373-433: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:372
    Mass (Da):42,008
    Checksum:i915FFBB4216E8BF6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311V → A in BAA09530. (PubMed:8893817)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181V → I.1 Publication
    Corresponds to variant rs2236264 [ dbSNP | Ensembl ].
    VAR_024588

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei341 – 39757Missing in isoform 2. 1 PublicationVSP_056454Add
    BLAST
    Alternative sequencei341 – 37232ARHLI…SERAP → DKIVHGPRVPWSLLKSCLLE AFPSVSAPPTVC in isoform 3. 1 PublicationVSP_056455Add
    BLAST
    Alternative sequencei373 – 43361Missing in isoform 3. 1 PublicationVSP_056456Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09862 mRNA. Translation: CAA70989.1.
    D55696 mRNA. Translation: BAA09530.1.
    BX161380 mRNA. Translation: CAD61872.1.
    BX161422 mRNA. Translation: CAD61895.1.
    AL132987 Genomic DNA. No translation available.
    AL136332 Genomic DNA. No translation available.
    BC003061 mRNA. Translation: AAH03061.1.
    CCDSiCCDS9904.1.
    RefSeqiNP_001008530.1. NM_001008530.2.
    NP_005597.3. NM_005606.6.
    XP_005267919.1. XM_005267862.2.
    XP_005267920.1. XM_005267863.2.
    UniGeneiHs.18069.

    Genome annotation databases

    EnsembliENST00000334869; ENSP00000334052; ENSG00000100600.
    ENST00000393218; ENSP00000376911; ENSG00000100600.
    ENST00000555699; ENSP00000451861; ENSG00000100600.
    ENST00000557434; ENSP00000452572; ENSG00000100600.
    GeneIDi5641.
    KEGGihsa:5641.
    UCSCiuc001yav.3. human.

    Polymorphism databases

    DMDMi2842759.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09862 mRNA. Translation: CAA70989.1 .
    D55696 mRNA. Translation: BAA09530.1 .
    BX161380 mRNA. Translation: CAD61872.1 .
    BX161422 mRNA. Translation: CAD61895.1 .
    AL132987 Genomic DNA. No translation available.
    AL136332 Genomic DNA. No translation available.
    BC003061 mRNA. Translation: AAH03061.1 .
    CCDSi CCDS9904.1.
    RefSeqi NP_001008530.1. NM_001008530.2.
    NP_005597.3. NM_005606.6.
    XP_005267919.1. XM_005267862.2.
    XP_005267920.1. XM_005267863.2.
    UniGenei Hs.18069.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AW9 X-ray 2.20 A 26-309 [» ]
    4AWA X-ray 2.50 A 26-309 [» ]
    4AWB X-ray 2.70 A/B 26-309 [» ]
    4FGU X-ray 3.90 A/B 18-433 [» ]
    ProteinModelPortali Q99538.
    SMRi Q99538. Positions 28-433.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111624. 11 interactions.
    IntActi Q99538. 4 interactions.
    MINTi MINT-4537529.
    STRINGi 9606.ENSP00000334052.

    Chemistry

    BindingDBi Q99538.
    ChEMBLi CHEMBL4244.

    Protein family/group databases

    MEROPSi C13.004.

    PTM databases

    PhosphoSitei Q99538.

    Polymorphism databases

    DMDMi 2842759.

    Proteomic databases

    MaxQBi Q99538.
    PaxDbi Q99538.
    PRIDEi Q99538.

    Protocols and materials databases

    DNASUi 5641.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334869 ; ENSP00000334052 ; ENSG00000100600 .
    ENST00000393218 ; ENSP00000376911 ; ENSG00000100600 .
    ENST00000555699 ; ENSP00000451861 ; ENSG00000100600 .
    ENST00000557434 ; ENSP00000452572 ; ENSG00000100600 .
    GeneIDi 5641.
    KEGGi hsa:5641.
    UCSCi uc001yav.3. human.

    Organism-specific databases

    CTDi 5641.
    GeneCardsi GC14M093170.
    HGNCi HGNC:9472. LGMN.
    HPAi HPA000799.
    HPA001426.
    MIMi 602620. gene.
    neXtProti NX_Q99538.
    PharmGKBi PA30354.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5206.
    HOGENOMi HOG000236335.
    HOVERGENi HBG031304.
    InParanoidi Q99538.
    KOi K01369.
    OMAi KVMQFQG.
    PhylomeDBi Q99538.
    TreeFami TF313403.

    Enzyme and pathway databases

    BRENDAi 3.4.22.34. 2681.
    Reactomei REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_121399. MHC class II antigen presentation.
    REACT_13523. Vitamin D (calciferol) metabolism.
    SABIO-RK Q99538.

    Miscellaneous databases

    ChiTaRSi LGMN. human.
    GeneWikii LGMN.
    GenomeRNAii 5641.
    NextBioi 21918.
    PMAP-CutDB Q99538.
    PROi Q99538.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99538.
    Bgeei Q99538.
    CleanExi HS_LGMN.
    Genevestigatori Q99538.

    Family and domain databases

    InterProi IPR001096. Peptidase_C13.
    [Graphical view ]
    PANTHERi PTHR12000. PTHR12000. 1 hit.
    Pfami PF01650. Peptidase_C13. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF019663. Legumain. 1 hit.
    PRINTSi PR00776. HEMOGLOBNASE.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase."
      Chen J.-M., Dando P.M., Rawlings N.D., Brown M.A., Young N.E., Stevens R.A.E., Hewitt E., Watts C., Barrett A.J.
      J. Biol. Chem. 272:8090-8098(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1."
      Tanaka T., Inazawa J., Nakamura Y.
      Cytogenet. Cell Genet. 74:120-123(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Neuroblastoma and Placenta.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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), VARIANT ILE-18.
      Tissue: Placenta.
    6. "Activation of human prolegumain by cleavage at a C-terminal asparagine residue."
      Chen J.-M., Fortunato M., Barrett A.J.
      Biochem. J. 352:327-334(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-24 AND 324-330, PROTEOLYTIC PROCESSING.
    7. "Autocatalytic activation of human legumain at aspartic acid residues."
      Halfon S., Patel S., Vega F., Zurawski S., Zurawski G.
      FEBS Lett. 438:114-118(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF ACTIVITY ON ASPARTATE BONDS, AUTOCATALYTIC CLEAVAGE.
    8. "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-91 AND ASN-167.
      Tissue: Liver.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation."
      Dall E., Brandstetter H.
      Proc. Natl. Acad. Sci. U.S.A. 110:10940-10945(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-309, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, PROPEPTIDE, GLYCOSYLATION AT ASN-91; ASN-167; ASN-263 AND ASN-272, SUBUNIT, DOMAIN, MUTAGENESIS OF GLU-190, AUTOCATALYTIC PROCESSING.

    Entry informationi

    Entry nameiLGMN_HUMAN
    AccessioniPrimary (citable) accession number: Q99538
    Secondary accession number(s): O00123
    , Q86TV2, Q86TV3, Q9BTY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 135 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 14
      Human chromosome 14: 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