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P05981

- HEPS_HUMAN

UniProt

P05981 - HEPS_HUMAN

Protein

Serine protease hepsin

Gene

HPN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Plays an essential role in cell growth and maintenance of cell morphology. May mediate the activating cleavage of HGF and MST1/HGFL. Plays a role in the proteolytic processing of ACE2.3 Publications

    Catalytic activityi

    Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei203 – 2031Charge relay systemBy similarity
    Active sitei257 – 2571Charge relay systemBy similarity
    Active sitei353 – 3531Charge relay systemBy similarity

    GO - Molecular functioni

    1. calcium-activated potassium channel activity Source: UniProtKB
    2. peptidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. serine-type endopeptidase activity Source: UniProtKB
    5. serine-type exopeptidase activity Source: InterPro
    6. serine-type peptidase activity Source: UniProtKB

    GO - Biological processi

    1. basement membrane disassembly Source: UniProtKB
    2. cochlea morphogenesis Source: UniProtKB
    3. detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
    4. epithelium development Source: Ensembl
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of epithelial cell proliferation Source: UniProtKB
    7. negative regulation of epithelial to mesenchymal transition Source: UniProtKB
    8. pilomotor reflex Source: UniProtKB
    9. positive regulation by host of viral transcription Source: UniProtKB
    10. positive regulation of cell growth Source: UniProtKB
    11. positive regulation of gene expression Source: UniProtKB
    12. positive regulation of hepatocyte proliferation Source: UniProtKB
    13. positive regulation of plasminogen activation Source: UniProtKB
    14. positive regulation of thyroid hormone generation Source: UniProtKB
    15. potassium ion transmembrane transport Source: UniProtKB
    16. proteolysis Source: UniProtKB
    17. regulation of cell shape Source: UniProtKB
    18. response to thyroid hormone Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    BRENDAi3.4.21.106. 2681.

    Protein family/group databases

    MEROPSiS01.224.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine protease hepsin (EC:3.4.21.106)
    Alternative name(s):
    Transmembrane protease serine 1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:HPN
    Synonyms:TMPRSS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5155. HPN.

    Subcellular locationi

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cell surface Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: UniProtKB
    6. integral component of plasma membrane Source: UniProtKB
    7. neuronal cell body Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29425.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 162162Serine protease hepsin non-catalytic chainSequence AnalysisPRO_0000027841Add
    BLAST
    Chaini163 – 417255Serine protease hepsin catalytic chainSequence AnalysisPRO_0000027842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi77 ↔ 1401 PublicationPROSITE-ProRule annotation
    Disulfide bondi90 ↔ 1501 PublicationPROSITE-ProRule annotation
    Glycosylationi112 – 1121N-linked (GlcNAc...)1 Publication
    Disulfide bondi119 ↔ 1381 PublicationPROSITE-ProRule annotation
    Disulfide bondi153 ↔ 277Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
    Disulfide bondi188 ↔ 2041 PublicationPROSITE-ProRule annotation
    Disulfide bondi291 ↔ 3591 PublicationPROSITE-ProRule annotation
    Disulfide bondi322 ↔ 3381 PublicationPROSITE-ProRule annotation
    Disulfide bondi349 ↔ 3811 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP05981.
    PaxDbiP05981.
    PeptideAtlasiP05981.
    PRIDEiP05981.

    PTM databases

    PhosphoSiteiP05981.

    Miscellaneous databases

    PMAP-CutDBP05981.

    Expressioni

    Tissue specificityi

    Present in most tissues, with the highest level in liver.

    Gene expression databases

    ArrayExpressiP05981.
    BgeeiP05981.
    CleanExiHS_HPN.
    GenevestigatoriP05981.

    Organism-specific databases

    HPAiHPA006804.

    Interactioni

    Protein-protein interaction databases

    BioGridi109486. 1 interaction.
    STRINGi9606.ENSP00000262626.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 564
    Turni58 – 603
    Beta strandi62 – 676
    Turni68 – 714
    Beta strandi72 – 776
    Helixi82 – 9312
    Beta strandi98 – 1058
    Helixi106 – 1094
    Beta strandi116 – 1205
    Turni122 – 1243
    Helixi125 – 1273
    Helixi131 – 1344
    Beta strandi135 – 1384
    Beta strandi144 – 1507
    Beta strandi177 – 1826
    Beta strandi185 – 20016
    Helixi202 – 2043
    Helixi207 – 2093
    Helixi212 – 2143
    Beta strandi215 – 2206
    Beta strandi229 – 2324
    Beta strandi234 – 2407
    Helixi244 – 2463
    Beta strandi259 – 2657
    Beta strandi290 – 30011
    Beta strandi310 – 3178
    Helixi319 – 3224
    Turni325 – 3306
    Beta strandi336 – 3405
    Beta strandi345 – 3473
    Beta strandi356 – 3616
    Beta strandi368 – 38215
    Beta strandi388 – 3925
    Helixi393 – 3964
    Helixi397 – 40610
    Turni407 – 4093
    Beta strandi412 – 4165

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O5EX-ray1.75H163-417[»]
    L46-159[»]
    1O5FX-ray1.78H163-417[»]
    L46-159[»]
    1P57X-ray1.75A46-159[»]
    B163-417[»]
    1Z8GX-ray1.55A46-417[»]
    3T2NX-ray2.55A/B46-417[»]
    ProteinModelPortaliP05981.
    SMRiP05981. Positions 49-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05981.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2323CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini45 – 417373ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei24 – 4421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 15198SRCRAdd
    BLAST
    Domaini163 – 405243Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 1 SRCR domain.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251822.
    HOVERGENiHBG013304.
    InParanoidiP05981.
    KOiK08665.
    OMAiLTCVLTP.
    OrthoDBiEOG75B84T.
    PhylomeDBiP05981.
    TreeFamiTF351678.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    InterProiIPR015352. Hepsin-SRCR_dom.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF09272. Hepsin-SRCR. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    ProDomiPD021735. Hepsin-SRCR. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05981-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQKEGGRTV PCCSRPKVAA LTAGTLLLLT AIGAASWAIV AVLLRSDQEP    50
    LYPVQVSSAD ARLMVFDKTE GTWRLLCSSR SNARVAGLSC EEMGFLRALT 100
    HSELDVRTAG ANGTSGFFCV DEGRLPHTQR LLEVISVCDC PRGRFLAAIC 150
    QDCGRRKLPV DRIVGGRDTS LGRWPWQVSL RYDGAHLCGG SLLSGDWVLT 200
    AAHCFPERNR VLSRWRVFAG AVAQASPHGL QLGVQAVVYH GGYLPFRDPN 250
    SEENSNDIAL VHLSSPLPLT EYIQPVCLPA AGQALVDGKI CTVTGWGNTQ 300
    YYGQQAGVLQ EARVPIISND VCNGADFYGN QIKPKMFCAG YPEGGIDACQ 350
    GDSGGPFVCE DSISRTPRWR LCGIVSWGTG CALAQKPGVY TKVSDFREWI 400
    FQAIKTHSEA SGMVTQL 417
    Length:417
    Mass (Da):45,011
    Last modified:November 1, 1988 - v1
    Checksum:iB2086FF661E551D7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18930 mRNA. Translation: AAA36013.1.
    X07732 mRNA. Translation: CAA30558.1.
    X07002 mRNA. Translation: CAA30058.1.
    AK315655 mRNA. Translation: BAG38021.1.
    BC025716 mRNA. Translation: AAH25716.1.
    CCDSiCCDS32993.1.
    PIRiS00845.
    RefSeqiNP_002142.1. NM_002151.2.
    NP_892028.1. NM_182983.2.
    UniGeneiHs.182385.

    Genome annotation databases

    EnsembliENST00000262626; ENSP00000262626; ENSG00000105707.
    ENST00000392226; ENSP00000376060; ENSG00000105707.
    GeneIDi3249.
    KEGGihsa:3249.
    UCSCiuc002nxq.2. human.

    Polymorphism databases

    DMDMi123057.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18930 mRNA. Translation: AAA36013.1 .
    X07732 mRNA. Translation: CAA30558.1 .
    X07002 mRNA. Translation: CAA30058.1 .
    AK315655 mRNA. Translation: BAG38021.1 .
    BC025716 mRNA. Translation: AAH25716.1 .
    CCDSi CCDS32993.1.
    PIRi S00845.
    RefSeqi NP_002142.1. NM_002151.2.
    NP_892028.1. NM_182983.2.
    UniGenei Hs.182385.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O5E X-ray 1.75 H 163-417 [» ]
    L 46-159 [» ]
    1O5F X-ray 1.78 H 163-417 [» ]
    L 46-159 [» ]
    1P57 X-ray 1.75 A 46-159 [» ]
    B 163-417 [» ]
    1Z8G X-ray 1.55 A 46-417 [» ]
    3T2N X-ray 2.55 A/B 46-417 [» ]
    ProteinModelPortali P05981.
    SMRi P05981. Positions 49-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109486. 1 interaction.
    STRINGi 9606.ENSP00000262626.

    Chemistry

    BindingDBi P05981.
    ChEMBLi CHEMBL2079849.
    DrugBanki DB00036. Coagulation factor VIIa.

    Protein family/group databases

    MEROPSi S01.224.

    PTM databases

    PhosphoSitei P05981.

    Polymorphism databases

    DMDMi 123057.

    Proteomic databases

    MaxQBi P05981.
    PaxDbi P05981.
    PeptideAtlasi P05981.
    PRIDEi P05981.

    Protocols and materials databases

    DNASUi 3249.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262626 ; ENSP00000262626 ; ENSG00000105707 .
    ENST00000392226 ; ENSP00000376060 ; ENSG00000105707 .
    GeneIDi 3249.
    KEGGi hsa:3249.
    UCSCi uc002nxq.2. human.

    Organism-specific databases

    CTDi 3249.
    GeneCardsi GC19P035531.
    H-InvDB HIX0137465.
    HGNCi HGNC:5155. HPN.
    HPAi HPA006804.
    MIMi 142440. gene.
    neXtProti NX_P05981.
    PharmGKBi PA29425.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251822.
    HOVERGENi HBG013304.
    InParanoidi P05981.
    KOi K08665.
    OMAi LTCVLTP.
    OrthoDBi EOG75B84T.
    PhylomeDBi P05981.
    TreeFami TF351678.

    Enzyme and pathway databases

    BRENDAi 3.4.21.106. 2681.

    Miscellaneous databases

    EvolutionaryTracei P05981.
    GeneWikii HPN_(gene).
    GenomeRNAii 3249.
    NextBioi 12917.
    PMAP-CutDB P05981.
    PROi P05981.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05981.
    Bgeei P05981.
    CleanExi HS_HPN.
    Genevestigatori P05981.

    Family and domain databases

    Gene3Di 3.10.250.10. 1 hit.
    InterProi IPR015352. Hepsin-SRCR_dom.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF09272. Hepsin-SRCR. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    ProDomi PD021735. Hepsin-SRCR. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells."
      Leytus S.P., Loeb K.R., Hagen F.S., Kurachi K., Davie E.W.
      Biochemistry 27:1067-1074(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "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: Mammary gland.
    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].
      Tissue: Pancreas and Spleen.
    4. "Hepsin, a cell membrane-associated protease. Characterization, tissue distribution, and gene localization."
      Tsuji A., Torres-Rosado A., Arai T., le Beau M.M., Lemons R.S., Chou S.H., Kurachi K.
      J. Biol. Chem. 266:16948-16953(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth."
      Torres-Rosado A., O'Shea K.S., Tsuji A., Chou S.-H., Kurachi K.
      Proc. Natl. Acad. Sci. U.S.A. 90:7181-7185(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "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-112.
      Tissue: Liver.
    7. Cited for: FUNCTION.
    8. "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
      Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
      J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers."
      Herter S., Piper D.E., Aaron W., Gabriele T., Cutler G., Cao P., Bhatt A.S., Choe Y., Craik C.S., Walker N., Meininger D., Hoey T., Austin R.J.
      Biochem. J. 390:125-136(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 46-417, DISULFIDE BONDS, FUNCTION.

    Entry informationi

    Entry nameiHEPS_HUMAN
    AccessioniPrimary (citable) accession number: P05981
    Secondary accession number(s): B2RDS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 147 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3