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Q92743

- HTRA1_HUMAN

UniProt

Q92743 - HTRA1_HUMAN

Protein

Serine protease HTRA1

Gene

HTRA1

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 Feb 1997)
      Previous versions | rss
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    Functioni

    Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei169 – 1691Involved in trimer stabilization
    Sitei171 – 1711Involved in trimer stabilization
    Active sitei220 – 2201Charge relay systemSequence Analysis
    Active sitei250 – 2501Charge relay systemSequence Analysis
    Sitei278 – 2781Involved in trimer stabilization
    Active sitei328 – 3281Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: ProtInc
    2. serine-type peptidase activity Source: UniProtKB

    GO - Biological processi

    1. negative regulation of BMP signaling pathway Source: Ensembl
    2. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    3. proteolysis Source: UniProtKB
    4. regulation of cell growth Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Growth factor binding

    Protein family/group databases

    MEROPSiS01.277.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine protease HTRA1 (EC:3.4.21.-)
    Alternative name(s):
    High-temperature requirement A serine peptidase 1
    L56
    Serine protease 11
    Gene namesi
    Name:HTRA1
    Synonyms:HTRA, PRSS11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9476. HTRA1.

    Subcellular locationi

    Secreted. Cytoplasmcytosol
    Note: Predominantly secreted. Also found associated with the plasma membrane.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. extracellular space Source: ProtInc
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Macular degeneration, age-related, 7 (ARMD7) [MIM:610149]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.2 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Cerebral arteriopathy with subcortical infarcts and leukoencephalopathy, autosomal recessive (CARASIL) [MIM:600142]: A cerebrovascular disease characterized by non-hypertensive arteriopathy of cerebral small vessels with subcortical infarcts, alopecia, and spondylosis. Small cerebral arteries show arteriosclerotic changes, fibrous intimal proliferation, and hyaline degeneration with splitting of the intima and/or the internal elastic membrane. Neurologic features include progressive dementia, gait disturbances, extrapyramidal and pyramidal signs, and demyelination of the cerebral white matter with sparing of U fibers.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti252 – 2521A → T in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
    Corresponds to variant rs113993968 [ dbSNP | Ensembl ].
    VAR_063148
    Natural varianti297 – 2971V → M in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
    Corresponds to variant rs113993969 [ dbSNP | Ensembl ].
    VAR_063149

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi328 – 3281S → A: Loss of activity. 2 Publications

    Keywords - Diseasei

    Age-related macular degeneration, Disease mutation

    Organism-specific databases

    MIMi600142. phenotype.
    610149. phenotype.
    Orphaneti279. Age-related macular degeneration.
    199354. CARASIL.
    PharmGKBiPA33829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 480458Serine protease HTRA1PRO_0000026943Add
    BLAST

    Proteomic databases

    PaxDbiQ92743.
    PeptideAtlasiQ92743.
    PRIDEiQ92743.

    PTM databases

    PhosphoSiteiQ92743.

    Expressioni

    Tissue specificityi

    Widely expressed, with strongest expression in placenta (at protein level). Secreted by synovial fibroblasts. Up-regulated in osteoarthritis and rheumatoid arthritis synovial fluids and cartilage as compared with non-arthritic (at protein level).3 Publications

    Developmental stagei

    In the placenta, in the first trimester of gestation, low expression in the cells surrounding villi both in the inner layer of the cytotrophoblast and in the outer layer of the syncytiotrophoblast (at protein level). In the third trimester of gestation, very strong expression in the outer layer forming the syncytiotrophoblast and lower in the cytotrophoblast (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ92743.
    BgeeiQ92743.
    CleanExiHS_HTRA1.
    GenevestigatoriQ92743.

    Organism-specific databases

    HPAiHPA036655.

    Interactioni

    Subunit structurei

    Forms homotrimers. In the presence of substrate, may form higher-order multimers in a PDZ-independent manner. Interacts with TGF-beta family members, including BMP4, TGFB1, TGFB2, activin A and GDF5 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi111635. 6 interactions.
    DIPiDIP-33195N.
    IntActiQ92743. 6 interactions.
    MINTiMINT-1198897.
    STRINGi9606.ENSP00000357980.

    Structurei

    Secondary structure

    1
    480
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 453
    Beta strandi57 – 593
    Beta strandi65 – 684
    Beta strandi74 – 774
    Beta strandi87 – 904
    Beta strandi108 – 1136
    Beta strandi118 – 1236
    Beta strandi125 – 1284
    Helixi129 – 14113
    Helixi165 – 1684
    Helixi171 – 1799
    Helixi180 – 1823
    Beta strandi183 – 1919
    Beta strandi193 – 1964
    Beta strandi198 – 20811
    Turni211 – 2133
    Beta strandi214 – 2185
    Turni219 – 2213
    Beta strandi224 – 2318
    Beta strandi233 – 2353
    Beta strandi237 – 24610
    Turni247 – 2504
    Beta strandi251 – 2555
    Helixi270 – 2723
    Beta strandi278 – 2869
    Beta strandi289 – 29911
    Helixi304 – 3063
    Beta strandi317 – 3215
    Turni325 – 3295
    Beta strandi330 – 3334
    Beta strandi339 – 34810
    Beta strandi351 – 3566
    Helixi357 – 36812
    Beta strandi380 – 3823
    Beta strandi384 – 3896
    Helixi392 – 40110
    Beta strandi411 – 4177
    Beta strandi419 – 4213
    Helixi422 – 4265
    Beta strandi433 – 4375
    Helixi445 – 45410
    Beta strandi456 – 4649
    Beta strandi467 – 4737
    Beta strandi476 – 4783

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JOANMR-A380-480[»]
    2YTWNMR-A370-480[»]
    3NUMX-ray2.75A158-480[»]
    3NWUX-ray3.20A/B/C158-375[»]
    3NZIX-ray2.75A158-480[»]
    3TJNX-ray3.00A/B/D161-367[»]
    3TJOX-ray2.30A/B/D161-370[»]
    3TJQX-ray2.00A35-156[»]
    ProteinModelPortaliQ92743.
    SMRiQ92743. Positions 36-154, 160-370, 380-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92743.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 10068IGFBP N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini98 – 15760Kazal-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini365 – 467103PDZPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni204 – 364161Serine proteaseAdd
    BLAST

    Domaini

    The IGFBP N-terminal domain mediates interaction with TSC2 substrate.

    Sequence similaritiesi

    Belongs to the peptidase S1B family.Curated
    Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
    Contains 1 Kazal-like domain.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0265.
    HOGENOMiHOG000223641.
    HOVERGENiHBG052044.
    InParanoidiQ92743.
    KOiK08784.
    OMAiQRGACGQ.
    OrthoDBiEOG7V1FR7.
    PhylomeDBiQ92743.
    TreeFamiTF323480.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR009030. Growth_fac_rcpt_N_dom.
    IPR000867. IGFBP-like.
    IPR002350. Kazal_dom.
    IPR001478. PDZ.
    IPR001940. Peptidase_S1C.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00219. IGFBP. 1 hit.
    PF07648. Kazal_2. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    PRINTSiPR00834. PROTEASES2C.
    SMARTiSM00121. IB. 1 hit.
    SM00280. KAZAL. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEiPS51323. IGFBP_N_2. 1 hit.
    PS51465. KAZAL_2. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q92743-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQIPRAALLP LLLLLLAAPA SAQLSRAGRS APLAAGCPDR CEPARCPPQP    50
    EHCEGGRARD ACGCCEVCGA PEGAACGLQE GPCGEGLQCV VPFGVPASAT 100
    VRRRAQAGLC VCASSEPVCG SDANTYANLC QLRAASRRSE RLHRPPVIVL 150
    QRGACGQGQE DPNSLRHKYN FIADVVEKIA PAVVHIELFR KLPFSKREVP 200
    VASGSGFIVS EDGLIVTNAH VVTNKHRVKV ELKNGATYEA KIKDVDEKAD 250
    IALIKIDHQG KLPVLLLGRS SELRPGEFVV AIGSPFSLQN TVTTGIVSTT 300
    QRGGKELGLR NSDMDYIQTD AIINYGNSGG PLVNLDGEVI GINTLKVTAG 350
    ISFAIPSDKI KKFLTESHDR QAKGKAITKK KYIGIRMMSL TSSKAKELKD 400
    RHRDFPDVIS GAYIIEVIPD TPAEAGGLKE NDVIISINGQ SVVSANDVSD 450
    VIKRESTLNM VVRRGNEDIM ITVIPEEIDP 480
    Length:480
    Mass (Da):51,287
    Last modified:February 1, 1997 - v1
    Checksum:iCA20A99480FB2330
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti323 – 3231I → T in AAC97211. (PubMed:9852107)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti252 – 2521A → T in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
    Corresponds to variant rs113993968 [ dbSNP | Ensembl ].
    VAR_063148
    Natural varianti297 – 2971V → M in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity. 1 Publication
    Corresponds to variant rs113993969 [ dbSNP | Ensembl ].
    VAR_063149

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07921 mRNA. Translation: CAA69226.1.
    AF157623 Genomic DNA. Translation: AAD41525.1.
    CH471066 Genomic DNA. Translation: EAW49312.1.
    CH471066 Genomic DNA. Translation: EAW49313.1.
    AF097709 mRNA. Translation: AAC97211.1.
    CCDSiCCDS7630.1.
    RefSeqiNP_002766.1. NM_002775.4.
    UniGeneiHs.501280.

    Genome annotation databases

    EnsembliENST00000368984; ENSP00000357980; ENSG00000166033.
    GeneIDi5654.
    KEGGihsa:5654.
    UCSCiuc001lgj.2. human.

    Polymorphism databases

    DMDMi18202620.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07921 mRNA. Translation: CAA69226.1 .
    AF157623 Genomic DNA. Translation: AAD41525.1 .
    CH471066 Genomic DNA. Translation: EAW49312.1 .
    CH471066 Genomic DNA. Translation: EAW49313.1 .
    AF097709 mRNA. Translation: AAC97211.1 .
    CCDSi CCDS7630.1.
    RefSeqi NP_002766.1. NM_002775.4.
    UniGenei Hs.501280.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JOA NMR - A 380-480 [» ]
    2YTW NMR - A 370-480 [» ]
    3NUM X-ray 2.75 A 158-480 [» ]
    3NWU X-ray 3.20 A/B/C 158-375 [» ]
    3NZI X-ray 2.75 A 158-480 [» ]
    3TJN X-ray 3.00 A/B/D 161-367 [» ]
    3TJO X-ray 2.30 A/B/D 161-370 [» ]
    3TJQ X-ray 2.00 A 35-156 [» ]
    ProteinModelPortali Q92743.
    SMRi Q92743. Positions 36-154, 160-370, 380-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111635. 6 interactions.
    DIPi DIP-33195N.
    IntActi Q92743. 6 interactions.
    MINTi MINT-1198897.
    STRINGi 9606.ENSP00000357980.

    Protein family/group databases

    MEROPSi S01.277.

    PTM databases

    PhosphoSitei Q92743.

    Polymorphism databases

    DMDMi 18202620.

    Proteomic databases

    PaxDbi Q92743.
    PeptideAtlasi Q92743.
    PRIDEi Q92743.

    Protocols and materials databases

    DNASUi 5654.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368984 ; ENSP00000357980 ; ENSG00000166033 .
    GeneIDi 5654.
    KEGGi hsa:5654.
    UCSCi uc001lgj.2. human.

    Organism-specific databases

    CTDi 5654.
    GeneCardsi GC10P124221.
    GeneReviewsi HTRA1.
    HGNCi HGNC:9476. HTRA1.
    HPAi HPA036655.
    MIMi 600142. phenotype.
    602194. gene.
    610149. phenotype.
    neXtProti NX_Q92743.
    Orphaneti 279. Age-related macular degeneration.
    199354. CARASIL.
    PharmGKBi PA33829.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0265.
    HOGENOMi HOG000223641.
    HOVERGENi HBG052044.
    InParanoidi Q92743.
    KOi K08784.
    OMAi QRGACGQ.
    OrthoDBi EOG7V1FR7.
    PhylomeDBi Q92743.
    TreeFami TF323480.

    Miscellaneous databases

    ChiTaRSi HTRA1. human.
    EvolutionaryTracei Q92743.
    GeneWikii HTRA1.
    GenomeRNAii 5654.
    NextBioi 21974.
    PROi Q92743.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92743.
    Bgeei Q92743.
    CleanExi HS_HTRA1.
    Genevestigatori Q92743.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR009030. Growth_fac_rcpt_N_dom.
    IPR000867. IGFBP-like.
    IPR002350. Kazal_dom.
    IPR001478. PDZ.
    IPR001940. Peptidase_S1C.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00219. IGFBP. 1 hit.
    PF07648. Kazal_2. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    PRINTSi PR00834. PROTEASES2C.
    SMARTi SM00121. IB. 1 hit.
    SM00280. KAZAL. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi PS51323. IGFBP_N_2. 1 hit.
    PS51465. KAZAL_2. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of a putative serine protease specific for IGF-binding proteins."
      Zumbrunn J., Trueb B.
      FEBS Lett. 398:187-192(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Genomic organization and promoter characterization of the human HTRA (PRSS11) gene."
      Crowl R.M., Luk D., Milnamow M.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage."
      Hu S.I., Carozza M., Klein M., Nantermet P., Luk D., Crowl R.M.
      J. Biol. Chem. 273:34406-34412(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-480, PROTEIN SEQUENCE OF 33-44, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-328.
      Tissue: Cartilage.
    5. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    6. Cited for: FUNCTION, TISSUE SPECIFICITY.
    7. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ARMD7.
    8. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ARMD7.
    9. "The serine protease HtrA1 specifically interacts and degrades the tuberous sclerosis complex 2 protein."
      Campioni M., Severino A., Manente L., Tuduce I.L., Toldo S., Caraglia M., Crispi S., Ehrmann M., He X., Maguire J., De Falco M., De Luca A., Shridhar V., Baldi A.
      Mol. Cancer Res. 8:1248-1260(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Solution structure of the PDZ-domain of human protease HTRA 1 precursor."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 367-480.
    11. "Substrate-induced remodeling of the active site regulates human HTRA1 activity."
      Truebestein L., Tennstaedt A., Monig T., Krojer T., Canellas F., Kaiser M., Clausen T., Ehrmann M.
      Nat. Struct. Mol. Biol. 18:386-388(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 158-480, HOMOTRIMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-328.
    12. Cited for: VARIANTS CARASIL THR-252 AND MET-297, CHARACTERIZATION OF VARIANTS CARASIL THR-252 AND MET-297.

    Entry informationi

    Entry nameiHTRA1_HUMAN
    AccessioniPrimary (citable) accession number: Q92743
    Secondary accession number(s): D3DRE4, Q9UNS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: February 1, 1997
    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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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