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Q9UBX1

- CATF_HUMAN

UniProt

Q9UBX1 - CATF_HUMAN

Protein

Cathepsin F

Gene

CTSF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

    Catalytic activityi

    The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (k(cat)/K(m)) comparable to that of cathepsin L.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei295 – 29511 Publication
    Active sitei431 – 43111 Publication
    Active sitei451 – 4511By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: ProtInc

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. cell death Source: UniProtKB-KW
    3. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.

    Protein family/group databases

    MEROPSiC01.018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin F (EC:3.4.22.41)
    Short name:
    CATSF
    Gene namesi
    Name:CTSF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2531. CTSF.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. lysosomal lumen Source: Reactome
    3. lysosome Source: ProtInc

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Ceroid lipofuscinosis, neuronal, 13 (CLN13) [MIM:615362]: A form of neuronal ceroid lipofuscinosis characterized by adult onset of progressive cognitive decline and motor dysfunction leading to dementia and often early death. Some patients develop seizures. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti231 – 2311Y → C in CLN13. 1 Publication
    VAR_070159
    Natural varianti321 – 3211Q → R in CLN13. 1 Publication
    VAR_070160
    Natural varianti458 – 4581G → A in CLN13. 1 Publication
    VAR_070161
    Natural varianti480 – 4801S → L in CLN13. 1 Publication
    VAR_070162

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Neuronal ceroid lipofuscinosis

    Organism-specific databases

    MIMi615362. phenotype.
    Orphaneti352709. CLN13 disease.
    PharmGKBiPA27031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 270251Activation peptidePRO_0000026202Add
    BLAST
    Chaini271 – 484214Cathepsin FPRO_0000026203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi292 ↔ 3331 Publication
    Disulfide bondi326 ↔ 3661 Publication
    Glycosylationi367 – 3671N-linked (GlcNAc...)1 Publication
    Glycosylationi378 – 3781N-linked (GlcNAc...)1 Publication
    Disulfide bondi424 ↔ 472By similarity
    Glycosylationi440 – 4401N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9UBX1.
    PaxDbiQ9UBX1.
    PeptideAtlasiQ9UBX1.
    PRIDEiQ9UBX1.

    PTM databases

    PhosphoSiteiQ9UBX1.

    Expressioni

    Tissue specificityi

    High expression levels in heart, skeletal muscle, brain, testis and ovary; moderate levels in prostate, placenta, liver and colon; and no detectable expression in peripheral leukocytes and thymus.

    Gene expression databases

    ArrayExpressiQ9UBX1.
    BgeeiQ9UBX1.
    CleanExiHS_CTSF.
    GenevestigatoriQ9UBX1.

    Organism-specific databases

    HPAiCAB002141.
    HPA031431.
    HPA055610.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000310832.

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi277 – 2804
    Beta strandi291 – 2933
    Helixi295 – 31218
    Helixi320 – 3267
    Beta strandi328 – 3303
    Helixi338 – 34811
    Turni354 – 3563
    Helixi370 – 3723
    Beta strandi378 – 3825
    Helixi387 – 39711
    Beta strandi400 – 4045
    Helixi407 – 4115
    Beta strandi414 – 4174
    Helixi421 – 4233
    Beta strandi431 – 44111
    Beta strandi444 – 4507
    Beta strandi462 – 4698
    Helixi471 – 4733
    Turni474 – 4774
    Beta strandi479 – 4824

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D5Umodel-A271-484[»]
    1M6DX-ray1.70A/B271-484[»]
    ProteinModelPortaliQ9UBX1.
    SMRiQ9UBX1. Positions 194-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBX1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiQ9UBX1.
    KOiK01373.
    OMAiDYSYQGH.
    OrthoDBiEOG7DJSKG.
    PhylomeDBiQ9UBX1.
    TreeFamiTF314550.

    Family and domain databases

    InterProiIPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UBX1-1 [UniParc]FASTAAdd to Basket

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    MAPWLQLLSL LGLLPGAVAA PAQPRAASFQ AWGPPSPELL APTRFALEMF    50
    NRGRAAGTRA VLGLVRGRVR RAGQGSLYSL EATLEEPPCN DPMVCRLPVS 100
    KKTLLCSFQV LDELGRHVLL RKDCGPVDTK VPGAGEPKSA FTQGSAMISS 150
    LSQNHPDNRN ETFSSVISLL NEDPLSQDLP VKMASIFKNF VITYNRTYES 200
    KEEARWRLSV FVNNMVRAQK IQALDRGTAQ YGVTKFSDLT EEEFRTIYLN 250
    TLLRKEPGNK MKQAKSVGDL APPEWDWRSK GAVTKVKDQG MCGSCWAFSV 300
    TGNVEGQWFL NQGTLLSLSE QELLDCDKMD KACMGGLPSN AYSAIKNLGG 350
    LETEDDYSYQ GHMQSCNFSA EKAKVYINDS VELSQNEQKL AAWLAKRGPI 400
    SVAINAFGMQ FYRHGISRPL RPLCSPWLID HAVLLVGYGN RSDVPFWAIK 450
    NSWGTDWGEK GYYYLHRGSG ACGVNTMASS AVVD 484
    Length:484
    Mass (Da):53,366
    Last modified:May 1, 2000 - v1
    Checksum:i1D5D551B489D822B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti305 – 3051E → K in AAF13146. 1 PublicationCurated
    Sequence conflicti442 – 48443SDVPF…SAVVD → EFRCLSCIQPGHRQGWDHSI SGPLEGK(PubMed:17974005)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti153 – 1531Q → R.
    Corresponds to variant rs11550508 [ dbSNP | Ensembl ].
    VAR_051513
    Natural varianti231 – 2311Y → C in CLN13. 1 Publication
    VAR_070159
    Natural varianti321 – 3211Q → R in CLN13. 1 Publication
    VAR_070160
    Natural varianti458 – 4581G → A in CLN13. 1 Publication
    VAR_070161
    Natural varianti480 – 4801S → L in CLN13. 1 Publication
    VAR_070162

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007331 mRNA. Translation: CAB42883.1.
    AF088886 mRNA. Translation: AAD26616.2.
    AF132894 Genomic DNA. Translation: AAD41790.1.
    AF136279 mRNA. Translation: AAF13146.1.
    AF071748 mRNA. Translation: AAC78838.1.
    AF071749 mRNA. Translation: AAC78839.1.
    AK313657 mRNA. Translation: BAG36411.1.
    BC011682 mRNA. Translation: AAH11682.1.
    BC036451 mRNA. Translation: AAH36451.1.
    AL137742 mRNA. Translation: CAB70900.1.
    CCDSiCCDS8144.1.
    RefSeqiNP_003784.2. NM_003793.3.
    UniGeneiHs.11590.

    Genome annotation databases

    EnsembliENST00000310325; ENSP00000310832; ENSG00000174080.
    GeneIDi8722.
    KEGGihsa:8722.
    UCSCiuc001oip.3. human.

    Polymorphism databases

    DMDMi12643325.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007331 mRNA. Translation: CAB42883.1 .
    AF088886 mRNA. Translation: AAD26616.2 .
    AF132894 Genomic DNA. Translation: AAD41790.1 .
    AF136279 mRNA. Translation: AAF13146.1 .
    AF071748 mRNA. Translation: AAC78838.1 .
    AF071749 mRNA. Translation: AAC78839.1 .
    AK313657 mRNA. Translation: BAG36411.1 .
    BC011682 mRNA. Translation: AAH11682.1 .
    BC036451 mRNA. Translation: AAH36451.1 .
    AL137742 mRNA. Translation: CAB70900.1 .
    CCDSi CCDS8144.1.
    RefSeqi NP_003784.2. NM_003793.3.
    UniGenei Hs.11590.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D5U model - A 271-484 [» ]
    1M6D X-ray 1.70 A/B 271-484 [» ]
    ProteinModelPortali Q9UBX1.
    SMRi Q9UBX1. Positions 194-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000310832.

    Chemistry

    BindingDBi Q9UBX1.
    ChEMBLi CHEMBL2517.

    Protein family/group databases

    MEROPSi C01.018.

    PTM databases

    PhosphoSitei Q9UBX1.

    Polymorphism databases

    DMDMi 12643325.

    Proteomic databases

    MaxQBi Q9UBX1.
    PaxDbi Q9UBX1.
    PeptideAtlasi Q9UBX1.
    PRIDEi Q9UBX1.

    Protocols and materials databases

    DNASUi 8722.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310325 ; ENSP00000310832 ; ENSG00000174080 .
    GeneIDi 8722.
    KEGGi hsa:8722.
    UCSCi uc001oip.3. human.

    Organism-specific databases

    CTDi 8722.
    GeneCardsi GC11M066332.
    GeneReviewsi CTSF.
    HGNCi HGNC:2531. CTSF.
    HPAi CAB002141.
    HPA031431.
    HPA055610.
    MIMi 603539. gene.
    615362. phenotype.
    neXtProti NX_Q9UBX1.
    Orphaneti 352709. CLN13 disease.
    PharmGKBi PA27031.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi Q9UBX1.
    KOi K01373.
    OMAi DYSYQGH.
    OrthoDBi EOG7DJSKG.
    PhylomeDBi Q9UBX1.
    TreeFami TF314550.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.

    Miscellaneous databases

    ChiTaRSi CTSF. human.
    EvolutionaryTracei Q9UBX1.
    GeneWikii Cathepsin_F.
    GenomeRNAii 8722.
    NextBioi 32715.
    PROi Q9UBX1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBX1.
    Bgeei Q9UBX1.
    CleanExi HS_CTSF.
    Genevestigatori Q9UBX1.

    Family and domain databases

    InterProi IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain."
      Santamaria I., Velasco G., Pendas A.M., Paz A., Lopez-Otin C.
      J. Biol. Chem. 274:13800-13809(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Prostate.
    2. "Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen."
      Naegler D.K., Sulea T., Menard R.
      Biochem. Biophys. Res. Commun. 257:313-318(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    3. "The human cathepsin F gene -- a fusion product between an ancestral cathepsin and cystatin gene."
      Wex T., Wex H., Broemme D.
      Biol. Chem. 380:1439-1442(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Human cathepsins F and W: a new subgroup of cathepsins."
      Wex T., Levy B., Wex H., Bromme D.
      Biochem. Biophys. Res. Commun. 259:401-407(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cathepsin F, a novel cysteine protease with an extremely long propeptide."
      Deussing J., Tisljar K., Papazoglou A., Peters C.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    6. "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].
    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: Lung and Testis.
    8. "Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization."
      Wang B., Shi G.-P., Yao P.M., Li Z., Chapman H.A., Broemme D.
      J. Biol. Chem. 273:32000-32008(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-484, CHARACTERIZATION.
      Tissue: Brain and Smooth muscle.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-484.
      Tissue: Testis.
    10. "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-367; ASN-378 AND ASN-440.
      Tissue: Liver.
    11. "The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators."
      Somoza J.R., Palmer J.T., Ho J.D.
      J. Mol. Biol. 322:559-568(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-484, ACTIVE SITE, DISULFIDE BONDS.
    12. Cited for: VARIANTS CLN13 CYS-231; ARG-321; ALA-458 AND LEU-480.

    Entry informationi

    Entry nameiCATF_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBX1
    Secondary accession number(s): B2R964
    , O95240, Q9NSU4, Q9UKQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 137 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 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