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P09668

- CATH_HUMAN

UniProt

P09668 - CATH_HUMAN

Protein

Pro-cathepsin H

Gene

CTSH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    Important for the overall degradation of proteins in lysosomes.

    Catalytic activityi

    Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei141 – 1411By similarity
    Active sitei281 – 2811By similarity
    Active sitei301 – 3011By similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    3. cysteine-type endopeptidase activity Source: UniProtKB
    4. cysteine-type peptidase activity Source: UniProtKB
    5. endopeptidase activity Source: UniProtKB
    6. HLA-A specific activating MHC class I receptor activity Source: UniProtKB
    7. peptidase activity Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. serine-type endopeptidase activity Source: UniProtKB
    10. thyroid hormone binding Source: UniProtKB

    GO - Biological processi

    1. adaptive immune response Source: UniProtKB
    2. antigen processing and presentation Source: UniProtKB
    3. bradykinin catabolic process Source: UniProtKB
    4. cellular response to thyroid hormone stimulus Source: UniProtKB
    5. dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
    6. ERK1 and ERK2 cascade Source: UniProtKB
    7. immune response-regulating signaling pathway Source: UniProtKB
    8. membrane protein proteolysis Source: UniProtKB
    9. metanephros development Source: UniProtKB
    10. negative regulation of apoptotic process Source: UniProtKB
    11. neuropeptide catabolic process Source: UniProtKB
    12. positive regulation of angiogenesis Source: UniProtKB
    13. positive regulation of apoptotic signaling pathway Source: Ensembl
    14. positive regulation of cell migration Source: UniProtKB
    15. positive regulation of cell proliferation Source: UniProtKB
    16. positive regulation of epithelial cell migration Source: UniProtKB
    17. positive regulation of gene expression Source: UniProtKB
    18. positive regulation of peptidase activity Source: UniProtKB
    19. protein destabilization Source: UniProtKB
    20. proteolysis Source: UniProtKB
    21. response to retinoic acid Source: UniProtKB
    22. spermatogenesis Source: Ensembl
    23. surfactant homeostasis Source: UniProtKB
    24. T cell mediated cytotoxicity Source: UniProtKB
    25. zymogen activation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.16. 2681.
    ReactomeiREACT_121399. MHC class II antigen presentation.
    SABIO-RKP09668.

    Protein family/group databases

    MEROPSiC01.040.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pro-cathepsin H
    Cleaved into the following 4 chains:
    Gene namesi
    Name:CTSH
    Synonyms:CPSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2535. CTSH.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. alveolar lamellar body Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. lysosome Source: UniProtKB
    7. outer dense fiber Source: Ensembl

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2073. Narcolepsy-cataplexy.
    PharmGKBiPA27033.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Propeptidei23 – 9775Activation peptide1 PublicationPRO_0000026206Add
    BLAST
    Peptidei98 – 1058Cathepsin H mini chainPRO_0000026207
    Propeptidei106 – 115101 PublicationPRO_0000026208
    Chaini116 – 335220Cathepsin HPRO_0000026209Add
    BLAST
    Chaini116 – 292177Cathepsin H heavy chainPRO_0000026210Add
    BLAST
    Chaini293 – 33543Cathepsin H light chainPRO_0000026211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
    Disulfide bondi102 ↔ 327By similarity
    Disulfide bondi138 ↔ 181By similarity
    Disulfide bondi172 ↔ 214By similarity
    Glycosylationi230 – 2301N-linked (GlcNAc...)2 Publications
    Disulfide bondi272 ↔ 322By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP09668.
    PaxDbiP09668.
    PRIDEiP09668.

    PTM databases

    PhosphoSiteiP09668.

    Expressioni

    Gene expression databases

    ArrayExpressiP09668.
    BgeeiP09668.
    CleanExiHS_CTSH.
    GenevestigatoriP09668.

    Organism-specific databases

    HPAiCAB000458.
    HPA003524.

    Interactioni

    Subunit structurei

    Composed of a mini chain and a large chain. The large chain may be split into heavy and light chain. All chains are held together by disulfide bonds.

    Protein-protein interaction databases

    BioGridi107892. 4 interactions.
    IntActiP09668. 1 interaction.
    STRINGi9606.ENSP00000220166.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi123 – 1264
    Helixi141 – 15818
    Helixi166 – 1727
    Helixi180 – 1823
    Turni186 – 1883
    Helixi189 – 1968
    Turni202 – 2043
    Helixi237 – 2459
    Beta strandi249 – 2524
    Helixi258 – 2614
    Beta strandi273 – 2753
    Beta strandi283 – 2919
    Beta strandi294 – 3007
    Turni304 – 3107
    Beta strandi326 – 3294

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BZNmodel-B116-335[»]
    ProteinModelPortaliP09668.
    SMRiP09668. Positions 34-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiP09668.
    KOiK01366.
    OMAiHKYLWSE.
    OrthoDBiEOG70KGPX.
    PhylomeDBiP09668.
    TreeFamiTF328985.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. 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]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. 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.

    P09668-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWATLPLLCA GAWLLGVPVC GAAELCVNSL EKFHFKSWMS KHRKTYSTEE    50
    YHHRLQTFAS NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ 100
    NCSATKSNYL RGTGPYPPSV DWRKKGNFVS PVKNQGACGS CWTFSTTGAL 150
    ESAIAIATGK MLSLAEQQLV DCAQDFNNHG CQGGLPSQAF EYILYNKGIM 200
    GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV EAVALYNPVS 250
    FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK 300
    NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV 335
    Length:335
    Mass (Da):37,394
    Last modified:February 9, 2010 - v4
    Checksum:iE2CF3A5EEA59C1D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti306 – 3061Q → E AA sequence (PubMed:3342889)Curated
    Sequence conflicti306 – 3061Q → E AA sequence 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111G → R.
    Corresponds to variant rs2289702 [ dbSNP | Ensembl ].
    VAR_057038
    Natural varianti23 – 231A → T.
    Corresponds to variant rs35001431 [ dbSNP | Ensembl ].
    VAR_057039
    Natural varianti26 – 261C → S.3 Publications
    Corresponds to variant rs1036938 [ dbSNP | Ensembl ].
    VAR_060368
    Natural varianti126 – 1261G → R in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036478
    Natural varianti179 – 1791H → Y.3 Publications
    Corresponds to variant rs1130856 [ dbSNP | Ensembl ].
    VAR_067717

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16832 mRNA. Translation: CAA34734.1.
    AF426247 mRNA. Translation: AAL23961.1.
    AK314698 mRNA. Translation: BAG37247.1.
    AC011944 Genomic DNA. No translation available.
    BC002479 mRNA. Translation: AAH02479.1.
    X07549 mRNA. Translation: CAA30428.1.
    X07549 mRNA. Translation: CAA30429.1.
    CCDSiCCDS10308.1.
    PIRiS12486. KHHUH.
    RefSeqiNP_004381.2. NM_004390.3.
    UniGeneiHs.148641.

    Genome annotation databases

    EnsembliENST00000220166; ENSP00000220166; ENSG00000103811.
    GeneIDi1512.
    KEGGihsa:1512.
    UCSCiuc021srk.1. human.

    Polymorphism databases

    DMDMi288558851.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16832 mRNA. Translation: CAA34734.1 .
    AF426247 mRNA. Translation: AAL23961.1 .
    AK314698 mRNA. Translation: BAG37247.1 .
    AC011944 Genomic DNA. No translation available.
    BC002479 mRNA. Translation: AAH02479.1 .
    X07549 mRNA. Translation: CAA30428.1 .
    X07549 mRNA. Translation: CAA30429.1 .
    CCDSi CCDS10308.1.
    PIRi S12486. KHHUH.
    RefSeqi NP_004381.2. NM_004390.3.
    UniGenei Hs.148641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BZN model - B 116-335 [» ]
    ProteinModelPortali P09668.
    SMRi P09668. Positions 34-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107892. 4 interactions.
    IntActi P09668. 1 interaction.
    STRINGi 9606.ENSP00000220166.

    Chemistry

    ChEMBLi CHEMBL2111441.

    Protein family/group databases

    MEROPSi C01.040.

    PTM databases

    PhosphoSitei P09668.

    Polymorphism databases

    DMDMi 288558851.

    Proteomic databases

    MaxQBi P09668.
    PaxDbi P09668.
    PRIDEi P09668.

    Protocols and materials databases

    DNASUi 1512.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220166 ; ENSP00000220166 ; ENSG00000103811 .
    GeneIDi 1512.
    KEGGi hsa:1512.
    UCSCi uc021srk.1. human.

    Organism-specific databases

    CTDi 1512.
    GeneCardsi GC15M079213.
    H-InvDB HIX0012481.
    HGNCi HGNC:2535. CTSH.
    HPAi CAB000458.
    HPA003524.
    MIMi 116820. gene.
    neXtProti NX_P09668.
    Orphaneti 2073. Narcolepsy-cataplexy.
    PharmGKBi PA27033.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi P09668.
    KOi K01366.
    OMAi HKYLWSE.
    OrthoDBi EOG70KGPX.
    PhylomeDBi P09668.
    TreeFami TF328985.

    Enzyme and pathway databases

    BRENDAi 3.4.22.16. 2681.
    Reactomei REACT_121399. MHC class II antigen presentation.
    SABIO-RK P09668.

    Miscellaneous databases

    GeneWikii Cathepsin_H.
    GenomeRNAii 1512.
    NextBioi 6261.
    PROi P09668.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09668.
    Bgeei P09668.
    CleanExi HS_CTSH.
    Genevestigatori P09668.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    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 PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase."
      Fuchs R., Gassen H.G.
      Nucleic Acids Res. 17:9471-9471(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-26 AND TYR-179.
      Tissue: Liver.
    2. "Analysis of a truncated form of cathepsin H in human prostate tumor cells."
      Waghray A., Keppler D., Sloane B.F., Schuger L., Chen Y.Q.
      J. Biol. Chem. 277:11533-11538(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-179.
    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], VARIANT SER-26.
      Tissue: Lung.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [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], VARIANT SER-26.
      Tissue: Eye.
    6. "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H."
      Fuchs R., Machleidt W., Gassen H.G.
      Biol. Chem. Hoppe-Seyler 369:469-475(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 88-335, VARIANT TYR-179.
      Tissue: Kidney.
    7. "Amino acid sequences of the human kidney cathepsins H and L."
      Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.
      FEBS Lett. 228:341-345(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 98-105 AND 114-335, GLYCOSYLATION AT ASN-101 AND ASN-230.
      Tissue: Kidney.
    8. "Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens."
      Machleidt W., Ritonja A., Popovic T., Kotnik M., Brzin J., Turk V., Machleidt I., Mueller-Esterl W.
      (In) Turk V. (eds.); Cysteine proteinases and their inhibitors, pp.3-18, Walter de Gruyter, Berlin and New York (1986)
      Cited for: PROTEIN SEQUENCE OF 99-105; 116-159 AND 294-335.
    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-230.
      Tissue: Liver.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-126.

    Entry informationi

    Entry nameiCATH_HUMAN
    AccessioniPrimary (citable) accession number: P09668
    Secondary accession number(s): B2RBK0, Q96NY6, Q9BUM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 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 15
      Human chromosome 15: 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