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1 to 25 of 162  Show
  1. 1
    "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence."
    Aoki K., Imajoh S., Ohno S., Emori Y., Koike M., Kosaki G., Suzuki K.
    FEBS Lett. 205:313-317(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Category: Expression, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "A novel member of the calcium-dependent cysteine protease family."
    Sorimachi H., Ohmi S., Emori Y., Kawasaki H., Saido T.C., Ohno S., Minami Y., Suzuki K.
    Biol. Chem. Hoppe-Seyler 371:171-176(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Category: Function, Expression, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  3. 3
    "Identification of a human cell proliferation inducing gene."
    Kim J.W.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-103; PRO-433; ARG-492 AND ILE-676.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 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 PRO-433.
    Category: Sequences.
    Tissue: Kidney, Pancreas and Placenta.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50448 other entries.

  6. 6
    "Modulation of the calpain autoproteolysis by calpastatin and phospholipids."
    Melloni E., Michetti M., Salamino F., Minafra R., Pontremoli S.
    Biochem. Biophys. Res. Commun. 229:193-197(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVITY REGULATION, AUTOPROTEOLYTIC PROCESSING, COFACTOR, TISSUE SPECIFICITY.
    Category: Function, PTM / Processing, Expression.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization."
    Michetti M., Salamino F., Tedesco I., Averna M., Minafra R., Melloni E., Pontremoli S.
    FEBS Lett. 392:11-15(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Category: Subcellular Location, PTM / Processing, Expression.
    Source: UniProtKB/Swiss-Prot (reviewed).
  8. 8
    "Calcium-binding properties of human erythrocyte calpain."
    Michetti M., Salamino F., Minafra R., Melloni E., Pontremoli S.
    Biochem. J. 325:721-726(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVITY REGULATION, COFACTOR, CALCIUM-BINDING DATA, TISSUE SPECIFICITY.
    Category: Function, Expression.
    Source: UniProtKB/Swiss-Prot (reviewed).
  9. 9
    "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 5354 and mapped to 17 other entries.

  10. 10
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 18117 other entries.

  11. 11
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.
    Category: Function, Subcellular Location.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 and mapped to 4 other entries.

  12. 12
    "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3280 other entries.

  13. 13
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 5469 and mapped to 3 other entries.

  14. 14
    "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Tissue: Erythroleukemia.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 13412 other entries.

  15. 15
    "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Tissue: Liver.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 11551 other entries.

  16. 16
    Category: Pathology & Biotech, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 8 other entries.

  17. 17
    "Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core."
    Li Q., Hanzlik R.P., Weaver R.F., Schonbrunn E.
    Biochemistry 45:701-708(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-353 OF MUTANT ALA-213, CATALYTIC ACTIVITY, CALCIUM-BINDING REGIONS.
    Category: Function, Pathology & Biotech, Structure, Family & Domains.
    Source: UniProtKB/Swiss-Prot (reviewed).
  18. 18
    "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium."
    Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H., Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H., Suzuki K., Bode W.
    Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-3828038, Reactome:R-HSA-3288367.

    This publication is cited by 1 and mapped to 4 other entries.

  19. 19
    "Neurotoxicity induces cleavage of p35 to p25 by calpain."
    Lee M.-S., Kwon Y.T., Li M., Peng J., Friedlander R.M., Tsai L.-H.
    Nature 405:360-364(2000) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-3828038, Reactome:R-HSA-3288367.

    This publication is mapped to 6 other entries.

  20. 20
    "Cleavage and shedding of E-cadherin after induction of apoptosis."
    Steinhusen U., Weiske J., Badock V., Tauber R., Bommert K., Huber O.
    J. Biol. Chem. 276:4972-4980(2001) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-3288367.

    This publication is mapped to 2 other entries.

  21. 21
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-3828038, Reactome:R-HSA-3288367.

    This publication is mapped to 2 other entries.

  22. 22
    "Calpain is a signal transducer and activator of transcription (STAT) 3 and STAT5 protease."
    Oda A., Wakao H., Fujita H.
    Blood 99:1850-1852(2002) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Calpain (mu-calpain) is a signal transducer and activator of transcription (STAT) 3 and STAT5 protease.
    Source: GeneRIF:823.

    This publication is mapped to 17 other entries.

  23. 23
    Category: Function.
    Source: MEROPS:C02.001.

    This publication is mapped to 16 other entries.

  24. 24
    "SNAP-23 is a target for calpain cleavage in activated platelets."
    Rutledge T.W., Whiteheart S.W.
    J. Biol. Chem. 277:37009-37015(2002) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: cleaves SNAP-23 in activated platelets.
    Source: GeneRIF:823.

    This publication is mapped to 7 other entries.

  25. 25
    "Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation."
    Chien A.J., Presland R.B., Kuechle M.K.
    Biochem. Biophys. Res. Commun. 296:911-917(2002) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: MEROPS:C02.001.

    This publication is mapped to 4 other entries.

1 to 25 of 162  Show
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