Calpain - OmicsDI

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Disease

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Metabolite Name

Thr-Pro-Arg (1)
Thr-Gly-Arg (1)
Ser-Asp-Arg (1)
Pyroglu-Asn-Arg (1)
L-valine, n-[[1-(5-fluoropentyl)-1h-indol-3-yl]carbonyl]-, methyl ester (1)
Cys-His-Arg (1)
5-methoxy-4-methyl-3-phenylcoumarin (1)
4-phenylbutan-2-ol (1)
3-quinolinecarboxamide, 1,4-dihydro-8-methoxy-4-oxo-1-pentyl-n-tricyclo[3.3.1.13,7]dec-1-yl- (1)
2-methyl-6(s)-(3-pyridyl)tetrahydro-1,2-oxazine (1)
2-furancarboxylic acid, 5-[3-[4-[2-(4-fluorophenyl)ethoxy]phenyl]propyl]- (1)
1h-indole-3-carboxylic acid, 1-(5-fluoropentyl)-, 8-quinolinyl ester (1)
[1,1':4',1''-terphenyl]-3,4'',5-triol (1)
[[4-[5r-chloro-2z-[3r-cyclohexyl-3s-hydroxy-1r-propenyl]-3s-hydroxycyclopentyl]-2r-butenyl]oxy]-acetic acid, isopropyl ester (1)
(s)-n-(1-amino-1-oxo-3-phenylpropan-2-yl)-1-pentyl-1h-indole-3-carboxamide (1)
(3as,5r,5as,8as,9ar)-5,8a-dimethyl-1-methylidene-3a,4,5,5a,6,7,9,9a-octahydroazuleno[6,7-b]furan-2,8-dione (1)
L-myo-inositol-1,4,5-triphosphate (1)
Arg-asp (1)
2-hdeahpda [dmed-fahfa] (1)
Mepirapim (1)
Tyr-His-Arg (1)
Solasodine base + 2h, 1o, o-hex-hex-hex (1)
Cyanidin 3-o-[2''-o-(xylosyl)-6''-o-(p-o-(glucosyl)-p-coumaroyl) glucoside] 5-o-glucoside (1)
Combrestatin a4 (1)
6-oxomometasone furoate (1)
(z)-2-octylpent-2-enedioic acid (1)
Cocamidoprpylbetaine (1)
Ser-Ser-Arg (1)
Glycerol trioleate (1)
.alpha.-galactosyl-n-stearoylsphingosine (1)

First Public Date

2014 (12)
2025 (8)
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2017 (4)
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2015 (1)
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Classification

protozoa (1)

Modification

-17.026549 (1)
-18.010565 (1)
15.994915 (1)
42.010565 (1)
57.021464 (1)

Study type

Transcription profiling by array (40)
RNA-seq of coding RNA (5)
ChIP-seq (4)
Methylation profiling by high throughput sequencing (3)
RNA-seq of coding RNA from single cells (2)
ATAC-seq (1)
Other (1)
DNA-seq (1)
RNA-seq of total RNA (1)
RNA-seq of non coding RNA (1)

Release Date

2016 (91)
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Lab affiliation

Department of Biochemistry and Molecular Biology, University of Calgary, Alberta, Canada; Department of Physiology and Pharmacology, University of Calgary, Alberta, Canada; The Hotchkiss Brain Institute, University of Calgary, Alberta, Canada; McCaig Institute for Bone and Joint Health, University of Calgary, Alberta, Canada (2)
1 - College of Pharmacy, University of Sharjah, Sharjah 2 - Sharjah Institute for Medical Research, University of Sharjah, Sharjah (1)
1. Department of Clinical Genetics, Erasmus University Medical Center, 3015 GE Rotterdam, The Netherlands 2. Department of Pediatrics, Erasmus University Medical Center, 3015 GE Rotterdam, The Netherlands 3. Center for Lysosomal and Metabolic Diseases, Erasmus Medical Center, 3015 GE Rotterdam, The Netherlands (1)
1Department of Pathology; University of California San Diego; La Jolla, CA 92093; USA (1)
Bioanalytics, Department of Clinical Chemistry, University Medical Center Goettingen (1)
Calpain Project Department of Advanced Science for Biomolecules Igakuken (Tokyo Metropolitan Institute of Medical Science) 2-1-6 Kamikitazawa, Setagaya-ku Tokyo 156-8506, Japan (1)
Cell Biology and Physiology, The University of North Carolina at Chapel Hill (1)
Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium Department of Biochemistry, Ghent University, 9000 Ghent, Belgium (1)
Chemical Proteomics, Division of Chemistry I, Department of Medical Biochemistry and Biophysiscs (MBB), Karolinska Institutet, Stockholm, Sweden (1)
Children's Medical Research Insitute (1)
Children's Medical Research Institute, Westmead, Sydney, Australia (1)
Core Facility Proteomics, Department of Clinical Chemistry, University Medical Center Göttingen, Germany (1)
Core Unit Proteomics, Berlin Institute of Health at Charité-Universitätsmedizin Berlin and Max Delbrück Center for Molecular Medicine, Berlin, Germany (1)
Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies University of Freiburg, 79104 Freiburg, Germany (1)
Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies University of Freiburg, 79104 Freiburg, Germany (1)
Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, University of Freiburg (1)
Department of Biochemistry, University of Washington, Seattle, WA, USA. Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA Institute for Protein Design, University of Washington, Seattle, WA, USA (1)
Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts, USA (1)
Department of Physiology and Pharmacology, Cumming School of Medicine, University of Calgary, Alberta T2N 1N4 Canada Snyder Insitute for Chronic Diseases, Cumming School of Medicine, University of Calgary, Alberta T2N 1N4 Canada (1)
Departments of Medicine (Division of Cardiology), Virginia Commonwealth University, Richmond, VA, 23298 (1)
Director, MaineHealth Institute for Research, Proteomics and Lipidomics Laboratory (1)
Director, Proteomics and Lipidomics Core Facility, Mainehealth (1)
Division of Cardiology, Department of Medicine; Columbia University, Vagelos College of Physicians and Surgeons, 622 West 168th Street, New York, NY 10032. Department of Pharmacology and Molecular Signaling, Columbia University, Vagelos College of Physicians and Surgeons (1)
Institute of Neurology (Edinger Institute), University Hospital Frankfurt, Goethe University, Frankfurt, Germany (1)
La Trobe University, Bundoora, VIC 3086, Australia (1)
Leibniz-Institut für Analytische Wissenschaften - ISAS - e.V. (1)
Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V. (1)
Mass Spectrometry Technology Access Center at the McDonnell Genome Institute, Washington University School of Medicine, St. Louis, MO, USA (1)
Medical Proteomics Unit, Office for Research and Development, Faculty of Medicine Siriraj Hospital, and Center forResearch in Complex Systems Science, Mahidol University, Bangkok, Thailand (1)
Research and Development, NHS Blood and Transplant Nuffield Department of Surgical Sciences, and Oxford Biomedical Research Centre, University of Oxford (1)

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In vitro TroponinT digestion by calpain and autolysis of calpain.

TroponinT was incubated with calpain. Incubation time and labels are described in the sample information. Triplicated LC-MS data were merged and processed with ProteinPilot (ver5).

ORGANISM(S): Homo Sapiens (human) Cellular Organisms

2020-11-04 | PXD017015 | JPOST Repository

FLNc Calpain GluC SRM Analysis

Human filamin C (FLNc) is a target of the protease calpain at Y2625. To confirm the dependency of calpain cleavage from FLNc phosphorylation at position S2623/S2624 by PKCa, FLNc was overexpressed in HEK293 cells and cells were treated with PMA to stimulated kinase activity, with Gö6976 to inhibit k...

ORGANISM(S): Homo sapiens (Human)

2017-01-02 | PXD005097 | Pride

Proteomic QSAR analysis of calpain substrate specificity

Calpains are intracellular Ca2+-regulated cysteine proteases that are essential for various cellular functions. Mammalian conventional calpains (calpain-1 and calpain-2) modulate the structure and function of their substrates by limited proteolysis; however, their substrate specificity remains uncle...

ORGANISM(S): Bos taurus (Bovine) Oryctolagus cuniculus algirus Mus musculus (Mouse) Homo sapiens (Human) Gallus gallus (Chicken) Ovis aries Sus scrofa domesticus (domestic pig) Rattus norvegicus (Rat)

2016-07-19 | PXD002532 | Pride

Calpain Pls Qsar Substrate specificity

DEK1 calpain overexpression

Aim: To understand the role of DEK1 in Arabidopsis development. Background: DEK1 has an essential role during embryogenesis and is involved in the maintenance of the epidermis. Tissues: Comparison of wild-type and ADEK1 calpain-overexpressing line. 9 samples were used in this experiment.

ORGANISM(S): Arabidopsis thaliana

2009-12-09 | E-GEOD-19268 | biostudies-arrayexpress

Calpain activity is regulated by a KCTD7–cullin 3 complex via non-degradative ubiquitination

Calpains are a class of non-lysosomal cysteine proteases that exert their regulatory functions via limited proteolysis of their substrates. Similar to the lysosomal and proteasomal systems, calpain dysregulation is implicated in the pathogenesis of neurodegenerative disease and cancer. Despite inten...

ORGANISM(S): Homo sapiens (Human)

2023-05-10 | PXD038842 | Pride

Human Pasef Calpain

Calpain-2 participates in the process of calpain-1 inactivation.

Not available

S-EPMC7610153 | biostudies-literature

Calpain chronicle--an enzyme family under multidisciplinary characterization.

Not available

S-EPMC3153876 | biostudies-literature

mRNA expression profile in murine bone marrow-derived macrophages that were isolated from calpain-6 wild-type and deficient mice

Transcriptional profiling of calpain-6-deficient murine bone marrow-derived macrophages comparing with calpain-6 wild-type macrophages. Total RNA was extracted from the pooled cells. Two-condition experiment, wild-type macrophages vs. calpain-6-deficiennt macrophages. The cells were derived from fou...

ORGANISM(S): Mus musculus

2016-06-29 | E-GEOD-83815 | biostudies-arrayexpress

Mitochondrial dysfunction and consequences in calpain-3-deficient muscle

PRJNA820860 | ENA

Calpain Cleavage of Junctophilin-2 generates a Spectrum of Calcium-dependent Cleavage Products and DNA-rich NT1-Fragment Domains in Cardiomyocytes

Calpains are calcium (Ca2+) activated neutral proteases that are involved in several essential signaling pathways. One Calpain-specific proteolytic target is Junctophilin-2 (JP2), an important structural protein of Ca2+ release units required for the excitation-contraction coupling in cardiomyocytes...

ORGANISM(S): Mus musculus (Mouse)

2022-08-12 | PXD031321 | Pride

Junctophilin Ryanodine Calcium Calpain Cardiomyocyte

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