CTSG | ENSG00000100448 | NCBI 1511

Details for: CTSG

Gene ID: 1511

Symbol: CTSG

Ensembl ID: ENSG00000100448

Description: cathepsin G

Associated with

Activation of matrix metalloproteinases
(R-HSA-1592389)
Antimicrobial peptides
(R-HSA-6803157)
Bacterial infection pathways
(R-HSA-9824439)
Cell recruitment (pro-inflammatory response)
(R-HSA-9664424)
Cytokine signaling in immune system
(R-HSA-1280215)
Degradation of the extracellular matrix
(R-HSA-1474228)
Disease
(R-HSA-1643685)
Extracellular matrix organization
(R-HSA-1474244)
Immune system
(R-HSA-168256)
Infection with mycobacterium tuberculosis
(R-HSA-9635486)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Interleukin-1 family signaling
(R-HSA-446652)
Interleukin-1 processing
(R-HSA-448706)
Leishmania infection
(R-HSA-9658195)
Metabolism of angiotensinogen to angiotensins
(R-HSA-2022377)
Metabolism of proteins
(R-HSA-392499)
Neutrophil degranulation
(R-HSA-6798695)
Parasitic infection pathways
(R-HSA-9824443)
Peptide hormone metabolism
(R-HSA-2980736)
Purinergic signaling in leishmaniasis infection
(R-HSA-9660826)
Regulation of insulin-like growth factor (igf) transport and uptake by insulin-like growth factor binding proteins (igfbps)
(R-HSA-381426)
Response of mtb to phagocytosis
(R-HSA-9637690)
Signaling by interleukins
(R-HSA-449147)
Suppression of apoptosis
(R-HSA-9635465)
Angiotensin maturation
(GO:0002003)
Antibacterial humoral response
(GO:0019731)
Azurophil granule lumen
(GO:0035578)
Biofilm matrix disassembly
(GO:0098786)
Caspase binding
(GO:0089720)
Cellular response to lipopolysaccharide
(GO:0071222)
Collagen-containing extracellular matrix
(GO:0062023)
Cytokine-mediated signaling pathway
(GO:0019221)
Cytoplasmic stress granule
(GO:0010494)
Cytosol
(GO:0005829)
Defense response to fungus
(GO:0050832)
Defense response to gram-negative bacterium
(GO:0050829)
Defense response to gram-positive bacterium
(GO:0050830)
Extracellular exosome
(GO:0070062)
Extracellular matrix disassembly
(GO:0022617)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Heparin binding
(GO:0008201)
Immune response
(GO:0006955)
Lysosome
(GO:0005764)
Membrane
(GO:0016020)
Monocyte chemotaxis
(GO:0002548)
Negative regulation of t cell activation
(GO:0050868)
Neutrophil-mediated killing of gram-positive bacterium
(GO:0070946)
Neutrophil activation
(GO:0042119)
Nucleus
(GO:0005634)
Peptidase activity
(GO:0008233)
Plasma membrane
(GO:0005886)
Platelet activation
(GO:0030168)
Positive regulation of immune response
(GO:0050778)
Positive regulation of platelet aggregation
(GO:1901731)
Protein binding
(GO:0005515)
Protein maturation
(GO:0051604)
Protein phosphorylation
(GO:0006468)
Protein processing
(GO:0016485)
Proteolysis
(GO:0006508)
Purinergic nucleotide receptor signaling pathway
(GO:0035590)
Receptor ligand activity
(GO:0048018)
Secretory granule
(GO:0030141)
Serine-type endopeptidase activity
(GO:0004252)
Serine-type peptidase activity
(GO:0008236)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 20.4442
Cell Significance Index: -3.1800
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 11.9169
Cell Significance Index: 318.7700
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 7.9260
Cell Significance Index: -3.2200
Cell Name: late promyelocyte (CL0002151)
Fold Change: 7.2820
Cell Significance Index: 48.3100
Cell Name: early promyelocyte (CL0002154)
Fold Change: 5.6300
Cell Significance Index: 35.9400
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 2.4818
Cell Significance Index: -3.0600
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 0.8971
Cell Significance Index: -3.5400
Cell Name: skin fibroblast (CL0002620)
Fold Change: 0.7016
Cell Significance Index: 1.6200
Cell Name: fallopian tube secretory epithelial cell (CL4030006)
Fold Change: 0.2831
Cell Significance Index: 4.3800
Cell Name: inhibitory interneuron (CL0000498)
Fold Change: 0.1815
Cell Significance Index: 2.1700
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.1335
Cell Significance Index: 8.6100
Cell Name: pro-T cell (CL0000827)
Fold Change: 0.0031
Cell Significance Index: 0.0800
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.0005
Cell Significance Index: -0.0200
Cell Name: helper T cell (CL0000912)
Fold Change: -0.0007
Cell Significance Index: -0.0100
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.0012
Cell Significance Index: -0.0600
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0016
Cell Significance Index: -2.9900
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0049
Cell Significance Index: -3.1200
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0049
Cell Significance Index: -3.7400
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0072
Cell Significance Index: -3.2500
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: -0.0090
Cell Significance Index: -0.1000
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: -0.0132
Cell Significance Index: -1.8100
Cell Name: neoplastic cell (CL0001063)
Fold Change: -0.0135
Cell Significance Index: -2.6700
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0135
Cell Significance Index: -0.6300
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: -0.0167
Cell Significance Index: -3.0100
Cell Name: squamous epithelial cell (CL0000076)
Fold Change: -0.0189
Cell Significance Index: -0.2300
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: -0.0211
Cell Significance Index: -2.6000
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0227
Cell Significance Index: -3.8800
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.0237
Cell Significance Index: -0.6600
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.0239
Cell Significance Index: -2.7900
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.0283
Cell Significance Index: -1.4700
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.0287
Cell Significance Index: -0.7800
Cell Name: lactocyte (CL0002325)
Fold Change: -0.0291
Cell Significance Index: -3.7600
Cell Name: neural progenitor cell (CL0011020)
Fold Change: -0.0293
Cell Significance Index: -0.2900
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.0299
Cell Significance Index: -3.1100
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.0308
Cell Significance Index: -0.7900
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.0309
Cell Significance Index: -3.5500
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0342
Cell Significance Index: -3.5000
Cell Name: duct epithelial cell (CL0000068)
Fold Change: -0.0376
Cell Significance Index: -0.5200
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.0407
Cell Significance Index: -3.1200
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -0.0458
Cell Significance Index: -0.7900
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.0495
Cell Significance Index: -3.6900
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.0512
Cell Significance Index: -3.1400
Cell Name: astrocyte of the cerebral cortex (CL0002605)
Fold Change: -0.0555
Cell Significance Index: -0.9600
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.0579
Cell Significance Index: -3.8900
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.0606
Cell Significance Index: -3.4000
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.0620
Cell Significance Index: -3.2300
Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
Fold Change: -0.0663
Cell Significance Index: -0.8400
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.0714
Cell Significance Index: -2.6200
Cell Name: CD14-low, CD16-positive monocyte (CL0002396)
Fold Change: -0.0718
Cell Significance Index: -1.7400
Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
Fold Change: -0.0747
Cell Significance Index: -0.8300
Cell Name: smooth muscle cell of prostate (CL1000487)
Fold Change: -0.0752
Cell Significance Index: -0.8700
Cell Name: connective tissue cell (CL0002320)
Fold Change: -0.0757
Cell Significance Index: -0.7300
Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
Fold Change: -0.0770
Cell Significance Index: -0.8400
Cell Name: myoblast (CL0000056)
Fold Change: -0.0804
Cell Significance Index: -0.7900
Cell Name: myeloid lineage restricted progenitor cell (CL0000839)
Fold Change: -0.0819
Cell Significance Index: -1.1500
Cell Name: skeletal muscle satellite cell (CL0000594)
Fold Change: -0.0860
Cell Significance Index: -0.9100
Cell Name: hematopoietic cell (CL0000988)
Fold Change: -0.0899
Cell Significance Index: -1.3200
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0917
Cell Significance Index: -4.3100
Cell Name: oligodendrocyte precursor cell (CL0002453)
Fold Change: -0.0942
Cell Significance Index: -1.2300
Cell Name: preadipocyte (CL0002334)
Fold Change: -0.0963
Cell Significance Index: -1.8800
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: -0.0989
Cell Significance Index: -0.7100
Cell Name: Langerhans cell (CL0000453)
Fold Change: -0.1024
Cell Significance Index: -0.9800
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.1059
Cell Significance Index: -3.1200
Cell Name: keratinocyte (CL0000312)
Fold Change: -0.1061
Cell Significance Index: -2.6500
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.1083
Cell Significance Index: -3.4700
Cell Name: common myeloid progenitor (CL0000049)
Fold Change: -0.1156
Cell Significance Index: -1.3600
Cell Name: erythrocyte (CL0000232)
Fold Change: -0.1234
Cell Significance Index: -3.1500
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.1267
Cell Significance Index: -3.7200
Cell Name: muscle fibroblast (CL1001609)
Fold Change: -0.1273
Cell Significance Index: -0.7800
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.1288
Cell Significance Index: -3.4500
Cell Name: chondroblast (CL0000058)
Fold Change: -0.1346
Cell Significance Index: -0.7900
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.1361
Cell Significance Index: -3.9000
Cell Name: CD8-positive, alpha-beta thymocyte (CL0000811)
Fold Change: -0.1394
Cell Significance Index: -1.2900
Cell Name: thymocyte (CL0000893)
Fold Change: -0.1432
Cell Significance Index: -1.8100
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.1442
Cell Significance Index: -3.8500
Cell Name: hematopoietic multipotent progenitor cell (CL0000837)
Fold Change: -0.1483
Cell Significance Index: -1.7900
Cell Name: mast cell (CL0000097)
Fold Change: -0.1520
Cell Significance Index: -2.0000
Cell Name: caudal ganglionic eminence derived cortical interneuron (CL4023064)
Fold Change: -0.1560
Cell Significance Index: -3.1100
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.1562
Cell Significance Index: -3.8100
Cell Name: peg cell (CL4033014)
Fold Change: -0.1571
Cell Significance Index: -3.6300
Cell Name: erythroid progenitor cell (CL0000038)
Fold Change: -0.1583
Cell Significance Index: -2.0700
Cell Name: CD14-positive monocyte (CL0001054)
Fold Change: -0.1596
Cell Significance Index: -3.1200
Cell Name: early T lineage precursor (CL0002425)
Fold Change: -0.1605
Cell Significance Index: -2.3300
Cell Name: leukocyte (CL0000738)
Fold Change: -0.1619
Cell Significance Index: -2.7500
Cell Name: megakaryocyte (CL0000556)
Fold Change: -0.1698
Cell Significance Index: -2.7500
Cell Name: hematopoietic stem cell (CL0000037)
Fold Change: -0.1714
Cell Significance Index: -2.9300
Cell Name: hepatoblast (CL0005026)
Fold Change: -0.1730
Cell Significance Index: -2.9100
Cell Name: myeloid cell (CL0000763)
Fold Change: -0.1738
Cell Significance Index: -2.3100
Cell Name: granulocyte (CL0000094)
Fold Change: -0.1766
Cell Significance Index: -2.1300
Cell Name: pro-B cell (CL0000826)
Fold Change: -0.1795
Cell Significance Index: -1.9300
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: -0.1816
Cell Significance Index: -2.4900
Cell Name: cytotoxic T cell (CL0000910)
Fold Change: -0.1846
Cell Significance Index: -2.6900
Cell Name: granulocyte monocyte progenitor cell (CL0000557)
Fold Change: -0.1870
Cell Significance Index: -2.0900
Cell Name: enteric smooth muscle cell (CL0002504)
Fold Change: -0.1877
Cell Significance Index: -0.9900
Cell Name: immature innate lymphoid cell (CL0001082)
Fold Change: -0.1892
Cell Significance Index: -2.3400
Cell Name: fraction A pre-pro B cell (CL0002045)
Fold Change: -0.1904
Cell Significance Index: -2.2500
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -0.1932
Cell Significance Index: -3.5700
Cell Name: erythroid lineage cell (CL0000764)
Fold Change: -0.1941
Cell Significance Index: -2.1400
Cell Name: proerythroblast (CL0000547)
Fold Change: -0.1996
Cell Significance Index: -2.8600
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.2008
Cell Significance Index: -3.3600

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** CTSG is a 51-kDa protein with a molecular weight of 51 kDa. It is a serine-type endopeptidase, meaning it requires a serine residue for catalysis. CTSG is a cysteine protease, but its catalytic site is not accessible due to the presence of a disulfide bond. This unique structure allows CTSG to degrade a wide range of substrates, including antimicrobial peptides, extracellular matrix proteins, and other proteins. **Pathways and Functions** CTSG is involved in several key pathways and functions, including: 1. **Antimicrobial Defense**: CTSG is crucial for the degradation of antimicrobial peptides, such as defensins, which help to protect against bacterial and fungal infections. 2. **Extracellular Matrix Degradation**: CTSG degrades extracellular matrix proteins, such as collagen and elastin, which is essential for tissue remodeling and repair. 3. **Immune Response**: CTSG is involved in the regulation of immune responses, including the processing and presentation of antigens to T-cells. 4. **Cell Signaling**: CTSG can interact with various signaling molecules, including cytokines and growth factors, to regulate cell proliferation, migration, and survival. 5. **Protein Degradation**: CTSG is involved in the degradation of various proteins, including those involved in inflammation, cell signaling, and protein homeostasis. **Clinical Significance** Dysregulation of CTSG has been implicated in several diseases, including: 1. **Periodontitis**: CTSG has been shown to contribute to the progression of periodontitis by degrading antimicrobial peptides and extracellular matrix proteins. 2. **Rheumatoid Arthritis**: CTSG has been implicated in the pathogenesis of rheumatoid arthritis by degrading extracellular matrix proteins and contributing to joint inflammation. 3. **Cancer**: CTSG has been shown to contribute to cancer progression by degrading proteins involved in cell signaling and protein homeostasis. 4. **Neurodegenerative Diseases**: CTSG has been implicated in neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease, by degrading proteins involved in cell signaling and protein homeostasis. In conclusion, CTSG is a crucial enzyme involved in various physiological and pathological processes. Its dysregulation has been implicated in several diseases, highlighting the importance of understanding its role in immune response, protein degradation, and cell signaling. Further research is needed to elucidate the mechanisms by which CTSG contributes to disease and to develop therapeutic strategies to target its dysregulation.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Cathepsin G

Genular Protein ID: 3261836550

Symbol: CATG_HUMAN

Name: Cathepsin G

UniProtKB Accession Codes:

P08311 Q6IBJ6 Q9UCA5 Q9UCU6

Database IDs:

Citations:

PubMed ID: 3304423

Title: Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases.

PubMed ID: 3304423

DOI: 10.1021/bi00382a032

PubMed ID: 2569462

Title: Genomic organization and chromosomal localization of the human cathepsin G gene.

PubMed ID: 2569462

DOI: 10.1016/s0021-9258(18)80012-6

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8194606

Title: Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G.

PubMed ID: 8194606

DOI: 10.1016/0014-5793(94)00410-2

PubMed ID: 3799965

Title: Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors.

PubMed ID: 3799965

DOI: 10.1016/0003-2697(86)90612-3

PubMed ID: 2501794

Title: Antibiotic proteins of human polymorphonuclear leukocytes.

PubMed ID: 2501794

DOI: 10.1073/pnas.86.14.5610

PubMed ID: 1861080

Title: Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G.

PubMed ID: 1861080

PubMed ID: 7897245

Title: Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis.

PubMed ID: 7897245

DOI: 10.1016/0022-1759(94)00295-8

PubMed ID: 26274980

Title: Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G.

PubMed ID: 26274980

DOI: 10.3390/biom5031832

PubMed ID: 3390156

Title: Cathepsin G is a strong platelet agonist released by neutrophils.

PubMed ID: 3390156

DOI: 10.1042/bj2510293

PubMed ID: 2383548

Title: An unusual specificity in the activation of neutrophil serine proteinase zymogens.

PubMed ID: 2383548

DOI: 10.1021/bi00474a013

PubMed ID: 2116408

Title: Identification of the primary antimicrobial domains in human neutrophil cathepsin G.

PubMed ID: 2116408

DOI: 10.1016/s0021-9258(18)77388-2

PubMed ID: 2117044

Title: Listericidal activity of human neutrophil cathepsin G.

PubMed ID: 2117044

DOI: 10.1099/00221287-136-6-997

PubMed ID: 2126324

Title: Molecular mechanism for the antigonococcal action of lysosomal cathepsin G.

PubMed ID: 2126324

DOI: 10.1111/j.1365-2958.1990.tb00706.x

PubMed ID: 1937776

Title: Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa.

PubMed ID: 1937776

DOI: 10.1128/iai.59.11.4193-4200.1991

PubMed ID: 7842483

Title: Stimulation of human lymphocytes by cathepsin G.

PubMed ID: 7842483

DOI: 10.1016/0008-8749(95)80005-4

PubMed ID: 7744748

Title: Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G.

PubMed ID: 7744748

DOI: 10.1074/jbc.270.19.11168

PubMed ID: 7499346

Title: Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D.

PubMed ID: 7499346

DOI: 10.1074/jbc.270.47.28413

PubMed ID: 8920993

Title: Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation.

PubMed ID: 8920993

DOI: 10.1042/bj3190873

PubMed ID: 9000539

Title: Cathepsin G binds to human lymphocytes.

PubMed ID: 9000539

DOI: 10.1002/jlb.61.1.73

PubMed ID: 9536127

Title: Cathepsin G enhances human natural killer cytotoxicity.

PubMed ID: 9536127

DOI: 10.1046/j.1365-2567.1998.00397.x

PubMed ID: 10702240

Title: Cathepsin G activates protease-activated receptor-4 in human platelets.

PubMed ID: 10702240

DOI: 10.1074/jbc.275.10.6819

PubMed ID: 11259672

Title: The human brm protein is cleaved during apoptosis: the role of cathepsin G.

PubMed ID: 11259672

DOI: 10.1073/pnas.071057398

PubMed ID: 15385470

Title: The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli.

PubMed ID: 15385470

DOI: 10.1128/iai.72.10.5712-5721.2004

PubMed ID: 15210802

Title: Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor.

PubMed ID: 15210802

DOI: 10.4049/jimmunol.173.1.428

PubMed ID: 15100291

Title: Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes.

PubMed ID: 15100291

DOI: 10.4049/jimmunol.172.9.5495

PubMed ID: 16963625

Title: N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant.

PubMed ID: 16963625

DOI: 10.1189/jlb.0406290

PubMed ID: 18586676

Title: The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase.

PubMed ID: 18586676

DOI: 10.1074/jbc.m710286200

PubMed ID: 18217133

Title: Cathepsin G, a leukocyte protease, activates coagulation factor VIII.

PubMed ID: 18217133

DOI: 10.1160/th07-08-0495

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22275911

Title: Inhibition of the plasma-membrane-associated serine protease cathepsin G by Mycobacterium tuberculosis Rv3364c suppresses caspase-1 and pyroptosis in macrophages.

PubMed ID: 22275911

DOI: 10.3389/fmicb.2011.00281

PubMed ID: 22879591

Title: Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions.

PubMed ID: 22879591

DOI: 10.1074/jbc.m112.394452

PubMed ID: 22307629

Title: IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G.

PubMed ID: 22307629

DOI: 10.1073/pnas.1115884109

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 29077095

Title: Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts.

PubMed ID: 29077095

DOI: 10.1038/cdd.2017.167

PubMed ID: 29652924

Title: Extended cleavage specificity of human neutrophil cathepsin G: A low activity protease with dual chymase and tryptase-type specificities.

PubMed ID: 29652924

DOI: 10.1371/journal.pone.0195077

PubMed ID: 30804664

Title: Cathepsin G cleaves and activates IL-36gamma and promotes the inflammation of psoriasis.

PubMed ID: 30804664

DOI: 10.2147/dddt.s194765

PubMed ID: 32144329

Title: Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of Lubricin, a Synovial Mucin.

PubMed ID: 32144329

DOI: 10.1038/s41598-020-61161-5

PubMed ID: 33589665

Title:

PubMed ID: 33589665

DOI: 10.1038/s41598-020-77619-5

PubMed ID: 32995850

Title: Cathepsin G Degrades Staphylococcus aureus Biofilms.

PubMed ID: 32995850

DOI: 10.1093/infdis/jiaa612

PubMed ID: 8896442

Title: The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities.

PubMed ID: 8896442

DOI: 10.1002/j.1460-2075.1996.tb00933.x

PubMed ID: 11942800

Title: Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design.

PubMed ID: 11942800

DOI: 10.1021/ja017506h

PubMed ID: 15741158

Title: A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo.

PubMed ID: 15741158

DOI: 10.1074/jbc.m501302200

PubMed ID: 32303641

Title: Local structural plasticity of the Staphylococcus aureus evasion protein EapH1 enables engagement with multiple neutrophil serine proteases.

PubMed ID: 32303641

DOI: 10.1074/jbc.ra120.013601

PubMed ID: 8454293

Title: Sequence variant of the human cathepsin G gene.

PubMed ID: 8454293

DOI: 10.1007/bf00230230

Sequence Information:

Length: 255
Mass: 28837
Checksum: 6228E741E6A43889
Sequence:

MQPLLLLLAF LLPTGAEAGE IIGGRESRPH SRPYMAYLQI QSPAGQSRCG GFLVREDFVL 
TAAHCWGSNI NVTLGAHNIQ RRENTQQHIT ARRAIRHPQY NQRTIQNDIM LLQLSRRVRR 
NRNVNPVALP RAQEGLRPGT LCTVAGWGRV SMRRGTDTLR EVQLRVQRDR QCLRIFGSYD 
PRRQICVGDR RERKAAFKGD SGGPLLCNNV AHGIVSYGKS SGVPPEVFTR VSSFLPWIRT 
TMRSFKLLDQ METPL

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: CTSG

Associated with

Cells (max top 100)

Other Information

Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases. PubMed ID: 3304423

Genomic organization and chromosomal localization of the human cathepsin G gene. PubMed ID: 2569462

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. PubMed ID: 8194606

Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors. PubMed ID: 3799965

Antibiotic proteins of human polymorphonuclear leukocytes. PubMed ID: 2501794

Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. PubMed ID: 1861080

Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis. PubMed ID: 7897245

Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G. PubMed ID: 26274980

Cathepsin G is a strong platelet agonist released by neutrophils. PubMed ID: 3390156

An unusual specificity in the activation of neutrophil serine proteinase zymogens. PubMed ID: 2383548

Identification of the primary antimicrobial domains in human neutrophil cathepsin G. PubMed ID: 2116408

Listericidal activity of human neutrophil cathepsin G. PubMed ID: 2117044

Molecular mechanism for the antigonococcal action of lysosomal cathepsin G. PubMed ID: 2126324

Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. PubMed ID: 1937776

Stimulation of human lymphocytes by cathepsin G. PubMed ID: 7842483

Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G. PubMed ID: 7744748

Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D. PubMed ID: 7499346

Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation. PubMed ID: 8920993

Cathepsin G binds to human lymphocytes. PubMed ID: 9000539

Cathepsin G enhances human natural killer cytotoxicity. PubMed ID: 9536127

Cathepsin G activates protease-activated receptor-4 in human platelets. PubMed ID: 10702240

The human brm protein is cleaved during apoptosis: the role of cathepsin G. PubMed ID: 11259672

The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli. PubMed ID: 15385470

Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor. PubMed ID: 15210802

Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. PubMed ID: 15100291

N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant. PubMed ID: 16963625

The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase. PubMed ID: 18586676

Cathepsin G, a leukocyte protease, activates coagulation factor VIII. PubMed ID: 18217133

Initial characterization of the human central proteome. PubMed ID: 21269460

Inhibition of the plasma-membrane-associated serine protease cathepsin G by Mycobacterium tuberculosis Rv3364c suppresses caspase-1 and pyroptosis in macrophages. PubMed ID: 22275911

Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions. PubMed ID: 22879591

IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G. PubMed ID: 22307629

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts. PubMed ID: 29077095

Extended cleavage specificity of human neutrophil cathepsin G: A low activity protease with dual chymase and tryptase-type specificities. PubMed ID: 29652924

Cathepsin G cleaves and activates IL-36gamma and promotes the inflammation of psoriasis. PubMed ID: 30804664

Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of Lubricin, a Synovial Mucin. PubMed ID: 32144329