HUMAN:CATG

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CTSG
Protein Name(s)	Cathepsin G CG
External Links
UniProt	P08311
EMBL	M16117 J04990 CR456807 CR541704 CH471078 BC014460
CCDS	CCDS9631.1
PIR	A32627
RefSeq	NP_001902.1
UniGene	Hs.421724
PDB	1AU8 1CGH 1KYN 1T32
PDBsum	1AU8 1CGH 1KYN 1T32
ProteinModelPortal	P08311
SMR	P08311
BioGrid	107891
IntAct	P08311
MINT	MINT-4054534
STRING	9606.ENSP00000216336
BindingDB	P08311
ChEMBL	CHEMBL4071
GuidetoPHARMACOLOGY	2348
MEROPS	S01.133
PhosphoSite	P08311
DMDM	115725
MaxQB	P08311
PaxDb	P08311
PeptideAtlas	P08311
PRIDE	P08311
DNASU	1511
Ensembl	ENST00000216336
GeneID	1511
KEGG	hsa:1511
UCSC	uc001wpq.3
CTD	1511
GeneCards	GC14M025042
HGNC	HGNC:2532
HPA	CAB000110 HPA047737
MIM	116830
neXtProt	NX_P08311
PharmGKB	PA27032
eggNOG	COG5640
GeneTree	ENSGT00760000118895
HOGENOM	HOG000251820
HOVERGEN	HBG013304
InParanoid	P08311
KO	K01319
OMA	QHITARR
OrthoDB	EOG7RRF7Z
PhylomeDB	P08311
TreeFam	TF333630
BRENDA	3.4.21.20
Reactome	REACT_118572 REACT_118682 REACT_147707 REACT_15428
SABIO-RK	P08311
EvolutionaryTrace	P08311
GeneWiki	Cathepsin_G
GenomeRNAi	1511
NextBio	6257
PMAP-CutDB	P08311
PRO	PR:P08311
Proteomes	UP000005640
Bgee	P08311
CleanEx	HS_CTSG
Genevestigator	P08311
GO	GO:0009986 GO:0005576 GO:0005615 GO:0070062 GO:0005634 GO:0005886 GO:0030141 GO:0008201 GO:0008233 GO:0004252 GO:0002003 GO:0044267 GO:0050832 GO:0022617 GO:0030198 GO:0006955 GO:0044130 GO:0070946 GO:0050778 GO:0006508 GO:0032496
InterPro	IPR001254 IPR018114 IPR001314 IPR009003
Pfam	PF00089
PRINTS	PR00722
SMART	SM00020
SUPFAM	SSF50494
PROSITE	PS50240 PS00134 PS00135

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006468	protein phosphorylation	PMID:8573071^[1]	ECO:0000314			P		Figure 4 Time course of protein phosphorylation in platelets challenged with cathepsin G or thrombin.	complete CACAO 6088
	GO:0030168	platelet activation	PMID:8573071^[1]	ECO:0000314			P		Fig 1,2. Figure 5 Effect of GF 109203X on platelet activation induced by cathepsin G or thrombin.	complete CACAO 6089
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28344315^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002371)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28675934^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0003688)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001155)	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:27068509^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0007318)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:27559042^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0006618) part_of:(UBERON:0002302)	Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	PMID:1937776^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071222	cellular response to lipopolysaccharide	PMID:1937776^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	PMID:1937776^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050829	defense response to Gram-negative bacterium	PMID:1937776^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019731	antibacterial humoral response	PMID:1937776^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:8573071^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:12504904^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q9UIV8)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
colocalizes_with	GO:0062023	collagen-containing extracellular matrix	PMID:20551380^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001496)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:20551380^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001496)	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:1861080^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:1861080^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:8194606^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[15]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:109267 PANTHER:PTN000668264	C		Seeded From UniProt	complete
part_of	GO:0030141	secretory granule	PMID:11907569^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:11907569^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008201	heparin binding	PMID:11907569^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:11907569^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070946	neutrophil mediated killing of gram-positive bacterium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28293 ensembl:ENSMUSP00000015583	P		Seeded From UniProt	complete
involved_in	GO:0050832	defense response to fungus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28293 ensembl:ENSMUSP00000015583	P		Seeded From UniProt	complete
involved_in	GO:0050830	defense response to Gram-positive bacterium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28293 ensembl:ENSMUSP00000015583	P		Seeded From UniProt	complete
involved_in	GO:0050778	positive regulation of immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28293 ensembl:ENSMUSP00000015583	P		Seeded From UniProt	complete
involved_in	GO:0044130	negative regulation of growth of symbiont in host	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28293 ensembl:ENSMUSP00000015583	P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28293 ensembl:ENSMUSP00000015583	P		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001254 InterPro:IPR001314 InterPro:IPR018114	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001254 InterPro:IPR001314 InterPro:IPR018114	P		Seeded From UniProt	complete
involved_in	GO:0006955	immune response	PMID:2569462^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035578	azurophil granule lumen	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0022617	extracellular matrix disassembly	Reactome:R-HSA-1474228	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019730	antimicrobial humoral response	Reactome:R-HSA-6803157	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-381500 Reactome:R-HSA-3785684 Reactome:R-HSA-2022411	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6813659 Reactome:R-HSA-6798751 Reactome:R-HSA-1592316	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	Reactome:R-HSA-3785684	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002003	angiotensin maturation	Reactome:R-HSA-2022411	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042742	defense response to bacterium	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0044	P		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0310	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Si-Tahar, M et al. (1996) The phospholipase C/protein kinase C pathway is involved in cathepsin G-induced human platelet activation: comparison with thrombin. Biochem. J. 313 ( Pt 2) 401-8 PubMed GONUTS page
↑ Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
↑ Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page
↑ ^4.0 ^4.1 Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page
↑ Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page
↑ Barallobre-Barreiro, J et al. (2016) Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. Circulation 134 817-32 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Wasiluk, KR et al. (1991) Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. Infect. Immun. 59 4193-200 PubMed GONUTS page
↑ Jayakumar, A et al. (2003) Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (SERPINB13): a kinetic analysis. Arch. Biochem. Biophys. 409 367-74 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ ^12.0 ^12.1 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page
↑ ^13.0 ^13.1 Maison, CM et al. (1991) Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J. Immunol. 147 921-6 PubMed GONUTS page
↑ Avril, LE et al. (1994) Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. FEBS Lett. 345 81-6 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Reeves, EP et al. (2002) Killing activity of neutrophils is mediated through activation of proteases by K+ flux. Nature 416 291-7 PubMed GONUTS page
↑ Hohn, PA et al. (1989) Genomic organization and chromosomal localization of the human cathepsin G gene. J. Biol. Chem. 264 13412-9 PubMed GONUTS page

[PMID:8573071-1] 1.0 ^1.1 ^1.2 Si-Tahar, M et al. (1996) The phospholipase C/protein kinase C pathway is involved in cathepsin G-induced human platelet activation: comparison with thrombin. Biochem. J. 313 ( Pt 2) 401-8 PubMed GONUTS page

[PMID:28344315-2] Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page

[PMID:28675934-3] Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page

[PMID:25037231-4] 4.0 ^4.1 Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page

[PMID:27068509-5] Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page

[PMID:27559042-6] Barallobre-Barreiro, J et al. (2016) Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. Circulation 134 817-32 PubMed GONUTS page

[PMID:1937776-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Wasiluk, KR et al. (1991) Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. Infect. Immun. 59 4193-200 PubMed GONUTS page

[PMID:12504904-8] Jayakumar, A et al. (2003) Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (SERPINB13): a kinetic analysis. Arch. Biochem. Biophys. 409 367-74 PubMed GONUTS page

[PMID:23533145-9] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-10] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:21630459-11] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:20551380-12] 12.0 ^12.1 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page

[PMID:1861080-13] 13.0 ^13.1 Maison, CM et al. (1991) Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J. Immunol. 147 921-6 PubMed GONUTS page

[PMID:8194606-14] Avril, LE et al. (1994) Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. FEBS Lett. 345 81-6 PubMed GONUTS page

[PMID:21873635-15] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:11907569-16] 16.0 ^16.1 ^16.2 ^16.3 Reeves, EP et al. (2002) Killing activity of neutrophils is mediated through activation of proteases by K+ flux. Nature 416 291-7 PubMed GONUTS page

[PMID:2569462-17] Hohn, PA et al. (1989) Genomic organization and chromosomal localization of the human cathepsin G gene. J. Biol. Chem. 264 13412-9 PubMed GONUTS page

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HUMAN:CATG

Contents

Annotations

Notes

References

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