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Information on EC 3.4.21.B25 - PACE4 proprotein convertase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC3.4.21.B25preliminary BRENDA-supplied EC number
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3.4.21.B25 PACE4 proprotein convertaseSpecify your search results
Word Map
- 3.4.21.B25
-
convertases
- furin
-
prohormone
- endoproteases
-
furin-deficient
-
furin-like
- alpha1-pdx
-
dibasic
-
pro-proteins
- alpha1-antitrypsin
- portland
-
endoproteolysis
- diagnostics
- kexin
-
kexin-like
- ski-1
-
cys-rich
- medicine
-
subtilisin-related
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
releases mature proteins from their proproteins by cleavage of Arg-Xaa-Yaa-Arg-Zaa bonds, where Xaa can be any amino acid and Yaa is Arg or Lys
Synonyms
pace4, pace-4, proprotein convertase pace4, paired basic amino acid-cleaving enzyme 4, xpace4, pace 4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PACE 4
PACE4
PACE4
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
cleavage of C-N-linkage
-
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY
151662-24-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human immunodeficiency virus type 1 Vpr + H2O
?
undergoes proteolytic processing at a very well conserved proprotein convertase cleavage site, R85QRR88-/-, proprotein convertases PC5 and PACE4 can efficiently process extracellular Vpr
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pro-beta site APP cleaving enzyme + H2O
beta site APP cleaving enzyme + ?
-
i.e. BACE, weak substrate
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin-7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
ir
insulin receptor isoform B zymogen + H2O
mature insulin receptor isoform B + ?
-
-
-
?
insulin receptor isoform B zymogen + H2O
mature insulin receptor isoform B + ?
maturation
-
-
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
-
-
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
-
-
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
-
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
cleavage requires both the P4 arginine and the P2 lysine
-
?
additional information
?
-
-
enzyme cleaves at sites with paired basic amino acid residues
-
?
additional information
?
-
-
PACE4-CS recognizes the motifs X-Ala and X-Pro
-
?
additional information
?
-
-
enzyme binds tightly to heparin and anchors heparan sulfate proteoglycans at the extracellular matrix, role in spatiotemporal regulation of TGFbeta-related factors' biological activity
-
?
additional information
?
-
no activity with insulin receptor isoform A zymogen
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human immunodeficiency virus type 1 Vpr + H2O
?
undergoes proteolytic processing at a very well conserved proprotein convertase cleavage site, R85QRR88-/-, proprotein convertases PC5 and PACE4 can efficiently process extracellular Vpr
-
-
?
insulin receptor isoform B zymogen + H2O
mature insulin receptor isoform B + ?
maturation
-
-
?
additional information
?
-
-
enzyme binds tightly to heparin and anchors heparan sulfate proteoglycans at the extracellular matrix, role in spatiotemporal regulation of TGFbeta-related factors' biological activity
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
A23187
-
if reticulocalbin-3 binds to proPACE4 transiently during its biosynthesis, this Ca2+-specific ionophore can block the maturation of proPACE4 to PACE4, accumulation of the proPaCE4-recticulocalbin-3 complex in the cells
alpha1-antitrypsin variant PDX
-
50% inhibition above 0.00002 mM, forms a complex with the enzyme
-
alpha1-antitrypsin variant Portland
-
contains a minimal consensus sequence (Arg-X-X-Arg) for efficient cleavage by furin in its reactive site loop
-
alpha1-antitrypsin variant RRRRSA
-
rat alpha-antitrypsin showing substitution of Arg-Arg-Arg-Arg for Ala-Val-Pro-Met352 at P4-P1 and Ala for Leu354 at P2'
-
alpha1-antitrypsin variant RRRRSL
-
rat alpha-antitrypsin showing substitution of Arg-Arg-Arg-Arg for Ala-Val-Pro-Met352 at P4-P1
-
alpha1-antitrypsin variant RVRR
-
50% inhibition at 0.000005 mM, forms a complex with the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reticulocalbin-3
-
efficiency of PACE4 secretion increases 2fold by coexpression with wild type reticulocalbin-3
-
additional information
-
selective and transient association of reticulocalbin-3 with the precursor of PACE4 plays an important role in the biosynthesis of PACE4
-
additional information
-
the E2F1 transcription factor upregulates the expression of PACE4
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00011
Ac-LLLLR-((2S)-amino-3S-guanidinobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00051
Ac-LLLLR-((2S,3R)-diaminobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00027
Ac-LLLLR-((2S,3S)-diaminobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00066
Ac-LLLLR-(2,3-diaminobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00216
Ac-LLLLR-(2,3-diaminopropionyl)-KR-NH2
pH and temperature not specified in the publication
0.00055
Ac-LLLLR-(2-amino-3-guanidinopropionyl)-KR-NH2
pH and temperature not specified in the publication
0.000087
Ac-LLLLR-(2-amino-4-guanidinobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.000105
Ac-LLLLR-Orn-KR-NH2
pH and temperature not specified in the publication
0.000195
Ac-LLLLRAKR-NH2
pH and temperature not specified in the publication
0.000083
Ac-LLLLRKKR-NH2
pH and temperature not specified in the publication
0.000088
Ac-LLLLRRKR-NH2
pH and temperature not specified in the publication
0.000022
Ac-LLLLRVKR-NH2
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
Ac-[C8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.08
Ac-[C8]LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.07
Ac-[PEG8](D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.09
H2N-[C8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.015
H2N-[C8]LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-(D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.21
Ac-(D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.025
Ac-(D)LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-(D)LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.07
Ac-LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.09
Ac-LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.025
Ac-LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.04
Ac-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.11
Ac-[PEG8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.15
Ac-[PEG8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.06
H2N-[C8](D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.09
H2N-[C8](D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.04
H2N-[C8]LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.13
H2N-[C8]LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.046
H2N-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.047
H2N-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.013
[C8]LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
preference of the enzyme for cleaving substrates at neutral pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme expression in non-small cell lung cancer cells is significantly higher than in normal lung cell and tissues
-
PACE4 is limited to the glia and the retina of the optic nerve head
the enzyme regulates apoptosis in human pancreatic cancer PANC-1 cells via the mitochondrial signaling pathway
enzyme expression in non-small cell lung cancer cells is significantly higher than in normal lung cell and tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is constitutively secreted into the extracellular media and localizes at the cell surface and in the extracellular matrix
-
-
activated at the cell surface where it is tethered to heparan sulfate proteoglycans
the enzyme is constitutively secreted into the extracellular media and localizes at the cell surface and in the extracellular matrix
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
when the PACE4 gene is silenced by small interfering RNA the knockdown of human breast cancer MDA-MB-231 cells shows significantly reduced proliferation, migration and invasion rates
metabolism
insulin receptor requires the proteolytic cleavage of its proform by intra-Golgi furin-like activity. In mammalian cells, insulin receptor is expressed as two isoforms B and A that are responsible for insulin action, but only isozyme A transmits the growth-promoting and mitogenic effects of insulin-like growth factor 2. The two insulin receptor isoforms are similarly cleaved by furin, but when this furin-dependent maturation is inefficient, insulin receptor proforms move to the cell surface where the proprotein convertase PACE4 selectively supports insulin receptor B maturation
physiological function
physiological function
the enzyme is involved in the maturation of insulin receptor isoform B, thereby reducing the specific insulin receptor-dependent effects of insulin-like growth factor 2, IGF2
physiological function
the enzyme participate in the post-translational activation of inactive proteins, leading to mature, biologically active proteins. It regulates proliferation, migration and invasion in human breast cancer MDA-MB-231 cells
physiological function
the enzyme play an important role in prostate cancer cell proliferation
physiological function
the enzyme regulates apoptosis in human pancreatic cancer PANC-1 cells via the mitochondrial signaling pathway
physiological function
the enzyme regulates apoptosis in human prostate cancer cells via endoplasmic reticulum stress and mitochondrial signaling pathways
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
103000
110000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
precursor protein can exist as a dimer as well as a monomer, sedimentation velocity experiments and chemical cross-linking analysis
monomer
-
mature protein and precursor protein, sedimentation velocity experiments and chemical cross-linking analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
autocatalytic processing, cleavage of proprotein after Arg-Val-Lys-Arg149 results in mature protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
deletion of 25 amino acids at the C-terminus results in accelerated maturation of the protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full length PACE4-A, C-terminally truncated PACE4-C which lacks 11 amino acids a t the end of its chaperone-like P-domain, C-terminally shortened version of PACE4-C and PACE4-CS
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
expression of the enzyme correlates with prognosis in non-small cell lung cancer patients. Overall survival is significantly prolonged in PACE4 negative group when compared with PACE4 positive group (5-year survival rates, 23.1% vs. 54.5%, log-rank test), as is disease-free survival (5-year survival rates, 23.4% vs. 55.4%). Positive expression of PACE4 is an independent factor for non-small cell lung cancer patients and it might serve as a potential prognostic biomarker for patients with non-small cell lung cancer
medicine
additional information
-
selective and transient association of reticulocalbin-3 with the precursor of PACE4 plays an important role in the biosynthesis of PACE4
medicine
PACE4 siRNA may exert antitumor activity through the mitochondrial pathway and is expected to be a promising therapeutic strategy for the treatment of pancreatic cancer
medicine
the enzyme has an important role in prostate cancer cell proliferation and is a potential therapeutic target
medicine
the inhibition of the enzyme slows prostate cancer progression and is emerging as a promising therapeutic strategy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taniguchi, T.; Kuroda, R.; Sakurai, K.; Nagahama, M.; Wada, I.; Tsuji, A.; Matsuda, Y.
A critical role for the carboxy terminal region of the proprotein convertase, PACE4A, in the regulation of its autocatalytic activation coupled with secretion
Biochem. Biophys. Res. Commun.
290
878-884
2002
Homo sapiens
Sucic, J.F.; Moehring, J.M.; Inocencio, N.M.; Luchini, J.W.; Moehring, T.J.
Endoprotease PACE4 is Ca2+-dependent and temperature-sensitive and can partly rescue the phenotype of a furin-deficient cell strain
Biochem. J.
339
639-647
1999
Homo sapiens
Rehemtulla, A.; Barr, P.J.; Rhodes, C.J.; Kaufman, R.J.
PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE
Biochemistry
32
11586-11590
1993
Homo sapiens
Tsuji, A.; Sakurai, K.; Kiyokage, E.; Yamazaki, T.; Koide, S.; Toida, K.; Ishimura, K.; Matsuda, Y.
Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix
Biochim. Biophys. Acta
1645
95-104
2003
Homo sapiens
Pinnix, I.; Council, J.E.; Roseberry, B.; Onstead, L.; Mallender, W.; Sucic, J.; Sambamurti, K.
Convertases other than furin cleave beta-secretase to its mature form
FASEB J.
15
1810-1812
2001
Homo sapiens
Creemers, J.W.; Groot Kormelink, P.J.; Roebroek, A.J.; Nakayama, K.; Van de Ven, W.J.
Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4
FEBS Lett.
336
65-69
1993
Homo sapiens
Zhong, M.; Benjannet, S.; Lazure, C.; Munzer, S.; Seidah, N.G.
Functional analysis of human PACE4-A and PACE4-C isoforms: identification of a new PACE4-CS isoform
FEBS Lett.
396
31-36
1996
Homo sapiens
Nagahama, M.; Taniguchi, T.; Hashimoto, E.; Imamaki, A.; Mori, K.; Tsuji, A.; Matsuda, Y.
Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4)
FEBS Lett.
434
155-159
1998
Homo sapiens
Mori, K.; Kii, S.; Tsuji, A.; Nagahama, M.; Imamaki, A.; Hayashi, K.; Akamatsu, T.; Nagamune, H.; Matsuda, Y.
A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus
J. Biochem.
121
941-948
1997
Homo sapiens (P29122), Homo sapiens
Mori, K.; Imamaki, A.; Nagata, K.; Yonetomi, Y.; Kiyokage-Yoshimoto, R.; Martin, T.J.; Gillespie, M.T.; Nagahama, M.; Tsuji, A.; Matsuda, Y.
Subtilisin-like proprotein convertases, PACE4 and PC8, as well as furin, are endogenous proalbumin convertases in HepG2 cells
J. Biochem.
125
627-633
1999
Homo sapiens
Tsuji, A.; Ikoma, T.; Hashimoto, E.; Matsuda, Y.
Development of selectivity of alpha1-antitrypsin variant by mutagenesis in its reactive site loop against proprotein convertase. A crucial role of the P4 arginine in PACE4 inhibition
Protein Eng.
15
123-130
2002
Homo sapiens
Tsuji, A.; Kikuchi, Y.; Sato, Y.; Koide, S.; Yuasa, K.; Nagahama, M.; Matsuda, Y.
A proteomic approach reveals transient association of reticulocalbin-3, a novel member of the CREC family, with the precursor of subtilisin-like proprotein convertase, PACE4
Biochem. J.
396
51-59
2006
Homo sapiens
Mains, R.E.
Proprotein convertase PACE4
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press
2
1871-1874
2004
Aplysia sp., Mus musculus, Homo sapiens (P29122), Rattus norvegicus (Q63415)
-
Lapierre, M.; Siegfried, G.; Scamuffa, N.; Bontemps, Y.; Calvo, F.; Seidah, N.G.; Khatib, A.M.
Opposing function of the proprotein convertases furin and PACE4 on breast cancer cells malignant phenotypes: role of tissue inhibitors of metalloproteinase-1
Cancer Res.
67
9030-9034
2007
Homo sapiens
Page, R.E.; Klein-Szanto, A.J.; Litwin, S.; Nicolas, E.; Al-Jumaily, R.; Alexander, P.; Godwin, A.K.; Ross, E.A.; Schilder, R.J.; Bassi, D.E.
Increased expression of the pro-protein convertase furin predicts decreased survival in ovarian cancer
Cell. Oncol.
29
289-299
2007
Homo sapiens
Yuasa, K.; Suzue, K.; Nagahama, M.; Matsuda, Y.; Tsuji, A.
Transcriptional regulation of subtilisin-like proprotein convertase PACE4 by E2F: possible role of E2F-mediated upregulation of PACE4 in tumor progression
Gene
402
103-110
2007
Homo sapiens
Seidah, N.G.; Mayer, G.; Zaid, A.; Rousselet, E.; Nassoury, N.; Poirier, S.; Essalmani, R.; Prat, A.
The activation and physiological functions of the proprotein convertases
Int. J. Biochem. Cell Biol.
40
1111-1125
2008
Homo sapiens
Tsuji, A.; Kanie, H.; Makise, H.; Yuasa, K.; Nagahama, M.; Matsuda, Y.
Engineering of alpha 1-antitrypsin variants selective for subtilisin-like proprotein convertases PACE4 and PC6: importance of the P2 residue in stable complex formation of the serpin with proprotein convertase
Protein Eng. Des. Sel.
20
163-170
2007
Homo sapiens
Freyer, C.; Kilpatrick, L.M.; Salamonsen, L.A.; Nie, G.
Pro-protein convertases (PCs) other than PC6 are not tightly regulated for implantation in the human endometrium
Reproduction
133
1189-1197
2007
Homo sapiens (P29122), Homo sapiens
Remacle, A.G.; Shiryaev, S.A.; Oh, E.S.; Cieplak, P.; Srinivasan, A.; Wei, G.; Liddington, R.C.; Ratnikov, B.I.; Parent, A.; Desjardins, R.; Day, R.; Smith, J.W.; Lebl, M.; Strongin, A.Y.
Substrate cleavage analysis of furin and related proprotein convertases. A comparative study
J. Biol. Chem.
283
20897-20906
2008
Homo sapiens (P29122), Homo sapiens
Xiao, Y.; Chen, G.; Richard, J.; Rougeau, N.; Li, H.; Seidah, N.G.; Cohen, E.A.
Cell-surface processing of extracellular human immunodeficiency virus type 1 Vpr by proprotein convertases
Virology
372
384-397
2008
Homo sapiens (Q6UW60), Homo sapiens
Fuller, J.A.; Brun-Zinkernagel, A.M.; Clark, A.F.; Wordinger, R.J.
Subtilisin-like proprotein convertase expression, localization, and activation in the human retina and optic nerve head
Invest. Ophthalmol. Vis. Sci.
50
5759-5768
2009
Homo sapiens
Kara, I.; Poggi, M.; Bonardo, B.; Govers, R.; Landrier, J.F.; Tian, S.; Leibiger, I.; Day, R.; Creemers, J.W.; Peiretti, F.
The paired basic amino acid-cleaving enzyme 4 (PACE4) is involved in the maturation of insulin receptor isoform B: an opportunity to reduce the specific insulin receptor-dependent effects of insulin-like growth factor 2 (IGF2)
J. Biol. Chem.
290
2812-2821
2015
Homo sapiens (P29122)
Kwiatkowska, A.; Couture, F.; Levesque, C.; Ly, K.; Beauchemin, S.; Desjardins, R.; Neugebauer, W.; Dory, Y.L.; Day, R.
Novel insights into structure-activity relationships of N-terminally modified PACE4 inhibitors
ChemMedChem
11
289-301
2016
Homo sapiens (P29122)
Dianati, V.; Shamloo, A.; Kwiatkowska, A.; Desjardins, R.; Soldera, A.; Day, R.; Dory, Y.L.
Rational design of a highly potent and selective peptide inhibitor of PACE4 by salt bridge interaction with D160 at position P3
ChemMedChem
12
1169-1172
2017
Homo sapiens (P29122)
Yao, Z.; Sun, B.; Hong, Q.; Yan, J.; Mu, D.; Li, J.; Sheng, H.; Guo, H.
PACE4 regulates apoptosis in human prostate cancer cells via endoplasmic reticulum stress and mitochondrial signaling pathways
Drug Des. Devel. Ther.
9
5911-5923
2015
Homo sapiens (P29122), Homo sapiens
Lin, Y.E.; Wu, Q.N.; Lin, X.D.; Li, G.Q.; Zhang, Y.J.
Expression of paired basic amino acid-cleaving enzyme 4 (PACE4) correlated with prognosis in non-small cell lung cancer (NSCLC) patients
J. Thorac. Dis.
7
850-860
2015
Homo sapiens (P29122), Homo sapiens
Wang, F.; Wang, L.; Pan, J.
PACE4 regulates proliferation, migration and invasion in human breast cancer MDA-MB-231 cells
Mol. Med. Rep.
11
698-704
2015
Homo sapiens (P29122), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 3.4.21.B25)
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Release 2023.1 (January 2023)
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