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Information on EC 3.4.21.106 - hepsin and Organism(s) Homo sapiens and UniProt Accession P05981

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.106 hepsin
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P05981 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cleavage after basic amino-acid residues, with Arg strongly preferred to Lys
Synonyms
hepsin, S01.224, TMPRSS1, transmembrane serine protease 1, type II transmembrane serine protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TMPRSS1
247
-
transmembrane serine protease 1
281502
-
type II transmembrane serine protease
247
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY hide
112398-23-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hepatocyte growth factor precursor + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-KQLR-7-amido-4-methylcoumarin + H2O
N-acetyl-KQLR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
S2366 + H2O
?
show the reaction diagram
-
-
-
?
single-chain hepatocyte growth factor + H2O
two-chain hepatocyte growth factor
show the reaction diagram
efficiently converted by soluble form of hepsin comprising the entire extracellular domain
-
-
?
Abz-KQSRKFVPY(3-NO2) + H2O
Abz-KQSR + KFVPY(3-NO2)
show the reaction diagram
-
peptide sequence from trask
-
-
?
Abz-RAARVVGGY(3-NO2) + H2O
Abz-RAAR + VVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RKRRGSRGY(3-NO2) + H2O
Abz-RKRR + GSRGY(3-NO2)
show the reaction diagram
-
peptide sequence from filaggrin
-
-
?
Abz-RLARVVGGY(3-NO2) + H2O
Abz-RLAR + VVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RQARAVGGY(3-NO2) + H2O
Abz-RQAR + AVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RQARVVGGY(3-NO2) + H2O
Abz-RQAR + VVGGY(3-NO2)
show the reaction diagram
Abz-RQARYVGGY(3-NO2) + H2O
Abz-RQAR + YVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RQLRVVGGY(3-NO2) + H2O
Abz-RQLR + VVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RQRRALEKY(3-NO2) + H2O
Abz-RQRR + ALEKY(3-NO2)
show the reaction diagram
-
peptide sequence from alphaEbeta7 integrin
-
-
?
Abz-RQRRVVGGY(3-NO2) + H2O
Abz-RQRR + VVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RQYRVVGGY(3-NO2) + H2O
Abz-RQYR + VVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-RRARVVGGY(3-NO2) + H2O
Abz-RRAR + VVGGY(3-NO2)
show the reaction diagram
-
-
-
-
?
Abz-SKGRSLIGY(3-NO2) + H2O
Abz-SKGR + SLIGY(3-NO2)
show the reaction diagram
-
peptide sequence from PAR-2
-
-
?
Abz-SKLRVVGGY(3-NO2) + H2O
Abz-SKLR + VVGGY(3-NO2)
show the reaction diagram
-
peptide sequence from proMSP-1
-
-
?
acetyl-DQLR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-KKTR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-KQLR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
most active tetrapeptide substrate
-
-
?
acetyl-PVDR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
least active tetrapeptide substrate
-
-
?
blood clotting factor IX + H2O
active blood clotting factor IX
show the reaction diagram
-
-
-
-
?
blood clotting factor VII + H2O
active blood clotting factor VII
show the reaction diagram
-
-
-
-
?
blood clotting factor XII + H2O
active blood clotting factor XII
show the reaction diagram
-
-
-
-
?
Boc-Gln-Ala-Arg-AMC + H2O
?
show the reaction diagram
-
-
-
-
?
epidermal growth factor receptor + H2O
?
show the reaction diagram
-
hepsin cleavage of epidermal growth factor receptor is not dependent on receptor tyrosine phosphorylation
-
-
?
factor X + H2O
?
show the reaction diagram
-
activates factor X in the presence of factor VII
-
?
Glu-Pro-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
hepatocyte growth factor precursor + H2O
?
show the reaction diagram
L-Asp-L-Ala-L-Ala-L-Arg-4-nitroanilide + H2O
L-Asp-L-Ala-L-Ala-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Asp-L-Lys-(gamma-Cbo)-L-Pro-L-Arg-4-nitroanilide + H2O
L-Asp-L-Lys-(gamma-Cbo)-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
laminin-332 + H2O
?
show the reaction diagram
-
by Western blotting and mass spectrometry, it is shown that hepsin cleaves the beta3 chain of rat Laminin-332. N-terminal sequencing identifies the cleavage site at beta3 Arg245, in a sequence context (SQLR245 cleavage LQGSCFC) conserved among species and in remarkable agreement with reported consensus target sequences for hepsin activity
-
-
?
N-acetyl-L-Lys-L-Arg-L-Leu-L-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-Ile-Glu-Phe-Ser-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
N-benzoyl-Leu-Ser-Arg-4-nitroanilide + H2O
?
show the reaction diagram
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
pro-hepatocyte growth factor + H2O
active hepatocyte growth factor
show the reaction diagram
-
hepsin-mediated pro-HGF activation may be critical in the pathogenesis of human prostate cancer
-
-
?
pro-macrophage-stimulating protein + H2O
?
show the reaction diagram
-
the cleavage site is between Arg(483) and Val(484). At least 50% of the substrate is processed within 1 h at a hepsin concentration of 2.4 nM and at a molar enzyme to substrate ratio of 1:500
-
-
?
pro-urokinase + H2O
active urokinase
show the reaction diagram
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
active high molecular weight urokinase-type plasminogen activator
show the reaction diagram
-
cleavage at the Lys158-Ile159 (P1-P1') peptide bond
-
-
?
prostasin pro-peptide + H2O
prostasin
show the reaction diagram
-
hepsin activates prostasin, cleavage occurs at Arg44
-
-
?
Protein + H2O
?
show the reaction diagram
zymogen factor VII + H2O
factor VIIa
show the reaction diagram
-
cleaves between Arg152 and Ile153
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hepatocyte growth factor precursor + H2O
?
show the reaction diagram
-
-
-
-
?
hepatocyte growth factor precursor + H2O
?
show the reaction diagram
-
potential substrate for hepsin in vivo
-
-
?
Protein + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
optimal concentration: 5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hepatocyte growth factor activator inhibitor-1B
-
potent inhibitor of hepsin
-
hepatocyte growth factor activator inhibitor-2
-
potent inhibitor of hepsin
-
4-(2-aminoethyl)-benzenesulfonylfluoride hydrochloride
-
residual hepsin activity: 0%
4-amidinophenylmethylsulfonyl fluoride
-
complete inhibition at 1 mM
4-methylumbelliferyl p-guanidinobenzoate
-
irreversible inhibitor
alpha1-Aantichymotrypsin
-
residual hepsin activity: 88%
-
alpha1-antitrypsin
-
residual hepsin activity: 67%
-
alpha2-antiplasmin
-
residual hepsin activity: 1%
-
anthralin
-
at 0.067 mM anthralin the hepsin activity is reduced by more than 70%
antithrombin III
-
Aprotinin
Glu-Gly-Arg-chloromethyl ketone
-
irreversible covalent inhibitor
HAI-2
-
is a potent inhibitor
-
hepatocyte growth factor activator inhibitor-1
-
potent inhibitor of hepsin activity
-
hepatocyte growth factor activator inhibitor-1-derived Kunitz domain inhibitor
-
KD1, inhibits cleavage of laminin-332 in a dose-dependent manner
-
hepatocyte growth factor activator inhibitor-2
-
potent inhibitor of hepsin activity
-
HI-10331
-
reversible active site inhibitor
KD1
-
HAI-1B-derived Kunitz domain inhibitor
-
leupeptin
-
residual hepsin activity: 4%
plasminogen activator inhibitor-1
-
residual hepsin activity: 0%
Soybean trypsin inhibitor
-
residual hepsin activity: 78%
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
resveratrol
-
hepsin activity increases in dose-dependent manner in the presence of resveratrol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.114
Abz-KQSRKFVPY(3-NO2)
-
peptide sequence from trask
0.22
Abz-RAARVVGGY(3-NO2)
-
-
0.189
Abz-RKRRGSRGY(3-NO2)
-
peptide sequence from filaggrin
0.29
Abz-RLARVVGGY(3-NO2)
-
-
0.191
Abz-RQARAVGGY(3-NO2)
-
-
0.369
Abz-RQARVVGGY(3-NO2)
-
; peptide sequence from matriptase
0.175
Abz-RQARYVGGY(3-NO2)
-
-
0.068
Abz-RQLRVVGGY(3-NO2)
-
-
0.085
Abz-RQRRALEKY(3-NO2)
-
peptide sequence from alphaEbeta7 integrin
0.07
Abz-RQRRVVGGY(3-NO2)
-
-
0.109
Abz-RQYRVVGGY(3-NO2)
-
-
0.072
Abz-RRARVVGGY(3-NO2)
-
-
0.373
Abz-SKGRSLIGY(3-NO2)
-
peptide sequence from PAR-2
0.14
Abz-SKLRVVGGY(3-NO2)
-
peptide sequence from proMSP-1
0.05
L-Asp-L-Ala-L-Ala-L-Arg-4-nitroanilide
-
in 0.3M Tris-HCl, 0.3 M imidazole, and 0.5 M NaCl, pH 8.4, at 37°C
0.05
L-Asp-L-Lys-(gamma-Cbo)-L-Pro-L-Arg-4-nitroanilide
-
in 0.3M Tris-HCl, 0.3 M imidazole, and 0.5 M NaCl, pH 8.4, at 37°C
0.0341
pro-urokinase-type plasminogen activator
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
Abz-KQSRKFVPY(3-NO2)
-
peptide sequence from trask
0.5
Abz-RAARVVGGY(3-NO2)
-
-
66
Abz-RKRRGSRGY(3-NO2)
-
peptide sequence from filaggrin
0.6
Abz-RLARVVGGY(3-NO2)
-
-
0.5
Abz-RQARAVGGY(3-NO2)
-
-
1.4
Abz-RQARVVGGY(3-NO2)
-
; peptide sequence from matriptase
0.5
Abz-RQARYVGGY(3-NO2)
-
-
1.5
Abz-RQLRVVGGY(3-NO2)
-
-
39
Abz-RQRRALEKY(3-NO2)
-
peptide sequence from alphaEbeta7 integrin
1.4
Abz-RQRRVVGGY(3-NO2)
-
-
1.1
Abz-RQYRVVGGY(3-NO2)
-
-
0.5
Abz-RRARVVGGY(3-NO2)
-
-
15
Abz-SKGRSLIGY(3-NO2)
-
peptide sequence from PAR-2
16
Abz-SKLRVVGGY(3-NO2)
-
peptide sequence from proMSP-1
0.00145
pro-urokinase-type plasminogen activator
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
hepatocyte growth factor activator inhibitor-1B, hepatocyte growth factor activator inhibitor-2
-
completely inhibits
-
0.00026
HAI-2
-
-
-
0.0416
HI-10331
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
-
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
strongest transformation on anchorage-independent cell growth; transient transfection of hepsin increases the progress of apoptosis/supresses proliferation. Inhibition of cell growth in monolayer culture. Increased accumulation of p53-dependent apoptosis and caspases-3, -6, and -7 in stabley transfected BG-1 cells
Manually annotated by BRENDA team
-
non-transmembrane isoform highly expressed, whereas transmembrane hepsin is expressed at a relatively lower level
Manually annotated by BRENDA team
-
upregulation of hepsin mRNA in estrogen receptor alpha-positive breast tumors compared with estrogen receptor alpha-negative breast tumors
Manually annotated by BRENDA team
-
non-transmembrane isoform expressed at highest level among investigated cell lines, transmembrane isoform hardly detectable
Manually annotated by BRENDA team
-
hepsin expression is significantly higher in endometrial cancer compared to normal endometrium and endometrial hyperplasia. High levels of hepsin expression are associated with advanced stage, high grade, depth of myometrial invasion, cervical involvement, lymph node metastasis, lymph vascular space involvement, ovarian metastasis, and peritoneal cytology of endometrial cancer
Manually annotated by BRENDA team
-
transmembrane isoform only
Manually annotated by BRENDA team
-
two isoforms expressed with different molecular weight
Manually annotated by BRENDA team
-
non-transmembrane and transmembrane isoform highly expressed
Manually annotated by BRENDA team
-
non-transmembrane and transmembrane isoform
Manually annotated by BRENDA team
-
lower levels
Manually annotated by BRENDA team
-
lower levels
Manually annotated by BRENDA team
-
upregulation of hepsin
Manually annotated by BRENDA team
-
used as positive control
Manually annotated by BRENDA team
-
hepsin mRNA levels in early stage cancer are similar to that in normal controls but mRNA levels decrease in more advanced cancers. Patients with lower hepsin mRNA levels have poorer survival rate. In contrast, another study reports lower hepsin mRNA expression in early stage cancers, in some cases of advanced cancer overexpression of hepsin mRNA and patients with high hepsin mRNA levels with poorer survival rates
Manually annotated by BRENDA team
-
transmembrane isoform only
Manually annotated by BRENDA team
-
transmembrane isoform only
Manually annotated by BRENDA team
-
non-transmembrane and transmembrane isoform highly expressed
Manually annotated by BRENDA team
-
transmembrane isoform only
Manually annotated by BRENDA team
-
lower levels
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
hepsin inhibits the internal ribosome entry site activity and expression of CDK11p58,which is associated with cell cycle progression and pro-apoptotic signaling in prostate cancer. Hepsin suppresses CDK11p58 internal ribosome entry site activity in prostate cancer by modulating transacting factor unr expression and eIF-2alpha phosphorylation. Hepsin inhibits the expression of unr by directly binding to unr internal ribosome entry site element and suppressing its activity, and also represses eIF-2alpha phosphorylation through down-regulating the expression and phosphorylation of general control nonderepressible-2
physiological function
-
the macrophage-stimulating protein/RON signaling pathway is regulated by hepsin in tissue homeostasis and in disease pathologies, such as in cancer and immune disorders
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
HEPS_HUMAN
417
1
45011
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
x * 51000 + x * 28000
30000
-
SDS-PAGE, autocatalytically processed form consisting of amino acids 163-417
35000
-
amino sequence analysis in both non-reduction and reduction conditions of non-transmembrane isoform
42038
-
x * 42038, calculated from amino acid sequence
43000
-
x * 43000, SDS-PAGE
44000
-
SDS-PAGE, enzyme after cell-free translation assay
45000
51000
75000
-
Western blot analysis, SDS-PAGE, non-transmembrane isoform expressed in HEK-293T cells
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
larger size of enzyme in cell extracts as compared to cell-free translation assay may be due to glycosylation, possible site for N-linked carbohydrate chain attachment is at amino acid 112
proteolytic modification
-
gene contains a cleavage site for protease activation
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hepsin in complex with antibody hH35, hanging drop vapor diffusion method, using 18% (w/v) PEG 3350, 0.15 M Mg2SO4 and 0.01 M BaCl2
-
by sitting-drop method
-
extracellular portion of hepsin, starting at residue 46 and continuing to the end of the coding region, hanging drop vapor diffusion method
-
has scavenger receptor-like cysteine-rich domain and a large loop between residues 241 and 256, which may represent a major determinant for its substrate recognition
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H203A/D257A/S353A
-
overexpression of catalytically inactive mutant hepsin abrogates its ability to induce tumor growth in a mouse model
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
anti EE-antibody-protein G Sepharose column chromatography
-
by Ni-affinity chromatography
-
by gel filtration
-
by nickel-nitrilotriacetic acid affinity chromatography, ion-exchange chromatography or affinity chromatography
-
gel filtration
-
Ni-IDA.Sepharose column chromatography and Q-Sepharose column chromatography
-
using HisTrap FF columns
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cDNA of full lenth hepsin inserted into vector pRK5E, His-tagged hepsin cDNA inserted into vector pCMV.PD5, expression in a chinese hamster ovary expression system
-
cloned into vector pCMV-HA and vector pCMV-flag
expressed in FS-293 and HEK-293 cells
-
expression in LNCaP and PC-3 cells
-
expressed in Escherichia coli strains BL21(DE3), BL21(DE3) Codon Plus RIL, and Rosetta pLysS
-
expressed in LNCaP cells
-
expressed in Pichia pastoris
-
expressed in stably transfected CHO cells
-
fragment containing amino acids 45-417 is expressed as a C-terminal His-tagged fusion protein in Drosophila S2 cells
-
full-length hepsin cDNA construct transiently transfected in BG-1 cell lines. Hepsin stable transfectant BG-1 cells injected in nude mice
-
fusion protein with maltose-binding protein
-
inserted in a baculovirus expression vector under the control of a polyhedrin promoter and expressed in T.in.Pro cells. cDNA of full-length hepsin inserted into a mammalian expression vector overexpressed in LNCaP cells
-
prostate cancer cell lines stably transfected with a hepsin expressing plasmid. Stable transfection of hepsin cDNA in ovarian cancer cell lines. Overexpression in transgenic mice
-
transmembrane isoform and non-transmembrane isoform cloned into vector pcDNA3/Myc-His-(-C), both isoforms expressed in BHK-21 cells, non-transmembrane isoform expressed in bacteria strain DE3, overexpression of myc-tagged non-transmembrane hepsin in HEK-293 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
biotechnology
-
the aim of this study is to establish a cell line that directly secrets rFVIIa into cell culture medium: Factor VII and hepsin cDNAs are isolated from HepG2 cell line and cloned into pcDNA3-1 vector. The constructs are co-trasfected to CHO cell line. A cell line that permanently expresses recombinant factor VII (rFVII) and hepsin is established. FVIIa protein is secreted to medium of CHO cells co-transfected with pcNDA3-1-FVII and pcNDA3-1-hepsin. A three- to fourfold decrease in clotting time is observed when human FVII-depleted plasma is used in combination with human thromboplastin in the presence of rFVII, confirming the biological activity of rFVII. A cell line is established expressing FVIIa using genetic engineering methods
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leytus, S.P.; Loeb, K.R.; Hagen, F.S.; Kurachi, K.; Davie, E.W.
A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells
Biochemistry
27
1067-1074
1988
Homo sapiens
Manually annotated by BRENDA team
Tsuji, A.; Torres-Rosado, A.; Arai, T.; Chou, S.H.; Kurachi, K.
Characterization of hepsin, a membrane bound protease
Biomed. Biochim. Acta
50
791-793
1991
Homo sapiens, Papio ursinus
Manually annotated by BRENDA team
Srikantan, V.; Valladares, M.; Rhim, J.S.; Moul, J.W.; Srivastava, S.
Hepsin inhibits cell growth/invasion in prostate cancer cells
Cancer Res.
62
6812-6816
2002
Homo sapiens
Manually annotated by BRENDA team
Tsuji, A.; Torres-Rosado, A.; Arai, T.; Le Beau, M.M.; Lemons, R.S.; Chou, S.H.; Kurachi, K.
Hepsin, a cell membrane-associated protease. Characterization, tissue distribution, and gene localization
J. Biol. Chem.
266
16948-16953
1991
Homo sapiens, Papio ursinus
Manually annotated by BRENDA team
Kazama, Y.; Hamamoto, T.; Foster, D.C.; Kisiel, W.
Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation
J. Biol. Chem.
270
66-72
1995
Homo sapiens
Manually annotated by BRENDA team
Kurachi, K.; Torres-Rosado, A.; Tsuji, A.
Hepsin
Methods Enzymol.
244
100-114
1994
Cricetulus griseus, Homo sapiens, Papio ursinus
Manually annotated by BRENDA team
Torres-Rosado, A.; O'Shea, K.S.; Tsuji, A.; Chou, S.H.; Kurachi, K.
Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth
Proc. Natl. Acad. Sci. USA
90
7181-7185
1993
Homo sapiens
Manually annotated by BRENDA team
Somoza, J.R.; Ho, J.D.; Luong, C.; Ghate, M.; Sprengeler, P.A.; Mortara, K.; Shrader, W.D.; Sperandio, D.; Chan, H.; McGrath, M.E.; Katz, B.A.
The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain
Structure
11
1123-1131
2003
Homo sapiens
Manually annotated by BRENDA team
Zhang, J.L.; Zhao, W.G.; Wu, K.L.; Wang, K.; Zhang, X.; Gu, C.F.; Li, Y.; Zhu, Y.; Wu, J.G.
Human hepatitis B virus X protein promotes cell proliferation and inhibits cell apoptosis through interacting with a serine protease hepsin
Arch. Virol.
150
721-741
2005
Homo sapiens, Homo sapiens (P05981)
Manually annotated by BRENDA team
Herter, S.; Piper, D.E.; Aaron, W.; Gabriele, T.; Cutler, G.; Cao, P.; Bhatt, A.S.; Choe, Y.; Craik, C.S.; Walker, N.; Meininger, D.; Hoey, T.; Austin, R.J.
Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers
Biochem. J.
390
125-136
2005
Homo sapiens
Manually annotated by BRENDA team
Li, Y.; Yu, Z.; Zhao, X.; Shen, S.
Identification and characterization of hepsin/-TM, a non-transmembrane hepsin isoform
Biochim. Biophys. Acta
1681
157-165
2005
Homo sapiens
Manually annotated by BRENDA team
Kirchhofer, D.; Peek, M.; Lipari, M.T.; Billeci, K.; Fan, B.; Moran, P.
Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2
FEBS Lett.
579
1945-1950
2005
Homo sapiens (P05981)
Manually annotated by BRENDA team
Nakamura, K.; Nasu, Y.; Hongo, A.; Matsuo, T.; Kodama, J.; Ebara, S.; Nagai, A.; Abrzua, F.; Kumon, H.; Hiramatsu, Y.
Hepsin shows inhibitory effects through apoptotic pathway on ovarian cancer cell lines
Int. J. Oncol.
28
393-398
2006
Homo sapiens
Manually annotated by BRENDA team
Roemer, A.; Schwettmann, L.; Jung, M.; Stephan, C.; Roigas, J.; Kristiansen, G.; Loening, S.A.; Lichtinghagen, R.; Jung, K.
The membrane proteases adams and hepsin are differentially expressed in renal cell carcinoma. Are they potential tumor markers?
J. Urol.
172
2162-2166
2004
Homo sapiens, Homo sapiens (P05981)
Manually annotated by BRENDA team
Matsuo, T.; Nakamura, K.; Takamoto, N.; Kodama, J.; Hongo, A.; Abrzua, F.; Nasu, Y.; Kumon, H.; Hiramatsu, Y.
Expression of the serine protease hepsin and clinical outcome of human endometrial cancer
Anticancer Res.
28
159-164
2008
Homo sapiens
Manually annotated by BRENDA team
Wu, Q.; Parry, G.
Hepsin and prostate cancer
Front. Biosci.
12
5052-5059
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Pal, P.; Xi, H.; Kaushal, R.; Sun, G.; Jin, C.H.; Jin, L.; Suarez, B.K.; Catalona, W.J.; Deka, R.
Variants in the HEPSIN gene are associated with prostate cancer in men of European origin
Hum. Genet.
120
187-192
2006
Homo sapiens
Manually annotated by BRENDA team
Moran, P.; Li, W.; Fan, B.; Vij, R.; Eigenbrot, C.; Kirchhofer, D.
Pro-urokinase-type plasminogen activator is a substrate for hepsin
J. Biol. Chem.
281
30439-30446
2006
Homo sapiens
Manually annotated by BRENDA team
Beliveau, F.; Desilets, A.; Leduc, R.
Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
FEBS J.
276
2213-2226
2009
Homo sapiens
Manually annotated by BRENDA team
Miao, J.; Mu, D.; Ergel, B.; Singavarapu, R.; Duan, Z.; Powers, S.; Oliva, E.; Orsulic, S.
Hepsin colocalizes with desmosomes and induces progression of ovarian cancer in a mouse model
Int. J. Cancer
123
2041-2047
2008
Homo sapiens (P05981)
Manually annotated by BRENDA team
Nakamura, K.; Takamoto, N.; Abarzua, F.; Hongo, A.; Kodama, J.; Nasu, Y.; Kumon, H.; Hiramatsu, Y.
Hepsin inhibits the cell growth of endometrial cancer
Int. J. Mol. Med.
22
389-397
2008
Homo sapiens
Manually annotated by BRENDA team
Tripathi, M.; Nandana, S.; Yamashita, H.; Ganesan, R.; Kirchhofer, D.; Quaranta, V.
Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression
J. Biol. Chem.
283
30576-30584
2008
Homo sapiens
Manually annotated by BRENDA team
Halabian, R.; Roudkenar, M.H.; Esmaeili, N.S.; Masroori, N.; Roushandeh, A.M.; Najafabadi, A.J.
Establishment of a cell line expressing recombinant factor VII and its subsequent conversion to active form FVIIa through hepsin by genetic engineering method
Vox Sang.
96
309-315
2009
Homo sapiens
Manually annotated by BRENDA team
Owen, K.A.; Qiu, D.; Alves, J.; Schumacher, A.M.; Kilpatrick, L.M.; Li, J.; Harris, J.L.; Ellis, V.
Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA
Biochem. J.
426
219-228
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, M.; Chen, L.M.; Lin, C.Y.; Chai, K.X.
Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor
Mol. Cell. Biochem.
337
259-266
2010
Homo sapiens
Manually annotated by BRENDA team
Holt, S.K.; Kwon, E.M.; Lin, D.W.; Ostrander, E.A.; Stanford, J.L.
Association of hepsin gene variants with prostate cancer risk and prognosis
Prostate
70
1012-1019
2010
Homo sapiens
Manually annotated by BRENDA team
Koschubs, T.; Dengl, S.; Duerr, H.; Kaluza, K.; Georges, G.; Hartl, C.; Jennewein, S.; Lanzendoerfer, M.; Auer, J.; Stern, A.; Huang, K.S.; Packman, K.; Gubler, U.; Kostrewa, D.; Ries, S.; Hansen, S.; Kohnert, U.; Cramer, P.; Mundigl, O.
Allosteric antibody inhibition of human Hepsin protease
Biochem. J.
442
483-494
2012
Homo sapiens, Homo sapiens (P05981)
Manually annotated by BRENDA team
Raevskaya, A.A.; Kuznetsova, E.M.; Savvateeva, M.V.; Severin, S.E.
Isolation, purification, and study of properties of recombinant hepsin from Escherichia coli
Biochemistry
75
866-872
2010
Homo sapiens
Manually annotated by BRENDA team
Ganesan, R.; Kolumam, G.A.; Lin, S.J.; Xie, M.H.; Santell, L.; Wu, T.D.; Lazarus, R.A.; Chaudhuri, A.; Kirchhofer, D.
Proteolytic activation of pro-macrophage-stimulating protein by hepsin
Mol. Cancer Res.
9
1175-1186
2011
Homo sapiens
Manually annotated by BRENDA team
Zhang, C.; Zhang, M.; Wu, Q.; Peng, J.; Ruan, Y.; Gu, J.
Hepsin inhibits CDK11p58 IRES activity by suppressing unr expression and eIF-2alpha phosphorylation in prostate cancer
Cell. Signal.
27
789-797
2015
Homo sapiens (P05981)
Manually annotated by BRENDA team
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