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Information on EC 3.4.21.B43 - kallikrein 12 and Organism(s) Homo sapiens and UniProt Accession Q9UKR0
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3.4.21.B43 kallikrein 12Specify your search results
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
Synonyms
klk12, kallikrein 12, kallikrein-related peptidase 12, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kallikrein-related peptidase 12
-
S01.020
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
342900-25-8
-
9001-01-8
-
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
Boc-VPR-7-amido-4-methylcoumarin + H2O
Boc-VPR + 7-amino-4-methylcoumarin
-
-
-
?
CCN1 protein + H2O
?
i.e. (cyr61,ctgf, nov), the main cleavage site is localized in the hinge region between the first and second half of the recombinant protein at Lys88-Gly89, Lys208-Arg209, Arg218-Ile219, Lys291-Lys292, and Lys345-Asn346
-
-
?
high molecular weight kininogen + H2O
?
proteolysis pattern, overview. Release of bradykinin, a fragment containing the C-terminal end of kinins. The kininogenase activity of the enzyme is poor due to the resistance of hydrolysis of the K-R bond on the N-terminal side of the bradykinin sequence in the kininogen
-
-
?
platelet-derived growth factor B precursor + H2O
mature platelet-derived growth factor B + ?
D-Val-Leu-Lys-thiobenzyl ester + H2O
D-Val-Leu-Lys + thiobenzyl alcohol
-
100% activity
-
-
?
tert-butyloxycarbonyl-DPR-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-DPR + 7-amino-4-methylcoumarin
-
55% activity compared to D-Val-Leu-Lys-thiobenzyl ester
-
-
?
tert-butyloxycarbonyl-FSR-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-FSR + 7-amino-4-methylcoumarin
-
13% activity compared to D-Val-Leu-Lys-thiobenzyl ester
-
-
?
tert-butyloxycarbonyl-QAR-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-QAR + 7-amino-4-methylcoumarin
-
98% activity compared to D-Val-Leu-Lys-thiobenzyl ester
-
-
?
tert-butyloxycarbonyl-VPR-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-VPR + 7-amino-4-methylcoumarin
-
85% activity compared to D-Val-Leu-Lys-thiobenzyl ester
-
-
?
Fibronectin + H2O
?
the enzyme cleaves the human extracellular matrix proteins fibronectin and tenascin, both of which are involved in the regulation of endothelial cell adhesion and migration. KLK12-mediated fibronectin proteolysis antagonizes fibronectin polymerization and fibronectin fibril formation by endothelial cells, leading to an increase in cell migration
-
-
?
influenza hemagglutinin precursor + H2O
mature influenza hemagglutinin + ?
the enzyme shows a preference for the H1 and H2 subtypes, the amino acids neighboring the arginine cleavage site affect cleavage efficiency
-
-
?
influenza hemagglutinin precursor + H2O
mature influenza hemagglutinin + ?
the enzyme shows a preference for the H1 and H2 subtypes, essentially no cleavage of the H3 subtype, the amino acids neighboring the arginine cleavage site affect cleavage efficiency
-
-
?
platelet-derived growth factor B precursor + H2O
mature platelet-derived growth factor B + ?
membrane bound zymogen
soluble mature paracrine factor, soluble mature protein
-
?
platelet-derived growth factor B precursor + H2O
mature platelet-derived growth factor B + ?
-
membrane bound zymogen
soluble mature protein
-
?
polypeptide + H2O
peptides
involved in posttranslational processing of polypeptide precursors
-
?
tenascin + H2O
?
the enzyme cleaves the human extracellular matrix proteins fibronectin and tenascin, both of which are involved in the regulation of endothelial cell adhesion and migration
-
-
?
additional information
?
-
hormonal reglation of enzyme expression, overview
-
-
?
additional information
?
-
-
hormonal reglation of enzyme expression, overview
-
-
?
additional information
?
-
active KLK12 possesses trypsin-like activity, targeting peptide bonds featuring either arginine or lysine at their P1 position
-
-
?
additional information
?
-
Abz-GPFTDVRAAVY-(3-NO2-Tyr) is not efficiently hydrolyzed
-
-
?
additional information
?
-
-
Abz-GPFTDVRAAVY-(3-NO2-Tyr) is not efficiently hydrolyzed
-
-
?
additional information
?
-
-
no cleavage is observed for tert-butyloxycarbonyl-QGR-7-amido-4-methylcoumarin, benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin, L-Pro-Phe-Arg-7-amido-4-methylcoumarin, succinyl-AFK-7-amido-4-methylcoumarin, succinyl-AAPF-7-amido-4-methylcoumarin, succinyl-ALPF-7-amido-4-methylcoumarin, succinyl-LLVY-7-amido-4-methylcoumarin, L-Tyr-7-amido-4-methylcoumarin, and S2586
-
-
?
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
CCN1 protein + H2O
?
i.e. (cyr61,ctgf, nov), the main cleavage site is localized in the hinge region between the first and second half of the recombinant protein at Lys88-Gly89, Lys208-Arg209, Arg218-Ile219, Lys291-Lys292, and Lys345-Asn346
-
-
?
Fibronectin + H2O
?
the enzyme cleaves the human extracellular matrix proteins fibronectin and tenascin, both of which are involved in the regulation of endothelial cell adhesion and migration. KLK12-mediated fibronectin proteolysis antagonizes fibronectin polymerization and fibronectin fibril formation by endothelial cells, leading to an increase in cell migration
-
-
?
influenza hemagglutinin precursor + H2O
mature influenza hemagglutinin + ?
the enzyme shows a preference for the H1 and H2 subtypes, the amino acids neighboring the arginine cleavage site affect cleavage efficiency
-
-
?
platelet-derived growth factor B precursor + H2O
mature platelet-derived growth factor B + ?
membrane bound zymogen
soluble mature paracrine factor
-
?
polypeptide + H2O
peptides
involved in posttranslational processing of polypeptide precursors
-
?
tenascin + H2O
?
the enzyme cleaves the human extracellular matrix proteins fibronectin and tenascin, both of which are involved in the regulation of endothelial cell adhesion and migration
-
-
?
additional information
?
-
hormonal reglation of enzyme expression, overview
-
-
?
additional information
?
-
-
hormonal reglation of enzyme expression, overview
-
-
?
additional information
?
-
active KLK12 possesses trypsin-like activity, targeting peptide bonds featuring either arginine or lysine at their P1 position
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
compared to the absence of calcium, a 2fold, 2.5fold, and 3fold increase in activity could be obtained by adding Ca2+ concentration of 0.1, 1, and 10 mM, respectively, however, it is not increased further by higher concentrations of Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha1-antitrypsin
-
less than 50% inhibition at 5fold molecular inhibitor excess
-
antithrombin-III
-
less than 50% inhibition at 5fold molecular inhibitor excess
-
Zn2+
-
10 mM Zn2+ is sufficient to inhibit 50% of the KLK12 enzyme activity, more than 95% suppression can be achieved by 0.2 mM Zn2+
additional information
-
no inhibition is observed for soybean trypsin inhibitor at concentrations up to 500 nM, alpha1-antichymotrypsin, kallistatin, plasminogen activator inhibitor-1, and alpha2-macroglobulin
-
additional information
-
not inhibited by alpha1-antichymotrypsin, kallistatin, and plasminogen activator inhibitor-1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the activity of KLK12 can be tightly regulated by autodegradation, by interaction with zinc ions, and by covalent complex formation with alpha2-antiplasmin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0294
D-Val-Leu-Lys-thiobenzyl ester
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.35
tert-butyloxycarbonyl-DPR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.565
tert-butyloxycarbonyl-FSR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.0686
tert-butyloxycarbonyl-QAR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.2
tert-butyloxycarbonyl-VPR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
additional information
additional information
enzyme reaction kinetics, overview
-
additional information
additional information
-
enzyme reaction kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.42
D-Val-Leu-Lys-thiobenzyl ester
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.017
tert-butyloxycarbonyl-DPR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
32.65
tert-butyloxycarbonyl-DPR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.052 - 2.1
tert-butyloxycarbonyl-FSR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
10.06
tert-butyloxycarbonyl-FSR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
0.97
tert-butyloxycarbonyl-QAR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
17.26
tert-butyloxycarbonyl-QAR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
8.1
tert-butyloxycarbonyl-VPR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
25.81
tert-butyloxycarbonyl-VPR-7-amido-4-methylcoumarin
-
in 0.1 M Tris, 10 mM CaCl2, 0.15 M NaCl, pH 8.0, at 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
discriminative value of KLK12sv1/2 and KLK12sv3 splive varients between benign and malignant breast tumors
additional information
enzyme splice variant KLK12sv3 is more frequently expressed in tumors of lower grade, early patient TNM stage, and smaller tumor size, overview
additional information
no enzyme in heart, adrenal gland, spleen, placenta, skeletal muscle, testis, cerebellum, liver, spinal cord, kidney, and bone marrow
additional information
-
no enzyme in heart, adrenal gland, spleen, placenta, skeletal muscle, testis, cerebellum, liver, spinal cord, kidney, and bone marrow
additional information
not detected in brain, heart, kidney, liver, muscle, ovary, skin, spinal cord, spleen, and tonsil
additional information
determination of enzyme content in nasal wash sample: about 0.000012 mg/ml
additional information
-
determination of enzyme content in nasal wash sample: about 0.000012 mg/ml
additional information
KLK12 is a trypsin-like kallikrein-related peptidase that is abundant in a variety of human tissues
additional information
-
KLK12 is a trypsin-like kallikrein-related peptidase that is abundant in a variety of human tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
PDGF-B is probably one of the molecules linking the interaction between enzyme-induced endothelial cells and fibroblasts. Expression of both KLK12 and PDGFB genes is regulated by hypoxia in the lung tumor microenvironment
physiological function
additional information
physiological function
fragmentation of CCN1 or CCN5 by KLK12 prevents vascular endothelial growth factor165 binding, whereas it also triggers the release of intact vascular endothelial growth factor and bone morphogenetic protein 2 from the CCN protein complexes. The KLK12-mediated release of transforming growth factor-beta1 and fibroblast growth factor-2 is concentration-dependent. KLK12 may indirectly regulate the bioavailability and activity of several growth factors through processing of their CCN binding partners
physiological function
cleavage of the influenza hemagglutinin precursor by host proteases, e.g. kallikrein-related peptidase 12, is a critical step in the virus life cycle. Cleavage activation of influenza hemagglutinin enables fusion with the host endosome, allowing for release of the viral genome into the host cel
physiological function
expression profile of the splice variants KLK12sv3 and KLK12sv1/KLK12sv2 of kallikrein-related peptidase 12 in breast cancer patients and their clinical significance, overview. Positive KLK12sv3 expression is associated with longer patient disease-free survival and higher progesterone receptor concentration. KLK12sv1/KLK12sv2 expression is statistically associated with KLK12sv3 expression
physiological function
proangiogenic activity of the enzyme in lung endothelial cells. The enzyme may interfere with kininostatin-related antiangiogenic activity by cleaving the D5 domain
physiological function
the enzyme induces the formation of pulmonary endothelial cell tubule-like structures. The enzyme converts the extracellular matrix- or membrane-bound precursor of platelet-derived growth factor B (PDGF-B) into a soluble active form. Both PDGF-B and vascular endothelial growth factor A (VEGF-A) take part in the induction of angiogenesis by enzyme KLK12 in a coculture model of angiogenesis that mimics endothelial tubule formation. Release of mature PDGF-B by enzyme KLK12 leads to the fibroblast-mediated secretion of VEGF-A, which stimulates endothelial cell differentiation and the formation of capillary tube-like structures. PDGF-B signaling ultimately results in cell growth, migration, and protection against apoptosis, overview
physiological function
the enzyme stimulates endothelial cell migration by remodeling the fibronectin matrix
additional information
KLK12 is a trypsin-like kallikrein-related peptidase that is abundant in a variety of human tissues
additional information
-
KLK12 is a trypsin-like kallikrein-related peptidase that is abundant in a variety of human tissues
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
24500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
activation of the proform of the enzyme, pro-KLK12
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
when the pH is decreased to less than 5.0, KLK12 enzyme activity becomes undetectable, KLK12 activity is very sensitive to pH changes in the range 6.5-7.0 (within this range, a decrease of 0.5 pH units results in a more than 60% reduction in activity)
678534
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Brij-35
-
adding 10-20% glycerol and 0.05% Brij-35 to the KLK12 autoactivation mixture can slow down activation
Glycerol
-
adding 10-20% glycerol and 0.05% Brij-35 to the KLK12 autoactivation mixture can slow down activation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37°C, 12.5 mM MES, 75 mM NaCl, after 16 h, 24 h, 48 h, and 72 h only 50%, 35%, 20%, and 10% of the initial activity is detected
-
37°C, in the presence of 10-20% glycerol and 0.05% Brij-35, 72 h, 10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and reversed-phase high performance liquid chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene KLK12, formerly KLK5, DNA sequence determination and analysis, chromosome mapping to 19q13.3-13.4, splice variants identification, genomic organization
molecular cloning of four novel splice variants of the human KLK12 gene, discovered by combining 3' rapid amplification of cDNA ends (3' RACE), NGS technology, advanced bioinformatic analysis, and Sanger sequencing
the gene is located on chromosome 19q13.4, splice variants KLK12sv3 and KLK12sv1/KLK12sv2 in breast cancer cells by quantitative real-time PCR as well as semi-quantitative PCR expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Expression of both KLK12 and PDGFB genes is regulated by hypoxia in the lung tumor microenvironment
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
diagnostics
enzyme splice variant KLK12sv3 can be regarded as a marker of good prognosis in breast cancer
diagnostics
kallikrein 12 splice variants discriminate benign from cancerous breast tumors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (Q9UKR0)
Yousef, G.M.; Magklara, A.; Diamandis, E.P.
KLK12 is a novel serine protease and a new member of the human kallikrein gene family-differential expression in breast cancer
Genomics
69
331-341
2000
Homo sapiens (Q9UKR0), Homo sapiens
Shinmura, K.; Tao, H.; Yamada, H.; Kataoka, H.; Sanjar, R.; Wang, J.; Yoshimura, K.; Sugimura, H.
Splice-site genetic polymorphism of the human kallikrein 12 (KLK12) gene correlates with no substantial expression of KLK12 protein having serine protease activity
Hum. Mutat.
24
273-274
2004
Homo sapiens
Luo, L.; Jiang, W.
Inhibition profiles of human tissue kallikreins by serine protease inhibitors
Biol. Chem.
387
813-816
2006
Homo sapiens
Memari, N.; Jiang, W.; Diamandis, E.P.; Luo, L.Y.
Enzymatic properties of human kallikrein-related peptidase 12 (KLK12)
Biol. Chem.
388
427-435
2007
Homo sapiens
Shaw, J.L.; Diamandis, E.P.
Distribution of 15 human kallikreins in tissues and biological fluids
Clin. Chem.
53
1423-1432
2007
Homo sapiens (Q9UKR0)
Memari, N.; Diamandis, E.P.; Earle, T.; Campbell, A.; Van Dekken, H.; Van der Kwast, T.H.
Human kallikrein-related peptidase 12: antibody generation and immunohistochemical localization in prostatic tissues
Prostate
67
1465-1474
2007
Homo sapiens (Q9UKR0), Homo sapiens
Guillon-Munos, A.; Oikonomopoulou, K.; Michel, N.; Smith, C.R.; Petit-Courty, A.; Canepa, S.; Reverdiau, P.; Heuze-Vourch, N.; Diamandis, E.P.; Courty, Y.
Kallikrein-related peptidase 12 hydrolyzes matricellular proteins of the CCN family and modifies interactions of CCN1 and CCN5 with growth factors
J. Biol. Chem.
286
25505-25518
2011
Homo sapiens (Q9UKR0)
Kryza, T.; Lalmanach, G.; Lavergne, M.; Lecaille, F.; Reverdiau, P.; Courty, Y.; Heuze-Vourch, N.
Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor
Biol. Chem.
394
385-391
2013
Homo sapiens (Q9UKR0), Homo sapiens
Kryza, T.; Achard, C.; Parent, C.; Marchand-Adam, S.; Guillon-Munos, A.; Iochmann, S.; Korkmaz, B.; Respaud, R.; Courty, Y.; Heuze-Vourch, N.
Angiogenesis stimulated by human kallikrein-related peptidase 12 acting via a platelet-derived growth factor B-dependent paracrine pathway
FASEB J.
28
740-751
2014
Homo sapiens (Q9UKR0), Homo sapiens
Hamilton, B.S.; Whittaker, G.R.
Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12
J. Biol. Chem.
288
17399-17407
2013
Homo sapiens (Q9UKR0), Homo sapiens
Talieri, M.; Devetzi, M.; Scorilas, A.; Pappa, E.; Tsapralis, N.; Missitzis, I.; Ardavanis, A.
Human kallikrein-related peptidase 12 (KLK12) splice variants expression in breast cancer and their clinical impact
Tumour Biol.
33
1075-1084
2012
Homo sapiens (Q9UKR0), Homo sapiens
Adamopoulos, P.G.; Kontos, C.K.; Scorilas, A.
Novel splice variants of the human kallikrein-related peptidases 11 (KLK11) and 12 (KLK12), unraveled by next-generation sequencing technology
Biol. Chem.
399
1065-1071
2018
Homo sapiens (Q9UKR0), Homo sapiens
Papachristopoulou, G.; Tsapralis, N.; Michaelidou, K.; Ardavanis-Loukeris, G.; Griniatsos, I.; Scorilas, A.; Talieri, M.
Human kallikrein-related peptidase 12 (KLK12) splice variants discriminate benign from cancerous breast tumors
Clin. Biochem.
58
78-85
2018
Homo sapiens (Q9UKR0), Homo sapiens
Kryza, T.; Parent, C.; Pardessus, J.; Petit, A.; Burlaud-Gaillard, J.; Reverdiau, P.; Iochmann, S.; Labas, V.; Courty, Y.; Heuze-Vourch, N.
Human kallikrein-related peptidase 12 stimulates endothelial cell migration by remodeling the fibronectin matrix
Sci. Rep.
8
6331
2018
Homo sapiens (Q9UKR0), Homo sapiens
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