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Information on EC 3.4.14.10 - tripeptidyl-peptidase II and Organism(s) Homo sapiens and UniProt Accession P29144
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3.4.14.10 tripeptidyl-peptidase IISpecify your search results
Word Map
- 3.4.14.10
-
exopeptidase
- tppii
-
ceroid
- butabindide
-
subtilisin-like
-
oligopeptidase
-
collagen-related
- cholecystokinin-8
-
gly-pro-x
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tripeptidyl peptidase, tripeptidyl-peptidase ii, ptp-a, tripeptidylpeptidase ii, dtpp ii, tripeptidyl aminopeptidase i, tpp-ii, tpp-2, ty-21 tpp, tripeptidyl-peptidase-ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, tripeptidyl, II
-
-
-
-
cholecystokinin-inactivating peptidase
-
-
-
-
TPP II
tripeptidyl aminopeptidase
-
-
-
-
tripeptidyl aminopeptidase II
tripeptidyl peptidase
-
-
-
-
tripeptidyl peptidase II
TPP II
-
-
-
-
tripeptidyl aminopeptidase II
-
-
-
-
tripeptidyl peptidase II
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
101149-94-4
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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
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
-
-
?
KKE-5-[(2-aminoethyl) amino]-naphthalene-1-sulfonic acid-Q9K-4'-dimethylaminoazobenzene-4'-sulfonyl + H2O
?
-
-
-
?
Ala-Ala-Phe 2-naphthylamide + H2O
Ala-Ala-Phe + 2-naphthylamine
-
at 41% the rate of Ala-Ala-Phe 7-amido-4-methylcoumarin
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
best chromogenic tripeptyl substrate
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-Ala-(dehydro)Ala-Val-Ala + H2O
?
-
inhibitor, at 0.05% the rate of Arg-Arg-Ala-(phospho)Ser-Val-Ala hydrolysis
-
-
?
His-Leu-His 2-naphthylamide + H2O
His-Leu-His + 2-naphthylamine
-
at 12% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
-
at 6% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
Val-Gly-Ala-His-Ala-Gly-Glu-Tyr-Gly-Ala-Glu-Ala-Leu-Glu-Arg + H2O
Val-Gly-Ala + His-Ala-Gly + Glu-Tyr-Gly + Ala-Glu-Ala + Leu-Glu-Arg
-
peptide derived from human hemoglobin alpha-chain, residues 17-31, sequential release of tripeptides from free N-terminus, cleaved into 5 tripeptides by human enzyme, cleavage of Gly25-Ala bond occurs at a lower rate than Ala19-His and Gly22-Glu
-
?
Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Val-Leu-Arg + Arg-Ala-Ser-Val-Ala
-
-
the latter product is cleaved at a higher rate than the substrate
?
Val-Tyr-Ser 2-naphthylamide + H2O
Val-Tyr-Ser + 2-naphthylamine
-
at 3% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
additional information
?
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
no activity against Q20RRGRR and KKQ30KK
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide, aminoacyl or dipeptidyl methylcoumarylamides
-
-
?
additional information
?
-
-
no substrates are peptides with proline residues around cleavage sites
-
-
?
additional information
?
-
-
association/dissociation may be a way of regulating the enzyme activity in vivo
-
-
?
additional information
?
-
-
the enzyme is important for the degradation of some specific substrates, e.g. the neuropeptide cholecystokinin. It is likely that the main biological function of tripeptidyl-peptidase II is to participate in a general intracellular protein turnover. This peptidase may act on oligopeptides generated by the proteasome, or other endopeptidases, and the tripeptides formed would subsequently be good substrates for other exopeptidases. Tripeptidyl-peptidase II activity is increased in sepsis-induced muscle wasting, a situation of enhanced protein turnover
-
-
?
additional information
?
-
-
TPPII plays an important role in antigen processing, as most proteasomal products require further processing by TPPII for MHC class I presentation. As a consequence, peptide generation for MHCclass I is severely hampered when TPPII activitis inhibited
-
-
?
additional information
?
-
-
tripeptidyl peptidase II plays a role in cross-presentation of CTL epitopes restricted to diverse HLA alleles
-
-
?
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
additional information
?
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
-
association/dissociation may be a way of regulating the enzyme activity in vivo
-
-
?
additional information
?
-
-
the enzyme is important for the degradation of some specific substrates, e.g. the neuropeptide cholecystokinin. It is likely that the main biological function of tripeptidyl-peptidase II is to participate in a general intracellular protein turnover. This peptidase may act on oligopeptides generated by the proteasome, or other endopeptidases, and the tripeptides formed would subsequently be good substrates for other exopeptidases. Tripeptidyl-peptidase II activity is increased in sepsis-induced muscle wasting, a situation of enhanced protein turnover
-
-
?
additional information
?
-
-
TPPII plays an important role in antigen processing, as most proteasomal products require further processing by TPPII for MHC class I presentation. As a consequence, peptide generation for MHCclass I is severely hampered when TPPII activitis inhibited
-
-
?
additional information
?
-
-
tripeptidyl peptidase II plays a role in cross-presentation of CTL epitopes restricted to diverse HLA alleles
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphenyl [1-([1-[(2S)-2-aminobutanoyl]-2,3-dihydro-1H-indole-2-carbonyl]amino)-3-methylbutyl]phosphonate
irreversible variant of butabindide. almost 60fold more potent than butabindide
Arg-Arg-Ala-(dehydro)Ala-Val-Ala
-
less effective than Arg-Ala-(dehydro)Ala-Val-Ala
additional information
-
no inhibition by Val-Leu-Arg, isovaleryl-Val-Leu-Arg-Arg-Ala-Ser-Val-Ala, EDTA (with or without DTT)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the subunits form an active complexwith a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassiciation is accompanied by a reactivation. At 30°C more than 7fold activation after 2 h. Arg-Arg-Ala and Ser-Val-Ala at 0.01 mM enhance reactivation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
isoform TPP II has a bell-shaped pH dependence of kcat app/KM probably due to deprotonation of the N-terminal amino group of the substrate at higher pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
TPP2 inhibition indirectlybut rapidly decreases the levels of active, diphosphorylated extracellular signal-regulated kinase ERK1 and ERK2 in the nucleus, thereby down-regulating signal transduction downstream of growth factors and mitogenic stimuli. TPP2 inhibition of neurons in the hippocampus leads to an excessive strengthening of synapses
malfunction
suppression of TPP2 expression with shRNA significantly inhibits cellular proliferation compared with the control cells
physiological function
-
isoform TPPII physically interacts with the tumor suppressor MYBBP1A and the cell cycle regulator protein CDK2. HEK-293 cells overexpressing TPPII form highly enzymatically active oligomeric complexes, and the cytoplasmic interaction frequency of TPPII with MYBBP1A increases with the protein expression of TPPII in serum-free cell growth conditions. A specific reversible inhibitor of TPPII, butabindide, suppresses the cytoplasmic interactions of TPPII and MYBBP1A both in control HEK-293 and cells overexpressing murine TPPII. A gene expression study during anoikis shows that overexpression of TPP II decreases mRNA expression level of MYBBP1A at the cell detachment conditions
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). TPP2_HUMAN
1249
0
138350
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1000000
138000
138000
-
x * 138000, the subunits form an active complex with a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassociation is accompanied by a reactivation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 138000, the subunits form an active complex with a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassociation is accompanied by a reactivation
additional information
-
conformation of the native complex, transmission electron microscopy, the complex dissociates into MW 270000 dimers upon dialysis against Tris-HCl buffer
additional information
-
compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues and is active as an oligomeric complex. The insert is important for the formation of the active high-molecular mass complex
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cryoelectron microscopy and single-particle analysis show that the complex is built from two strands forming a quasihelical structure harboring a complex system of inner cavities. The dimensions of the TPP2 spindle are 55 x 28 nm and the strands are built of nine stacked dimers. The interior of each strand is permeated by a cavity system that features a suite of chambers at each dimer-dimer interface
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D44A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme
H264A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme
N362A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme, mutation effects the quarternary structure of the endogenously expressed TPP II, resulting in formation of an active, larger complex of more than 10000 Da
S449A
-
inactive mutant enzyme, mutation effects the quarternary structure of the endogenously expressed TPP II, resulting in formation of an active, larger complex of more than 10000 Da
additional information
-
the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 2 mM Tris-HCl dissociation buffer, 0.5 mM 2-mercaptoethanol, 3% w/v glycerol, pH 8, gradually decreases activity, 30% glycerol stabilizes
-
purified enzyme undergos a spontaneous dissociation upon storage, the dissociated enzyme has a specific activity which is 1/10th of that of the normal high MW complex
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography and Resource RPC hydrophobic column chromatography
using polyethyleneimine precipitation, (NH4)2SO4 precipitation, dialysis, anion-exchange chromatography, hydrophobic interaction chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
an 8 kb NcoI fragment covering the 5'-flanking region of the TPP2 gene, including the initiation codon, is cloned into a luciferase-containing reporter vector. HEK-293 cells and NIH3T3 cells are transiently transfected with the construct. Through sequential deletions and analysis of short PCR-fragments, the promoter can be localized to a 215 bp fragment upstream of the initiation codon
-
overexpression in 293-cells, enzyme i mainly in a nonassociated, inactive state
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
TPP2 mRNA and protein are significantly up-regulated in oral squamous cell carcinoma-derived cells compared with human normal oral keratinocytes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
TPP2 mRNA and protein are significantly up-regulated in oral squamous cell carcinoma-derived cells compared with human normal oral keratinocytes. Suppression of TPP2 expression with shRNA significantly inhibit cellular proliferation compared with the control cells. In addition, appropriate localization of cellular proliferation and spindle assembly checkpoint molecules MAD2 and upregulation of CCNB1 are observed in TPP2 knockdown oral squamous cell carcinoma cells. TPP2 expression in primary oral squamous cell carcinomas is significantly greater than that in the normal oral counterparts, and the TPP2-positive cases are significantly correlated with tumor size
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tomkinson, B.; Wernstedt, C.; Hellman, U.; Zetterquist, .
Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type
Proc. Natl. Acad. Sci. USA
84
7508-7512
1987
Homo sapiens
Balw, R.M.; Tomkinson, B.; Ragnarsson, U.; Zetterquist, .
Purification, substrate specificity, and classification of tripeptidyl peptidase II
J. Biol. Chem.
261
2409-2417
1986
Homo sapiens, Rattus norvegicus
Macpherson, E.; Tomkinson, B.; Balw, R.M.; Hglund, S.; Zetterquist, .
Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity
Biochem. J.
248
259-263
1987
Homo sapiens
Balw, R.M.; Eriksson, I.
Tripeptidyl peptidase II in haemolysates and liver homogenates of various species
Biochem. J.
241
75-80
1987
Bos taurus, Equus caballus, Gallus gallus, Homo sapiens, no activity in Escherichia coli, Oryctolagus cuniculus, Platyrrhini, Rattus norvegicus, Sus scrofa
Tomkinson, B.; Zetterquist, .
Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin
Biochem. J.
267
149-154
1990
Homo sapiens
Tomkinson, B.; Grehn, L.; Fransson, B.; Zetterquist, ?.
Use of a dehydroalanine-containing peptide as an efficient inhibitor of tripeptidyl peptidase II
Arch. Biochem. Biophys.
314
276-279
1994
Homo sapiens
Matrinsson, T.; Vujic, M.; Tomkinson, B.
Localization of the human tripeptidyl peptidase II gene (TPP2) to 13q32-q33 by nonradioactive in situ hybridization and somatic cell hybrids
Genomics
17
493-495
1993
Homo sapiens
Wilson, C.; Gibosn, A.M.; McDermott, J.R.
Purification and characterization of tripeptidylpeptidase-II from post-mortem human brain
Neurochem. Res.
18
743-749
1993
Homo sapiens
Tomkinson, B.
Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II
Biomed. Biochim. Acta
50
727-729
1991
Homo sapiens
Harris, J.; Tomkinson, B.
Electron microscopical and biochemical studies on the oligomeric states of human erythrocyte tripeptidyl peptidase-II
Micron Microsc. Acta
21
77-89
1990
Homo sapiens
-
Tomkinson, B.
Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity
Arch. Biochem. Biophys.
376
275-280
2000
Homo sapiens
Tomkinson, B.; Ni Laoi, B.; Wellington, K.
The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex
Eur. J. Biochem.
269
1438-1443
2002
Homo sapiens, Mus musculus
Hilbi, H.; Jozsa, E.; Tomkinson, B.
Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis
Biochim. Biophys. Acta
1601
149-154
2002
Homo sapiens
Radu, D.; Tomkinson, B.; Zachrisson, O.; Weber, G.; de Belleroche, J.; Hirsch, S.; Lindefors, N.
Overlapping regional distribution of CCK and TPPII mRNAs in Cynomolgus monkey brain and correlated levels in human cerebral cortex (BA 10)
Brain Res.
1104
175-182
2006
Homo sapiens (P29144), Macaca fascicularis, Rattus norvegicus
Lindas, A.C.; Tomkinson, B.
Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II
Gene
345
249-257
2005
Homo sapiens
Reits, E.; Neijssen, J.; Herberts, C.; Benckhuijsen, W.; Janssen, L.; Drijfhout, J.W.; Neefjes, J.
A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
Immunity
20
495-506
2004
Homo sapiens
Tomkinson, B.; Lindas, A.C.
Tripeptidyl-peptidase II: a multi-purpose peptidase
Int. J. Biochem. Cell Biol.
37
1933-1937
2005
Homo sapiens
Naujokat, C.; Fuchs, D.; Berges, C.
Adaptive modification and flexibility of the proteasome system in response to proteasome inhibition
Biochim. Biophys. Acta
1773
1389-1397
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Levengood, M.R.; van der Donk, W.A.
Use of lantibiotic synthetases for the preparation of bioactive constrained peptides
Bioorg. Med. Chem. Lett.
18
3025-3028
2008
Homo sapiens
Hong, X.; Lei, L.; Kuenert, B.; Naredla, R.; Applequist, S.E.; Grandien, A.; Glas, R.
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors
Cancer Res.
67
7165-7174
2007
Homo sapiens
Bhutani, N.; Venkatraman, P.; Goldberg, A.L.
Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
EMBO J.
26
1385-1396
2007
Homo sapiens (P29144)
Basler, M.; Groettrup, M.
No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes
Eur. J. Immunol.
37
896-904
2007
Homo sapiens
Endert, P.
Role of tripeptidyl peptidase II in MHC class I antigen processing - the end of controversies?
Eur. J. Immunol.
38
609-613
2008
Homo sapiens
Marcilla, M.; Villasevil, E.M.; de Castro, J.A.
Tripeptidyl peptidase II is dispensable for the generation of both proteasome-dependent and proteasome-independent ligands of HLA-B27 and other class I molecules
Eur. J. Immunol.
38
631-639
2008
Homo sapiens
Lindas, A.C.; Tomkinson, B.
Characterization of the promoter of the gene encoding human tripeptidyl-peptidase II and identification of upstream silencer elements
Gene
393
62-69
2007
Homo sapiens
Preuss, K.D.; Held, G.; Kubuschok, B.; Hung, C.Z.; Malatsidze, N.; Wagner, M.; Pfreundschuh, M.
Identification of antigenic targets of paraproteins by expression cloning does not support a causal role of chronic antigenic stimulation in the pathogenesis of multiple myeloma and MGUS
Int. J. Cancer
121
459-461
2007
Homo sapiens
Guil, S.; Rodriguez-Castro, M.; Aguilar, F.; Villasevil, E.M.; Anton, L.C.; Del Val, M.
Need for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimental
J. Biol. Chem.
281
39925-39934
2006
Homo sapiens
Anton, L.C.; Villasevil, E.M.
Is there an alternative to the proteasome in cytosolic protein degradation?
Biochem. Soc. Trans.
36
839-842
2008
Homo sapiens
Schnurr, M.; Orban, M.; Robson, N.C.; Shin, A.; Braley, H.; Airey, D.; Cebon, J.; Maraskovsky, E.; Endres, S.
ISCOMATRIX adjuvant induces efficient cross-presentation of tumor antigen by dendritic cells via rapid cytosolic antigen delivery and processing via tripeptidyl peptidase II
J. Immunol.
182
1253-1259
2009
Homo sapiens
Nahalkova, J.; Tomkinson, B.
TPPII, MYBBP1A and CDK2 form a protein-protein interaction network
Arch. Biochem. Biophys.
564
128-135
2014
Homo sapiens
Eklund, S.; Lindas, A.C.; Hamnevik, E.; Widersten, M.; Tomkinson, B.
Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics
Biochim. Biophys. Acta
1824
561-570
2012
Drosophila melanogaster, Drosophila melanogaster (Q9V6K1), Homo sapiens, Mus musculus, Mus musculus (Q64514)
Usukura, K.; Kasamatsu, A.; Okamoto, A.; Kouzu, Y.; Higo, M.; Koike, H.; Sakamoto, Y.; Ogawara, K.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Tripeptidyl peptidase II in human oral squamous cell carcinoma
J. Cancer Res. Clin. Oncol.
139
123-130
2013
Homo sapiens, Homo sapiens (P29144)
Schoenegge, A.M.; Villa, E.; Foerster, F.; Hegerl, R.; Peters, J.; Baumeister, W.; Rockel, B.
The structure of human tripeptidyl peptidase II as determined by a hybrid approach
Structure
20
593-603
2012
Homo sapiens (P29144), Homo sapiens
Wiemhoefer, A.; Stargardt, A.; van der Linden, W.A.; Renner, M.C.; van Kesteren, R.E.; Stap, J.; Raspe, M.A.; Tomkinson, B.; Kessels, H.W.; Ovaa, H.; Overkleeft, H.S.; Florea, B.; Reits, E.A.
Tripeptidyl peptidase II mediates levels of nuclear phosphorylated ERK1 and ERK2
Mol. Cell. Proteomics
14
2177-2193
2015
Homo sapiens (P29144)
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