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Information on EC 3.4.17.24 - tubulin-glutamate carboxypeptidase and Organism(s) Homo sapiens and UniProt Accession Q9UPW5

for references in articles please use BRENDA:EC3.4.17.24
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Homo sapiens
UNIPROT: Q9UPW5 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
This is a subfamily of enzymes that cleave C-terminal and/or side chain amino acids from tubulins. The dual-specificity enzymes can cleave both alpha- and gamma-linked L-glutamate from tubulins, removing the posttranslationally added polyglutamyl side chains from the C-terminal regions. In addition, the enzyme removes two glutamate residues from the C-terminus of beta-tubulin and detyrosinated alpha-tubulin (from which the C-terminal L-tyrosine has been removed by EC 3.4.17.17, tubulinyl-Tyr carboxypeptidase). The latter is cleaved to delta2-tubulin and further to delta3-tubulin.
Synonyms
deglutamylase, ccpp-1, agbl5, cytosolic carboxypeptidase 1, ccpp-6, cytosolic carboxypeptidase 6, cytosolic carboxypeptidase ccp1, cytosolic carboxypeptidase 5, cytosolic carboxypeptidase-like protein 5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytosolic carboxypeptidase 1
-
cytosolic carboxypeptidase-like protein 5
-
tubulinyl-Glu carboxypeptidase
-
-
-
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[40S ribosomal protein S9]-KNAKKGQGGAGAGDDEEED + H2O
[40S ribosomal protein S9]-KNAKKGQGGAGAGDD + Glu-Glu-Glu-Asp
show the reaction diagram
-
-
-
?
[40S ribosomal protein S9]-KNAKKGQGGAGAGDDEEED + H2O
[40S ribosomal protein S9]-KNAKKGQGGAGAGDDE + Glu-Glu-Asp
show the reaction diagram
-
-
-
?
[alpha-tubulin 1A/1B]-EDMAALEKDYEEVGVDSVEGEGEEEGEE + H2O
[alpha-tubulin 1A/1B]-EDMAALEKDYEEVGVDSVEGEGEEEG + Glu-Glu
show the reaction diagram
in the case of alpha-tubulin, it is considered that CCP1 uses as substrate the pool of detyrosinated tubulin naturally present in the cell
-
-
?
[alpha-tubulin 1C]-EDMAALEKDYEEVGADSADGEDEGEE + H2O
[alpha-tubulin 1C]-EDMAALEKDYEEVGADSADGEDEG + Glu-Glu
show the reaction diagram
in the case of alpha-tubulin, it is considered that CCP1 uses as substrate the pool of detyrosinated tubulin naturally present in the cell
-
-
?
[eukaryotic translation initiation factor 4H]-EEVVQKEQE + H2O
[eukaryotic translation initiation factor 4H]-EEVVQKEQ + Glu
show the reaction diagram
-
-
-
?
[high mobility group protein B1]-EEEEDEEDEEDEEEEEDEEDEDEEEDDDDE + H2O
[high mobility group protein B1] + EEEEDEEDEEDEEEEEDEEDEDEEEDDDDE
show the reaction diagram
-
-
-
?
[high mobility group protein B2]-EDEEEEEEEEDEDEEEEDEDEE + H2O
[high mobility group protein B2] + EDEEEEEEEEDEDEEEEDEDEE
show the reaction diagram
-
-
-
?
[high mobility group protein B3]-KKVEEEDEEEEEEEEEEEEEEDE + H2O
[high mobility group protein B3]-KKVEEED + EEEEEEEEEEEEEEDE
show the reaction diagram
-
-
-
?
[high mobility group protein B3]-KKVEEEDEEEEEEEEEEEEEEDE + H2O
[high mobility group protein B3]-KKVEEEDE + EEEEEEEEEEEEEDE
show the reaction diagram
-
-
-
?
[myosin light chain kinase 1/telokinc]-EEEEEE + H2O
[myosin light chain kinase 1/telokinc] + EEEEEE
show the reaction diagram
-
-
-
?
[stathmin]-KNKESKDPADETEAD + H2O
[stathmin]-KNKESKDPADETEA + Asp
show the reaction diagram
-
-
-
?
[TRAF-type zinc finger domain-containing protein]-TAKAKPSKQQGAGDAEEEEEE + H2O
[TRAF-type zinc finger domain-containing protein]-TAKAKPSKQQGAGDA + Glu-Glu-Glu-Glu-Glu-Glu
show the reaction diagram
-
-
-
?
detyrosinated alpha-tubulin + H2O
DELTA2-tubulin + L-glutamate
show the reaction diagram
-
porcine brain tubulin
i.e. tubulin lacking two C-terminal amino acids
-
?
monoglutamyl alpha-tubulin + H2O
alpha-tubulin + L-Glu
show the reaction diagram
-
-
-
r
monoglutamyl beta-tubulin + H2O
beta-tubulin + L-Glu
show the reaction diagram
-
-
-
r
polymerized microtubules + H2O
DELTA2-tubulin + ?
show the reaction diagram
-
-
i.e. tubulin lacking two C-terminal amino acids
-
?
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CCP1-mediated shortening of acidic protein tails might regulate protein-protein and protein-DNA interactions
physiological function
-
overexpression or knockdown (80–90%) of isoform CCP1 in human embryonic kidney 293T cells does not affect the levels of most intracellular peptides but alters the levels of alpha-tubulin lacking two C-terminal amino acids more than 5fold, suggesting that tubulin processing is the primary function of CCP1
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPC1_HUMAN
1226
0
138448
Swiss-Prot
other Location (Reliability: 4)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rogowski, K.; van Dijk, J.; Magiera, M.M.; Bosc, C.; Deloulme, J.C.; Bosson, A.; Peris, L.; Gold, N.D.; Lacroix, B.; Bosch Grau, M.; Bec, N.; Larroque, C.; Desagher, S.; Holzer, M.; Andrieux, A.; Moutin, M.J.; Janke, C.
A family of protein-deglutamylating enzymes associated with neurodegeneration
Cell
143
564-578
2010
Homo sapiens (Q8NDL9)
Manually annotated by BRENDA team
Berezniuk, I.; Vu, H.; Lyons, P.; Sironi, J.; Xiao, H.; Burd, B.; Setou, M.; Angeletti, R.; Ikegami, K.; Fricker, L.
Cytosolic carboxypeptidase 1 is involved in processing alpha- and beta-tubulin
J. Biol. Chem.
287
6503-6517
2012
Homo sapiens, Mus musculus (Q09M02), Mus musculus
Manually annotated by BRENDA team
Tanco, S.; Tort, O.; Demol, H.; Aviles, F.X.; Gevaert, K.; Van Damme, P.; Lorenzo, J.
C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini
Mol. Cell. Proteomics
14
177-190
2015
Homo sapiens (Q9UPW5)
Manually annotated by BRENDA team