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Information on EC 3.6.5.2 - small monomeric GTPase

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EC Tree
IUBMB Comments
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
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This record set is specific for:
UNIPROT: P15153
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
k-ras, cdc42, h-ras, small gtpase, ef-tu, rho gtpase, rab11, rab3a, rab27a, rap1a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
RhoGTPase
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small GTPase
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GTP-phosphohydrolase
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GTPase
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guanine triphosphatase
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guanosine 5'-triphosphatase
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guanosine triphosphatase
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ribosomal GTPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (cell-regulating)
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
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
GTP + H2O
GDP + phosphate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
the activation state of Rac1 depends on the release of guanosine diphosphate and the binding of guanosine triphosphate. This cycling is regulated by the guanine nucleotide exchange factors, as activators, and by the GTPase activating proteins
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
the activation state of Rac1 depends on the release of guanosine diphosphate and the binding of guanosine triphosphate. This cycling is regulated by the guanine nucleotide exchange factors, as activators, and by the GTPase activating proteins
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
part of invadosomes, specialized plasma-membrane actin-based microdomains that combine adhesive properties with matrix degrading and/or mechanosensor activities
Manually annotated by BRENDA team
part of invadosomes, specialized plasma-membrane actin-based microdomains that combine adhesive properties with matrix degrading and/or mechanosensor activities
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the superfamily of small GTPase proteins
malfunction
Rac2 deficiency results in complete loss of podosomes in macrophages
metabolism
RhoGTPases are involved in podosome assembly and sequential mechanism for invadopodium formation, regulation, detailed overview
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RAC2_HUMAN
192
0
21429
Swiss-Prot
other Location (Reliability: 3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
the enzyme is a pharmacological target for the treatment of cardiovascular diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ferri, N.; Contini, A.; Bernini, S.K.; Corsini, A.
Role of small GTPase protein Rac1 in cardiovascular diseases: development of new selective pharmacological inhibitors
J. Cardiovasc. Pharmacol.
62
425-435
2013
Homo sapiens (P15153), Homo sapiens (P60763), Homo sapiens (P63000)
Manually annotated by BRENDA team
Spuul, P.; Ciufici, P.; Veillat, V.; Leclercq, A.; Daubon, T.; Kramer, I.; Genot, E.
Importance of RhoGTPases in formation, characteristics, and functions of invadosomes
Small GTPases
5
e28195
2014
Homo sapiens (P15153), Homo sapiens (P60953), Homo sapiens (P61586), Homo sapiens (P63000)
Manually annotated by BRENDA team