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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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UNIPROT: P08134
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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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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
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?
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
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
cell adhesion and migration are regulated through the concerted action of cytoskeletal dynamics and adhesion proteins, the activity of which is governed by RhoGTPases. Specific RhoGTPase signaling requires spatio-temporal activation and coordination of subsequent protein-protein and protein-lipid interactions. The nature, location and duration of these interactions are dependent on polarized extracellular triggers, such as cell-cell contact, and intracellular modifying events, such as phosphorylation. RhoA, RhoB, and RhoC are highly homologous GTPases that, however, succeed in generating specific intracellular responses
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RHOC_HUMAN
193
0
22006
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
the C-terminus of RhoGTPases comprises, next to the hypervariable region, the CAAX-box to which a lipid anchor is attached allowing GTPase binding to membranes. RhoA, RhoB and RhoC differ in this posttranslational lipid modification which has consequences for their subcellular localization. The lipid anchor regulates the interaction with RhoGDIs and with regions within the plasma membrane (RhoA, RhoC) or endosomal vesicles (RhoB). RhoA and RhoC are geranylgeranylated, whereas RhoB has both a palmitoyl anchor and a farnesyl or geranylgeranyl group
phosphoprotein
RhoC, but not RhoA, is phosphorylated on Ser73 in the alpha2-helix by the kinase Akt in SUM149 breast cancer cells54 although Ser73 is highly conserved among all 3 Rho-isoforms. Intriguingly, phosphorylation of RhoC is required for downstream signaling and invasiveness, which contrasts markedly with the inactivating phosphorylation at Ser188 in RhoA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schaefer, A.; Reinhard, N.R.; Hordijk, P.L.
Toward understanding RhoGTPase specificity: structure, function and local activation
Small GTPases
5
6
2014
Homo sapiens (P08134), Homo sapiens (P61586), Homo sapiens (P62745)
Manually annotated by BRENDA team