Rac1
entrez
19353
canonical
uniprot
P63001
canonical
ensembl
ENSMUSG00000001847
resolver
ensp
ENSMUSP00000079380
resolver
ensp
ENSMUSP00000098058
resolver
enst
ENSMUST00000080537
resolver
enst
ENSMUST00000100489
resolver
genesymbol
Rac1
resolver
uniprot
F6WAS0
resolver
uniprot
K7Q7T7
resolver
uniprot
O95501
resolver
uniprot
P15154
resolver
uniprot
Q3TLP8
resolver
uniprot
Q9BTB4
resolver
uniprot_entry
F6WAS0_MOUSE
resolver
uniprot_entry
K7Q7T7_MOUSE
resolver
uniprot_entry
Q3TLP8_MOUSE
resolver
uniprot_entry
RAC1_MOUSE
resolver
uniprot_sec
O95501
resolver
uniprot_sec
P15154
resolver
uniprot_sec
Q9BTB4
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase. GTP hydrolysis is stimulated by ARHGAP30 and ARHGAP44. {ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129}.
uniprot
proteins
amino_acid_sequence
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states (PubMed:24352656). In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. In neurons, is involved in dendritic spine formation and synaptic plasticity (PubMed:24352656, PubMed:26969129). In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX (PubMed:12695502). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in PAK1 activation and eventually F-actin stabilization (By similarity). Required for DSG3 translocation to cell-cell junctions, DSG3-mediated organization of cortical F-actin bundles and anchoring of actin at cell junctions; via interaction with DSG3 (By similarity). Subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (By similarity). {ECO:0000250|UniProtKB:P63000, ECO:0000250|UniProtKB:Q6RUV5, ECO:0000269|PubMed:12695502, ECO:0000269|PubMed:19007770, ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129}.
uniprot
proteins
mass_dalton
21450
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="G->V: Constitutively active. Interacts with PARD6 proteins."; /evidence="ECO:0000269|PubMed:10934474
uniprot
proteins
post_translational_modification
PTM: GTP-bound active form is ubiquitinated at Lys-147 by HACE1, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P63000}.; PTM: Phosphorylated by AKT at Ser-71. {ECO:0000250|UniProtKB:P63000}.; PTM: Ubiquitinated at Lys-166 in a FBXL19-mediated manner; leading to proteasomal degradation. {ECO:0000250|UniProtKB:P63000}.
uniprot
proteins
protein_family
Rho family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10679324
uniprot
proteins
pubmed
10934474
uniprot
proteins
pubmed
10934475
uniprot
proteins
pubmed
12695502
uniprot
proteins
pubmed
14634666
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16002401
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17116687
uniprot
proteins
pubmed
17403031
uniprot
proteins
pubmed
19007770
uniprot
proteins
pubmed
19029984
uniprot
proteins
pubmed
1905006
uniprot
proteins
pubmed
19737524
uniprot
proteins
pubmed
20696765
uniprot
proteins
pubmed
20974804
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22959435
uniprot
proteins
pubmed
23963642
uniprot
proteins
pubmed
24352656
uniprot
proteins
pubmed
26969129
uniprot
proteins
pubmed
9707409
uniprot
proteins
sequence_length
192
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63000}; Lipid-anchor {ECO:0000250|UniProtKB:P63000}; Cytoplasmic side {ECO:0000250|UniProtKB:P63000}. Melanosome {ECO:0000250|UniProtKB:P63000}. Cytoplasm {ECO:0000269|PubMed:17116687}. Cell projection, lamellipodium {ECO:0000269|PubMed:22959435}. Cell projection, dendrite {ECO:0000269|PubMed:24352656}. Synapse {ECO:0000250|UniProtKB:Q6RUV5}. Nucleus {ECO:0000250|UniProtKB:P63000}. Note=Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine (By similarity). Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts (By similarity). Localizes to the lamellipodium in a SH3RF1-dependent manner. In macrophages, cytoplasmic location increases upon CSF1 stimulation (PubMed:17116687). Activation by GTP-binding promotes nuclear localization (By similarity). {ECO:0000250|UniProtKB:P63000, ECO:0000269|PubMed:17116687, ECO:0000269|PubMed:22959435}.
uniprot
proteins