RALA
entrez
5898
canonical
uniprot
P11233
canonical
ensembl
ENSG00000006451
resolver
ensp
ENSP00000005257
resolver
ensp
ENSP00000530234
resolver
ensp
ENSP00000530235
resolver
ensp
ENSP00000530236
resolver
ensp
ENSP00000530237
resolver
ensp
ENSP00000530238
resolver
ensp
ENSP00000530239
resolver
ensp
ENSP00000589617
resolver
ensp
ENSP00000589618
resolver
ensp
ENSP00000627878
resolver
ensp
ENSP00000627879
resolver
ensp
ENSP00000627880
resolver
ensp
ENSP00000627881
resolver
ensp
ENSP00000627882
resolver
ensp
ENSP00000760584
resolver
enst
ENST00000005257
resolver
enst
ENST00000860175
resolver
enst
ENST00000860176
resolver
enst
ENST00000860177
resolver
enst
ENST00000860178
resolver
enst
ENST00000860179
resolver
enst
ENST00000860180
resolver
enst
ENST00000919558
resolver
enst
ENST00000919559
resolver
enst
ENST00000957819
resolver
enst
ENST00000957820
resolver
enst
ENST00000957821
resolver
enst
ENST00000957822
resolver
enst
ENST00000957823
resolver
genesymbol
RALA
resolver
genesymbol_syn
RAL
resolver
hgnc
HGNC:9839
resolver
uniprot
A4D1W3
resolver
uniprot_entry
RALA_HUMAN
resolver
uniprot_sec
A4D1W3
resolver
activity_regulation
ACTIVITY REGULATION: Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).
uniprot
proteins
amino_acid_sequence
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL
uniprot
proteins
disease_involvement
DISEASE: Hiatt-Neu-Cooper neurodevelopmental syndrome (HINCONS) [MIM:619311]: An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, delayed walking or inability to walk, impaired intellectual development, poor or absent speech, axial hypotonia, and facial dysmorphism. Additional variable features may include seizures, autistic or behavioral abnormalities, and brain abnormalities. {ECO:0000269|PubMed:30500825, ECO:0000269|PubMed:30761613}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors (PubMed:18756269, PubMed:19306925, PubMed:20005108, PubMed:21822277, PubMed:30500825). Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling (PubMed:20005108). Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells (PubMed:19306925). During mitosis, supports the stabilization and elongation of the intracellular bridge between dividing cells. Cooperates with EXOC2 to recruit other components of the exocyst to the early midbody (PubMed:18756269). During mitosis, also controls mitochondrial fission by recruiting to the mitochondrion RALBP1, which mediates the phosphorylation and activation of DNM1L by the mitotic kinase cyclin B-CDK1 (PubMed:21822277). {ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:20005108, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:30500825}.
uniprot
proteins
mass_dalton
23567
uniprot
proteins
mutagenesis
MUTAGEN 1..11; /note="Missing: Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with L-72."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 23; /note="G->V: Impaired cytokinesis, as shown by increased number of binucleate cells. No effect on interaction with EXOC2 and EXOC8. No effect on cytokinesis; when associated with R-38 or W-48. Decreased interaction with EXOC2 and EXOC8; when associated with R-38 or W-48."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 38; /note="E->R: Impaired cytokinesis, as shown by increased number of binucleate cells. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 46; /note="T->A: Abolished monoglucosylation by P.sordellii toxin TcsL."; /evidence="ECO:0000269|PubMed:8858106"; MUTAGEN 47; /note="K->E: Strongly reduces interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 47; /note="K->I: No effect on interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 48; /note="A->W: Impaired cytokinesis, as shown by increased number of binucleate cells. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 48; /note="A->W: Strongly reduces interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 49; /note="D->E: No effect on cytokinesis; when associated with L-72."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 49; /note="D->N: No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with L-72."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 50; /note="S->W: Strongly reduces interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 52; /note="R->A: Strongly reduces interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 52; /note="R->W: No effect on interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 72; /note="Q->L: Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with N-49 or 1-M--S-11. No effect on cytokinesis; when associated with E-49."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 81; /note="N->A: No effect on interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 81; /note="N->R: Strongly reduces interaction with EXOC8."; /evidence="ECO:0000269|PubMed:15920473"; MUTAGEN 194; /note="S->A: Decreased localization to mitochondrion. Loss of function in mitochondrial fission."; /evidence="ECO:0000269|PubMed:21822277"; MUTAGEN 194; /note="S->D: Increased localization to mitochondrion."; /evidence="ECO:0000269|PubMed:21822277"; MUTAGEN 203; /note="C->S: Loss of geranylgeranylation and membrane localization."; /evidence="ECO:0000269|PubMed:17875936"; MUTAGEN 206; /note="L->S: Converts geranyl-geranylation to farnesylation. No effect on membrane localization. Fails to deflect GGTI-induced apoptosis of adherent cell cultures, but rescues anchorage-independent cell proliferation."; /evidence="ECO:0000269|PubMed:17875936
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation at Ser-194 by AURKA/Aurora kinase A, during mitosis, induces RALA localization to the mitochondrion where it regulates mitochondrial fission. {ECO:0000269|PubMed:21822277}.; PTM: Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant do not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs). {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:1903399}.; PTM: (Microbial infection) Glucosylated at Thr-46 by P.sordellii toxin TcsL from strain 6018 (PubMed:8858106). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form (PubMed:8858106). Not glucosylated by TcsL from strain VPI 9048 (PubMed:8858106). {ECO:0000269|PubMed:8858106}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10747847
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14525976
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15809419
uniprot
proteins
pubmed
15920473
uniprot
proteins
pubmed
16177825
uniprot
proteins
pubmed
16213214
uniprot
proteins
pubmed
17875936
uniprot
proteins
pubmed
18756269
uniprot
proteins
pubmed
1903399
uniprot
proteins
pubmed
19306925
uniprot
proteins
pubmed
20005108
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21822277
uniprot
proteins
pubmed
2550440
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2662142
uniprot
proteins
pubmed
30500825
uniprot
proteins
pubmed
30761613
uniprot
proteins
pubmed
7673236
uniprot
proteins
pubmed
8858106
uniprot
proteins
sequence_length
206
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925}; Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side. Cleavage furrow {ECO:0000269|PubMed:18756269}. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Mitochondrion {ECO:0000269|PubMed:21822277}. Note=Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles (PubMed:19306925). May colocalize with CNTRL/centriolin at the midbody ring (PubMed:16213214). However, localization at the midbody at late cytokinesis was not confirmed (PubMed:18756269). Relocalizes to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277). {ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:21822277}.
uniprot
proteins