RALB
entrez
5899
canonical
uniprot
P11234
canonical
ensembl
ENSG00000144118
resolver
ensp
ENSP00000272519
resolver
ensp
ENSP00000398162
resolver
ensp
ENSP00000414224
resolver
ensp
ENSP00000593699
resolver
ensp
ENSP00000641200
resolver
genesymbol
RALB
resolver
hgnc
HGNC:9840
resolver
uniprot
B4E040
resolver
uniprot
Q53T32
resolver
uniprot
Q6ZS74
resolver
uniprot_entry
RALB_HUMAN
resolver
uniprot_sec
B4E040
resolver
uniprot_sec
Q53T32
resolver
uniprot_sec
Q6ZS74
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
MAANKSKGQSSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDKIPLLVVGNKSDLEERRQVPVEEARSKAEEWGVQYVETSAKTRANVDKVFFDLMREIRTKKMSENKDKNGKKSSKNKKSFKERCCLL
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 (PubMed:10393179, PubMed:17875936, PubMed:18756269). Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis (PubMed:17875936). In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission (PubMed:18756269). Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors (PubMed:10393179). {ECO:0000250|UniProtKB:P36860, ECO:0000269|PubMed:10393179, ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}.
uniprot
proteins
mass_dalton
23409
uniprot
proteins
mutagenesis
MUTAGEN 1..11; /note="Missing: No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with V-23."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 23; /note="G->V: Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with 1-M--S-11 or N-49. No effect on cytokinesis; when associated with R-38, W-48 or E-49. No effect on interaction with EXOC2 and EXOC8. Decreased interaction with EXOC2 and EXOC8; when associated with R-38 or W-48."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 38; /note="E->R: No effect on cytokinesis. 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: Reduces the binding affinity to EXOC2 effector."; /evidence="ECO:0000269|PubMed:19166349"; MUTAGEN 46; /note="T->S: Reduces the binding affinity to EXOC2 effector."; /evidence="ECO:0000269|PubMed:19166349"; MUTAGEN 48; /note="A->W: Impaired abscission, the last step of cytokinesis, as shown by the accumulation of bridged 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 49; /note="D->E: Impaired abscission, the last step of cytokinesis. No effect on cytokinesis; when associated with V-23."; /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 V-23."; /evidence="ECO:0000269|PubMed:18756269"; MUTAGEN 72; /note="Q->L: Loss of GTPase activity."; /evidence="ECO:0000269|PubMed:19166349"; 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. Confers resistance to GGTI-induced pancreatic cancer cell apoptosis, but not to GGTI-dependent inhibition of anchorage-independent proliferation."; /evidence="ECO:0000269|PubMed:17875936
uniprot
proteins
post_translational_modification
PTM: Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs). {ECO:0000269|PubMed:17875936}.; PTM: The farnesylated form confers resistance to the proapoptotic and anti-anchorage-dependent growth effects of geranylgeranyltransferase I inhibitors, including GGTI-2417. {ECO:0000269|PubMed:17875936}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10393179
uniprot
proteins
pubmed
14525976
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17875936
uniprot
proteins
pubmed
18756269
uniprot
proteins
pubmed
19166349
uniprot
proteins
pubmed
20696399
uniprot
proteins
pubmed
2120779
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2662142
uniprot
proteins
pubmed
7673236
uniprot
proteins
sequence_length
206
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936}; Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side {ECO:0000269|PubMed:17875936}. Midbody {ECO:0000269|PubMed:18756269}. Note=During late cytokinesis, enriched at the midbody. {ECO:0000269|PubMed:18756269}.
uniprot
proteins