Ralb
entrez
116546
canonical
uniprot
P36860
canonical
ensembl
ENSRNOG00000002440
resolver
ensembl
ENSRNOG00055013141
resolver
ensembl
ENSRNOG00060005469
resolver
ensembl
ENSRNOG00065009578
resolver
ensp
ENSRNOP00000087562
resolver
ensp
ENSRNOP00055018279
resolver
ensp
ENSRNOP00060006858
resolver
ensp
ENSRNOP00065011543
resolver
enst
ENSRNOT00000096405
resolver
enst
ENSRNOT00055022511
resolver
enst
ENSRNOT00060009099
resolver
enst
ENSRNOT00065015348
resolver
genesymbol
Ralb
resolver
genesymbol_syn
Ral-b
resolver
uniprot_entry
RALB_RAT
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
MAANKGKSQGSLVLHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDKIPLLVVGNKSDLEERRQVPVEEARGKAEEWGVQYVETSAKTRANVDKVFFDLMREIRAKKMSENKDKNGRKSGKSKKSFKERCCLL
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. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles (PubMed:17202486). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (PubMed:16382162). Required for suppression of apoptosis (By similarity). In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission (By similarity). Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors (By similarity). {ECO:0000250|UniProtKB:P11234, ECO:0000269|PubMed:16382162, ECO:0000269|PubMed:17202486}.
uniprot
proteins
mass_dalton
23317
uniprot
proteins
post_translational_modification
PTM: Prenylation is essential for membrane localization. {ECO:0000250|UniProtKB:P11234}.; PTM: The farnesylated form confers resistance to the proapoptotic and anti-anchorage-dependent growth effects of some geranylgeranyltransferase I inhibitors. {ECO:0000250|UniProtKB:P11234}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16382162
uniprot
proteins
pubmed
17202486
uniprot
proteins
pubmed
7687439
uniprot
proteins
sequence_length
206
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11234}; Lipid-anchor {ECO:0000250|UniProtKB:P11234}; Cytoplasmic side {ECO:0000250|UniProtKB:P11234}. Midbody {ECO:0000250|UniProtKB:P11234}. Note=During late cytokinesis, enriched at the midbody. {ECO:0000250|UniProtKB:P11234}.
uniprot
proteins