Ralb
entrez
64143
canonical
uniprot
Q9JIW9
canonical
ensembl
ENSMUSG00000004451
resolver
ensp
ENSMUSP00000004565
resolver
ensp
ENSMUSP00000190863
resolver
ensp
ENSMUSP00000190881
resolver
enst
ENSMUST00000004565
resolver
genesymbol
Ralb
resolver
uniprot
Q3TVS5
resolver
uniprot
Q8CCG5
resolver
uniprot_entry
Q8CCG5_MOUSE
resolver
uniprot_entry
RALB_MOUSE
resolver
uniprot_sec
Q3TVS5
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
MAANKGKSQGSLVLHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKSEEDKIPLLVVGNKSDLEERRQVPVDEARGKAEEWGVQYVETSAKTRANVDKVFFDLMREIRAKKMSENKDKNGRKSSKSKKSFKERCCLL
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 (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 (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:0000250|UniProtKB:P36860}.
uniprot
proteins
mass_dalton
23349
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
11025226
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
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