RALBP1
entrez
10928
canonical
uniprot
Q15311
canonical
ensembl
ENSG00000017797
resolver
ensp
ENSP00000019317
resolver
ensp
ENSP00000372924
resolver
ensp
ENSP00000564032
resolver
ensp
ENSP00000592060
resolver
ensp
ENSP00000592061
resolver
ensp
ENSP00000592062
resolver
ensp
ENSP00000592068
resolver
ensp
ENSP00000592069
resolver
ensp
ENSP00000592070
resolver
ensp
ENSP00000592071
resolver
ensp
ENSP00000592072
resolver
ensp
ENSP00000613897
resolver
ensp
ENSP00000613898
resolver
ensp
ENSP00000613899
resolver
enst
ENST00000019317
resolver
enst
ENST00000383432
resolver
enst
ENST00000893973
resolver
enst
ENST00000922001
resolver
enst
ENST00000922002
resolver
enst
ENST00000922003
resolver
enst
ENST00000922009
resolver
enst
ENST00000922010
resolver
enst
ENST00000922011
resolver
enst
ENST00000922012
resolver
enst
ENST00000922013
resolver
enst
ENST00000943838
resolver
enst
ENST00000943839
resolver
enst
ENST00000943840
resolver
genesymbol
RALBP1
resolver
genesymbol_syn
RLIP
resolver
genesymbol_syn
RLIP1
resolver
genesymbol_syn
RLIP76
resolver
hgnc
HGNC:9841
resolver
uniprot
D3DUI0
resolver
uniprot_entry
RBP1_HUMAN
resolver
uniprot_sec
D3DUI0
resolver
amino_acid_sequence
MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSSESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAKAEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI
uniprot
proteins
ec_number
7.6.2.2
uniprot
proteins
ec_number
7.6.2.3
uniprot
proteins
function
FUNCTION: Multifunctional protein that functions as a downstream effector of RALA and RALB (PubMed:7673236). As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity (PubMed:7673236). As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis (PubMed:10910768, PubMed:12775724). During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle (PubMed:12775724). During mitosis, also controls mitochondrial fission as an effector of RALA (PubMed:21822277). Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (PubMed:21822277). {ECO:0000269|PubMed:10910768, ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:7673236}.; FUNCTION: Could also function as a primary ATP-dependent active transporter for glutathione conjugates of electrophiles. May also actively catalyze the efflux of a wide range of substrates including xenobiotics like doxorubicin (DOX) contributing to cell multidrug resistance. {ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11300797, ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:9548755}.
uniprot
proteins
mass_dalton
76063
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="K->M: Loss of ATP-binding and transport-associated ATPase activity."; /evidence="ECO:0000305|PubMed:11300797"; MUTAGEN 425; /note="K->M: Loss of ATP-binding and transport-associated ATPase activity."; /evidence="ECO:0000305|PubMed:11300797
uniprot
proteins
post_translational_modification
PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF. {ECO:0000250|UniProtKB:Q62172}.; PTM: May undergo proteolytic cleavage to give peptides which reassemble to form a transporter complex. {ECO:0000305|PubMed:11300797}.
uniprot
proteins
pubmed
10910768
uniprot
proteins
pubmed
10924126
uniprot
proteins
pubmed
11300797
uniprot
proteins
pubmed
11437348
uniprot
proteins
pubmed
12775724
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15610018
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20696399
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21822277
uniprot
proteins
pubmed
22319010
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24207123
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
7673236
uniprot
proteins
pubmed
9422736
uniprot
proteins
pubmed
9548755
uniprot
proteins
sequence_length
655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11437348}; Peripheral membrane protein {ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:15610018}. Cytoplasm, cytosol {ECO:0000269|PubMed:15610018, ECO:0000269|PubMed:22319010}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q62796}. Nucleus {ECO:0000269|PubMed:22319010}. Mitochondrion {ECO:0000269|PubMed:21822277}. Note=Cytosolic protein that transiently associates with the mitotic spindle poles in early prophase, and dissociates from them after completion of mitosis (By similarity). Targeted to the plasma membrane through its interaction with RALB, directed by FGF signaling. Docking on the membrane is required to transduce the Ral signal (By similarity). Recruited by RALA to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277). Nuclear localization is cell cycle dependent while membrane localization is seen in adherent cells (PubMed:22319010). The region involved in membrane association could form transmembrane domains and expose a part of the protein extracellularly (Probable). {ECO:0000250|UniProtKB:Q62796, ECO:0000250|UniProtKB:Q9PT60, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:22319010, ECO:0000305|PubMed:15610018}.
uniprot
proteins