RALBP1

RalA-binding protein 1

655 amino acids

Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.

76.063 kDa

MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSSESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAKAEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI

Ralbp1

RalA-binding protein 1

648 amino acids

Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin (By similarity).

75.043 kDa

MTECFLPPSSSPSEHRRAEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDVLHEPPDTVSDDDKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKVKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQMDAPSVKPIFGVPLVDAVERTMMYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVLFTHVQELFGTVVLKQVTRPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESESEDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAKSEQQPQEEEEPERRGGIGPPPCDGVLEVRVAKEQAKASPSKDRKETPI

Ralbp1

RalA-binding protein 1

647 amino acids

Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin (By similarity). Involved in the assembly and function of the mitotic apparatus.

75.252 kDa

MTECFLPPTSSPSEHRRAEHGSGLTRTPSSEEISPTKFPELYRTGEPSPPHDILHEPPDIVSDDEKDHGKKKGKFKKKEKRTEGYVAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKCKDFTAADVVKQWKEKKKKKKPTQEPEVPQTDAPSLRPIFGAPFADAVERTMMYDGIRLPAVFRECVDYMEKHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTEVEKVQEFQRLLRELPEYNHLLLSWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVLFTHVQELFGTVLLKQVTRPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDFSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEETNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQHGRSETEEYSSDSESESEDEEELQIILEDLQRQNEELEIKNNHLNQAVHEEREAIVELRVQLRLLQMLRAKSEQQLQEEEEPERRGGTGPLPCEGVLEVRAAKEQAKPSPSKDRKETPI