RBP1_HUMAN
ID RBP1_HUMAN Reviewed; 655 AA.
AC Q15311; D3DUI0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=RalA-binding protein 1 {ECO:0000250|UniProtKB:Q62796};
DE Short=RalBP1 {ECO:0000250|UniProtKB:Q62796};
DE AltName: Full=76 kDa Ral-interacting protein {ECO:0000303|PubMed:7673236};
DE AltName: Full=Dinitrophenyl S-glutathione ATPase {ECO:0000303|PubMed:10924126, ECO:0000303|PubMed:9548755};
DE Short=DNP-SG ATPase {ECO:0000303|PubMed:10924126, ECO:0000303|PubMed:9548755};
DE EC=7.6.2.2 {ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:9548755};
DE EC=7.6.2.3 {ECO:0000269|PubMed:10924126};
DE AltName: Full=Ral-interacting protein 1 {ECO:0000303|PubMed:7673236};
GN Name=RALBP1 {ECO:0000312|HGNC:HGNC:9841};
GN Synonyms=RLIP {ECO:0000303|PubMed:22319010},
GN RLIP1 {ECO:0000303|PubMed:7673236}, RLIP76 {ECO:0000303|PubMed:7673236};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDC42; RAC1; RALA
RP AND RALB, AND REGION.
RX PubMed=7673236; DOI=10.1074/jbc.270.38.22473;
RA Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S.,
RA Berger R., Tavitian A., Gacon G., Camonis J.H.;
RT "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac
RT GTPase-activating protein activity.";
RL J. Biol. Chem. 270:22473-22477(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-15; 409-438 AND 472-486,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Bone marrow;
RX PubMed=10924126; DOI=10.1021/bi992964c;
RA Awasthi S., Cheng J., Singhal S.S., Saini M.K., Pandya U., Pikula S.,
RA Bandorowicz-Pikula J., Singh S.V., Zimniak P., Awasthi Y.C.;
RT "Novel function of human RLIP76: ATP-dependent transport of glutathione
RT conjugates and doxorubicin.";
RL Biochemistry 39:9327-9334(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9548755; DOI=10.1021/bi972131r;
RA Awasthi S., Singhal S.S., Pikula S., Piper J.T., Srivastava S.K.,
RA Torman R.T., Bandorowicz-Pikula J., Lin J.T., Singh S.V., Zimniak P.,
RA Awasthi Y.C.;
RT "ATP-Dependent human erythrocyte glutathione-conjugate transporter. II.
RT Functional reconstitution of transport activity.";
RL Biochemistry 37:5239-5248(1998).
RN [6]
RP INTERACTION WITH REPS2.
RC TISSUE=Brain;
RX PubMed=9422736; DOI=10.1074/jbc.273.2.814;
RA Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.;
RT "Identification and characterization of a novel protein interacting with
RT Ral-binding protein 1, a putative effector protein of Ral.";
RL J. Biol. Chem. 273:814-821(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH AP2M1.
RX PubMed=10910768; DOI=10.1242/jcs.113.16.2837;
RA Jullien-Flores V., Mahe Y., Mirey G., Leprince C., Meunier-Bisceuil B.,
RA Sorkin A., Camonis J.H.;
RT "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex:
RT involvement of the Ral pathway in receptor endocytosis.";
RL J. Cell Sci. 113:2837-2844(2000).
RN [8]
RP FUNCTION, ATP-BINDING, MUTAGENESIS OF LYS-74 AND LYS-425, AND PROCESSING.
RX PubMed=11300797; DOI=10.1021/bi002182f;
RA Awasthi S., Cheng J.Z., Singhal S.S., Pandya U., Sharma R., Singh S.V.,
RA Zimniak P., Awasthi Y.C.;
RT "Functional reassembly of ATP-dependent xenobiotic transport by the N- and
RT C-terminal domains of RLIP76 and identification of ATP binding sequences.";
RL Biochemistry 40:4159-4168(2001).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11437348; DOI=10.1006/abbi.2001.2395;
RA Sharma R., Singhal S.S., Cheng J., Yang Y., Sharma A., Zimniak P.,
RA Awasthi S., Awasthi Y.C.;
RT "RLIP76 is the major ATP-dependent transporter of glutathione-conjugates
RT and doxorubicin in human erythrocytes.";
RL Arch. Biochem. Biophys. 391:171-179(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH MITOTIC KINASE CYCLIN B-CDK1; EPN1; NUMB AND
RP TFAP2A.
RX PubMed=12775724; DOI=10.1074/jbc.m302191200;
RA Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
RT "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
RT phosphorylate epsin during the switch off of endocytosis in mitosis.";
RL J. Biol. Chem. 278:30597-30604(2003).
RN [11]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND REGION.
RX PubMed=15610018; DOI=10.1021/bi0482811;
RA Yadav S., Singhal S.S., Singhal J., Wickramarachchi D., Knutson E.,
RA Albrecht T.B., Awasthi Y.C., Awasthi S.;
RT "Identification of membrane-anchoring domains of RLIP76 using deletion
RT mutant analyses.";
RL Biochemistry 43:16243-16253(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP FUNCTION, INTERACTION WITH DNM1L AND RALA, AND SUBCELLULAR LOCATION.
RX PubMed=21822277; DOI=10.1038/ncb2310;
RA Kashatus D.F., Lim K.H., Brady D.C., Pershing N.L., Cox A.D., Counter C.M.;
RT "RALA and RALBP1 regulate mitochondrial fission at mitosis.";
RL Nat. Cell Biol. 13:1108-1115(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=22319010; DOI=10.1096/fj.11-196451;
RA Fillatre J., Delacour D., Van Hove L., Bagarre T., Houssin N., Soulika M.,
RA Veitia R.A., Moreau J.;
RT "Dynamics of the subcellular localization of RalBP1/RLIP through the cell
RT cycle: the role of targeting signals and of protein-protein interactions.";
RL FASEB J. 26:2164-2174(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-30; SER-34; SER-62;
RP SER-92; SER-93; SER-461 AND SER-463, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44; SER-48; SER-62; SER-92;
RP SER-93; SER-463 AND SER-645, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25] {ECO:0007744|PDB:2KWH, ECO:0007744|PDB:2KWI}
RP STRUCTURE BY NMR OF 393-446 IN COMPLEX WITH RALB, INTERACTION WITH RALB,
RP AND REGION.
RX PubMed=20696399; DOI=10.1016/j.str.2010.05.013;
RA Fenwick R.B., Campbell L.J., Rajasekar K., Prasannan S., Nietlispach D.,
RA Camonis J., Owen D., Mott H.R.;
RT "The RalB-RLIP76 complex reveals a novel mode of ral-effector
RT interaction.";
RL Structure 18:985-995(2010).
RN [26] {ECO:0007744|PDB:2MBG}
RP STRUCTURE BY NMR OF 184-446.
RX PubMed=24207123; DOI=10.1016/j.str.2013.09.007;
RA Rajasekar K.V., Campbell L.J., Nietlispach D., Owen D., Mott H.R.;
RT "The structure of the RLIP76 RhoGAP-Ral binding domain dyad: fixed position
RT of the domains leads to dual engagement of small G proteins at the
RT membrane.";
RL Structure 21:2131-2142(2013).
CC -!- FUNCTION: Multifunctional protein that functions as a downstream
CC effector of RALA and RALB (PubMed:7673236). As a GTPase-activating
CC protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase
CC activity (PubMed:7673236). As part of the Ral signaling pathway, may
CC also regulate ligand-dependent EGF and insulin receptors-mediated
CC endocytosis (PubMed:10910768, PubMed:12775724). During mitosis, may act
CC as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the
CC mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase
CC of the cell cycle (PubMed:12775724). During mitosis, also controls
CC mitochondrial fission as an effector of RALA (PubMed:21822277).
CC Recruited to mitochondrion by RALA, acts as a scaffold to foster the
CC mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of
CC DNM1L (PubMed:21822277). {ECO:0000269|PubMed:10910768,
CC ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:21822277,
CC ECO:0000269|PubMed:7673236}.
CC -!- FUNCTION: Could also function as a primary ATP-dependent active
CC transporter for glutathione conjugates of electrophiles. May also
CC actively catalyze the efflux of a wide range of substrates including
CC xenobiotics like doxorubicin (DOX) contributing to cell multidrug
CC resistance. {ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11300797,
CC ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:9548755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000269|PubMed:10924126, ECO:0000269|PubMed:11437348,
CC ECO:0000269|PubMed:9548755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000305|PubMed:10924126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:10924126,
CC ECO:0000269|PubMed:11437348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:11437348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000305|PubMed:11437348};
CC -!- SUBUNIT: Interacts with the GTP-bound form of RALA (via effector
CC domain); during mitosis, recruits RALBP1 to the mitochondrion where it
CC promotes DNM1L phosphorylation and mitochondrial fission
CC (PubMed:7673236, PubMed:21822277). Interacts with DNM1L; mediates its
CC mitotic kinase cyclin B-CDK1-mediated phosphorylation during mitosis to
CC promote mitochondrial fission (PubMed:21822277). Interacts with the
CC mitotic kinase cyclin B-CDK1 during mitosis (PubMed:12775724,
CC PubMed:21822277). Interacts with the GTP-bound form of RALB (via
CC effector domain) (PubMed:7673236, PubMed:20696399). Interacts with
CC REPS1; the interaction is direct and does not affect RALA-binding nor
CC GTPase activator activity of RALBP1 (By similarity). Interacts with
CC REPS2; the interaction is direct and does not affect RALA-binding nor
CC GTPase activator activity of RALBP1 (PubMed:9422736). Interacts with
CC EPN1, NUMB and TFAP2A during interphase and mitosis (PubMed:12775724).
CC Interacts with AP2M1; as part of the AP2 complex (PubMed:10910768).
CC Interacts with CDC42 (Probable). Interacts with RAC1 (PubMed:7673236).
CC {ECO:0000250|UniProtKB:Q62172, ECO:0000269|PubMed:10910768,
CC ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:20696399,
CC ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:7673236,
CC ECO:0000269|PubMed:9422736, ECO:0000305|PubMed:7673236}.
CC -!- INTERACTION:
CC Q15311; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-749285, EBI-746752;
CC Q15311; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-749285, EBI-10187270;
CC Q15311; Q8TAB5: C1orf216; NbExp=6; IntAct=EBI-749285, EBI-747505;
CC Q15311; Q9Y3M2: CBY1; NbExp=4; IntAct=EBI-749285, EBI-947308;
CC Q15311; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-749285, EBI-10961312;
CC Q15311; Q16204: CCDC6; NbExp=7; IntAct=EBI-749285, EBI-1045350;
CC Q15311; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-749285, EBI-347573;
CC Q15311; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-749285, EBI-10175300;
CC Q15311; P78556: CCL20; NbExp=2; IntAct=EBI-749285, EBI-3913209;
CC Q15311; Q86XR8: CEP57; NbExp=4; IntAct=EBI-749285, EBI-308614;
CC Q15311; P28329-3: CHAT; NbExp=3; IntAct=EBI-749285, EBI-25837549;
CC Q15311; Q9NS37: CREBZF; NbExp=4; IntAct=EBI-749285, EBI-632965;
CC Q15311; Q12959: DLG1; NbExp=5; IntAct=EBI-749285, EBI-357481;
CC Q15311; P78352: DLG4; NbExp=2; IntAct=EBI-749285, EBI-80389;
CC Q15311; P22607: FGFR3; NbExp=3; IntAct=EBI-749285, EBI-348399;
CC Q15311; O95995: GAS8; NbExp=3; IntAct=EBI-749285, EBI-1052570;
CC Q15311; Q13227: GPS2; NbExp=11; IntAct=EBI-749285, EBI-713355;
CC Q15311; Q14687: GSE1; NbExp=4; IntAct=EBI-749285, EBI-372619;
CC Q15311; P06396: GSN; NbExp=3; IntAct=EBI-749285, EBI-351506;
CC Q15311; Q96ED9: HOOK2; NbExp=3; IntAct=EBI-749285, EBI-743290;
CC Q15311; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-749285, EBI-10961706;
CC Q15311; P01112: HRAS; NbExp=3; IntAct=EBI-749285, EBI-350145;
CC Q15311; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-749285, EBI-2556193;
CC Q15311; O95751: LDOC1; NbExp=3; IntAct=EBI-749285, EBI-740738;
CC Q15311; Q8NCY6: MSANTD4; NbExp=4; IntAct=EBI-749285, EBI-7850168;
CC Q15311; Q15154-3: PCM1; NbExp=3; IntAct=EBI-749285, EBI-11742977;
CC Q15311; O60437: PPL; NbExp=5; IntAct=EBI-749285, EBI-368321;
CC Q15311; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-749285, EBI-1105153;
CC Q15311; P11233: RALA; NbExp=6; IntAct=EBI-749285, EBI-1036803;
CC Q15311; Q96D71: REPS1; NbExp=4; IntAct=EBI-749285, EBI-1171195;
CC Q15311; Q86UD0: SAPCD2; NbExp=6; IntAct=EBI-749285, EBI-2561646;
CC Q15311; Q14160: SCRIB; NbExp=2; IntAct=EBI-749285, EBI-357345;
CC Q15311; Q969G3: SMARCE1; NbExp=6; IntAct=EBI-749285, EBI-455078;
CC Q15311; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-749285, EBI-6872807;
CC Q15311; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-749285, EBI-529518;
CC Q15311; Q05BL0: TBRG1; NbExp=3; IntAct=EBI-749285, EBI-10223693;
CC Q15311; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-749285, EBI-3923210;
CC Q15311; P0C1Z6-2: TFPT; NbExp=5; IntAct=EBI-749285, EBI-10178002;
CC Q15311; Q15025: TNIP1; NbExp=4; IntAct=EBI-749285, EBI-357849;
CC Q15311; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-749285, EBI-11952721;
CC Q15311; P43897: TSFM; NbExp=4; IntAct=EBI-749285, EBI-1049298;
CC Q15311; P40337-3: VHL; NbExp=3; IntAct=EBI-749285, EBI-301270;
CC Q15311; Q96C28: ZNF707; NbExp=6; IntAct=EBI-749285, EBI-748111;
CC Q15311; Q9H6F0; NbExp=3; IntAct=EBI-749285, EBI-10307481;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11437348};
CC Peripheral membrane protein {ECO:0000269|PubMed:10924126,
CC ECO:0000269|PubMed:11437348, ECO:0000269|PubMed:15610018}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:15610018, ECO:0000269|PubMed:22319010}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q62796}.
CC Nucleus {ECO:0000269|PubMed:22319010}. Mitochondrion
CC {ECO:0000269|PubMed:21822277}. Note=Cytosolic protein that transiently
CC associates with the mitotic spindle poles in early prophase, and
CC dissociates from them after completion of mitosis (By similarity).
CC Targeted to the plasma membrane through its interaction with RALB,
CC directed by FGF signaling. Docking on the membrane is required to
CC transduce the Ral signal (By similarity). Recruited by RALA to the
CC mitochondrion during mitosis where it regulates mitochondrial fission
CC (PubMed:21822277). Nuclear localization is cell cycle dependent while
CC membrane localization is seen in adherent cells (PubMed:22319010). The
CC region involved in membrane association could form transmembrane
CC domains and expose a part of the protein extracellularly (Probable).
CC {ECO:0000250|UniProtKB:Q62796, ECO:0000250|UniProtKB:Q9PT60,
CC ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:22319010,
CC ECO:0000305|PubMed:15610018}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously but at low levels. Shows a
CC strong expression in the erythrocytes. {ECO:0000269|PubMed:11437348}.
CC -!- DOMAIN: The Rho-GAP domain mediates the GTPase activator activity
CC toward CDC42. {ECO:0000250|UniProtKB:Q62796}.
CC -!- PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF.
CC {ECO:0000250|UniProtKB:Q62172}.
CC -!- PTM: May undergo proteolytic cleavage to give peptides which reassemble
CC to form a transporter complex. {ECO:0000305|PubMed:11300797}.
CC -!- MISCELLANEOUS: Originally designated as dinitrophenyl S-glutathione
CC (DNP-SG) ATPase due to its ability to stimulate ATP hydrolysis in the
CC presence of DNP-SG. {ECO:0000303|PubMed:10924126}.
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DR EMBL; L42542; AAB00103.1; -; mRNA.
DR EMBL; CH471113; EAX01601.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01602.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01604.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01605.1; -; Genomic_DNA.
DR EMBL; BC013126; AAH13126.1; -; mRNA.
DR CCDS; CCDS11845.1; -.
DR PIR; F59435; F59435.
DR RefSeq; NP_006779.1; NM_006788.3.
DR PDB; 2KWH; NMR; -; A=393-446.
DR PDB; 2KWI; NMR; -; B=393-446.
DR PDB; 2MBG; NMR; -; A=184-446.
DR PDB; 6ZQT; X-ray; 1.51 A; C/D=393-446.
DR PDB; 6ZRN; X-ray; 1.48 A; C/D=393-446.
DR PDBsum; 2KWH; -.
DR PDBsum; 2KWI; -.
DR PDBsum; 2MBG; -.
DR PDBsum; 6ZQT; -.
DR PDBsum; 6ZRN; -.
DR AlphaFoldDB; Q15311; -.
DR BMRB; Q15311; -.
DR SMR; Q15311; -.
DR BioGRID; 116131; 176.
DR CORUM; Q15311; -.
DR IntAct; Q15311; 134.
DR MINT; Q15311; -.
DR STRING; 9606.ENSP00000019317; -.
DR DrugBank; DB00564; Carbamazepine.
DR DrugBank; DB00997; Doxorubicin.
DR DrugBank; DB00398; Sorafenib.
DR DrugBank; DB00541; Vincristine.
DR TCDB; 9.A.1.1.1; the non abc multidrug exporter (n-mde) family.
DR iPTMnet; Q15311; -.
DR PhosphoSitePlus; Q15311; -.
DR BioMuta; RALBP1; -.
DR DMDM; 34098413; -.
DR CPTAC; CPTAC-1747; -.
DR CPTAC; CPTAC-1748; -.
DR EPD; Q15311; -.
DR jPOST; Q15311; -.
DR MassIVE; Q15311; -.
DR MaxQB; Q15311; -.
DR PaxDb; Q15311; -.
DR PeptideAtlas; Q15311; -.
DR PRIDE; Q15311; -.
DR ProteomicsDB; 60526; -.
DR Antibodypedia; 21929; 517 antibodies from 37 providers.
DR DNASU; 10928; -.
DR Ensembl; ENST00000019317.8; ENSP00000019317.4; ENSG00000017797.13.
DR Ensembl; ENST00000383432.8; ENSP00000372924.3; ENSG00000017797.13.
DR GeneID; 10928; -.
DR KEGG; hsa:10928; -.
DR MANE-Select; ENST00000383432.8; ENSP00000372924.3; NM_006788.4; NP_006779.1.
DR UCSC; uc002kob.4; human.
DR CTD; 10928; -.
DR DisGeNET; 10928; -.
DR GeneCards; RALBP1; -.
DR HGNC; HGNC:9841; RALBP1.
DR HPA; ENSG00000017797; Low tissue specificity.
DR MIM; 605801; gene.
DR neXtProt; NX_Q15311; -.
DR OpenTargets; ENSG00000017797; -.
DR PharmGKB; PA34199; -.
DR VEuPathDB; HostDB:ENSG00000017797; -.
DR eggNOG; KOG4370; Eukaryota.
DR GeneTree; ENSGT00940000154639; -.
DR HOGENOM; CLU_028068_1_0_1; -.
DR InParanoid; Q15311; -.
DR OMA; IYKVEPI; -.
DR OrthoDB; 514124at2759; -.
DR PhylomeDB; Q15311; -.
DR TreeFam; TF315411; -.
DR BRENDA; 7.6.2.3; 2681.
DR PathwayCommons; Q15311; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q15311; -.
DR SIGNOR; Q15311; -.
DR BioGRID-ORCS; 10928; 73 hits in 1070 CRISPR screens.
DR ChiTaRS; RALBP1; human.
DR EvolutionaryTrace; Q15311; -.
DR GeneWiki; RALBP1; -.
DR GenomeRNAi; 10928; -.
DR Pharos; Q15311; Tbio.
DR PRO; PR:Q15311; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q15311; protein.
DR Bgee; ENSG00000017797; Expressed in renal medulla and 214 other tissues.
DR ExpressionAtlas; Q15311; baseline and differential.
DR Genevisible; Q15311; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:1900753; P:doxorubicin transport; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IDA:UniProtKB.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:UniProtKB.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12783; PTHR12783; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; GTPase activation; Membrane;
KW Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10924126,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..655
FT /note="RalA-binding protein 1"
FT /id="PRO_0000056733"
FT DOMAIN 192..380
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..119
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9PT60"
FT REGION 154..219
FT /note="Mediates association with membranes and could form
FT transmembrane domains"
FT /evidence="ECO:0000269|PubMed:15610018"
FT REGION 403..499
FT /note="Mediates interaction with RALA and RALB"
FT /evidence="ECO:0000269|PubMed:20696399,
FT ECO:0000269|PubMed:7673236"
FT REGION 500..655
FT /note="Mediates interaction with REPS1 and REPS2"
FT /evidence="ECO:0000250|UniProtKB:Q62796"
FT REGION 525..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:11300797"
FT BINDING 418..425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:11300797"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 617
FT /note="A -> V (in dbSNP:rs35867116)"
FT /id="VAR_049147"
FT MUTAGEN 74
FT /note="K->M: Loss of ATP-binding and transport-associated
FT ATPase activity."
FT /evidence="ECO:0000305|PubMed:11300797"
FT MUTAGEN 425
FT /note="K->M: Loss of ATP-binding and transport-associated
FT ATPase activity."
FT /evidence="ECO:0000305|PubMed:11300797"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:2MBG"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2MBG"
FT TURN 228..232
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 312..334
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:2MBG"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:6ZRN"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:2MBG"
FT HELIX 423..443
FT /evidence="ECO:0007829|PDB:6ZRN"
SQ SEQUENCE 655 AA; 76063 MW; EC6F75329FD8D062 CRC64;
MTECFLPPTS SPSEHRRVEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDILHEPPDV
VSDDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKMKRSKGIH VFKKPSFSKK
KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ
IDVPNLKPIF GIPLADAVER TMMYDGIRLP AVFRECIDYV EKYGMKCEGI YRVSGIKSKV
DELKAAYDRE ESTNLEDYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTETEKV
QEFQRLLKEL PECNYLLISW LIVHMDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVF
FTHVQELFGN VVLKQVMKPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI
KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN
ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIERLRAE IAEIQSRQQH GRSETEEYSS
ESESESEDEE ELQIILEDLQ RQNEELEIKN NHLNQAIHEE REAIIELRVQ LRLLQMQRAK
AEQQAQEDEE PEWRGGAVQP PRDGVLEPKA AKEQPKAGKE PAKPSPSRDR KETSI
