RALB_HUMAN
ID RALB_HUMAN Reviewed; 206 AA.
AC P11234; B4E040; Q53T32; Q6ZS74;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Ras-related protein Ral-B;
DE EC=3.6.5.2 {ECO:0000305};
DE Flags: Precursor;
GN Name=RALB;
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] (ISOFORM 1).
RX PubMed=2662142; DOI=10.1093/nar/17.11.4380;
RA Chardin P., Tavitian A.;
RT "Coding sequences of human ralA and ralB cDNAs.";
RL Nucleic Acids Res. 17:4380-4380(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=2120779; DOI=10.1007/bf01232469;
RA Hsieh C.-L., Swaroop A., Francke U.;
RT "Chromosomal localization and cDNA sequence of human ralB, a GTP binding
RT protein.";
RL Somat. Cell Mol. Genet. 16:407-410(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Caudate nucleus, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [9]
RP INTERACTION WITH RALBP1.
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 [10]
RP FUNCTION.
RX PubMed=10393179; DOI=10.1093/emboj/18.13.3629;
RA Nakashima S., Morinaka K., Koyama S., Ikeda M., Kishida M., Okawa K.,
RA Iwamatsu A., Kishida S., Kikuchi A.;
RT "Small G protein Ral and its downstream molecules regulate endocytosis of
RT EGF and insulin receptors.";
RL EMBO J. 18:3629-3642(1999).
RN [11]
RP INTERACTION WITH EXOC8.
RX PubMed=14525976; DOI=10.1074/jbc.m308702200;
RA Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L.,
RA Camonis J., White M.A.;
RT "Ral GTPases regulate exocyst assembly through dual subunit interactions.";
RL J. Biol. Chem. 278:51743-51748(2003).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-203, AND MUTAGENESIS
RP OF CYS-203 AND LEU-206.
RX PubMed=17875936; DOI=10.1128/mcb.00057-07;
RA Falsetti S.C., Wang D.A., Peng H., Carrico D., Cox A.D., Der C.J.,
RA Hamilton A.D., Sebti S.M.;
RT "Geranylgeranyltransferase I inhibitors target RalB to inhibit anchorage-
RT dependent growth and induce apoptosis and RalA to inhibit anchorage-
RT independent growth.";
RL Mol. Cell. Biol. 27:8003-8014(2007).
RN [13]
RP FUNCTION, INTERACTION WITH EXOC2 AND EXOC8, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 1-MET--SER-11; GLY-23; GLU-38; ALA-48 AND ASP-49.
RX PubMed=18756269; DOI=10.1038/emboj.2008.166;
RA Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M.,
RA Camonis J.;
RT "Distinct roles of RalA and RalB in the progression of cytokinesis are
RT supported by distinct RalGEFs.";
RL EMBO J. 27:2375-2387(2008).
RN [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY NMR OF 12-185 IN COMPLEX WITH GTP ANALOG, INTERACTION WITH
RP EXOC2, AND MUTAGENESIS OF THR-46 AND GLN-72.
RX PubMed=19166349; DOI=10.1021/bi802129d;
RA Fenwick R.B., Prasannan S., Campbell L.J., Nietlispach D., Evetts K.A.,
RA Camonis J., Mott H.R., Owen D.;
RT "Solution structure and dynamics of the small GTPase RalB in its active
RT conformation: significance for effector protein binding.";
RL Biochemistry 48:2192-2206(2009).
RN [17]
RP STRUCTURE BY NMR OF 8-185 IN COMPLEX WITH RALBP1, AND INTERACTION WITH
RP RALBP1.
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).
CC -!- FUNCTION: Multifunctional GTPase involved in a variety of cellular
CC processes including gene expression, cell migration, cell
CC proliferation, oncogenic transformation and membrane trafficking
CC (PubMed:10393179, PubMed:17875936, PubMed:18756269). Accomplishes its
CC multiple functions by interacting with distinct downstream effectors.
CC Acts as a GTP sensor for GTP-dependent exocytosis of dense core
CC vesicles (By similarity). Required both to stabilize the assembly of
CC the exocyst complex and to localize functional exocyst complexes to the
CC leading edge of migrating cells (By similarity). Required for
CC suppression of apoptosis (PubMed:17875936). In late stages of
CC cytokinesis, upon completion of the bridge formation between dividing
CC cells, mediates exocyst recruitment to the midbody to drive abscission
CC (PubMed:18756269). Involved in ligand-dependent receptor mediated
CC endocytosis of the EGF and insulin receptors (PubMed:10393179).
CC {ECO:0000250|UniProtKB:P36860, ECO:0000269|PubMed:10393179,
CC ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:18756269}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Interacts with EXOC2/Sec5 and EXOC8/Exo84 (PubMed:14525976,
CC PubMed:18756269, PubMed:19166349). Interacts (via effector domain) with
CC RALBP1 (PubMed:7673236, PubMed:20696399). {ECO:0000269|PubMed:14525976,
CC ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19166349,
CC ECO:0000269|PubMed:20696399, ECO:0000269|PubMed:7673236}.
CC -!- INTERACTION:
CC P11234; Q0VD86: INCA1; NbExp=3; IntAct=EBI-752162, EBI-6509505;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936};
CC Lipid-anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side
CC {ECO:0000269|PubMed:17875936}. Midbody {ECO:0000269|PubMed:18756269}.
CC Note=During late cytokinesis, enriched at the midbody.
CC {ECO:0000269|PubMed:18756269}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P11234-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11234-2; Sequence=VSP_055843;
CC Name=3;
CC IsoId=P11234-3; Sequence=VSP_055844;
CC -!- PTM: Prenylation is essential for membrane localization. The
CC geranylgeranylated form and the farnesylated mutant does not undergo
CC alternative prenylation in response to geranylgeranyltransferase I
CC inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).
CC {ECO:0000269|PubMed:17875936}.
CC -!- PTM: The farnesylated form confers resistance to the proapoptotic and
CC anti-anchorage-dependent growth effects of geranylgeranyltransferase I
CC inhibitors, including GGTI-2417. {ECO:0000269|PubMed:17875936}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; X15015; CAA33119.1; -; mRNA.
DR EMBL; M35416; AAA60250.1; -; mRNA.
DR EMBL; AF493911; AAM12625.1; -; mRNA.
DR EMBL; BT006953; AAP35599.1; -; mRNA.
DR EMBL; AK127675; BAC87080.1; -; mRNA.
DR EMBL; AK303214; BAG64302.1; -; mRNA.
DR EMBL; AK312453; BAG35360.1; -; mRNA.
DR EMBL; AC012363; AAY14800.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95240.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95242.1; -; Genomic_DNA.
DR EMBL; BC018163; AAH18163.1; -; mRNA.
DR CCDS; CCDS2131.1; -. [P11234-1]
DR PIR; S04597; TVHUAB.
DR RefSeq; NP_002872.1; NM_002881.2. [P11234-1]
DR RefSeq; XP_005263781.1; XM_005263724.1.
DR RefSeq; XP_005263784.1; XM_005263727.1.
DR RefSeq; XP_005263785.1; XM_005263728.1. [P11234-1]
DR RefSeq; XP_005263786.1; XM_005263729.2.
DR RefSeq; XP_016860111.1; XM_017004622.1.
DR PDB; 2KE5; NMR; -; A=12-185.
DR PDB; 2KWI; NMR; -; A=8-185.
DR PDB; 6ZQT; X-ray; 1.51 A; A/B=1-185.
DR PDB; 6ZRN; X-ray; 1.48 A; A/B=1-185.
DR PDBsum; 2KE5; -.
DR PDBsum; 2KWI; -.
DR PDBsum; 6ZQT; -.
DR PDBsum; 6ZRN; -.
DR AlphaFoldDB; P11234; -.
DR BMRB; P11234; -.
DR SMR; P11234; -.
DR BioGRID; 111835; 72.
DR IntAct; P11234; 48.
DR MINT; P11234; -.
DR STRING; 9606.ENSP00000272519; -.
DR ChEMBL; CHEMBL3879851; -.
DR iPTMnet; P11234; -.
DR PhosphoSitePlus; P11234; -.
DR SwissPalm; P11234; -.
DR BioMuta; RALB; -.
DR DMDM; 131835; -.
DR EPD; P11234; -.
DR jPOST; P11234; -.
DR MassIVE; P11234; -.
DR MaxQB; P11234; -.
DR PaxDb; P11234; -.
DR PeptideAtlas; P11234; -.
DR PRIDE; P11234; -.
DR ProteomicsDB; 52727; -. [P11234-1]
DR ProteomicsDB; 5648; -.
DR ProteomicsDB; 68195; -.
DR Antibodypedia; 33389; 373 antibodies from 36 providers.
DR DNASU; 5899; -.
DR Ensembl; ENST00000272519.10; ENSP00000272519.4; ENSG00000144118.14. [P11234-1]
DR Ensembl; ENST00000420510.5; ENSP00000414224.1; ENSG00000144118.14. [P11234-1]
DR GeneID; 5899; -.
DR KEGG; hsa:5899; -.
DR MANE-Select; ENST00000272519.10; ENSP00000272519.4; NM_002881.3; NP_002872.1.
DR UCSC; uc002tmk.4; human. [P11234-1]
DR CTD; 5899; -.
DR DisGeNET; 5899; -.
DR GeneCards; RALB; -.
DR HGNC; HGNC:9840; RALB.
DR HPA; ENSG00000144118; Tissue enriched (parathyroid).
DR MIM; 179551; gene.
DR neXtProt; NX_P11234; -.
DR OpenTargets; ENSG00000144118; -.
DR PharmGKB; PA34198; -.
DR VEuPathDB; HostDB:ENSG00000144118; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155984; -.
DR InParanoid; P11234; -.
DR OMA; QNITEMF; -.
DR PhylomeDB; P11234; -.
DR TreeFam; TF312796; -.
DR PathwayCommons; P11234; -.
DR Reactome; R-HSA-171007; p38MAPK events.
DR SignaLink; P11234; -.
DR SIGNOR; P11234; -.
DR BioGRID-ORCS; 5899; 11 hits in 1084 CRISPR screens.
DR ChiTaRS; RALB; human.
DR EvolutionaryTrace; P11234; -.
DR GeneWiki; RALB; -.
DR GenomeRNAi; 5899; -.
DR Pharos; P11234; Tbio.
DR PRO; PR:P11234; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P11234; protein.
DR Bgee; ENSG00000144118; Expressed in monocyte and 211 other tissues.
DR ExpressionAtlas; P11234; baseline and differential.
DR Genevisible; P11234; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0001928; P:regulation of exocyst assembly; ISS:UniProtKB.
DR GO; GO:0060178; P:regulation of exocyst localization; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR028412; Ral.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR PANTHER; PTHR24070:SF199; PTHR24070:SF199; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell cycle; Cell division;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..203
FT /note="Ras-related protein Ral-B"
FT /id="PRO_0000082698"
FT PROPEP 204..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281349"
FT REGION 180..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..51
FT /note="Effector region"
FT BINDING 21..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 158..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 203
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:17875936"
FT VAR_SEQ 1
FT /note="M -> MKQRQSALQWVICVSQPQKTSEM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055843"
FT VAR_SEQ 36..37
FT /note="YD -> NVSKSLAYDKKKYTANKKVEGIL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055844"
FT MUTAGEN 1..11
FT /note="Missing: No effect on cytokinesis. Impaired
FT cytokinesis, as shown by increased number of binucleate
FT cells; when associated with V-23."
FT /evidence="ECO:0000269|PubMed:18756269"
FT MUTAGEN 23
FT /note="G->V: Impaired cytokinesis, as shown by increased
FT number of binucleate cells. Impaired cytokinesis; when
FT associated with 1-M--S-11 or N-49. No effect on
FT cytokinesis; when associated with R-38, W-48 or E-49. No
FT effect on interaction with EXOC2 and EXOC8. Decreased
FT interaction with EXOC2 and EXOC8; when associated with R-38
FT or W-48."
FT /evidence="ECO:0000269|PubMed:18756269"
FT MUTAGEN 38
FT /note="E->R: No effect on cytokinesis. No effect on
FT cytokinesis; when associated with V-23. Decreased
FT interaction with EXOC2 and EXOC8; when associated with V-
FT 23."
FT /evidence="ECO:0000269|PubMed:18756269"
FT MUTAGEN 46
FT /note="T->A: Reduces the binding affinity to EXOC2
FT effector."
FT /evidence="ECO:0000269|PubMed:19166349"
FT MUTAGEN 46
FT /note="T->S: Reduces the binding affinity to EXOC2
FT effector."
FT /evidence="ECO:0000269|PubMed:19166349"
FT MUTAGEN 48
FT /note="A->W: Impaired abscission, the last step of
FT cytokinesis, as shown by the accumulation of bridged cells.
FT No effect on cytokinesis; when associated with V-23.
FT Decreased interaction with EXOC2 and EXOC8; when associated
FT with V-23."
FT /evidence="ECO:0000269|PubMed:18756269"
FT MUTAGEN 49
FT /note="D->E: Impaired abscission, the last step of
FT cytokinesis. No effect on cytokinesis; when associated with
FT V-23."
FT /evidence="ECO:0000269|PubMed:18756269"
FT MUTAGEN 49
FT /note="D->N: No effect on cytokinesis. Impaired
FT cytokinesis, as shown by increased number of binucleate
FT cells; when associated with V-23."
FT /evidence="ECO:0000269|PubMed:18756269"
FT MUTAGEN 72
FT /note="Q->L: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:19166349"
FT MUTAGEN 203
FT /note="C->S: Loss of geranylgeranylation and membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:17875936"
FT MUTAGEN 206
FT /note="L->S: Converts geranyl-geranylation to
FT farnesylation. No effect on membrane localization. Confers
FT resistance to GGTI-induced pancreatic cancer cell
FT apoptosis, but not to GGTI-dependent inhibition of
FT anchorage-independent proliferation."
FT /evidence="ECO:0000269|PubMed:17875936"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2KWI"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:6ZRN"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:6ZRN"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:6ZRN"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:6ZRN"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:6ZRN"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:6ZRN"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:6ZRN"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6ZRN"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6ZRN"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:6ZRN"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:6ZRN"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6ZRN"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:6ZRN"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:6ZRN"
SQ SEQUENCE 206 AA; 23409 MW; E0AC95130FB6452C CRC64;
MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK
IPLLVVGNKS DLEERRQVPV EEARSKAEEW GVQYVETSAK TRANVDKVFF DLMREIRTKK
MSENKDKNGK KSSKNKKSFK ERCCLL
