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 27-MAR-2024, entry version 226. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 78. DR IntAct; P11234; 49. 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; 9606-ENSP00000272519; -. DR PeptideAtlas; P11234; -. DR ProteomicsDB; 52727; -. [P11234-1] DR ProteomicsDB; 5648; -. DR ProteomicsDB; 68195; -. DR Pumba; P11234; -. DR Antibodypedia; 33389; 414 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 AGR; HGNC:9840; -. 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; DDTIPFI; -. DR OrthoDB; 8685at2759; -. 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; 16 hits in 1170 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 213 other cell types or tissues. DR ExpressionAtlas; P11234; baseline and differential. 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:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase. 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:0031623; P:receptor internalization; IGI:FlyBase. 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 CDD; cd04139; RalA_RalB; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR020849; Small_GTPase_Ras-type. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1. DR PANTHER; PTHR24070:SF199; RAS-RELATED PROTEIN RAL-B; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51421; RAS; 1. DR Genevisible; P11234; HS. 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 FT V-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 //