ID RAB1B_HUMAN Reviewed; 201 AA. AC Q9H0U4; A8K7S1; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 209. DE RecName: Full=Ras-related protein Rab-1B; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820}; GN Name=RAB1B; 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]. RA Zhao Y., Yu L., Xin Y.R., Zhang M., Chen S.Y., Zhao S.Y.; RT "Cloning and sequencing of a novel human cDNA homology to rat ras-related RT rab1B cDNA."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, and Synovium; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 PROTEIN SEQUENCE OF 1-21; 28-46; 59-69; 80-100 AND 138-170, ACETYLATION AT RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [6] RP ISOPRENYLATION AT CYS-200 AND CYS-201, INTERACTION WITH GDI1, AND RP MUTAGENESIS OF GLN-67. RX PubMed=8836150; DOI=10.1042/bj3181007; RA Wilson A.L., Sheridan K.M., Erdman R.A., Maltese W.A.; RT "Prenylation of a Rab1B mutant with altered GTPase activity is impaired in RT cell-free systems but not in intact mammalian cells."; RL Biochem. J. 318:1007-1014(1996). RN [7] RP INTERACTION WITH CHM, FUNCTION, AND MUTAGENESIS OF GLN-67; ILE-73; TYR-78; RP ALA-81; LEU-103; ALA-110; LYS-137 AND GLY-144. RX PubMed=9437002; DOI=10.1091/mbc.9.1.223; RA Overmeyer J.H., Wilson A.L., Erdman R.A., Maltese W.A.; RT "The putative 'switch 2' domain of the Ras-related GTPase, Rab1B, plays an RT essential role in the interaction with Rab escort protein."; RL Mol. Biol. Cell 9:223-235(1998). RN [8] RP SUBCELLULAR LOCATION, ISOPRENYLATION, INTERACTION WITH GDI1 AND CHM, AND RP MUTAGENESIS OF TYR-78. RX PubMed=11389151; DOI=10.1074/jbc.m101511200; RA Overmeyer J.H., Wilson A.L., Maltese W.A.; RT "Membrane targeting of a Rab GTPase that fails to associate with Rab escort RT protein (REP) or guanine nucleotide dissociation inhibitor (GDI)."; RL J. Biol. Chem. 276:20379-20386(2001). RN [9] RP INTERACTION WITH MICAL1; MICAL2 AND MICAL3. RX PubMed=15694364; DOI=10.1016/j.bbrc.2004.12.182; RA Fischer J., Weide T., Barnekow A.; RT "The MICAL proteins and rab1: a possible link to the cytoskeleton?"; RL Biochem. Biophys. Res. Commun. 328:415-423(2005). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-121. RX PubMed=20545908; DOI=10.1111/j.1600-0854.2010.01086.x; RA Zoppino F.C., Militello R.D., Slavin I., Alvarez C., Colombo M.I.; RT "Autophagosome formation depends on the small GTPase Rab1 and functional ER RT exit sites."; RL Traffic 11:1246-1261(2010). RN [11] RP INTERACTION WITH L.PNEUMOPHILA SIDD, AND DEAMPYLATION AT TYR-77. RX PubMed=21734656; DOI=10.1038/nature10307; RA Tan Y., Luo Z.Q.; RT "Legionella pneumophila SidD is a deAMPylase that modifies Rab1."; RL Nature 475:506-509(2011). RN [12] RP INTERACTION WITH L.PNEUMOPHILA ANKX (MICROBIAL INFECTION), PHOSPHORYLATION RP AT SER-76 (MICROBIAL INFECTION), AND MUTAGENESIS OF SER-76. RX PubMed=21822290; DOI=10.1038/nature10335; RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.; RT "Modulation of Rab GTPase function by a protein phosphocholine RT transferase."; RL Nature 477:103-106(2011). RN [13] RP INTERACTION WITH L.PNEUMOPHILA LEM3 (MICROBIAL INFECTION), AND RP PHOSPHORYLATION AT SER-76 (MICROBIAL INFECTION). RX PubMed=22158903; DOI=10.1073/pnas.1114023109; RA Tan Y., Arnold R.J., Luo Z.Q.; RT "Legionella pneumophila regulates the small GTPase Rab1 activity by RT reversible phosphorylcholination."; RL Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011). RN [14] RP INTERACTION WITH L.PNEUMOPHILA SIDD (MICROBIAL INFECTION), AND DEAMPYLATION RP AT TYR-77. RX PubMed=21680813; DOI=10.1126/science.1207193; RA Neunuebel M.R., Chen Y., Gaspar A.H., Backlund P.S. Jr., Yergey A., RA Machner M.P.; RT "De-AMPylation of the small GTPase Rab1 by the pathogen Legionella RT pneumophila."; RL Science 333:453-456(2011). RN [15] RP INTERACTION WITH L.PNEUMOPHILA ANKX AND LEM3 (MICROBIAL INFECTION), AND RP PHOSPHORYLATION AT SER-76 (MICROBIAL INFECTION). RX PubMed=22307087; DOI=10.1038/emboj.2012.16; RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S.; RT "Reversible phosphocholination of Rab proteins by Legionella pneumophila RT effector proteins."; RL EMBO J. 31:1774-1784(2012). RN [16] RP INTERACTION WITH MTMR6, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23188820; DOI=10.1074/jbc.m112.395087; RA Mochizuki Y., Ohashi R., Kawamura T., Iwanari H., Kodama T., Naito M., RA Hamakubo T.; RT "Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) RT is regulated by small GTPase Rab1B in the early secretory and autophagic RT pathways."; RL J. Biol. Chem. 288:1009-1021(2013). RN [17] RP FUNCTION. RX PubMed=26209634; DOI=10.1074/jbc.m115.669242; RA Aizawa M., Fukuda M.; RT "Small GTPase Rab2B and Its Specific Binding Protein Golgi-associated Rab2B RT Interactor-like 4 (GARI-L4) Regulate Golgi Morphology."; RL J. Biol. Chem. 290:22250-22261(2015). RN [18] 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 [19] RP GLYCOSYLATION (MICROBIAL INFECTION). RX PubMed=32974215; DOI=10.3389/fcimb.2020.00419; RA Gan J., Scott N.E., Newson J.P.M., Wibawa R.R., Wong Fok Lung T., RA Pollock G.L., Ng G.Z., van Driel I., Pearson J.S., Hartland E.L., RA Giogha C.; RT "The Salmonella effector SseK3 targets small Rab GTPases."; RL Front. Cell. Infect. Microbiol. 10:419-419(2020). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-174 IN COMPLEX WITH RP L.PNEUMOPHILA DRRA GEF DOMAIN, AND GTP-BINDING. RX PubMed=20064470; DOI=10.1016/j.molcel.2009.11.014; RA Schoebel S., Oesterlin L.K., Blankenfeldt W., Goody R.S., Itzen A.; RT "RabGDI displacement by DrrA from Legionella is a consequence of its RT guanine nucleotide exchange activity."; RL Mol. Cell 36:1060-1072(2009). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-174 IN COMPLEX WITH RP L.PNEUMOPHILA DRRA (MICROBIAL INFECTION), AMPYLATION AT TYR-77 (MICROBIAL RP INFECTION), IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-77, AND RP GTP-BINDING. RX PubMed=20651120; DOI=10.1126/science.1192276; RA Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S., Itzen A.; RT "The Legionella effector protein DrrA AMPylates the membrane traffic RT regulator Rab1b."; RL Science 329:946-949(2010). RN [22] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 3-174 IN COMPLEX WITH TBC1D20, RP MISCELLANEOUS, MUTAGENESIS OF GLN-67, AND GTP-BINDING. RX PubMed=23236136; DOI=10.1073/pnas.1214431110; RA Gavriljuk K., Gazdag E.M., Itzen A., Kotting C., Goody R.S., Gerwert K.; RT "Catalytic mechanism of a mammalian Rab.RabGAP complex in atomic detail."; RL Proc. Natl. Acad. Sci. U.S.A. 109:21348-21353(2012). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MICALCL, AND RP INTERACTION WITH MICAL1 AND MILCAL3. RX PubMed=27552051; DOI=10.7554/elife.18675; RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S., RA Gazdag E.M., Muller M.P.; RT "bMERB domains are bivalent Rab8 family effectors evolved by gene RT duplication."; RL Elife 5:E18675-E18675(2016). CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular CC membrane trafficking, from the formation of transport vesicles to their CC fusion with membranes (PubMed:20545908, PubMed:9437002). Rabs cycle CC between an inactive GDP-bound form and an active GTP-bound form that is CC able to recruit to membranes different set of downstream effectors CC directly responsible for vesicle formation, movement, tethering and CC fusion (PubMed:9437002). Plays a role in the initial events of the CC autophagic vacuole development which take place at specialized regions CC of the endoplasmic reticulum (PubMed:20545908). Regulates vesicular CC transport between the endoplasmic reticulum and successive Golgi CC compartments (By similarity). Required to modulate the compacted CC morphology of the Golgi (PubMed:26209634). Promotes the recruitment of CC lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate CC compartment (By similarity). {ECO:0000250|UniProtKB:P10536, CC ECO:0000269|PubMed:20545908, ECO:0000269|PubMed:26209634, CC ECO:0000269|PubMed:9437002}. 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:0000250|UniProtKB:P62820}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine CC exchange factor (GEF), while inactivation through hydrolysis of bound CC GTP is catalyzed by a GTPase activating protein (GAP). {ECO:0000305}. CC -!- SUBUNIT: Interacts with MICAL1 and MICAL2 (PubMed:15694364, CC PubMed:27552051). Interacts (in GTP-bound form) with MICALCL, MICAL1 CC and MILCAL3 (PubMed:15694364, PubMed:27552051). Interacts with GDI1; CC the interaction requires the GDP-bound state (PubMed:8836150, CC PubMed:11389151). Interacts with CHM/REP1; the interaction requires the CC GDP-bound form and is necessary for prenylation by GGTase II CC (PubMed:9437002, PubMed:11389151). Interacts with RabGAP TBC1D20 CC (PubMed:23236136). Interacts (in GDP-bound form) with lipid phosphatase CC MTMR6 (via GRAM domain); the interaction regulates MTMR6 recruitment to CC the endoplasmic reticulum-Golgi intermediate compartment CC (PubMed:23188820). Interacts (in GDP-bound form) with lipid phosphatase CC MTMR7 (By similarity). {ECO:0000250|UniProtKB:Q9D1G1, CC ECO:0000269|PubMed:11389151, ECO:0000269|PubMed:15694364, CC ECO:0000269|PubMed:23188820, ECO:0000269|PubMed:23236136, CC ECO:0000269|PubMed:27552051, ECO:0000269|PubMed:8836150, CC ECO:0000269|PubMed:9437002}. CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila AnkX CC (PubMed:21822290, PubMed:22307087). Interacts with L.pneumophila Lem3 CC (PubMed:22158903, PubMed:22307087). Interacts with L.pneumophila SidD CC (PubMed:21734656, PubMed:21680813). Interacts with L.pneumophila DrrA CC (PubMed:20064470, PubMed:20651120). {ECO:0000269|PubMed:20064470, CC ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:21680813, CC ECO:0000269|PubMed:21734656, ECO:0000269|PubMed:21822290, CC ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087}. CC -!- INTERACTION: CC Q9H0U4; Q5S007: LRRK2; NbExp=5; IntAct=EBI-1045214, EBI-5323863; CC Q9H0U4; Q01968: OCRL; NbExp=3; IntAct=EBI-1045214, EBI-6148898; CC Q9H0U4; Q9UKF7-1: PITPNC1; NbExp=4; IntAct=EBI-1045214, EBI-11687286; CC Q9H0U4; P47224: RABIF; NbExp=7; IntAct=EBI-1045214, EBI-713992; CC Q9H0U4; Q5ZWZ3: lpg0940; Xeno; NbExp=3; IntAct=EBI-1045214, EBI-6417967; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11389151}. Membrane CC {ECO:0000269|PubMed:11389151}; Lipid-anchor CC {ECO:0000269|PubMed:11389151}; Cytoplasmic side CC {ECO:0000269|PubMed:11389151}. Preautophagosomal structure membrane CC {ECO:0000269|PubMed:20545908}; Lipid-anchor {ECO:0000305}; Cytoplasmic CC side {ECO:0000305}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of CC specific subcellular compartments including endoplasmic reticulum, CC Golgi apparatus, and intermediate vesicles between these two CC compartments (PubMed:11389151). In the GDP-form, colocalizes with GDI CC in the cytoplasm (PubMed:11389151). Co-localizes with MTMR6 to the CC endoplasmic reticulum-Golgi intermediate compartment and to the peri- CC Golgi region (By similarity). {ECO:0000250|UniProtKB:P10536, CC ECO:0000269|PubMed:11389151}. CC -!- PTM: Prenylated; by GGTase II, only after interaction of the substrate CC with Rab escort protein 1 (REP1). {ECO:0000269|PubMed:11389151, CC ECO:0000269|PubMed:8836150}. CC -!- PTM: (Microbial infection) AMPylation at Tyr-77 by L.pneumophila DrrA CC occurs in the switch 2 region and leads to moderate inactivation of the CC GTPase activity. It appears to prolong the lifetime of the GTP state of CC RAB1B by restricting access of GTPase effectors to switch 2 and CC blocking effector-stimulated GTP hydrolysis, thereby rendering RAB1B CC constitutively active. It is later de-AMPylated by L.pneumophila SidD, CC releasing RAB1B from bacterial phagosomes. CC {ECO:0000269|PubMed:20651120}. CC -!- PTM: (Microbial infection) Phosphocholinated at Ser-76 by L.pneumophila CC AnkX, leading to displace GDP dissociation inhibitors (GDI) CC (PubMed:21822290, PubMed:22307087). Both GDP-bound and GTP-bound forms CC can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, CC restoring accessibility to L.pneumophila GTPase effector LepB CC (PubMed:22158903, PubMed:22307087). {ECO:0000269|PubMed:21822290, CC ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087}. CC -!- PTM: (Microbial infection) Glycosylated by S.typhimurium protein Ssek3: CC arginine GlcNAcylation prevents GTPase activity, thereby disrupting CC vesicular protein transport from the endoplasmic reticulum (ER) to the CC Golgi compartment. {ECO:0000269|PubMed:32974215}. CC -!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses low intrinsic CC GTPase activity. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab 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; AF092437; AAP97212.1; -; mRNA. DR EMBL; AL136635; CAB66570.1; -; mRNA. DR EMBL; AK292086; BAF84775.1; -; mRNA. DR EMBL; AK315333; BAG37733.1; -; mRNA. DR EMBL; BC071169; AAH71169.1; -; mRNA. DR CCDS; CCDS31613.1; -. DR RefSeq; NP_112243.1; NM_030981.2. DR PDB; 3JZA; X-ray; 1.80 A; A=3-174. DR PDB; 3NKV; X-ray; 1.70 A; A/B=3-174. DR PDB; 4HLQ; X-ray; 3.30 A; B/D/F/H/J=3-174. DR PDB; 4I1O; X-ray; 2.70 A; A/C/E/G=3-174. DR PDB; 5O74; X-ray; 2.50 A; B/D/F/H/J/L=3-174. DR PDB; 5SZH; X-ray; 2.30 A; B=1-201. DR PDB; 5SZK; X-ray; 2.80 A; B=2-201. DR PDB; 6SKU; X-ray; 3.20 A; B=3-174. DR PDB; 8ALK; X-ray; 2.15 A; B=3-174. DR PDBsum; 3JZA; -. DR PDBsum; 3NKV; -. DR PDBsum; 4HLQ; -. DR PDBsum; 4I1O; -. DR PDBsum; 5O74; -. DR PDBsum; 5SZH; -. DR PDBsum; 5SZK; -. DR PDBsum; 6SKU; -. DR PDBsum; 8ALK; -. DR AlphaFoldDB; Q9H0U4; -. DR SMR; Q9H0U4; -. DR BioGRID; 123619; 256. DR DIP; DIP-42462N; -. DR IntAct; Q9H0U4; 48. DR MINT; Q9H0U4; -. DR STRING; 9606.ENSP00000310226; -. DR GlyGen; Q9H0U4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H0U4; -. DR MetOSite; Q9H0U4; -. DR PhosphoSitePlus; Q9H0U4; -. DR SwissPalm; Q9H0U4; -. DR BioMuta; RAB1B; -. DR DMDM; 23396834; -. DR EPD; Q9H0U4; -. DR jPOST; Q9H0U4; -. DR MassIVE; Q9H0U4; -. DR MaxQB; Q9H0U4; -. DR PaxDb; 9606-ENSP00000310226; -. DR PeptideAtlas; Q9H0U4; -. DR PRIDE; Q9H0U4; -. DR ProteomicsDB; 80325; -. DR Pumba; Q9H0U4; -. DR TopDownProteomics; Q9H0U4; -. DR Antibodypedia; 4132; 344 antibodies from 32 providers. DR DNASU; 81876; -. DR Ensembl; ENST00000311481.11; ENSP00000310226.6; ENSG00000174903.16. DR GeneID; 81876; -. DR KEGG; hsa:81876; -. DR MANE-Select; ENST00000311481.11; ENSP00000310226.6; NM_030981.3; NP_112243.1. DR UCSC; uc001ohf.4; human. DR AGR; HGNC:18370; -. DR CTD; 81876; -. DR DisGeNET; 81876; -. DR GeneCards; RAB1B; -. DR HGNC; HGNC:18370; RAB1B. DR HPA; ENSG00000174903; Low tissue specificity. DR MIM; 612565; gene. DR neXtProt; NX_Q9H0U4; -. DR OpenTargets; ENSG00000174903; -. DR PharmGKB; PA34108; -. DR VEuPathDB; HostDB:ENSG00000174903; -. DR eggNOG; KOG0084; Eukaryota. DR GeneTree; ENSGT00940000155078; -. DR HOGENOM; CLU_041217_23_1_1; -. DR InParanoid; Q9H0U4; -. DR OMA; QRYACDS; -. DR OrthoDB; 8685at2759; -. DR PhylomeDB; Q9H0U4; -. DR TreeFam; TF300097; -. DR BRENDA; 3.6.5.2; 2681. DR PathwayCommons; Q9H0U4; -. DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR SABIO-RK; Q9H0U4; -. DR SignaLink; Q9H0U4; -. DR BioGRID-ORCS; 81876; 166 hits in 1158 CRISPR screens. DR ChiTaRS; RAB1B; human. DR EvolutionaryTrace; Q9H0U4; -. DR GeneWiki; RAB1B; -. DR GenomeRNAi; 81876; -. DR Pharos; Q9H0U4; Tbio. DR PRO; PR:Q9H0U4; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9H0U4; Protein. DR Bgee; ENSG00000174903; Expressed in mucosa of transverse colon and 201 other cell types or tissues. DR ExpressionAtlas; Q9H0U4; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB. DR GO; GO:0030133; C:transport vesicle; TAS:Reactome. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:UniProtKB. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; IGI:UniProtKB. DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:UniProtKB. DR GO; GO:0019068; P:virion assembly; IGI:UniProtKB. DR CDD; cd01869; Rab1_Ypt1; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR PANTHER; PTHR47977:SF54; RAS-RELATED PROTEIN RAB-1B; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. 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; PS51419; RAB; 1. DR Genevisible; Q9H0U4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Autophagy; Cytoplasm; Direct protein sequencing; KW Glycoprotein; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation; KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..201 FT /note="Ras-related protein Rab-1B" FT /id="PRO_0000121061" FT REGION 64..83 FT /note="Switch 2 region; required for interaction with FT REP1/CHM" FT REGION 174..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 37..45 FT /note="Effector region" FT /evidence="ECO:0000255" FT BINDING 15..23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20064470, FT ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, FT ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3JZA, FT ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, FT ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, FT ECO:0007744|PDB:5SZK" FT BINDING 33..40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20651120, FT ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, FT ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, FT ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK" FT BINDING 63..67 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20651120, FT ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, FT ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK" FT BINDING 121..124 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20651120, FT ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, FT ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, FT ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, FT ECO:0007744|PDB:5SZK" FT BINDING 151..153 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:20651120, FT ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, FT ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, FT ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, FT ECO:0007744|PDB:5SZK" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.5" FT MOD_RES 76 FT /note="(Microbial infection) O-(2-cholinephosphoryl)serine" FT /evidence="ECO:0000269|PubMed:21822290, FT ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087" FT MOD_RES 77 FT /note="(Microbial infection) O-AMP-tyrosine" FT /evidence="ECO:0000269|PubMed:20651120" FT MOD_RES 201 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000255" FT LIPID 200 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:8836150" FT LIPID 201 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:8836150" FT MUTAGEN 67 FT /note="Q->L: No effect on GDI1 binding. Reduces prenylation FT in vitro, but not in vivo. No effect on interaction with FT REP1/CHM; 100-fold refunction in intrinsic GTPase FT activity." FT /evidence="ECO:0000269|PubMed:23236136, FT ECO:0000269|PubMed:8836150, ECO:0000269|PubMed:9437002" FT MUTAGEN 73 FT /note="I->N: Abolishes interaction with REP1/CHM. No FT prenylation. Much lower GDP/GTP ratio." FT /evidence="ECO:0000269|PubMed:9437002" FT MUTAGEN 76 FT /note="S->A: Abolishes phosphocholination by Legionella FT AnkX." FT /evidence="ECO:0000269|PubMed:21822290" FT MUTAGEN 77 FT /note="Y->F: Abolishes AMPylation by Legionella DrrA." FT /evidence="ECO:0000269|PubMed:20651120" FT MUTAGEN 78 FT /note="Y->D: Abolishes interaction with REP1/CHM and GDI1. FT No prenylation. Much lower GDP/GTP ratio. No membrane FT association." FT /evidence="ECO:0000269|PubMed:11389151, FT ECO:0000269|PubMed:9437002" FT MUTAGEN 81 FT /note="A->D: Abolishes interaction with REP1/CHM. No FT prenylation. Lowers GDP/GTP ratio by half." FT /evidence="ECO:0000269|PubMed:9437002" FT MUTAGEN 103 FT /note="L->R: No effect on prenylation." FT /evidence="ECO:0000269|PubMed:9437002" FT MUTAGEN 110 FT /note="A->D: No effect on prenylation." FT /evidence="ECO:0000269|PubMed:9437002" FT MUTAGEN 121 FT /note="N->I: Prevent formation of autophagosomes." FT /evidence="ECO:0000269|PubMed:20545908" FT MUTAGEN 137 FT /note="K->E: No effect on prenylation." FT /evidence="ECO:0000269|PubMed:9437002" FT MUTAGEN 144 FT /note="G->N: No effect on prenylation." FT /evidence="ECO:0000269|PubMed:9437002" FT STRAND 6..16 FT /evidence="ECO:0007829|PDB:3NKV" FT STRAND 17..20 FT /evidence="ECO:0007829|PDB:4HLQ" FT HELIX 21..30 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 36..41 FT /evidence="ECO:0007829|PDB:3JZA" FT STRAND 42..52 FT /evidence="ECO:0007829|PDB:3NKV" FT STRAND 55..64 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:3NKV" FT TURN 76..80 FT /evidence="ECO:0007829|PDB:3NKV" FT STRAND 82..89 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 93..97 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 99..109 FT /evidence="ECO:0007829|PDB:3NKV" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:3NKV" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 133..142 FT /evidence="ECO:0007829|PDB:3NKV" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:3NKV" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:3NKV" FT HELIX 158..171 FT /evidence="ECO:0007829|PDB:3NKV" SQ SEQUENCE 201 AA; 22171 MW; 9812FF4DAC34B2BE CRC64; MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG GERPNLKIDS TPVKPAGGGC C //