RAB1B_HUMAN
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 03-AUG-2022, entry version 200.
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}.
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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 PDBsum; 3JZA; -.
DR PDBsum; 3NKV; -.
DR PDBsum; 4HLQ; -.
DR PDBsum; 4I1O; -.
DR PDBsum; 5O74; -.
DR PDBsum; 5SZH; -.
DR PDBsum; 5SZK; -.
DR PDBsum; 6SKU; -.
DR AlphaFoldDB; Q9H0U4; -.
DR SMR; Q9H0U4; -.
DR BioGRID; 123619; 201.
DR DIP; DIP-42462N; -.
DR IntAct; Q9H0U4; 43.
DR MINT; Q9H0U4; -.
DR STRING; 9606.ENSP00000310226; -.
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; Q9H0U4; -.
DR PeptideAtlas; Q9H0U4; -.
DR PRIDE; Q9H0U4; -.
DR ProteomicsDB; 80325; -.
DR TopDownProteomics; Q9H0U4; -.
DR Antibodypedia; 4132; 314 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 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; 1149105at2759; -.
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; 150 hits in 1079 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 199 other tissues.
DR ExpressionAtlas; Q9H0U4; baseline and differential.
DR Genevisible; Q9H0U4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
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
