Full text data of RAB1B
RAB1B
[Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-1B
Ras-related protein Rab-1B
UniProt
Q9H0U4
ID RAB1B_HUMAN Reviewed; 201 AA.
AC Q9H0U4; A8K7S1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Ras-related protein Rab-1B;
GN Name=RAB1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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-
RT related 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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,
RP ACETYLATION AT MET-1, AND 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;
RA Wilson A.L., Sheridan K.M., Erdman R.A., Maltese W.A.;
RT "Prenylation of a Rab1B mutant with altered GTPase activity is
RT impaired in 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;
RP TYR-78; 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,
RT plays an 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,
RP AND 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
RT escort protein (REP) or guanine nucleotide dissociation inhibitor
RT (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 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 [11]
RP INTERACTION WITH L.PNEUMOPHILA ANKX, CHOLINEPHOSPHORYLATION AT SER-76,
RP 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 [12]
RP INTERACTION WITH L.PNEUMOPHILA LEM3, AND DECHOLINEPHOSPHORYLATION AT
RP SER-76.
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 [13]
RP INTERACTION WITH L.PNEUMOPHILA ANKX AND LEM3, CHOLINEPHOSPHORYLATION
RP AT SER-76, AND DECHOLINEPHOSPHORYLATION AT SER-76.
RX PubMed=22307087; DOI=10.1038/emboj.2012.16;
RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A.,
RA Goody R.S.;
RT "Reversible phosphocholination of Rab proteins by Legionella
RT pneumophila effector proteins.";
RL EMBO J. 31:1774-1784(2012).
RN [14]
RP INTERACTION WITH L.PNEUMOPHILA SIDD, AND DEAMPYLATION 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 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-174 IN COMPLEX WITH
RP L.PNEUMOPHILA DRRA GEF DOMAIN.
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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-174 IN COMPLEX WITH
RP L.PNEUMOPHILA DRRA, AMPYLATION AT TYR-77, MASS SPECTROMETRY, AND
RP MUTAGENESIS OF TYR-77.
RX PubMed=20651120; DOI=10.1126/science.1192276;
RA Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S.,
RA Itzen A.;
RT "The Legionella effector protein DrrA AMPylates the membrane traffic
RT regulator Rab1b.";
RL Science 329:946-949(2010).
CC -!- FUNCTION: Protein transport. Regulates vesicular transport between
CC the endoplasmic reticulum and successive Golgi compartments.
CC -!- SUBUNIT: Interacts with MICAL1, MICAL2 and MICAL3. Interacts with
CC GDI1; the interaction requires the GDP-bound state. Interacts with
CC CHM/REP1; the interaction requires the GDP-bound form and is
CC necessary for prenylation by GGTase II.
CC -!- INTERACTION:
CC Q01968:OCRL; NbExp=2; IntAct=EBI-1045214, EBI-6148898;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasm. Note=Targeted by REP1 to membranes of specific
CC subcellular compartments including endoplasmic reticulum, Golgi
CC apparatus, and intermediate vesicles between these two
CC compartments. In the GDP-form, colocalizes with GDI in the
CC cytoplasm (By similarity).
CC -!- PTM: Prenylated; by GGTase II, only after interaction of the
CC substrate with Rab escort protein 1 (REP1).
CC -!- PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the
CC switch 2 region and leads to moderate inactivation of the GTPase
CC 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
CC RAB1B constitutively active. It is later de-AMPylated by
CC L.pneumophila SidD, releasing RAB1B from bacterial phagosomes.
CC -!- PTM: Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to
CC displace GDP dissociation inhibitors (GDI). Both GDP-bound and
CC GTP-bound forms can be phosphocholinated. Dephosphocholinated by
CC L.pneumophila Lem3, restoring accessibility to L.pneumophila
CC GTPase effector LepB.
CC -!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses intrinsic
CC GTPase activity (By similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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 RefSeq; NP_112243.1; NM_030981.2.
DR UniGene; Hs.300816; -.
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 PDBsum; 3JZA; -.
DR PDBsum; 3NKV; -.
DR PDBsum; 4HLQ; -.
DR PDBsum; 4I1O; -.
DR ProteinModelPortal; Q9H0U4; -.
DR SMR; Q9H0U4; 4-173.
DR DIP; DIP-42462N; -.
DR IntAct; Q9H0U4; 9.
DR MINT; MINT-1343701; -.
DR STRING; 9606.ENSP00000310226; -.
DR PhosphoSite; Q9H0U4; -.
DR DMDM; 23396834; -.
DR PaxDb; Q9H0U4; -.
DR PeptideAtlas; Q9H0U4; -.
DR PRIDE; Q9H0U4; -.
DR DNASU; 81876; -.
DR Ensembl; ENST00000311481; ENSP00000310226; ENSG00000174903.
DR GeneID; 81876; -.
DR KEGG; hsa:81876; -.
DR UCSC; uc001ohf.3; human.
DR CTD; 81876; -.
DR GeneCards; GC11P066036; -.
DR H-InvDB; HIX0034908; -.
DR H-InvDB; HIX0128663; -.
DR HGNC; HGNC:18370; RAB1B.
DR HPA; CAB010225; -.
DR MIM; 612565; gene.
DR neXtProt; NX_Q9H0U4; -.
DR PharmGKB; PA34108; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9H0U4; -.
DR KO; K07875; -.
DR OMA; VESYIST; -.
DR OrthoDB; EOG7VB2H4; -.
DR PhylomeDB; Q9H0U4; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; RAB1B; human.
DR EvolutionaryTrace; Q9H0U4; -.
DR GeneWiki; RAB1B; -.
DR GenomeRNAi; 81876; -.
DR NextBio; 72222; -.
DR PRO; PR:Q9H0U4; -.
DR ArrayExpress; Q9H0U4; -.
DR Bgee; Q9H0U4; -.
DR CleanEx; HS_RAB1B; -.
DR Genevestigator; Q9H0U4; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 201 Ras-related protein Rab-1B.
FT /FTId=PRO_0000121061.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT REGION 64 83 Switch 2 region; required for interaction
FT with REP1/CHM.
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 76 76 O-(2-cholinephosphoryl)serine; by
FT Legionella AnkX.
FT MOD_RES 77 77 O-AMP-tyrosine; by Legionella DrrA.
FT MOD_RES 201 201 Cysteine methyl ester (Potential).
FT LIPID 200 200 S-geranylgeranyl cysteine.
FT LIPID 201 201 S-geranylgeranyl cysteine.
FT MUTAGEN 67 67 Q->L: No effect on GDI1 binding. Reduces,
FT in vitro, but not, in vivo prenylation.
FT No effect on interaction with REP1/CHM
FT Much lower GDP/GTP ratio.
FT MUTAGEN 73 73 I->N: Abolishes interaction with
FT REP1/CHM. No prenylation. Much lower
FT GDP/GTP ratio.
FT MUTAGEN 76 76 S->A: Abolishes phosphocholination by
FT Legionella AnkX.
FT MUTAGEN 77 77 Y->F: Abolishes AMPylation by Legionella
FT DrrA.
FT MUTAGEN 78 78 Y->D: Abolishes interaction with REP1/CHM
FT and GDI1. No prenylation. Much lower
FT GDP/GTP ratio. No membrane association.
FT MUTAGEN 81 81 A->D: Abolishes interaction with
FT REP1/CHM. No prenylation. Lowers GDP/GTP
FT ratio by half.
FT MUTAGEN 103 103 L->R: No effect on prenylation.
FT MUTAGEN 110 110 A->D: No effect on prenylation.
FT MUTAGEN 137 137 K->E: No effect on prenylation.
FT MUTAGEN 144 144 G->N: No effect on prenylation.
FT STRAND 6 16
FT STRAND 17 20
FT HELIX 21 30
FT HELIX 36 41
FT STRAND 42 52
FT STRAND 55 64
FT HELIX 68 70
FT HELIX 71 75
FT TURN 76 80
FT STRAND 82 89
FT HELIX 93 97
FT HELIX 99 109
FT STRAND 115 121
FT TURN 126 128
FT HELIX 133 142
FT STRAND 147 149
FT TURN 152 154
FT HELIX 158 171
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
//
ID RAB1B_HUMAN Reviewed; 201 AA.
AC Q9H0U4; A8K7S1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Ras-related protein Rab-1B;
GN Name=RAB1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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-
RT related 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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,
RP ACETYLATION AT MET-1, AND 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;
RA Wilson A.L., Sheridan K.M., Erdman R.A., Maltese W.A.;
RT "Prenylation of a Rab1B mutant with altered GTPase activity is
RT impaired in 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;
RP TYR-78; 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,
RT plays an 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,
RP AND 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
RT escort protein (REP) or guanine nucleotide dissociation inhibitor
RT (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 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 [11]
RP INTERACTION WITH L.PNEUMOPHILA ANKX, CHOLINEPHOSPHORYLATION AT SER-76,
RP 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 [12]
RP INTERACTION WITH L.PNEUMOPHILA LEM3, AND DECHOLINEPHOSPHORYLATION AT
RP SER-76.
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 [13]
RP INTERACTION WITH L.PNEUMOPHILA ANKX AND LEM3, CHOLINEPHOSPHORYLATION
RP AT SER-76, AND DECHOLINEPHOSPHORYLATION AT SER-76.
RX PubMed=22307087; DOI=10.1038/emboj.2012.16;
RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A.,
RA Goody R.S.;
RT "Reversible phosphocholination of Rab proteins by Legionella
RT pneumophila effector proteins.";
RL EMBO J. 31:1774-1784(2012).
RN [14]
RP INTERACTION WITH L.PNEUMOPHILA SIDD, AND DEAMPYLATION 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 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-174 IN COMPLEX WITH
RP L.PNEUMOPHILA DRRA GEF DOMAIN.
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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-174 IN COMPLEX WITH
RP L.PNEUMOPHILA DRRA, AMPYLATION AT TYR-77, MASS SPECTROMETRY, AND
RP MUTAGENESIS OF TYR-77.
RX PubMed=20651120; DOI=10.1126/science.1192276;
RA Muller M.P., Peters H., Blumer J., Blankenfeldt W., Goody R.S.,
RA Itzen A.;
RT "The Legionella effector protein DrrA AMPylates the membrane traffic
RT regulator Rab1b.";
RL Science 329:946-949(2010).
CC -!- FUNCTION: Protein transport. Regulates vesicular transport between
CC the endoplasmic reticulum and successive Golgi compartments.
CC -!- SUBUNIT: Interacts with MICAL1, MICAL2 and MICAL3. Interacts with
CC GDI1; the interaction requires the GDP-bound state. Interacts with
CC CHM/REP1; the interaction requires the GDP-bound form and is
CC necessary for prenylation by GGTase II.
CC -!- INTERACTION:
CC Q01968:OCRL; NbExp=2; IntAct=EBI-1045214, EBI-6148898;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasm. Note=Targeted by REP1 to membranes of specific
CC subcellular compartments including endoplasmic reticulum, Golgi
CC apparatus, and intermediate vesicles between these two
CC compartments. In the GDP-form, colocalizes with GDI in the
CC cytoplasm (By similarity).
CC -!- PTM: Prenylated; by GGTase II, only after interaction of the
CC substrate with Rab escort protein 1 (REP1).
CC -!- PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the
CC switch 2 region and leads to moderate inactivation of the GTPase
CC 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
CC RAB1B constitutively active. It is later de-AMPylated by
CC L.pneumophila SidD, releasing RAB1B from bacterial phagosomes.
CC -!- PTM: Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to
CC displace GDP dissociation inhibitors (GDI). Both GDP-bound and
CC GTP-bound forms can be phosphocholinated. Dephosphocholinated by
CC L.pneumophila Lem3, restoring accessibility to L.pneumophila
CC GTPase effector LepB.
CC -!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses intrinsic
CC GTPase activity (By similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC -----------------------------------------------------------------------
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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 RefSeq; NP_112243.1; NM_030981.2.
DR UniGene; Hs.300816; -.
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 PDBsum; 3JZA; -.
DR PDBsum; 3NKV; -.
DR PDBsum; 4HLQ; -.
DR PDBsum; 4I1O; -.
DR ProteinModelPortal; Q9H0U4; -.
DR SMR; Q9H0U4; 4-173.
DR DIP; DIP-42462N; -.
DR IntAct; Q9H0U4; 9.
DR MINT; MINT-1343701; -.
DR STRING; 9606.ENSP00000310226; -.
DR PhosphoSite; Q9H0U4; -.
DR DMDM; 23396834; -.
DR PaxDb; Q9H0U4; -.
DR PeptideAtlas; Q9H0U4; -.
DR PRIDE; Q9H0U4; -.
DR DNASU; 81876; -.
DR Ensembl; ENST00000311481; ENSP00000310226; ENSG00000174903.
DR GeneID; 81876; -.
DR KEGG; hsa:81876; -.
DR UCSC; uc001ohf.3; human.
DR CTD; 81876; -.
DR GeneCards; GC11P066036; -.
DR H-InvDB; HIX0034908; -.
DR H-InvDB; HIX0128663; -.
DR HGNC; HGNC:18370; RAB1B.
DR HPA; CAB010225; -.
DR MIM; 612565; gene.
DR neXtProt; NX_Q9H0U4; -.
DR PharmGKB; PA34108; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q9H0U4; -.
DR KO; K07875; -.
DR OMA; VESYIST; -.
DR OrthoDB; EOG7VB2H4; -.
DR PhylomeDB; Q9H0U4; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; RAB1B; human.
DR EvolutionaryTrace; Q9H0U4; -.
DR GeneWiki; RAB1B; -.
DR GenomeRNAi; 81876; -.
DR NextBio; 72222; -.
DR PRO; PR:Q9H0U4; -.
DR ArrayExpress; Q9H0U4; -.
DR Bgee; Q9H0U4; -.
DR CleanEx; HS_RAB1B; -.
DR Genevestigator; Q9H0U4; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 201 Ras-related protein Rab-1B.
FT /FTId=PRO_0000121061.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 121 124 GTP (By similarity).
FT REGION 64 83 Switch 2 region; required for interaction
FT with REP1/CHM.
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 76 76 O-(2-cholinephosphoryl)serine; by
FT Legionella AnkX.
FT MOD_RES 77 77 O-AMP-tyrosine; by Legionella DrrA.
FT MOD_RES 201 201 Cysteine methyl ester (Potential).
FT LIPID 200 200 S-geranylgeranyl cysteine.
FT LIPID 201 201 S-geranylgeranyl cysteine.
FT MUTAGEN 67 67 Q->L: No effect on GDI1 binding. Reduces,
FT in vitro, but not, in vivo prenylation.
FT No effect on interaction with REP1/CHM
FT Much lower GDP/GTP ratio.
FT MUTAGEN 73 73 I->N: Abolishes interaction with
FT REP1/CHM. No prenylation. Much lower
FT GDP/GTP ratio.
FT MUTAGEN 76 76 S->A: Abolishes phosphocholination by
FT Legionella AnkX.
FT MUTAGEN 77 77 Y->F: Abolishes AMPylation by Legionella
FT DrrA.
FT MUTAGEN 78 78 Y->D: Abolishes interaction with REP1/CHM
FT and GDI1. No prenylation. Much lower
FT GDP/GTP ratio. No membrane association.
FT MUTAGEN 81 81 A->D: Abolishes interaction with
FT REP1/CHM. No prenylation. Lowers GDP/GTP
FT ratio by half.
FT MUTAGEN 103 103 L->R: No effect on prenylation.
FT MUTAGEN 110 110 A->D: No effect on prenylation.
FT MUTAGEN 137 137 K->E: No effect on prenylation.
FT MUTAGEN 144 144 G->N: No effect on prenylation.
FT STRAND 6 16
FT STRAND 17 20
FT HELIX 21 30
FT HELIX 36 41
FT STRAND 42 52
FT STRAND 55 64
FT HELIX 68 70
FT HELIX 71 75
FT TURN 76 80
FT STRAND 82 89
FT HELIX 93 97
FT HELIX 99 109
FT STRAND 115 121
FT TURN 126 128
FT HELIX 133 142
FT STRAND 147 149
FT TURN 152 154
FT HELIX 158 171
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
//
MIM
612565
*RECORD*
*FIELD* NO
612565
*FIELD* TI
*612565 RAS-ASSOCIATED PROTEIN RAB1B; RAB1B
*FIELD* TX
DESCRIPTION
Members of the RAB protein family, such as RAB1B, are low molecular mass
read moremonomeric GTPases localized on the cytoplasmic surfaces of distinct
membrane-bound organelles. RAB1B functions in the early secretory
pathway and is essential for vesicle transport between the endoplasmic
reticulum (ER) and Golgi (Chen et al., 1997; Alvarez et al., 2003).
CLONING
By PCR using degenerate primers based on conserved sequences in human
RAB transcripts, Chen et al. (1997) obtained a partial RAB1B cDNA from a
pigmented human melanoma cell cDNA library. The deduced 53-amino acid
stretch spans GTP-binding domains II and III and has only 1 or 2 amino
acid changes from the homologous stretch in rat Rab1b and human RAB1A
(179508), respectively. RAB1B appeared to be a low-abundance transcript
in the human melanoma cells.
By searching databases for RAS family members, followed by PCR, He et
al. (2002) cloned RAB1B. The deduced 201-amino acid RAB1B protein
contains 4 highly conserved GTPase motifs and a C-terminal
geranylgeranylation motif. Northern blot analysis detected strong
expression of a major transcript of about 2.4 kb in all tissues
examined.
GENE FUNCTION
Alvarez et al. (2003) found that expression of the RAB1B asn121-to-ile
(N121I) mutant, which is impaired in guanine nucleotide binding, blocked
forward transport of vesicles from the Golgi to the ER and induced Golgi
disruption in HeLa cells. The N121I mutant caused a phenotype analogous
to that induced by brefeldin A (BFA): it caused resident Golgi proteins
to relocate to the ER, and it induced redistribution of the ER-Golgi
intermediate compartment proteins ERGIC53 (LMAN1; 601567), GM130
(GOLGA2; 602580), and p115 (603344) to punctate structures. N121I caused
dissociation of beta-COP (COPB; 600959) from membranes, implicating
RAB1B in a pathway leading to the recruitment of the coatomer complex
(COPI; 601924). The N121I phenotype was rescued by expression of ARF1
(103180) and GBF1 (603698), which mediate COPI recruitment. Like
expression of ARF1 and GBF1, expression of a constitutively active RAB1B
gln67-to-leu (Q67L) mutant prevented Golgi fragmentation and beta-COP
dissociation in BFA-treated cells. Alvarez et al. (2003) concluded that
RAB1B has a role in the GBF1/ARF1-mediated pathway for COPI recruitment.
Monetta et al. (2007) found that the GTP-bound form of human RAB1B
enhanced membrane association of GBF1 and COPI at ER exit sites (ERES).
RAB1B also modulated ARF1-induced membrane association and dissociation
at the Golgi. Through an N-terminal domain, RAB1B-GTP, but not
RAB1B-GDP, interacted directly with GBF1, and RAB1B was required for
GBF1 membrane association at Golgi structures. In RAB1B-depleted HeLa
cells, GBF1 and beta-COP redistributed from the juxtanuclear region to a
diffuse, cytosolic pattern. RAB1B also colocalized with COPII (see
610511)/ERES, with transport-associated vesicular tubular clusters, and
with COPI structures. Monetta et al. (2007) proposed that RAB1B-GTP
induces GBF1 recruitment at the ERES interface and at the Golgi complex,
where it is required for COPII/COPI exchange or COPI vesicle formation,
respectively.
By mixing the Legionella pneumophila effector protein DrrA with RAB1B
and ATP, Mueller et al. (2010) found that the N-terminal domain of DrrA
transferred AMP to (i.e., AMPylated) tyr77 in the switch II region of
RAB1B, but not other RAB proteins. DrrA-mediated AMPylation was required
for the Legionella effector protein to mediate cytotoxicity.
GENE STRUCTURE
He et al. (2002) determined that the RAB1B gene contains 6 exons and
spans over 28.5 kb.
MAPPING
By radiation hybrid analysis, He et al. (2002) mapped the RAB1B gene to
chromosome 11q13.
Hartz (2009) mapped the RAB1B gene to chromosome 11q13.1 based on an
alignment of the RAB1B sequence (GenBank GENBANK AJ245875) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Alvarez, C.; Garcia-Mata, R.; Brandon, E.; Sztul, E.: COPI recruitment
is modulated by a Rab1b-dependent mechanism. Molec. Biol. Cell 14:
2116-2127, 2003.
2. Chen, D.; Guo, J.; Gahl, W. A.: RAB GTPases expressed in human
melanoma cells. Biochim. Biophys. Acta 1355: 1-6, 1997.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/29/2009.
4. He, H.; Dai, F.; Yu, L.; She, X.; Zhao, Y.; Jiang, J.; Chen, X.;
Zhao, S.: Identification and characterization of nine novel human
small GTPases showing variable expressions in liver cancer tissues. Gene
Expr. 10: 231-242, 2002.
5. Monetta, P.; Slavin, I.; Romero, N.; Alvarez, C.: Rab1b interacts
with GBF1 and modulates both ARF1 dynamics and COPI association. Molec.
Biol. Cell 18: 2400-2410, 2007.
6. Mueller, M. P.; Peters, H.; Blumer, J.; Blankenfeldt, W.; Goody,
R. S.; Itzen, A.: The Legionella effector protein DrrA AMPylates
the membrane traffic regulator Rab1b. Science 329: 946-949, 2010.
*FIELD* CN
Paul J. Converse - updated: 9/15/2010
Patricia A. Hartz - updated: 7/23/2009
*FIELD* CD
Patricia A. Hartz: 1/29/2009
*FIELD* ED
mgross: 09/20/2010
mgross: 9/20/2010
terry: 9/15/2010
mgross: 8/18/2009
terry: 7/23/2009
mgross: 1/29/2009
*RECORD*
*FIELD* NO
612565
*FIELD* TI
*612565 RAS-ASSOCIATED PROTEIN RAB1B; RAB1B
*FIELD* TX
DESCRIPTION
Members of the RAB protein family, such as RAB1B, are low molecular mass
read moremonomeric GTPases localized on the cytoplasmic surfaces of distinct
membrane-bound organelles. RAB1B functions in the early secretory
pathway and is essential for vesicle transport between the endoplasmic
reticulum (ER) and Golgi (Chen et al., 1997; Alvarez et al., 2003).
CLONING
By PCR using degenerate primers based on conserved sequences in human
RAB transcripts, Chen et al. (1997) obtained a partial RAB1B cDNA from a
pigmented human melanoma cell cDNA library. The deduced 53-amino acid
stretch spans GTP-binding domains II and III and has only 1 or 2 amino
acid changes from the homologous stretch in rat Rab1b and human RAB1A
(179508), respectively. RAB1B appeared to be a low-abundance transcript
in the human melanoma cells.
By searching databases for RAS family members, followed by PCR, He et
al. (2002) cloned RAB1B. The deduced 201-amino acid RAB1B protein
contains 4 highly conserved GTPase motifs and a C-terminal
geranylgeranylation motif. Northern blot analysis detected strong
expression of a major transcript of about 2.4 kb in all tissues
examined.
GENE FUNCTION
Alvarez et al. (2003) found that expression of the RAB1B asn121-to-ile
(N121I) mutant, which is impaired in guanine nucleotide binding, blocked
forward transport of vesicles from the Golgi to the ER and induced Golgi
disruption in HeLa cells. The N121I mutant caused a phenotype analogous
to that induced by brefeldin A (BFA): it caused resident Golgi proteins
to relocate to the ER, and it induced redistribution of the ER-Golgi
intermediate compartment proteins ERGIC53 (LMAN1; 601567), GM130
(GOLGA2; 602580), and p115 (603344) to punctate structures. N121I caused
dissociation of beta-COP (COPB; 600959) from membranes, implicating
RAB1B in a pathway leading to the recruitment of the coatomer complex
(COPI; 601924). The N121I phenotype was rescued by expression of ARF1
(103180) and GBF1 (603698), which mediate COPI recruitment. Like
expression of ARF1 and GBF1, expression of a constitutively active RAB1B
gln67-to-leu (Q67L) mutant prevented Golgi fragmentation and beta-COP
dissociation in BFA-treated cells. Alvarez et al. (2003) concluded that
RAB1B has a role in the GBF1/ARF1-mediated pathway for COPI recruitment.
Monetta et al. (2007) found that the GTP-bound form of human RAB1B
enhanced membrane association of GBF1 and COPI at ER exit sites (ERES).
RAB1B also modulated ARF1-induced membrane association and dissociation
at the Golgi. Through an N-terminal domain, RAB1B-GTP, but not
RAB1B-GDP, interacted directly with GBF1, and RAB1B was required for
GBF1 membrane association at Golgi structures. In RAB1B-depleted HeLa
cells, GBF1 and beta-COP redistributed from the juxtanuclear region to a
diffuse, cytosolic pattern. RAB1B also colocalized with COPII (see
610511)/ERES, with transport-associated vesicular tubular clusters, and
with COPI structures. Monetta et al. (2007) proposed that RAB1B-GTP
induces GBF1 recruitment at the ERES interface and at the Golgi complex,
where it is required for COPII/COPI exchange or COPI vesicle formation,
respectively.
By mixing the Legionella pneumophila effector protein DrrA with RAB1B
and ATP, Mueller et al. (2010) found that the N-terminal domain of DrrA
transferred AMP to (i.e., AMPylated) tyr77 in the switch II region of
RAB1B, but not other RAB proteins. DrrA-mediated AMPylation was required
for the Legionella effector protein to mediate cytotoxicity.
GENE STRUCTURE
He et al. (2002) determined that the RAB1B gene contains 6 exons and
spans over 28.5 kb.
MAPPING
By radiation hybrid analysis, He et al. (2002) mapped the RAB1B gene to
chromosome 11q13.
Hartz (2009) mapped the RAB1B gene to chromosome 11q13.1 based on an
alignment of the RAB1B sequence (GenBank GENBANK AJ245875) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Alvarez, C.; Garcia-Mata, R.; Brandon, E.; Sztul, E.: COPI recruitment
is modulated by a Rab1b-dependent mechanism. Molec. Biol. Cell 14:
2116-2127, 2003.
2. Chen, D.; Guo, J.; Gahl, W. A.: RAB GTPases expressed in human
melanoma cells. Biochim. Biophys. Acta 1355: 1-6, 1997.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/29/2009.
4. He, H.; Dai, F.; Yu, L.; She, X.; Zhao, Y.; Jiang, J.; Chen, X.;
Zhao, S.: Identification and characterization of nine novel human
small GTPases showing variable expressions in liver cancer tissues. Gene
Expr. 10: 231-242, 2002.
5. Monetta, P.; Slavin, I.; Romero, N.; Alvarez, C.: Rab1b interacts
with GBF1 and modulates both ARF1 dynamics and COPI association. Molec.
Biol. Cell 18: 2400-2410, 2007.
6. Mueller, M. P.; Peters, H.; Blumer, J.; Blankenfeldt, W.; Goody,
R. S.; Itzen, A.: The Legionella effector protein DrrA AMPylates
the membrane traffic regulator Rab1b. Science 329: 946-949, 2010.
*FIELD* CN
Paul J. Converse - updated: 9/15/2010
Patricia A. Hartz - updated: 7/23/2009
*FIELD* CD
Patricia A. Hartz: 1/29/2009
*FIELD* ED
mgross: 09/20/2010
mgross: 9/20/2010
terry: 9/15/2010
mgross: 8/18/2009
terry: 7/23/2009
mgross: 1/29/2009