RAB1A_HUMAN
ID RAB1A_HUMAN Reviewed; 205 AA.
AC P62820; P11476; Q6FIE7; Q96N61; Q9Y3T2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ras-related protein Rab-1A;
DE EC=3.6.5.2 {ECO:0000269|PubMed:22939626};
DE AltName: Full=YPT1-related protein;
GN Name=RAB1A; Synonyms=RAB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2501306; DOI=10.1016/s0021-9258(18)63872-4;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related to
RT yeast YPT1 and SEC4 products involved in secretion.";
RL J. Biol. Chem. 264:12394-12401(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-30; 52-58; 62-72; 75-111; 176-187 AND 192-198,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [10]
RP PHOSPHORYLATION AT SER-194 BY CDK1.
RX PubMed=1902553; DOI=10.1038/350715a0;
RA Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.;
RT "Phosphorylation of two small GTP-binding proteins of the Rab family by
RT p34cdc2.";
RL Nature 350:715-718(1991).
RN [11]
RP ISOPRENYLATION AT CYS-204 AND CYS-205, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=7991565; DOI=10.1073/pnas.91.25.11963;
RA Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.;
RT "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of
RT adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994).
RN [12]
RP REVIEW.
RX PubMed=19603039; DOI=10.1038/nrm2728;
RA Stenmark H.;
RT "Rab GTPases as coordinators of vesicle traffic.";
RL Nat. Rev. Mol. Cell Biol. 10:513-525(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ASN-124.
RX PubMed=20861236; DOI=10.1210/en.2010-0422;
RA Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.;
RT "Rab1 small GTP-binding protein regulates cell surface trafficking of the
RT human calcium-sensing receptor.";
RL Endocrinology 151:5114-5123(2010).
RN [15]
RP FUNCTION.
RX PubMed=20639577; DOI=10.1074/jbc.m110.141440;
RA Wang C., Yoo Y., Fan H., Kim E., Guan K.L., Guan J.L.;
RT "Regulation of integrin beta 1 recycling to lipid rafts by Rab1a to promote
RT cell migration.";
RL J. Biol. Chem. 285:29398-29405(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21303926; DOI=10.1242/jcs.079020;
RA Mukhopadhyay A., Nieves E., Che F.Y., Wang J., Jin L., Murray J.W.,
RA Gordon K., Angeletti R.H., Wolkoff A.W.;
RT "Proteomic analysis of endocytic vesicles: Rab1a regulates motility of
RT early endocytic vesicles.";
RL J. Cell Sci. 124:765-775(2011).
RN [18]
RP INTERACTION WITH L.PNEUMOPHILA ANKX (MICROBIAL INFECTION), AND
RP PHOSPHORYLATION AT SER-79 (MICROBIAL INFECTION).
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 [19]
RP INTERACTION WITH L.PNEUMOPHILA LEM3 (MICROBIAL INFECTION), AND
RP PHOSPHORYLATION AT SER-79 (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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GDI1.
RX PubMed=23815289; DOI=10.3109/09687688.2013.818725;
RA Kirsten M.L., Baron R.A., Seabra M.C., Ces O.;
RT "Rab1a and Rab5a preferentially bind to binary lipid compositions with
RT higher stored curvature elastic energy.";
RL Mol. Membr. Biol. 30:303-314(2013).
RN [23]
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 [24]
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 [25]
RP INTERACTION WITH C9ORF72.
RX PubMed=27334615; DOI=10.15252/embj.201694401;
RA Webster C.P., Smith E.F., Bauer C.S., Moller A., Hautbergue G.M.,
RA Ferraiuolo L., Myszczynska M.A., Higginbottom A., Walsh M.J.,
RA Whitworth A.J., Kaspar B.K., Meyer K., Shaw P.J., Grierson A.J.,
RA De Vos K.J.;
RT "The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate
RT initiation of autophagy.";
RL EMBO J. 35:1656-1676(2016).
RN [26]
RP GLYCOSYLATION AT ARG-72; ARG-74; ARG-82 AND ARG-111 (MICROBIAL INFECTION),
RP AND MUTAGENESIS OF 72-ARG--ARG-74; ARG-82 AND ARG-111.
RX PubMed=32504010; DOI=10.1038/s42003-020-1005-2;
RA Meng K., Zhuang X., Peng T., Hu S., Yang J., Wang Z., Fu J., Xue J.,
RA Pan X., Lv J., Liu X., Shao F., Li S.;
RT "Arginine GlcNAcylation of Rab small GTPases by the pathogen Salmonella
RT Typhimurium.";
RL Commun. Biol. 3:287-287(2020).
RN [27]
RP GLYCOSYLATION AT ARG-74; ARG-82 AND ARG-111 (MICROBIAL INFECTION), AND
RP MUTAGENESIS OF ARG-74; ARG-82 AND ARG-111.
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 [28]
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 6-177 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human RAB1A in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 4-178 OF MUTANT ILE-124 IN
RP COMPLEX WITH L.PNEUMOPHILA DRRA, GTP-BINDING, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GDI1 AND L.PNEUMOPHILA DRRA (MICROBIAL INFECTION).
RX PubMed=19942850; DOI=10.1038/emboj.2009.347;
RA Suh H.Y., Lee D.W., Lee K.H., Ku B., Choi S.J., Woo J.S., Kim Y.G.,
RA Oh B.H.;
RT "Structural insights into the dual nucleotide exchange and GDI displacement
RT activity of SidM/DrrA.";
RL EMBO J. 29:496-504(2010).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-177 IN COMPLEX WITH
RP L.PNEUMOPHILA DRRA, AND INTERACTION WITH GDI1 AND L.PNEUMOPHILA DRRA
RP (MICROBIAL INFECTION).
RX PubMed=20176951; DOI=10.1073/pnas.0914231107;
RA Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F.;
RT "Structural mechanism of host Rab1 activation by the bifunctional
RT Legionella type IV effector SidM/DrrA.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4699-4704(2010).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-176 IN COMPLEXES WITH GDP;
RP ARF6; E.COLI ESPG AND S.FLEXNERI VIRA, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ARF6 AND E.COLI
RP ESPG, AND INTERACTION WITH E.COLI ESPG AND S.FLEXNERI VIRA.
RX PubMed=22939626; DOI=10.1016/j.cell.2012.06.050;
RA Dong N., Zhu Y., Lu Q., Hu L., Zheng Y., Shao F.;
RT "Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1
RT inactivation to counteract host defenses.";
RL Cell 150:1029-1041(2012).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-176 IN COMPLEXES WITH GTP; GDP
RP AND L.PNEUMOPHILA LIDA, AND INTERACTION WITH L.PNEUMOPHILA LIDA.
RX PubMed=22416225; DOI=10.1371/journal.ppat.1002528;
RA Cheng W., Yin K., Lu D., Li B., Zhu D., Chen Y., Zhang H., Xu S., Chai J.,
RA Gu L.;
RT "Structural insights into a unique Legionella pneumophila effector LidA
RT recognizing both GDP and GTP bound Rab1 in their active state.";
RL PLoS Pathog. 8:E1002528-E1002528(2012).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP AND
RP L.DRANCOURTII LEPB, AND INTERACTION WITH L.PNEUMOPHILA AND L.DRANCOURTII
RP LEPB.
RX PubMed=23588383; DOI=10.1038/cr.2013.54;
RA Yu Q., Hu L., Yao Q., Zhu Y., Dong N., Wang D.C., Shao F.;
RT "Structural analyses of Legionella LepB reveal a new GAP fold that
RT catalytically mimics eukaryotic RasGAP.";
RL Cell Res. 23:775-787(2013).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 4-177 IN COMPLEX WITH GDP AND
RP L.PNEUMOPHILA LEPB, AND INTERACTION WITH L.PNEUMOPHILA LEPB.
RX PubMed=23821544; DOI=10.1074/jbc.m113.470625;
RA Mishra A.K., Del Campo C.M., Collins R.E., Roy C.R., Lambright D.G.;
RT "The Legionella pneumophila GTPase activating protein LepB accelerates Rab1
RT deactivation by a non-canonical hydrolytic mechanism.";
RL J. Biol. Chem. 288:24000-24011(2013).
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:20639577, PubMed:20861236,
CC PubMed:21303926, PubMed:22939626). Rabs cycle between an inactive GDP-
CC bound form and an active GTP-bound form that is able to recruit to
CC membranes different sets of downstream effectors directly responsible
CC for vesicle formation, movement, tethering and fusion (PubMed:20639577,
CC PubMed:20861236, PubMed:21303926, PubMed:22939626). RAB1A regulates
CC vesicular protein transport from the endoplasmic reticulum (ER) to the
CC Golgi compartment and on to the cell surface, and plays a role in IL-8
CC and growth hormone secretion (PubMed:21303926). Required to modulate
CC the compacted morphology of the Golgi (PubMed:26209634). Regulates the
CC level of CASR present at the cell membrane (PubMed:20861236). Plays a
CC role in cell adhesion and cell migration, via its role in protein
CC trafficking (PubMed:20639577). Plays a role in autophagosome assembly
CC and cellular defense reactions against pathogenic bacteria
CC (PubMed:22939626). Plays a role in microtubule-dependent protein
CC transport by early endosomes and in anterograde melanosome transport
CC (By similarity). {ECO:0000250|UniProtKB:P62821,
CC ECO:0000269|PubMed:20639577, ECO:0000269|PubMed:20861236,
CC ECO:0000269|PubMed:21303926, ECO:0000269|PubMed:22939626,
CC ECO:0000269|PubMed:26209634}.
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:0000269|PubMed:22939626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:22939626};
CC -!- SUBUNIT: May interact with YIPF5 (By similarity). Interacts with
CC C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1
CC kinase complex (PubMed:27334615). Interacts with GDI1; this promotes
CC dissociation from membranes (PubMed:23815289, PubMed:20176951).
CC {ECO:0000250|UniProtKB:P62822, ECO:0000269|PubMed:20176951,
CC ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:27334615}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila AnkX.
CC {ECO:0000269|PubMed:21822290}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila Lem3.
CC {ECO:0000269|PubMed:22158903}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila LidA.
CC {ECO:0000269|PubMed:22416225}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila DrrA; this
CC disrupts the interaction between RAB1A and GDI1 and promotes the
CC exchange of RAB1A-bound GDP with GTP. {ECO:0000269|PubMed:19942850,
CC ECO:0000269|PubMed:20176951}.
CC -!- SUBUNIT: (Microbial infection) Interacts with E.coli EspG and
CC S.flexneri VirA; this impairs ER to Golgi trafficking and protein
CC secretion. {ECO:0000269|PubMed:22939626}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila and
CC L.drancourtii LepB; this enhances RAB1A GTPase activity.
CC {ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544}.
CC -!- SUBUNIT: (Microbial infection) Identified in a complex composed of
CC RAB1A, ARF6 and E.coli EspG. {ECO:0000269|PubMed:22939626}.
CC -!- INTERACTION:
CC P62820; Q96LT7-1: C9orf72; NbExp=5; IntAct=EBI-716845, EBI-16693635;
CC P62820; Q96LT7-2: C9orf72; NbExp=4; IntAct=EBI-716845, EBI-16693673;
CC P62820; P31150: GDI1; NbExp=3; IntAct=EBI-716845, EBI-946999;
CC P62820; P42345: MTOR; NbExp=4; IntAct=EBI-716845, EBI-359260;
CC P62820; Q01968: OCRL; NbExp=8; IntAct=EBI-716845, EBI-6148898;
CC P62820; P47224: RABIF; NbExp=3; IntAct=EBI-716845, EBI-713992;
CC P62820; Q8N122: RPTOR; NbExp=4; IntAct=EBI-716845, EBI-1567928;
CC P62820; Q5ZSQ3: drrA; Xeno; NbExp=7; IntAct=EBI-716845, EBI-7632432;
CC P62820-1; P50395: GDI2; NbExp=2; IntAct=EBI-15666813, EBI-1049143;
CC P62820-1; Q29ST3: drrA; Xeno; NbExp=3; IntAct=EBI-15666813, EBI-15838677;
CC P62820-1; Q6X1Y7: lepB; Xeno; NbExp=2; IntAct=EBI-15666813, EBI-15666803;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:22939626}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:22939626}. Early endosome
CC {ECO:0000269|PubMed:21303926}. Cytoplasm, cytosol
CC {ECO:0000305|PubMed:19942850}. Membrane {ECO:0000269|PubMed:19942850,
CC ECO:0000269|PubMed:23815289}. Melanosome
CC {ECO:0000250|UniProtKB:P62821}. Note=Alternates between membrane-
CC associated and cytosolic forms. {ECO:0000305|PubMed:19942850}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P62820-1, P11476-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P62820-2, P11476-2;
CC Sequence=VSP_005525;
CC Name=3;
CC IsoId=P62820-3, P11476-3;
CC Sequence=VSP_005526;
CC -!- PTM: Phosphorylated by CDK1 kinase during mitosis.
CC {ECO:0000269|PubMed:1902553, ECO:0000269|PubMed:21822290,
CC ECO:0000269|PubMed:22158903}.
CC -!- PTM: (Microbial infection) Phosphocholinated at Ser-79 by L.pneumophila
CC AnkX, leading to displace GDP dissociation inhibitors (GDI)
CC (PubMed:21822290). Both GDP-bound and GTP-bound forms can be
CC phosphocholinated. Dephosphocholinated by L.pneumophila Lem3, restoring
CC accessibility to L.pneumophila GTPase effector LepB (PubMed:22158903).
CC {ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903}.
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:32504010,
CC ECO:0000269|PubMed:32974215}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M28209; AAA60240.1; -; mRNA.
DR EMBL; AL050268; CAB43369.1; -; mRNA.
DR EMBL; BX571747; CAE11872.1; -; mRNA.
DR EMBL; AK055927; BAB71048.1; -; mRNA.
DR EMBL; AF498929; AAM21077.1; -; mRNA.
DR EMBL; CR533479; CAG38510.1; -; mRNA.
DR EMBL; CH471053; EAW99921.1; -; Genomic_DNA.
DR EMBL; BC000905; AAH00905.1; -; mRNA.
DR CCDS; CCDS46305.1; -. [P62820-3]
DR CCDS; CCDS46306.1; -.
DR PIR; A34323; TVHUYP.
DR RefSeq; NP_004152.1; NM_004161.4. [P62820-1]
DR RefSeq; NP_056358.1; NM_015543.1. [P62820-3]
DR PDB; 2FOL; X-ray; 2.63 A; A=6-177.
DR PDB; 2WWX; X-ray; 1.50 A; A=4-178.
DR PDB; 3L0I; X-ray; 2.85 A; B/D=1-177.
DR PDB; 3SFV; X-ray; 1.73 A; A=1-176.
DR PDB; 3TKL; X-ray; 2.18 A; A=1-191.
DR PDB; 4FMB; X-ray; 3.20 A; B/D/F=6-176.
DR PDB; 4FMC; X-ray; 2.80 A; B/D=6-176, F=14-115.
DR PDB; 4FMD; X-ray; 3.05 A; B/D=6-176, F=13-176.
DR PDB; 4FME; X-ray; 4.10 A; B/E=6-176.
DR PDB; 4IRU; X-ray; 3.20 A; B/D/F=4-177.
DR PDB; 4JVS; X-ray; 2.78 A; B=1-177.
DR PDBsum; 2FOL; -.
DR PDBsum; 2WWX; -.
DR PDBsum; 3L0I; -.
DR PDBsum; 3SFV; -.
DR PDBsum; 3TKL; -.
DR PDBsum; 4FMB; -.
DR PDBsum; 4FMC; -.
DR PDBsum; 4FMD; -.
DR PDBsum; 4FME; -.
DR PDBsum; 4IRU; -.
DR PDBsum; 4JVS; -.
DR AlphaFoldDB; P62820; -.
DR SMR; P62820; -.
DR BioGRID; 111799; 333.
DR DIP; DIP-1063N; -.
DR IntAct; P62820; 87.
DR MINT; P62820; -.
DR STRING; 9606.ENSP00000387286; -.
DR ChEMBL; CHEMBL3879826; -.
DR GlyGen; P62820; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62820; -.
DR MetOSite; P62820; -.
DR PhosphoSitePlus; P62820; -.
DR SwissPalm; P62820; -.
DR BioMuta; RAB1A; -.
DR DMDM; 51338603; -.
DR EPD; P62820; -.
DR jPOST; P62820; -.
DR MassIVE; P62820; -.
DR MaxQB; P62820; -.
DR PaxDb; P62820; -.
DR PeptideAtlas; P62820; -.
DR PRIDE; P62820; -.
DR ProteomicsDB; 57426; -.
DR ProteomicsDB; 57427; -. [P62820-2]
DR ProteomicsDB; 57428; -. [P62820-3]
DR Antibodypedia; 3942; 188 antibodies from 31 providers.
DR DNASU; 5861; -.
DR Ensembl; ENST00000398529.7; ENSP00000381540.3; ENSG00000138069.18. [P62820-3]
DR Ensembl; ENST00000409784.8; ENSP00000387286.3; ENSG00000138069.18. [P62820-1]
DR Ensembl; ENST00000409892.5; ENSP00000386451.1; ENSG00000138069.18. [P62820-2]
DR Ensembl; ENST00000649427.1; ENSP00000497078.1; ENSG00000138069.18. [P62820-1]
DR GeneID; 5861; -.
DR KEGG; hsa:5861; -.
DR MANE-Select; ENST00000409784.8; ENSP00000387286.3; NM_004161.5; NP_004152.1.
DR UCSC; uc002sdn.4; human.
DR CTD; 5861; -.
DR DisGeNET; 5861; -.
DR GeneCards; RAB1A; -.
DR HGNC; HGNC:9758; RAB1A.
DR HPA; ENSG00000138069; Low tissue specificity.
DR MIM; 179508; gene.
DR neXtProt; NX_P62820; -.
DR OpenTargets; ENSG00000138069; -.
DR PharmGKB; PA34107; -.
DR VEuPathDB; HostDB:ENSG00000138069; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000154958; -.
DR HOGENOM; CLU_041217_10_7_1; -.
DR InParanoid; P62820; -.
DR OMA; DCTDLES; -.
DR PhylomeDB; P62820; -.
DR TreeFam; TF300097; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P62820; -.
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 SignaLink; P62820; -.
DR SIGNOR; P62820; -.
DR BioGRID-ORCS; 5861; 142 hits in 1105 CRISPR screens.
DR ChiTaRS; RAB1A; human.
DR EvolutionaryTrace; P62820; -.
DR GeneWiki; RAB1A; -.
DR GenomeRNAi; 5861; -.
DR Pharos; P62820; Tbio.
DR PRO; PR:P62820; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P62820; protein.
DR Bgee; ENSG00000138069; Expressed in sperm and 209 other tissues.
DR ExpressionAtlas; P62820; baseline and differential.
DR Genevisible; P62820; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0030252; P:growth hormone secretion; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; IGI:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0019068; P:virion assembly; IMP: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; Alternative splicing; Autophagy; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Endosome;
KW ER-Golgi transport; Glycoprotein; Golgi apparatus; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895"
FT CHAIN 2..205
FT /note="Ras-related protein Rab-1A"
FT /id="PRO_0000121056"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22416225,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383,
FT ECO:0000269|PubMed:23821544, ECO:0007744|PDB:2FOL,
FT ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL,
FT ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC,
FT ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME,
FT ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22416225,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383,
FT ECO:0000269|PubMed:23821544, ECO:0007744|PDB:2FOL,
FT ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL,
FT ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FME,
FT ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22416225,
FT ECO:0007744|PDB:3TKL"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22416225,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383,
FT ECO:0000269|PubMed:23821544, ECO:0007744|PDB:2FOL,
FT ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL,
FT ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC,
FT ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME,
FT ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22416225,
FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383,
FT ECO:0000269|PubMed:23821544, ECO:0007744|PDB:2FOL,
FT ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL,
FT ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC,
FT ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME,
FT ECO:0007744|PDB:4IRU, ECO:0007744|PDB:4JVS"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895"
FT MOD_RES 79
FT /note="(Microbial infection) O-(2-cholinephosphoryl)serine"
FT /evidence="ECO:0000269|PubMed:21822290,
FT ECO:0000269|PubMed:22158903"
FT MOD_RES 194
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000305|PubMed:1902553"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:7991565"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:7991565"
FT CARBOHYD 72
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:32504010"
FT CARBOHYD 74
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:32504010,
FT ECO:0000269|PubMed:32974215"
FT CARBOHYD 82
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:32504010,
FT ECO:0000269|PubMed:32974215"
FT CARBOHYD 111
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:32504010,
FT ECO:0000269|PubMed:32974215"
FT VAR_SEQ 33..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005525"
FT VAR_SEQ 65..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.6"
FT /id="VSP_005526"
FT MUTAGEN 72..74
FT /note="RFR->AFA: Abolished arginine GlcNAcylation; when
FT associated with A-82 and A-111."
FT /evidence="ECO:0000269|PubMed:32504010"
FT MUTAGEN 74
FT /note="R->A: Abolished arginine GlcNAcylation; when
FT associated with A-82 and A-111."
FT /evidence="ECO:0000269|PubMed:32974215"
FT MUTAGEN 82
FT /note="R->A: Abolished arginine GlcNAcylation; when
FT associated with A-74 and A-111. Abolished arginine
FT GlcNAcylation; when associated with 72-A--A-74 and A-111."
FT /evidence="ECO:0000269|PubMed:32504010,
FT ECO:0000269|PubMed:32974215"
FT MUTAGEN 111
FT /note="R->A: Abolished arginine GlcNAcylation; when
FT associated with A-74 and A-82. Abolished arginine
FT GlcNAcylation; when associated with 72-A--A-74 and A-82."
FT /evidence="ECO:0000269|PubMed:32504010,
FT ECO:0000269|PubMed:32974215"
FT MUTAGEN 124
FT /note="N->I: Dominant negative mutant. Strongly reduces the
FT levels of CASR present at the cell-surface."
FT /evidence="ECO:0000269|PubMed:20861236"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:2WWX"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:2WWX"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3L0I"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:2WWX"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:2WWX"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:2WWX"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2WWX"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2WWX"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3SFV"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:2WWX"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:2WWX"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2WWX"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3SFV"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:2WWX"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2WWX"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3SFV"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:2WWX"
SQ SEQUENCE 205 AA; 22678 MW; B2A8F4E3B0FB17D6 CRC64;
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA
TAGGAEKSNV KIQSTPVKQS GGGCC
