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 02-SEP-2026, entry version 206. 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 FUNCTION, UBIQUITINATION BY RNF115 AT LYS-49 AND LYS-61, AND MUTAGENESIS OF RP LYS-49 AND LYS-61. RX PubMed=35343654; DOI=10.1002/advs.202105391; RA Zhang Z.D., Li H.X., Gan H., Tang Z., Guo Y.Y., Yao S.Q., Liuyu T., RA Zhong B., Lin D.; RT "RNF115 Inhibits the Post-ER Trafficking of TLRs and TLRs-Mediated Immune RT Responses by Catalyzing K11-Linked Ubiquitination of RAB1A and RAB13."; RL Adv. Sci. 9:0-0(2022). RN [29] {ECO:0007744|PDB:2FOL} RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 6-177 IN COMPLEX WITH GDP AND RP MG(2+), AND COFACTOR. 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 [30] {ECO:0007744|PDB:2WWX} 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 [31] {ECO:0007744|PDB:3L0I} 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 [32] {ECO:0007744|PDB:4FMB, ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, ECO:0007744|PDB:4FME} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-176 IN COMPLEXES WITH GDP AND RP MG(2+); ARF6; E.COLI ESPG AND S.FLEXNERI VIRA, FUNCTION, CATALYTIC RP ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ARF6 AND RP E.COLI ESPG, INTERACTION WITH E.COLI ESPG AND S.FLEXNERI VIRA, AND RP COFACTOR. 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 [33] {ECO:0007744|PDB:3SFV, ECO:0007744|PDB:3TKL} RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1-176 IN COMPLEXES WITH GTP; GDP; RP MG(2+) AND L.PNEUMOPHILA LIDA, INTERACTION WITH L.PNEUMOPHILA LIDA, RP COFACTOR, AND DOMAIN. 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 [34] {ECO:0007744|PDB:4JVS} RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 1-177 IN COMPLEX WITH GDP; MG(2+) RP AND L.DRANCOURTII LEPB, INTERACTION WITH L.PNEUMOPHILA AND L.DRANCOURTII RP LEPB, AND COFACTOR. 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 [35] {ECO:0007744|PDB:4IRU} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 4-177 IN COMPLEX WITH GDP; MG(2+) RP AND L.PNEUMOPHILA LEPB, INTERACTION WITH L.PNEUMOPHILA LEPB, AND COFACTOR. 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 + phosphate + H(+); 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:22416225, ECO:0000269|PubMed:22939626, CC ECO:0000269|PubMed:23588383, ECO:0000269|PubMed:23821544, CC ECO:0000269|Ref.29}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP. Regulated CC by GTPase activating proteins (GAPs) which increase the GTP hydrolysis CC activity (Probable). Inhibited by GDP dissociation inhibitors (GDIs) CC (Probable). {ECO:0000305}. 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:20176951, PubMed:23815289). 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=7; 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=5; IntAct=EBI-716845, EBI-713992; CC P62820; Q8N122: RPTOR; NbExp=4; IntAct=EBI-716845, EBI-1567928; CC P62820; Q29ST3: drrA; Xeno; NbExp=2; IntAct=EBI-716845, EBI-15838677; CC P62820; Q5ZSQ3: drrA; Xeno; NbExp=7; IntAct=EBI-716845, EBI-7632432; CC P62820; Q5ZU30: setA; Xeno; NbExp=3; IntAct=EBI-716845, EBI-40253342; 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; Sequence=Displayed; CC Name=2; CC IsoId=P62820-2, P11476-2; Sequence=VSP_005525; CC Name=3; CC IsoId=P62820-3, P11476-3; Sequence=VSP_005526; CC -!- DOMAIN: Switch I, switch II and the interswitch regions are CC characteristic of Rab GTPases and mediate the interactions with Rab CC downstream effectors. The switch regions undergo conformational changes CC upon nucleotide binding which drive interaction with specific sets of CC effector proteins, with most effectors only binding to GTP-bound Rab. CC {ECO:0000269|PubMed:22416225}. 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 -!- PTM: Ubiquitinated via 'Lys-11'-linked ubiquitination on Lys-49 and CC Lys-61; impairing the recruitment of guanosine diphosphate (GDP) CC dissociation inhibitor 1/GDI1. {ECO:0000250|UniProtKB:P51153}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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_004161.5. [P62820-1] DR RefSeq; NP_056358.1; NM_015543.2. [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 PDB; 7EQ2; X-ray; 1.55 A; A/B=1-176. DR PDB; 9MHF; EM; 2.73 A; E=1-205. DR PDB; 9MHG; EM; 3.20 A; E=1-205. DR PDB; 9MHH; EM; 4.50 A; E=1-205. DR AlphaFoldDB; P62820; -. DR EMDB; EMD-48276; -. DR EMDB; EMD-48277; -. DR EMDB; EMD-48278; -. DR SASBDB; P62820; -. DR SMR; P62820; -. DR BioGRID; 111799; 485. DR DIP; DIP-1063N; -. DR FunCoup; P62820; 3469. DR IntAct; P62820; 153. DR MINT; P62820; -. DR NDEx; IQUERY-CP-RAB1A; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000387286; -. DR BindingDB; P62820; -. DR ChEMBL; CHEMBL3879826; -. DR GlyCosmos; P62820; 4 sites, No reported glycans. 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 jPOST; P62820; -. DR MassIVE; P62820; -. DR PaxDb; 9606-ENSP00000387286; -. DR PeptideAtlas; P62820; -. DR PRIDE; P62820; -. DR ProteomicsDB; 57426; -. DR ProteomicsDB; 57427; -. [P62820-2] DR ProteomicsDB; 57428; -. [P62820-3] DR Pumba; P62820; -. DR Antibodypedia; 3942; 211 antibodies from 32 providers. DR DNASU; 5861; -. DR YCharOS; P62820; Tested 7 antibodies from 5 manufacturers. DR Ensembl; ENST00000398529.7; ENSP00000381540.3; ENSG00000138069.19. [P62820-3] DR Ensembl; ENST00000409784.8; ENSP00000387286.3; ENSG00000138069.19. [P62820-1] DR Ensembl; ENST00000409892.5; ENSP00000386451.1; ENSG00000138069.19. [P62820-2] DR Ensembl; ENST00000649427.1; ENSP00000497078.1; ENSG00000138069.19. [P62820-1] DR Ensembl; ENST00000931493.1; ENSP00000601552.1; ENSG00000138069.19. [P62820-1] DR Ensembl; ENST00000931495.1; ENSP00000601554.1; ENSG00000138069.19. [P62820-1] DR Ensembl; ENST00000931496.1; ENSP00000601555.1; ENSG00000138069.19. [P62820-1] DR Ensembl; ENST00000970485.1; ENSP00000640544.1; ENSG00000138069.19. [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 AGR; HGNC:9758; -. DR ClinPGx; PA34107; -. 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 OpenTargets; ENSG00000138069; -. DR Orphanet; 717830; 2p14p15 microdeletion syndrome. DR VEuPathDB; HostDB:ENSG00000138069; -. DR eggNOG; KOG0084; Eukaryota. DR GeneTree; ENSGT00940000154958; -. DR HOGENOM; CLU_041217_10_7_1; -. DR InParanoid; P62820; -. DR OMA; IPHVEIS; -. DR OrthoDB; 9989112at2759; -. DR PAN-GO; P62820; 4 GO annotations based on evolutionary models. DR PhylomeDB; P62820; -. 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 Agora; ENSG00000138069; -. DR BioGRID-ORCS; 5861; 148 hits in 1187 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 211 other cell types or tissues. DR ExpressionAtlas; P62820; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005769; C:early endosome; EXP:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; EXP:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0042470; C:melanosome; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; EXP:UniProtKB. 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; IMP:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. 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: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 CDD; cd01869; Rab1_Ypt1; 1. DR FunFam; 3.40.50.300:FF:000069; Ras GTP-binding protein YPT1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR050227; Rab. DR InterPro; IPR057289; Rab1/Ypt1. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR 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 PDBsum; 7EQ2; -. DR PDBsum; 9MHF; -. DR PDBsum; 9MHG; -. DR PDBsum; 9MHH; -. 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 Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; KW Proteomics identification; Reference proteome; Transport; Ubl conjugation. 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 38..46 FT /note="Switch-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753, FT ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3SFV, FT ECO:0007744|PDB:3TKL" FT REGION 69..85 FT /note="Switch-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753, FT ECO:0000269|PubMed:22416225, ECO:0007744|PDB:3SFV, FT ECO:0007744|PDB:3TKL" FT REGION 178..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 25 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, FT ECO:0000269|PubMed:23821544, ECO:0000269|Ref.29, FT ECO:0007744|PDB:2FOL, 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 26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 38 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 43 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, FT ECO:0000269|PubMed:23821544, ECO:0000269|Ref.29, FT ECO:0007744|PDB:3TKL, ECO:0007744|PDB:4FMB, FT ECO:0007744|PDB:4FMC, ECO:0007744|PDB:4FMD, FT ECO:0007744|PDB:4FME, ECO:0007744|PDB:4IRU, FT ECO:0007744|PDB:4JVS" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0000269|PubMed:22939626, ECO:0000269|PubMed:23588383, FT ECO:0000269|Ref.29, 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:4JVS" FT BINDING 69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 124 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 127 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 155 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" FT BINDING 156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:22416225, FT ECO:0007744|PDB:3TKL" 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 CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51153" FT CROSSLNK 61 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51153" 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 49 FT /note="K->R: Promotes TLRs trafficking and TLRs-mediated FT signaling; when associated with A-61." FT /evidence="ECO:0000269|PubMed:35343654" FT MUTAGEN 61 FT /note="K->R: Promotes TLRs trafficking and TLRs-mediated FT signaling; when associated with A-49." FT /evidence="ECO:0000269|PubMed:35343654" 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 HELIX 4..7 FT /evidence="ECO:0007829|PDB:3SFV" 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:7EQ2" FT HELIX 136..146 FT /evidence="ECO:0007829|PDB:2WWX" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:2WWX" FT TURN 155..158 FT /evidence="ECO:0007829|PDB:7EQ2" 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 //