GBF1_HUMAN
ID GBF1_HUMAN Reviewed; 1859 AA.
AC Q92538; Q149P0; Q149P1; Q5VXX3; Q96CK6; Q96HZ3; Q9H473;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1;
DE Short=BFA-resistant GEF 1;
GN Name=GBF1; Synonyms=KIAA0248;
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=9828135; DOI=10.1006/geno.1998.5563;
RA Mansour S.J., Herbrick J.-A., Scherer S.W., Melancon P.;
RT "Human GBF1 is a ubiquitously expressed gene of the sec7 domain family
RT mapping to 10q24.";
RL Genomics 54:323-327(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney, and Muscle;
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12047556; DOI=10.1034/j.1600-0854.2002.30705.x;
RA Kawamoto K., Yoshida Y., Tamaki H., Torii S., Shinotsuka C., Yamashina S.,
RA Nakayama K.;
RT "GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors,
RT is localized to the cis-Golgi and involved in membrane association of the
RT COPI coat.";
RL Traffic 3:483-495(2002).
RN [8]
RP INTERACTION WITH USO1.
RX PubMed=12634853; DOI=10.1038/sj.embor.embor762;
RA Garcia-Mata R., Sztul E.;
RT "The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-
RT nucleotide-exchange factor.";
RL EMBO Rep. 4:320-325(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-794.
RX PubMed=12808027; DOI=10.1091/mbc.e02-11-0730;
RA Garcia-Mata R., Szul T., Alvarez C., Sztul E.;
RT "ADP-ribosylation factor/COPI-dependent events at the endoplasmic
RT reticulum-Golgi interface are regulated by the guanine nucleotide exchange
RT factor GBF1.";
RL Mol. Biol. Cell 14:2250-2261(2003).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; ARF3; ARF4 AND ARF5,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF MET-832.
RX PubMed=15616190; DOI=10.1091/mbc.e04-07-0599;
RA Niu T.K., Pfeifer A.C., Lippincott-Schwartz J., Jackson C.L.;
RT "Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the
RT Golgi.";
RL Mol. Biol. Cell 16:1213-1222(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15813748; DOI=10.1111/j.1600-0854.2005.00282.x;
RA Szul T., Garcia-Mata R., Brandon E., Shestopal S., Alvarez C., Sztul E.;
RT "Dissection of membrane dynamics of the ARF-guanine nucleotide exchange
RT factor GBF1.";
RL Traffic 6:374-385(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP FUNCTION.
RX PubMed=16926190; DOI=10.1242/jcs.03173;
RA Zhao X., Claude A., Chun J., Shields D.J., Presley J.F., Melancon P.;
RT "GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-Golgi
RT protein traffic.";
RL J. Cell Sci. 119:3743-3753(2006).
RN [14]
RP INTERACTION WITH POLIOVIRUS PROTEIN 3A (MICROBIAL INFECTION).
RX PubMed=17005635; DOI=10.1128/jvi.01225-06;
RA Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L.,
RA Melchers W.J., van Kuppeveld F.J.;
RT "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-
RT dependent COP-I recruitment.";
RL J. Virol. 80:11852-11860(2006).
RN [15]
RP SUBUNIT.
RX PubMed=17640864; DOI=10.1074/jbc.m705525200;
RA Ramaen O., Joubert A., Simister P., Belgareh-Touze N.,
RA Olivares-Sanchez M.C., Zeeh J.C., Chantalat S., Golinelli-Cohen M.P.,
RA Jackson C.L., Biou V., Cherfils J.;
RT "Interactions between conserved domains within homodimers in the BIG1,
RT BIG2, and GBF1 Arf guanine nucleotide exchange factors.";
RL J. Biol. Chem. 282:28834-28842(2007).
RN [16]
RP FUNCTION, AND INTERACTION WITH ARF1 AND ARF4.
RX PubMed=17956946; DOI=10.1242/jcs.010769;
RA Szul T., Grabski R., Lyons S., Morohashi Y., Shestopal S., Lowe M.,
RA Sztul E.;
RT "Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in
RT Golgi biogenesis and protein trafficking.";
RL J. Cell Sci. 120:3929-3940(2007).
RN [17]
RP INTERACTION WITH RAB1B.
RX PubMed=17429068; DOI=10.1091/mbc.e06-11-1005;
RA Monetta P., Slavin I., Romero N., Alvarez C.;
RT "Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI
RT association.";
RL Mol. Biol. Cell 18:2400-2410(2007).
RN [18]
RP FUNCTION, INTERACTION WITH GGA1; GGA2 AND GGA3, AND MUTAGENESIS OF GLU-794.
RX PubMed=17666033; DOI=10.1111/j.1600-0854.2007.00623.x;
RA Lefrancois S., McCormick P.J.;
RT "The Arf GEF GBF1 is required for GGA recruitment to Golgi membranes.";
RL Traffic 8:1440-1451(2007).
RN [19]
RP PHOSPHORYLATION AT THR-1337, AND MUTAGENESIS OF THR-1337.
RX PubMed=18063581; DOI=10.1074/jbc.m708296200;
RA Miyamoto T., Oshiro N., Yoshino K., Nakashima A., Eguchi S., Takahashi M.,
RA Ono Y., Kikkawa U., Yonezawa K.;
RT "AMP-activated protein kinase phosphorylates Golgi-specific brefeldin A
RT resistance factor 1 at Thr1337 to induce disassembly of Golgi apparatus.";
RL J. Biol. Chem. 283:4430-4438(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [21]
RP FUNCTION.
RX PubMed=18003980; DOI=10.1091/mbc.e07-04-0394;
RA Manolea F., Claude A., Chun J., Rosas J., Melancon P.;
RT "Distinct functions for Arf guanine nucleotide exchange factors at the
RT Golgi complex: GBF1 and BIGs are required for assembly and maintenance of
RT the Golgi stack and trans-Golgi network, respectively.";
RL Mol. Biol. Cell 19:523-535(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-1298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [25]
RP FUNCTION, INTERACTION WITH COPG1, AND MUTAGENESIS OF ASP-543.
RX PubMed=19039328; DOI=10.1038/embor.2008.221;
RA Deng Y., Golinelli-Cohen M.P., Smirnova E., Jackson C.L.;
RT "A COPI coat subunit interacts directly with an early-Golgi localized Arf
RT exchange factor.";
RL EMBO Rep. 10:58-64(2009).
RN [26]
RP FUNCTION.
RX PubMed=19461073; DOI=10.1242/jcs.045849;
RA Soni K.G., Mardones G.A., Sougrat R., Smirnova E., Jackson C.L.,
RA Bonifacino J.S.;
RT "Coatomer-dependent protein delivery to lipid droplets.";
RL J. Cell Sci. 122:1834-1841(2009).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1298; TYR-1316; SER-1335 AND
RP SER-1475, AND 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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
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 [31]
RP FUNCTION.
RX PubMed=22185782; DOI=10.1247/csf.11035;
RA Takashima K., Saitoh A., Hirose S., Nakai W., Kondo Y., Takasu Y.,
RA Kakeya H., Shin H.W., Nakayama K.;
RT "GBF1-Arf-COPI-ArfGAP-mediated Golgi-to-ER transport involved in regulation
RT of lipid homeostasis.";
RL Cell Struct. Funct. 36:223-235(2011).
RN [32]
RP INTERACTION WITH PNPLA2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-543.
RX PubMed=21789191; DOI=10.1371/journal.pone.0021889;
RA Ellong E.N., Soni K.G., Bui Q.T., Sougrat R., Golinelli-Cohen M.P.,
RA Jackson C.L.;
RT "Interaction between the triglyceride lipase ATGL and the Arf1 activator
RT GBF1.";
RL PLoS ONE 6:E21889-E21889(2011).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1298, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [34]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHATIDYLINOSITOL-PHOSPHATE-BINDING.
RX PubMed=22573891; DOI=10.1091/mbc.e12-01-0062;
RA Mazaki Y., Nishimura Y., Sabe H.;
RT "GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to
RT link PI3Kgamma activity with Arf1 activation involved in GPCR-mediated
RT neutrophil chemotaxis and superoxide production.";
RL Mol. Biol. Cell 23:2457-2467(2012).
RN [35]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23386609; DOI=10.1074/jbc.m112.438481;
RA Lowery J., Szul T., Styers M., Holloway Z., Oorschot V., Klumperman J.,
RA Sztul E.;
RT "The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
RT recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the
RT trans-Golgi network (TGN).";
RL J. Biol. Chem. 288:11532-11545(2013).
RN [36]
RP FUNCTION, AND PHOSPHORYLATION BY AMPK.
RX PubMed=23418352; DOI=10.1242/jcs.121954;
RA Mao L., Li N., Guo Y., Xu X., Gao L., Xu Y., Zhou L., Liu W.;
RT "AMPK phosphorylates GBF1 for mitotic Golgi disassembly.";
RL J. Cell Sci. 126:1498-1505(2013).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-1318 AND SER-1784,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [38]
RP FUNCTION.
RX PubMed=25190516; DOI=10.15252/embj.201489039;
RA Ackema K.B., Hench J., Boeckler S., Wang S.C., Sauder U., Mergentaler H.,
RA Westermann B., Bard F., Frank S., Spang A.;
RT "The small GTPase Arf1 modulates mitochondrial morphology and function.";
RL EMBO J. 33:2659-2675(2014).
RN [39]
RP FUNCTION.
RX PubMed=24213530; DOI=10.1242/jcs.130591;
RA Quilty D., Gray F., Summerfeldt N., Cassel D., Melancon P.;
RT "Arf activation at the Golgi is modulated by feed-forward stimulation of
RT the exchange factor GBF1.";
RL J. Cell Sci. 127:354-364(2014).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-352; SER-1298;
RP SER-1773 AND SER-1784, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [41]
RP INTERACTION WITH ARMH3, AND SUBCELLULAR LOCATION.
RX PubMed=31519766; DOI=10.1074/mcp.ra119.001645;
RA Chan C.J., Le R., Burns K., Ahmed K., Coyaud E., Laurent E.M.N., Raught B.,
RA Melancon P.;
RT "BioID performed on Golgi enriched fractions identify C10orf76 as aGBF1
RT Binding Protein essential for Golgi maintenance and secretion.";
RL Mol. Cell. Proteomics 18:2285-2297(2019).
CC -!- FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of the
CC Arf family of small GTPases involved in trafficking in the early
CC secretory pathway; its GEF activity initiates the coating of nascent
CC vesicles via the localized generation of activated ARFs through
CC replacement of GDP with GTP. Recruitment to cis-Golgi membranes
CC requires membrane association of Arf-GDP and can be regulated by ARF1,
CC ARF3, ARF4 and ARF5. Involved in the recruitment of the COPI coat
CC complex to the endoplasmic reticulum exit sites (ERES), and the
CC endoplasmic reticulum-Golgi intermediate (ERGIC) and cis-Golgi
CC compartments which implicates ARF1 activation. Involved in COPI
CC vesicle-dependent retrograde transport from the ERGIC and cis-Golgi
CC compartments to the endoplasmic reticulum (ER) (PubMed:16926190,
CC PubMed:17956946, PubMed:18003980, PubMed:12047556, PubMed:12808027,
CC PubMed:19039328, PubMed:24213530). Involved in the trans-Golgi network
CC recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and the AP-1 adapter
CC protein complex related to chlathrin-dependent transport; the function
CC requires its GEF activity (probably at least in part on ARF4 and ARF5)
CC (PubMed:23386609). Has GEF activity towards ARF1 (PubMed:15616190). Has
CC in vitro GEF activity towards ARF5 (By similarity). Involved in the
CC processing of PSAP (PubMed:17666033). Required for the assembly of the
CC Golgi apparatus (PubMed:12808027, PubMed:18003980). The AMPK-
CC phosphorylated form is involved in Golgi disassembly during mitotis and
CC under stress conditions (PubMed:18063581, PubMed:23418352). May be
CC involved in the COPI vesicle-dependent recruitment of PNPLA2 to lipid
CC droplets; however, this function is under debate (PubMed:19461073,
CC PubMed:22185782). In neutrophils, involved in G protein-coupled
CC receptor (GPCR)-mediated chemotaxis und superoxide production. Proposed
CC to be recruited by phosphatidylinositol-phosphates generated upon GPCR
CC stimulation to the leading edge where it recruits and activates ARF1,
CC and is involved in recruitment of GIT2 and the NADPH oxidase complex
CC (PubMed:22573891). Plays a role in maintaining mitochondrial morphology
CC (PubMed:25190516). {ECO:0000250|UniProtKB:Q9R1D7,
CC ECO:0000269|PubMed:12047556, ECO:0000269|PubMed:12808027,
CC ECO:0000269|PubMed:15616190, ECO:0000269|PubMed:16926190,
CC ECO:0000269|PubMed:17666033, ECO:0000269|PubMed:17956946,
CC ECO:0000269|PubMed:18003980, ECO:0000269|PubMed:18063581,
CC ECO:0000269|PubMed:19461073, ECO:0000269|PubMed:22185782,
CC ECO:0000269|PubMed:22573891, ECO:0000269|PubMed:23386609,
CC ECO:0000269|PubMed:23418352, ECO:0000269|PubMed:24213530,
CC ECO:0000269|PubMed:25190516, ECO:0000305|PubMed:19039328,
CC ECO:0000305|PubMed:22573891}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A (BFA) (PubMed:15616190).
CC Inhibited by golgicide A (GCA) (By similarity).
CC {ECO:0000250|UniProtKB:Q9R1D7, ECO:0000269|PubMed:15616190}.
CC -!- SUBUNIT: Can form homodimers and probably homotetramers
CC (PubMed:17640864). Interacts with COPG1; the interaction is independent
CC on ARF1 activation (PubMed:19039328). Interacts with ARF1, ARF3, ARF4
CC and ARF5 (PubMed:15616190, PubMed:17956946). Interacts with RAB1B (GTP-
CC bound form); required for GBF1 membrane association (PubMed:17429068).
CC Interacts with GGA1, GGA2 and GGA3 (PubMed:17666033). Interacts with
CC USO1 (PubMed:12634853). Interacts (via SEC7 domain) with PNPLA2 (via C-
CC terminus); the interaction is direct (PubMed:21789191). Interacts with
CC ARMH3 (PubMed:31519766). {ECO:0000250|UniProtKB:Q6DFZ1,
CC ECO:0000269|PubMed:15616190, ECO:0000269|PubMed:17429068,
CC ECO:0000269|PubMed:17666033, ECO:0000269|PubMed:17956946,
CC ECO:0000269|PubMed:19039328, ECO:0000269|PubMed:21789191,
CC ECO:0000269|PubMed:31519766, ECO:0000305|PubMed:12634853,
CC ECO:0000305|PubMed:17640864}.
CC -!- SUBUNIT: (Microbial infection) Interacts with poliovirus protein 3A.
CC {ECO:0000269|PubMed:17005635}.
CC -!- INTERACTION:
CC Q92538; Q9Y678: COPG1; NbExp=2; IntAct=EBI-359050, EBI-1049127;
CC Q92538; P53620: COPG1; Xeno; NbExp=2; IntAct=EBI-359050, EBI-8511600;
CC Q92538; P09613: GP; Xeno; NbExp=2; IntAct=EBI-359050, EBI-21497244;
CC Q92538; PRO_0000424692 [P03300]; Xeno; NbExp=8; IntAct=EBI-359050, EBI-21242141;
CC Q92538-3; Q9C0D3: ZYG11B; NbExp=3; IntAct=EBI-17724521, EBI-1811414;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:12047556, ECO:0000269|PubMed:12808027,
CC ECO:0000269|PubMed:15616190}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000269|PubMed:12808027}. Golgi apparatus, trans-Golgi
CC network {ECO:0000269|PubMed:23386609}. Golgi apparatus
CC {ECO:0000269|PubMed:31519766}. Cytoplasm {ECO:0000269|PubMed:22573891,
CC ECO:0000269|PubMed:31519766}. Lipid droplet
CC {ECO:0000269|PubMed:21789191}. Membrane; Peripheral membrane protein
CC {ECO:0000305}. Note=Cycles rapidly on and off early Golgi membranes
CC (PubMed:15616190). Stabilized on membranes when complexed with ARF1-GDP
CC and is released from both ARF1 and membranes after it catalyzes GDP
CC displacement and ARF1 binds GTP. Continuous cycles of recruitment and
CC dissociation of GBF1 to membranes are required for sustained ARF
CC activation and COP I recruitment (PubMed:15813748). In neutrophils is
CC translocated from the Golgi to the leading edge upon GPCR stimulation
CC (PubMed:22573891). Localization to lipid droplets is questionable
CC (PubMed:22185782). {ECO:0000269|PubMed:15616190,
CC ECO:0000269|PubMed:22185782, ECO:0000269|PubMed:22573891,
CC ECO:0000305|PubMed:15616190, ECO:0000305|PubMed:15813748}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92538-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92538-2; Sequence=VSP_057522, VSP_057523;
CC Name=3;
CC IsoId=Q92538-3; Sequence=VSP_057523;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The DCB (dimerization and cyclophiln-binding) and HUS (homology
CC upstream of Sec7) domains are necessary for dimerization. The DCB
CC domain is proposed to support constitutive homodimerization; the HUS
CC domain interacts with the DCB domain which may occur intramolecular or
CC intermolecular (By similarity). {ECO:0000250|UniProtKB:Q9R1D7}.
CC -!- PTM: AMPK-mediated phosphorylation at Thr-1337 is induced by 2-
CC deoxyglucose (2-DG) and AICA ribonucleotide, and occurs during mitosis
CC leading to membrane disassociation and inactivation of ARF1 during
CC mitosis. {ECO:0000269|PubMed:18063581, ECO:0000269|PubMed:23418352}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13379.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AF068755; AAD15903.1; -; mRNA.
DR EMBL; D87435; BAA13379.2; ALT_INIT; mRNA.
DR EMBL; AK025330; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL121928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007941; AAH07941.2; -; mRNA.
DR EMBL; BC117681; AAI17682.1; -; mRNA.
DR EMBL; BC117682; AAI17683.1; -; mRNA.
DR EMBL; BC014171; AAH14171.2; -; mRNA.
DR CCDS; CCDS7533.1; -. [Q92538-1]
DR RefSeq; NP_001186307.1; NM_001199378.1. [Q92538-2]
DR RefSeq; NP_001186308.1; NM_001199379.1. [Q92538-3]
DR RefSeq; NP_004184.1; NM_004193.2. [Q92538-1]
DR AlphaFoldDB; Q92538; -.
DR SMR; Q92538; -.
DR BioGRID; 114268; 394.
DR IntAct; Q92538; 44.
DR MINT; Q92538; -.
DR STRING; 9606.ENSP00000359000; -.
DR GlyGen; Q92538; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92538; -.
DR MetOSite; Q92538; -.
DR PhosphoSitePlus; Q92538; -.
DR SwissPalm; Q92538; -.
DR BioMuta; GBF1; -.
DR DMDM; 13124260; -.
DR EPD; Q92538; -.
DR jPOST; Q92538; -.
DR MassIVE; Q92538; -.
DR MaxQB; Q92538; -.
DR PaxDb; Q92538; -.
DR PeptideAtlas; Q92538; -.
DR PRIDE; Q92538; -.
DR ProteomicsDB; 75296; -.
DR Antibodypedia; 31405; 116 antibodies from 20 providers.
DR DNASU; 8729; -.
DR Ensembl; ENST00000676513.1; ENSP00000503207.1; ENSG00000107862.7. [Q92538-1]
DR Ensembl; ENST00000676939.1; ENSP00000503981.1; ENSG00000107862.7. [Q92538-1]
DR Ensembl; ENST00000676993.1; ENSP00000503918.1; ENSG00000107862.7. [Q92538-3]
DR Ensembl; ENST00000677240.1; ENSP00000503428.1; ENSG00000107862.7. [Q92538-2]
DR GeneID; 8729; -.
DR KEGG; hsa:8729; -.
DR UCSC; uc001kux.3; human. [Q92538-1]
DR CTD; 8729; -.
DR DisGeNET; 8729; -.
DR GeneCards; GBF1; -.
DR HGNC; HGNC:4181; GBF1.
DR HPA; ENSG00000107862; Low tissue specificity.
DR MalaCards; GBF1; -.
DR MIM; 603698; gene.
DR neXtProt; NX_Q92538; -.
DR OpenTargets; ENSG00000107862; -.
DR PharmGKB; PA28595; -.
DR VEuPathDB; HostDB:ENSG00000107862; -.
DR eggNOG; KOG0928; Eukaryota.
DR GeneTree; ENSGT00940000156925; -.
DR HOGENOM; CLU_001204_2_0_1; -.
DR InParanoid; Q92538; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; Q92538; -.
DR TreeFam; TF105934; -.
DR PathwayCommons; Q92538; -.
DR Reactome; R-HSA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q92538; -.
DR SIGNOR; Q92538; -.
DR BioGRID-ORCS; 8729; 710 hits in 1078 CRISPR screens.
DR ChiTaRS; GBF1; human.
DR GeneWiki; GBF1; -.
DR GenomeRNAi; 8729; -.
DR Pharos; Q92538; Tbio.
DR PRO; PR:Q92538; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q92538; protein.
DR Bgee; ENSG00000107862; Expressed in colonic epithelium and 186 other tissues.
DR ExpressionAtlas; Q92538; baseline and differential.
DR Genevisible; Q92538; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0002263; P:cell activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; TAS:Reactome.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0097111; P:endoplasmic reticulum-Golgi intermediate compartment organization; IMP:UniProtKB.
DR GO; GO:0061162; P:establishment of monopolar cell polarity; IMP:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:UniProtKB.
DR GO; GO:1903420; P:protein localization to endoplasmic reticulum tubular network; IMP:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903409; P:reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR032691; Sec7_N.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Host-virus interaction; Lipid droplet;
KW Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1859
FT /note="Golgi-specific brefeldin A-resistance guanine
FT nucleotide exchange factor 1"
FT /id="PRO_0000120210"
FT DOMAIN 692..882
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 1..380
FT /note="Interaction with RAB1B"
FT /evidence="ECO:0000269|PubMed:17429068"
FT REGION 1..211
FT /note="DCB; DCB:DCB domain and DCB:HUS domain interaction"
FT /evidence="ECO:0000250|UniProtKB:Q9R1D7"
FT REGION 215..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..550
FT /note="HUS; DCB:HUS domain interaction"
FT /evidence="ECO:0000250|UniProtKB:Q9R1D7"
FT REGION 619..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..1370
FT /note="Phosphatidylinositol-phosphate binding; required for
FT translocation to the leading edge and for ARF1 activation
FT upon GPCR signaling"
FT /evidence="ECO:0000269|PubMed:22573891"
FT REGION 1284..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1316
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1337
FT /note="Phosphothreonine; by AMPK"
FT /evidence="ECO:0000269|PubMed:18063581"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 337
FT /note="Q -> QQ (in isoform 2)"
FT /id="VSP_057522"
FT VAR_SEQ 1494..1497
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_057523"
FT VARIANT 1693
FT /note="G -> S (in dbSNP:rs11191274)"
FT /id="VAR_051926"
FT MUTAGEN 543
FT /note="D->A: Increases interaction with COPG1 and PNPLA2."
FT /evidence="ECO:0000269|PubMed:19039328,
FT ECO:0000269|PubMed:21789191"
FT MUTAGEN 794
FT /note="E->D: Inhibits Golgi membrane recruitment of GGA1,
FT GGA2 and GGA3; generates misprocessing of PSAP."
FT /evidence="ECO:0000269|PubMed:17666033"
FT MUTAGEN 794
FT /note="E->K: Arrests retrograde ERGIC/cis-Golgi-to-ER
FT transport at an early step and causes disassembly of the
FT Golgi and disassociation of COP1 from membranes."
FT /evidence="ECO:0000269|PubMed:12808027"
FT MUTAGEN 832
FT /note="M->L: Confers BFA tolerance."
FT /evidence="ECO:0000269|PubMed:15616190"
FT MUTAGEN 1337
FT /note="T->A: Prevents 2-DG-induced Golgi disassembly."
FT /evidence="ECO:0000269|PubMed:18063581"
FT CONFLICT 24
FT /note="A -> S (in Ref. 2; BAA13379)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="R -> C (in Ref. 4; AK025330)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="R -> C (in Ref. 6; AAI17682)"
FT /evidence="ECO:0000305"
FT CONFLICT 1811
FT /note="Q -> R (in Ref. 4; AK025330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1859 AA; 206446 MW; 5015D2BD70009CFA CRC64;
MVDKNIYIIQ GEINIVVGAI KRNARWSTHT PLDEERDPLL HSFGHLKEVL NSITELSEIE
PNVFLRPFLE VIRSEDTTGP ITGLALTSVN KFLSYALIDP THEGTAEGME NMADAVTHAR
FVGTDPASDE VVLMKILQVL RTLLLTPVGA HLTNESVCEI MQSCFRICFE MRLSELLRKS
AEHTLVDMVQ LLFTRLPQFK EEPKNYVGTN MKKLKMRAGG MSDSSKWKKQ KRSPRPPRHM
TKVTPGSELP TPNGTTLSSN LTGGMPFIDV PTPISSASSE AASAVVSPST DSGLEFSSQT
TSKEDLTDLE QPGSPGYSTA TEPGSSELGV PEQPDLQEGT HVEKSQSASV ESIPEVLEEC
TSPADHSDSA SVHDMDYVNP RGVRFTQSSQ KEGTALVPYG LPCIRELFRF LISLTNPHDR
HNSEVMIHMG LHLLTVALES APVAQCQTLL GLIKDEMCRH LFQLLSIERL NLYAASLRVC
FLLFESMREH LKFQMEMYIK KLMEIITVEN PKMPYEMKEM ALEAIVQLWR IPSFVTELYI
NYDCDYYCSN LFEELTKLLS KNAFPVSGQL YTTHLLSLDA LLTVIDSTEA HCQAKVLNSL
TQQEKKETAR PSCEIVDGTR EASNTERTAS DGKAVGMASD IPGLHLPGGG RLPPEHGKSG
CSDLEEAVDS GADKKFARKP PRFSCLLPDP RELIEIKNKK KLLITGTEQF NQKPKKGIQF
LQEKGLLTIP MDNTEVAQWL RENPRLDKKM IGEFVSDRKN IDLLESFVST FSFQGLRLDE
ALRLYLEAFR LPGEAPVIQR LLEAFTERWM NCNGSPFANS DACFSLAYAV IMLNTDQHNH
NVRKQNAPMT LEEFRKNLKG VNGGKDFEQD ILEDMYHAIK NEEIVMPEEQ TGLVRENYVW
NVLLHRGATP EGIFLRVPTA SYDLDLFTMT WGPTIAALSY VFDKSLEETI IQKAISGFRK
CAMISAHYGL SDVFDNLIIS LCKFTALSSE SIENLPSVFG SNPKAHIAAK TVFHLAHRHG
DILREGWKNI MEAMLQLFRA QLLPKAMIEV EDFVDPNGKI SLQREETPSN RGESTVLSFV
SWLTLSGPEQ SSVRGPSTEN QEAKRVALEC IKQCDPEKMI TESKFLQLES LQELMKALVS
VTPDEETYDE EDAAFCLEML LRIVLENRDR VGCVWQTVRD HLYHLCVQAQ DFCFLVERAV
VGLLRLAIRL LRREEISAQV LLSLRILLLM KPSVLSRVSH QVAYGLHELL KTNAANIHSG
DDWATLFTLL ECIGSGVKPP AALQATARAD APDAGAQSDS ELPSYHQNDV SLDRGYTSDS
EVYTDHGRPG KIHRSATDAD VVNSGWLVVG KDDVDNSKPG PSRPGPSPLI NQYSLTVGLD
LGPHDTKSLL KCVESLSFIV RDAAHITPDN FELCVKTLRI FVEASLNGGC KSQEKRGKSH
KYDSKGNRFK KKSKEGSMLR RPRTSSQHAS RGGQSDDDED EGVPASYHTV SLQVSQDLLD
LMHTLHTRAA SIYSSWAEEQ RHLETGGQKI EADSRTLWAH CWCPLLQGIA CLCCDARRQV
RMQALTYLQR ALLVHDLQKL DALEWESCFN KVLFPLLTKL LENISPADVG GMEETRMRAS
TLLSKVFLQH LSPLLSLSTF AALWLTILDF MDKYMHAGSS DLLSEAIPES LKNMLLVMDT
AEIFHSADAR GGGPSALWEI TWERIDCFLP HLRDELFKQT VIQDPMPMEP QGQKPLASAH
LTSAAGDTRT PGHPPPPEIP SELGACDFEK PESPRAASSS SPGSPVASSP SRLSPTPDGP
PPLAQPPLIL QPLASPLQVG VPPMTLPIIL NPALIEATSP VPLLATPRPT DPIPTSEVN
