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Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (BFA-resistant GEF 1)

 GBF1_HUMAN              Reviewed;        1859 AA.
Q92538; Q149P0; Q149P1; Q5VXX3; Q96CK6; Q96HZ3; Q9H473;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1999, sequence version 2.
30-AUG-2017, entry version 166.
RecName: Full=Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1;
Short=BFA-resistant GEF 1;
Name=GBF1; Synonyms=KIAA0248;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9828135; DOI=10.1006/geno.1998.5563;
Mansour S.J., Herbrick J.-A., Scherer S.W., Melancon P.;
"Human GBF1 is a ubiquitously expressed gene of the sec7 domain family
mapping to 10q24.";
Genomics 54:323-327(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Kidney, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12047556; DOI=10.1034/j.1600-0854.2002.30705.x;
Kawamoto K., Yoshida Y., Tamaki H., Torii S., Shinotsuka C.,
Yamashina S., Nakayama K.;
"GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
factors, is localized to the cis-Golgi and involved in membrane
association of the COPI coat.";
Traffic 3:483-495(2002).
[8]
INTERACTION WITH USO1.
PubMed=12634853; DOI=10.1038/sj.embor.embor762;
Garcia-Mata R., Sztul E.;
"The membrane-tethering protein p115 interacts with GBF1, an ARF
guanine-nucleotide-exchange factor.";
EMBO Rep. 4:320-325(2003).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-794.
PubMed=12808027; DOI=10.1091/mbc.E02-11-0730;
Garcia-Mata R., Szul T., Alvarez C., Sztul E.;
"ADP-ribosylation factor/COPI-dependent events at the endoplasmic
reticulum-Golgi interface are regulated by the guanine nucleotide
exchange factor GBF1.";
Mol. Biol. Cell 14:2250-2261(2003).
[10]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; ARF3; ARF4 AND
ARF5, ENZYME REGULATION, AND MUTAGENESIS OF MET-832.
PubMed=15616190; DOI=10.1091/mbc.E04-07-0599;
Niu T.K., Pfeifer A.C., Lippincott-Schwartz J., Jackson C.L.;
"Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the
Golgi.";
Mol. Biol. Cell 16:1213-1222(2005).
[11]
SUBCELLULAR LOCATION.
PubMed=15813748; DOI=10.1111/j.1600-0854.2005.00282.x;
Szul T., Garcia-Mata R., Brandon E., Shestopal S., Alvarez C.,
Sztul E.;
"Dissection of membrane dynamics of the ARF-guanine nucleotide
exchange factor GBF1.";
Traffic 6:374-385(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
FUNCTION.
PubMed=16926190; DOI=10.1242/jcs.03173;
Zhao X., Claude A., Chun J., Shields D.J., Presley J.F., Melancon P.;
"GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-
Golgi protein traffic.";
J. Cell Sci. 119:3743-3753(2006).
[14]
INTERACTION WITH POLIOVIRUS PROTEIN 3A.
PubMed=17005635; DOI=10.1128/JVI.01225-06;
Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L.,
Melchers W.J., van Kuppeveld F.J.;
"Effects of picornavirus 3A Proteins on Protein Transport and GBF1-
dependent COP-I recruitment.";
J. Virol. 80:11852-11860(2006).
[15]
SUBUNIT.
PubMed=17640864; DOI=10.1074/jbc.M705525200;
Ramaen O., Joubert A., Simister P., Belgareh-Touze N.,
Olivares-Sanchez M.C., Zeeh J.C., Chantalat S., Golinelli-Cohen M.P.,
Jackson C.L., Biou V., Cherfils J.;
"Interactions between conserved domains within homodimers in the BIG1,
BIG2, and GBF1 Arf guanine nucleotide exchange factors.";
J. Biol. Chem. 282:28834-28842(2007).
[16]
FUNCTION, AND INTERACTION WITH ARF1 AND ARF4.
PubMed=17956946; DOI=10.1242/jcs.010769;
Szul T., Grabski R., Lyons S., Morohashi Y., Shestopal S., Lowe M.,
Sztul E.;
"Dissecting the role of the ARF guanine nucleotide exchange factor
GBF1 in Golgi biogenesis and protein trafficking.";
J. Cell Sci. 120:3929-3940(2007).
[17]
INTERACTION WITH RAB1B.
PubMed=17429068; DOI=10.1091/mbc.E06-11-1005;
Monetta P., Slavin I., Romero N., Alvarez C.;
"Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI
association.";
Mol. Biol. Cell 18:2400-2410(2007).
[18]
FUNCTION, INTERACTION WITH GGA1; GGA2 AND GGA3, AND MUTAGENESIS OF
GLU-794.
PubMed=17666033; DOI=10.1111/j.1600-0854.2007.00623.x;
Lefrancois S., McCormick P.J.;
"The Arf GEF GBF1 is required for GGA recruitment to Golgi
membranes.";
Traffic 8:1440-1451(2007).
[19]
PHOSPHORYLATION AT THR-1337, AND MUTAGENESIS OF THR-1337.
PubMed=18063581; DOI=10.1074/jbc.M708296200;
Miyamoto T., Oshiro N., Yoshino K., Nakashima A., Eguchi S.,
Takahashi M., Ono Y., Kikkawa U., Yonezawa K.;
"AMP-activated protein kinase phosphorylates Golgi-specific brefeldin
A resistance factor 1 at Thr1337 to induce disassembly of Golgi
apparatus.";
J. Biol. Chem. 283:4430-4438(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[21]
FUNCTION.
PubMed=18003980; DOI=10.1091/mbc.E07-04-0394;
Manolea F., Claude A., Chun J., Rosas J., Melancon P.;
"Distinct functions for Arf guanine nucleotide exchange factors at the
Golgi complex: GBF1 and BIGs are required for assembly and maintenance
of the Golgi stack and trans-Golgi network, respectively.";
Mol. Biol. Cell 19:523-535(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-1298, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
FUNCTION, INTERACTION WITH COPG1, AND MUTAGENESIS OF ASP-543.
PubMed=19039328; DOI=10.1038/embor.2008.221;
Deng Y., Golinelli-Cohen M.P., Smirnova E., Jackson C.L.;
"A COPI coat subunit interacts directly with an early-Golgi localized
Arf exchange factor.";
EMBO Rep. 10:58-64(2009).
[26]
FUNCTION.
PubMed=19461073; DOI=10.1242/jcs.045849;
Soni K.G., Mardones G.A., Sougrat R., Smirnova E., Jackson C.L.,
Bonifacino J.S.;
"Coatomer-dependent protein delivery to lipid droplets.";
J. Cell Sci. 122:1834-1841(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1298; TYR-1316; SER-1335
AND SER-1475, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
FUNCTION.
PubMed=22185782; DOI=10.1247/csf.11035;
Takashima K., Saitoh A., Hirose S., Nakai W., Kondo Y., Takasu Y.,
Kakeya H., Shin H.W., Nakayama K.;
"GBF1-Arf-COPI-ArfGAP-mediated Golgi-to-ER transport involved in
regulation of lipid homeostasis.";
Cell Struct. Funct. 36:223-235(2011).
[32]
INTERACTION WITH PNPLA2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-543.
PubMed=21789191; DOI=10.1371/journal.pone.0021889;
Ellong E.N., Soni K.G., Bui Q.T., Sougrat R., Golinelli-Cohen M.P.,
Jackson C.L.;
"Interaction between the triglyceride lipase ATGL and the Arf1
activator GBF1.";
PLoS ONE 6:E21889-E21889(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1298, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[34]
FUNCTION, SUBCELLULAR LOCATION, AND
PHOSPHATIDYLINOSITOL-PHOSPHATE-BINDING.
PubMed=22573891; DOI=10.1091/mbc.E12-01-0062;
Mazaki Y., Nishimura Y., Sabe H.;
"GBF1 bears a novel phosphatidylinositol-phosphate binding module,
BP3K, to link PI3Kgamma activity with Arf1 activation involved in
GPCR-mediated neutrophil chemotaxis and superoxide production.";
Mol. Biol. Cell 23:2457-2467(2012).
[35]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23386609; DOI=10.1074/jbc.M112.438481;
Lowery J., Szul T., Styers M., Holloway Z., Oorschot V.,
Klumperman J., Sztul E.;
"The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
the trans-Golgi network (TGN).";
J. Biol. Chem. 288:11532-11545(2013).
[36]
FUNCTION, AND PHOSPHORYLATION BY AMPK.
PubMed=23418352; DOI=10.1242/jcs.121954;
Mao L., Li N., Guo Y., Xu X., Gao L., Xu Y., Zhou L., Liu W.;
"AMPK phosphorylates GBF1 for mitotic Golgi disassembly.";
J. Cell Sci. 126:1498-1505(2013).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-1318 AND
SER-1784, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
FUNCTION.
PubMed=24213530; DOI=10.1242/jcs.130591;
Quilty D., Gray F., Summerfeldt N., Cassel D., Melancon P.;
"Arf activation at the Golgi is modulated by feed-forward stimulation
of the exchange factor GBF1.";
J. Cell Sci. 127:354-364(2014).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-352; SER-1298;
SER-1773 AND SER-1784, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Guanine-nucleotide exchange factor (GEF) for members of
the Arf family of small GTPases involved in trafficking in the
early secretory pathway; its GEF activity initiates the coating of
nascent vesicles via the localized generation of activated ARFs
through replacement of GDP with GTP. Recruitment to cis-Golgi
membranes requires membrane association of Arf-GDP and can be
regulated by ARF1, ARF3, ARF4 and ARF5. Involved in the
recruitment of the COPI coat complex to the endoplasmic reticulum
exit sites (ERES), and the endoplasmic reticulum-Golgi
intermediate (ERGIC) and cis-Golgi compartments which implicates
ARF1 activation. Involved in COPI vesicle-dependent retrograde
transport from the ERGIC and cis-Golgi compartments to the
endoplasmic reticulum (ER) (PubMed:16926190, PubMed:17956946,
PubMed:18003980, PubMed:12047556, PubMed:12808027,
PubMed:19039328, PubMed:24213530). Involved in the trans-Golgi
network recruitment of GGA1, GGA2, GGA3, BIG1, BIG2, and the AP-1
adaptor protein complex related to chlathrin-dependent transport;
the function requires its GEF activity (probably at least in part
on ARF4 and ARF5) (PubMed:23386609). Has GEF activity towards ARF1
(PubMed:15616190). Has in vitro GEF activity towards ARF5 (By
similarity). Involved in the processing of PSAP (PubMed:17666033).
Required for the assembly of the Golgi apparatus (PubMed:12808027,
PubMed:18003980). The AMPK-phosphorylated form is involved in
Golgi disassembly during mitotis and under stress conditions
(PubMed:18063581, PubMed:23418352). May be involved in the COPI
vesicle-dependent recruitment of PNPLA2 to lipid droplets;
however, this function is under debate (PubMed:19461073,
PubMed:22185782). In neutrophils, involved in G protein-coupled
receptor (GPCR)-mediated chemotaxis und superoxide production.
Proposed to be recruited by phosphatidylinositol-phosphates
generated upon GPCR stimulation to the leading edge where it
recruits and activates ARF1, and is involved in recruitment of
GIT2 and the NADPH oxidase complex (PubMed:22573891).
{ECO:0000250|UniProtKB:Q9R1D7, ECO:0000269|PubMed:12047556,
ECO:0000269|PubMed:12808027, ECO:0000269|PubMed:15616190,
ECO:0000269|PubMed:16926190, ECO:0000269|PubMed:17666033,
ECO:0000269|PubMed:17956946, ECO:0000269|PubMed:18003980,
ECO:0000269|PubMed:18063581, ECO:0000269|PubMed:19461073,
ECO:0000269|PubMed:22185782, ECO:0000269|PubMed:22573891,
ECO:0000269|PubMed:23386609, ECO:0000269|PubMed:23418352,
ECO:0000269|PubMed:24213530, ECO:0000305|PubMed:19039328,
ECO:0000305|PubMed:22573891}.
-!- ENZYME REGULATION: Inhibited by brefeldin A (BFA)
(PubMed:15616190). Inhibited by golgicide A (GCA) (By similarity).
{ECO:0000250|UniProtKB:Q9R1D7, ECO:0000269|PubMed:15616190}.
-!- SUBUNIT: Can form homodimers and probably homotetramers
(PubMed:17640864). Interacts with COPG1; the interaction is
independent on ARF1 activation (PubMed:19039328). Interacts with
ARF1, ARF3, ARF4 and ARF5 (PubMed:15616190, PubMed:17956946).
Interacts with RAB1B (GTP-bound form); required for GBF1 membrane
association (PubMed:17429068). Interacts with GGA1, GGA2 and GGA3
(PubMed:17666033). Interacts with USO1 (PubMed:12634853).
Interacts (via SEC7 domain) with PNPLA2 (via C-terminus); the
interaction is direct (PubMed:21789191). Interacts with poliovirus
protein 3A (PubMed:17005635). {ECO:0000250|UniProtKB:Q6DFZ1,
ECO:0000269|PubMed:15616190, ECO:0000269|PubMed:17005635,
ECO:0000269|PubMed:17429068, ECO:0000269|PubMed:17666033,
ECO:0000269|PubMed:17956946, ECO:0000269|PubMed:19039328,
ECO:0000269|PubMed:21789191, ECO:0000305|PubMed:12634853,
ECO:0000305|PubMed:17640864}.
-!- INTERACTION:
P53620:COPG1 (xeno); NbExp=2; IntAct=EBI-359050, EBI-8511600;
Q9Y678:COPG1; NbExp=2; IntAct=EBI-359050, EBI-1049127;
-!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
{ECO:0000269|PubMed:12047556, ECO:0000269|PubMed:12808027,
ECO:0000269|PubMed:15616190}. Endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000269|PubMed:12808027}. Golgi
apparatus, trans-Golgi network {ECO:0000269|PubMed:23386609}.
Cytoplasm {ECO:0000269|PubMed:22573891}. Lipid droplet
{ECO:0000269|PubMed:21789191}. Membrane; Peripheral membrane
protein {ECO:0000305}. Note=Cycles rapidly on and off early Golgi
membranes (PubMed:15616190). Stabilized on membranes when
complexed with ARF1-GDP and is released from both ARF1 and
membranes after it catalyzes GDP displacement and ARF1 binds GTP.
Continuous cycles of recruitment and dissociation of GBF1 to
membranes are required for sustained ARF activation and COP I
recruitment (PubMed:15813748). In neutrophils is translocated from
the Golgi to the leading edge upon GPCR stimulation
(PubMed:22573891). Localization to lipid droplets is questionable
(PubMed:22185782). {ECO:0000269|PubMed:15616190,
ECO:0000269|PubMed:22185782, ECO:0000269|PubMed:22573891,
ECO:0000305|PubMed:15616190, ECO:0000305|PubMed:15813748}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92538-1; Sequence=Displayed;
Name=2;
IsoId=Q92538-2; Sequence=VSP_057522, VSP_057523;
Name=3;
IsoId=Q92538-3; Sequence=VSP_057523;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The DCB (dimerization and cyclophiln-binding) and HUS
(homology upstream of Sec7) domains are necessary for
dimerization. The DCB domain is proposed to support constitutive
homodimerization; the HUS domain interacts with the DCB domain
which may occur intramolecular or intermolecuar (By similarity).
{ECO:0000250|UniProtKB:Q9R1D7}.
-!- PTM: AMPK-mediated phosphorylation at Thr-1337 is induced by 2-
deoxyglucose (2-DG) and AICA ribonucleotide, and occurs during
mitosis leading to membrane disassociation and inactivation of
ARF1 during mitosis. {ECO:0000269|PubMed:18063581,
ECO:0000269|PubMed:23418352}.
-!- SEQUENCE CAUTION:
Sequence=BAA13379.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF068755; AAD15903.1; -; mRNA.
EMBL; D87435; BAA13379.2; ALT_INIT; mRNA.
EMBL; AK025330; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL356420; CAH72761.1; -; Genomic_DNA.
EMBL; AL121928; CAH72761.1; JOINED; Genomic_DNA.
EMBL; AL160011; CAH72761.1; JOINED; Genomic_DNA.
EMBL; AL121928; CAI12515.1; -; Genomic_DNA.
EMBL; AL160011; CAI12515.1; JOINED; Genomic_DNA.
EMBL; AL356420; CAI12515.1; JOINED; Genomic_DNA.
EMBL; AL160011; CAH71625.1; -; Genomic_DNA.
EMBL; AL121928; CAH71625.1; JOINED; Genomic_DNA.
EMBL; AL356420; CAH71625.1; JOINED; Genomic_DNA.
EMBL; BC007941; AAH07941.2; -; mRNA.
EMBL; BC117681; AAI17682.1; -; mRNA.
EMBL; BC117682; AAI17683.1; -; mRNA.
EMBL; BC014171; AAH14171.2; -; mRNA.
CCDS; CCDS7533.1; -. [Q92538-1]
RefSeq; NP_001186307.1; NM_001199378.1. [Q92538-2]
RefSeq; NP_001186308.1; NM_001199379.1. [Q92538-3]
RefSeq; NP_004184.1; NM_004193.2. [Q92538-1]
UniGene; Hs.290243; -.
ProteinModelPortal; Q92538; -.
SMR; Q92538; -.
BioGrid; 114268; 54.
IntAct; Q92538; 21.
MINT; MINT-5006508; -.
STRING; 9606.ENSP00000359000; -.
iPTMnet; Q92538; -.
PhosphoSitePlus; Q92538; -.
SwissPalm; Q92538; -.
BioMuta; GBF1; -.
DMDM; 13124260; -.
EPD; Q92538; -.
MaxQB; Q92538; -.
PaxDb; Q92538; -.
PeptideAtlas; Q92538; -.
PRIDE; Q92538; -.
Ensembl; ENST00000369983; ENSP00000359000; ENSG00000107862. [Q92538-1]
GeneID; 8729; -.
KEGG; hsa:8729; -.
UCSC; uc001kux.3; human. [Q92538-1]
CTD; 8729; -.
DisGeNET; 8729; -.
GeneCards; GBF1; -.
HGNC; HGNC:4181; GBF1.
HPA; HPA037759; -.
HPA; HPA037760; -.
MIM; 603698; gene.
neXtProt; NX_Q92538; -.
OpenTargets; ENSG00000107862; -.
PharmGKB; PA28595; -.
eggNOG; KOG0928; Eukaryota.
eggNOG; COG5307; LUCA.
GeneTree; ENSGT00890000139497; -.
HOGENOM; HOG000230678; -.
HOVERGEN; HBG005810; -.
InParanoid; Q92538; -.
KO; K18443; -.
OMA; DKYMHAG; -.
OrthoDB; EOG091G01OY; -.
PhylomeDB; Q92538; -.
TreeFam; TF105934; -.
Reactome; R-HSA-421837; Clathrin derived vesicle budding.
Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
SIGNOR; Q92538; -.
ChiTaRS; GBF1; human.
GeneWiki; GBF1; -.
GenomeRNAi; 8729; -.
PMAP-CutDB; Q92538; -.
PRO; PR:Q92538; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107862; -.
CleanEx; HS_GBF1; -.
Genevisible; Q92538; HS.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
GO; GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:GO_Central.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0002263; P:cell activation involved in immune response; IMP:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0048205; P:COPI coating of Golgi vesicle; IMP:UniProtKB.
GO; GO:0097111; P:endoplasmic reticulum-Golgi intermediate compartment organization; IMP:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0061162; P:establishment of monopolar cell polarity; IMP:UniProtKB.
GO; GO:0090166; P:Golgi disassembly; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:UniProtKB.
GO; GO:1903420; P:protein localization to endoplasmic reticulum tubular network; IMP:UniProtKB.
GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1903409; P:reactive oxygen species biosynthetic process; IMP:UniProtKB.
GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.1000.11; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR023394; Sec7_alpha_orthog.
InterPro; IPR000904; Sec7_dom.
InterPro; IPR032691; Sec7_N.
Pfam; PF01369; Sec7; 1.
Pfam; PF12783; Sec7_N; 1.
SMART; SM00222; Sec7; 1.
SUPFAM; SSF48371; SSF48371; 6.
SUPFAM; SSF48425; SSF48425; 1.
PROSITE; PS50190; SEC7; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Golgi apparatus;
Guanine-nucleotide releasing factor; Host-virus interaction;
Lipid droplet; Lipid-binding; Membrane; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Transport.
CHAIN 1 1859 Golgi-specific brefeldin A-resistance
guanine nucleotide exchange factor 1.
/FTId=PRO_0000120210.
DOMAIN 692 882 SEC7. {ECO:0000255|PROSITE-
ProRule:PRU00189}.
REGION 1 380 Interaction with RAB1B.
{ECO:0000269|PubMed:17429068}.
REGION 1 211 DCB; DCB:DCB domain and DCB:HUS domain
interaction.
{ECO:0000250|UniProtKB:Q9R1D7}.
REGION 530 550 HUS; DCB:HUS domain interaction.
{ECO:0000250|UniProtKB:Q9R1D7}.
REGION 886 1370 Phosphatidylinositol-phosphate binding;
required for translocation to the leading
edge and for ARF1 activation upon GPCR
signaling. {ECO:0000269|PubMed:22573891}.
COMPBIAS 1751 1854 Pro-rich.
MOD_RES 349 349 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 507 507 Phosphothreonine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1298 1298 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 1316 1316 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1318 1318 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1320 1320 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1335 1335 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1337 1337 Phosphothreonine; by AMPK.
{ECO:0000269|PubMed:18063581}.
MOD_RES 1475 1475 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1773 1773 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1784 1784 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 337 337 Q -> QQ (in isoform 2).
/FTId=VSP_057522.
VAR_SEQ 1494 1497 Missing (in isoform 2 and isoform 3).
/FTId=VSP_057523.
VARIANT 1693 1693 G -> S (in dbSNP:rs11191274).
/FTId=VAR_051926.
MUTAGEN 543 543 D->A: Increases interaction with COPG1
and PNPLA2. {ECO:0000269|PubMed:19039328,
ECO:0000269|PubMed:21789191}.
MUTAGEN 794 794 E->D: Inhibits Golgi membrane recruitment
of GGA1, GGA2 and GGA3; generates
misprocessing of PSAP.
{ECO:0000269|PubMed:17666033}.
MUTAGEN 794 794 E->K: Arrests retrograde ERGIC/cis-Golgi-
to-ER transport at an early step and
causes disassembly of the Golgi and
disassociation of COP1 from membranes.
{ECO:0000269|PubMed:12808027}.
MUTAGEN 832 832 M->L: Confers BFA tolerance.
{ECO:0000269|PubMed:15616190}.
MUTAGEN 1337 1337 T->A: Prevents 2-DG-induced Golgi
disassembly.
{ECO:0000269|PubMed:18063581}.
CONFLICT 24 24 A -> S (in Ref. 2; BAA13379).
{ECO:0000305}.
CONFLICT 459 459 R -> C (in Ref. 4; AK025330).
{ECO:0000305}.
CONFLICT 530 530 R -> C (in Ref. 6; AAI17682).
{ECO:0000305}.
CONFLICT 1811 1811 Q -> R (in Ref. 4; AK025330).
{ECO:0000305}.
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


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