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Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (Brefeldin A-inhibited GEP 1) (ADP-ribosylation factor guanine nucleotide-exchange factor 1) (p200 ARF guanine nucleotide exchange factor) (p200 ARF-GEP1)

 BIG1_HUMAN              Reviewed;        1849 AA.
Q9Y6D6; Q9NV46; Q9UFV2; Q9UNL0;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
28-MAR-2018, entry version 163.
RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 1;
Short=Brefeldin A-inhibited GEP 1;
AltName: Full=ADP-ribosylation factor guanine nucleotide-exchange factor 1;
AltName: Full=p200 ARF guanine nucleotide exchange factor;
AltName: Full=p200 ARF-GEP1;
Name=ARFGEF1; Synonyms=ARFGEP1, BIG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10212200; DOI=10.1074/jbc.274.18.12308;
Togawa A., Morinaga N., Ogasawara M., Moss J., Vaughan M.;
"Purification and cloning of a brefeldin A-inhibited guanine
nucleotide-exchange protein for ADP-ribosylation factors.";
J. Biol. Chem. 274:12308-12315(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10393931; DOI=10.1073/pnas.96.14.7968;
Mansour S.J., Skaug J., Zhao X.-H., Giordano J., Scherer S.W.,
Melancon P.;
"p200 ARF-GEP1: a Golgi-localized guanine nucleotide exchange protein
whose Sec7 domain is targeted by the drug brefeldin A.";
Proc. Natl. Acad. Sci. U.S.A. 96:7968-7973(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1341-1849.
TISSUE=Ovarian carcinoma;
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).
[4]
PROTEIN SEQUENCE OF 1569-1579, INTERACTION WITH TBC1D22A AND TBC1D22B,
AND MASS SPECTROMETRY.
PubMed=23572552; DOI=10.1128/mBio.00098-13;
Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
DeRisi J.L.;
"ACBD3 interaction with TBC1 domain 22 protein is differentially
affected by enteroviral and kobuviral 3A protein binding.";
MBio 4:E00098-E00098(2013).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1637-1849.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
SUBCELLULAR LOCATION, AND INTERACTION WITH ARFGEF2.
PubMed=10716990; DOI=10.1073/pnas.97.6.2567;
Yamaji R., Adamik R., Takeda K., Togawa A., Pacheco-Rodriguez G.,
Ferrans V.J., Moss J., Vaughan M.;
"Identification and localization of two brefeldin A-inhibited guanine
nucleotide-exchange proteins for ADP-ribosylation factors in a
macromolecular complex.";
Proc. Natl. Acad. Sci. U.S.A. 97:2567-2572(2000).
[7]
FUNCTION, INTERACTION WITH PRKAR1A AND PRKAR2A, AND SUBCELLULAR
LOCATION.
PubMed=12571360; DOI=10.1073/pnas.0337678100;
Li H., Adamik R., Pacheco-Rodriguez G., Moss J., Vaughan M.;
"Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited
guanine nucleotide-exchange protein 2 (BIG2).";
Proc. Natl. Acad. Sci. U.S.A. 100:1627-1632(2003).
[8]
INTERACTION WITH FKBP2.
PubMed=12606707; DOI=10.1073/pnas.2628047100;
Padilla P.I., Chang M.J., Pacheco-Rodriguez G., Adamik R., Moss J.,
Vaughan M.;
"Interaction of FK506-binding protein 13 with brefeldin A-inhibited
guanine nucleotide-exchange protein 1 (BIG1): effects of FK506.";
Proc. Natl. Acad. Sci. U.S.A. 100:2322-2327(2003).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH NCL AND NUP62.
PubMed=14973189; DOI=10.1073/pnas.0307345101;
Padilla P.I., Pacheco-Rodriguez G., Moss J., Vaughan M.;
"Nuclear localization and molecular partners of BIG1, a brefeldin A-
inhibited guanine nucleotide-exchange protein for ADP-ribosylation
factors.";
Proc. Natl. Acad. Sci. U.S.A. 101:2752-2757(2004).
[10]
FUNCTION, AND INTERACTION WITH MYO9B.
PubMed=15644318; DOI=10.1074/jbc.M413415200;
Saeki N., Tokuo H., Ikebe M.;
"BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase
activating protein activity.";
J. Biol. Chem. 280:10128-10134(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569, AND 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).
[12]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 712-LYS--LYS-714 AND SER-883.
PubMed=16467138; DOI=10.1073/pnas.0510571103;
Citterio C., Jones H.D., Pacheco-Rodriguez G., Islam A., Moss J.,
Vaughan M.;
"Effect of protein kinase A on accumulation of brefeldin A-inhibited
guanine nucleotide-exchange protein 1 (BIG1) in HepG2 cell nuclei.";
Proc. Natl. Acad. Sci. U.S.A. 103:2683-2688(2006).
[13]
HOMODIMERIZATION, AND MUTAGENESIS OF GLU-221.
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).
[14]
FUNCTION.
PubMed=17227842; DOI=10.1073/pnas.0610535104;
Shen X., Hong M.S., Moss J., Vaughan M.;
"BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is
required for correct glycosylation and function of integrin beta1.";
Proc. Natl. Acad. Sci. U.S.A. 104:1230-1235(2007).
[15]
PHOSPHORYLATION, AND INTERACTION WITH PPP1CC.
PubMed=17360629; DOI=10.1073/pnas.0611696104;
Kuroda F., Moss J., Vaughan M.;
"Regulation of brefeldin A-inhibited guanine nucleotide-exchange
protein 1 (BIG1) and BIG2 activity via PKA and protein phosphatase
1gamma.";
Proc. Natl. Acad. Sci. U.S.A. 104:3201-3206(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569, AND 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569, 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).
[18]
INTERACTION WITH NCL; FBL; NUP62 AND U3 SMALL NUCLEOLAR RNA, AND
IDENTIFICATION IN SMALL NUCLEAR RIBONUCLEOPROTEIN COMPLEX.
PubMed=18292223; DOI=10.1073/pnas.0712387105;
Padilla P.I., Uhart M., Pacheco-Rodriguez G., Peculis B.A., Moss J.,
Vaughan M.;
"Association of guanine nucleotide-exchange protein BIG1 in HepG2 cell
nuclei with nucleolin, U3 snoRNA, and fibrillarin.";
Proc. Natl. Acad. Sci. U.S.A. 105:3357-3361(2008).
[19]
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).
[20]
INTERACTION WITH DPY30.
PubMed=19651892; DOI=10.1083/jcb.200902146;
Xu Z., Gong Q., Xia B., Groves B., Zimmermann M., Mugler C., Mu D.,
Matsumoto B., Seaman M., Ma D.;
"A role of histone H3 lysine 4 methyltransferase components in
endosomal trafficking.";
J. Cell Biol. 186:343-353(2009).
[21]
INTERACTION WITH PDE3A.
PubMed=19332778; DOI=10.1073/pnas.0901558106;
Puxeddu E., Uhart M., Li C.C., Ahmad F., Pacheco-Rodriguez G.,
Manganiello V.C., Moss J., Vaughan M.;
"Interaction of phosphodiesterase 3A with brefeldin A-inhibited
guanine nucleotide-exchange proteins BIG1 and BIG2 and effect on ARF1
activity.";
Proc. Natl. Acad. Sci. U.S.A. 106:6158-6163(2009).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569, 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).
[24]
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).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KANK1.
PubMed=22084092; DOI=10.1073/pnas.1117011108;
Li C.C., Kuo J.C., Waterman C.M., Kiyama R., Moss J., Vaughan M.;
"Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1
and KANK1 proteins on cell polarity and directed migration during
wound healing.";
Proc. Natl. Acad. Sci. U.S.A. 108:19228-19233(2011).
[26]
FUNCTION.
PubMed=20360857; DOI=10.1371/journal.pone.0009898;
Boal F., Stephens D.J.;
"Specific functions of BIG1 and BIG2 in endomembrane organization.";
PLoS ONE 5:E9898-E9898(2010).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1079 AND SER-1569, 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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-397; SER-410 AND
SER-1569, 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569, 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).
[30]
VARIANT [LARGE SCALE ANALYSIS] GLU-316.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3.
Promotes the activation of ARF1/ARF3 through replacement of GDP
with GTP. Involved in vesicular trafficking. Required for the
maintenance of Golgi structure; the function may be independent of
its GEF activity. Required for the maturaion of integrin beta-1 in
the Golgi. Involved in the establishment and persistence of cell
polarity during directed cell movement in wound healing. Proposed
to act as A kinase-anchoring protein (AKAP) and may mediate
crosstalk between Arf and PKA pathways. Inhibits GAP activity of
MYO9B probably through competetive RhoA binding. The function in
the nucleus remains to be determined.
{ECO:0000269|PubMed:12571360, ECO:0000269|PubMed:15644318,
ECO:0000269|PubMed:17227842, ECO:0000269|PubMed:20360857,
ECO:0000269|PubMed:22084092}.
-!- ENZYME REGULATION: Inhibited by brefeldin A.
-!- SUBUNIT: Homodimer (PubMed:17640864). Interacts with ARFGEF2/BIG2;
both proteins are probably part of the same or very similar
macromolecular complexes (PubMed:10716990). Interacts with FKBP2
(PubMed:12606707). Interacts with MYO9B (PubMed:15644318).
Interacts with PRKAR1A and PRKAR2A (PubMed:12571360). Interacts
with PPP1CC (PubMed:17360629). Interacts with NCL, FBL, NUP62 and
U3 small nucleolar RNA (PubMed:14973189, PubMed:18292223).
Interacts with DPY30 (PubMed:19651892). Interacts with PDE3A
(PubMed:19332778). Interacts with KANK1 (PubMed:22084092).
Interacts with TBC1D22A and TBC1D22B (PubMed:23572552).
{ECO:0000269|PubMed:10716990, ECO:0000269|PubMed:12571360,
ECO:0000269|PubMed:12606707, ECO:0000269|PubMed:14973189,
ECO:0000269|PubMed:15644318, ECO:0000269|PubMed:17360629,
ECO:0000269|PubMed:17640864, ECO:0000269|PubMed:18292223,
ECO:0000269|PubMed:19332778, ECO:0000269|PubMed:19651892,
ECO:0000269|PubMed:22084092, ECO:0000269|PubMed:23572552}.
-!- INTERACTION:
Q9Y6D5:ARFGEF2; NbExp=12; IntAct=EBI-1044254, EBI-2837511;
Q14678:KANK1; NbExp=8; IntAct=EBI-1044254, EBI-2556221;
Q7Z4S6:KIF21A; NbExp=7; IntAct=EBI-1044254, EBI-2691397;
Q7Z4S6-2:KIF21A; NbExp=4; IntAct=EBI-1044254, EBI-6251716;
Q99417:MYCBP; NbExp=3; IntAct=EBI-1044254, EBI-716185;
Q13459-2:MYO9B; NbExp=2; IntAct=EBI-1044254, EBI-6251250;
P19338:NCL; NbExp=5; IntAct=EBI-1044254, EBI-346967;
Q14432:PDE3A; NbExp=6; IntAct=EBI-1044254, EBI-7192066;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Golgi apparatus. Golgi apparatus, trans-Golgi network
{ECO:0000250}. Nucleus. Nucleus, nucleolus. Nucleus matrix.
Membrane. Note=Translocates from cytoplasm to membranes and
nucleus upon cAMP treatment.
-!- TISSUE SPECIFICITY: Expressed in placenta, lung, heart, brain,
kidney and pancreas.
-!- PTM: Phosphorylated. In vitro phosphorylated by PKA reducing its
GEF activity and dephosphorylated by phosphatase PP1.
{ECO:0000269|PubMed:17360629}.
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EMBL; AF084520; AAD38427.1; -; mRNA.
EMBL; AF111162; AAD43651.1; -; mRNA.
EMBL; AK001788; BAA91912.1; -; mRNA.
EMBL; AL117446; CAB55931.1; -; mRNA.
CCDS; CCDS6199.1; -.
PIR; T17241; T17241.
RefSeq; NP_006412.2; NM_006421.4.
RefSeq; XP_005251191.1; XM_005251134.4.
UniGene; Hs.656902; -.
PDB; 3LTL; X-ray; 2.20 A; A/B=691-889.
PDB; 5EE5; X-ray; 2.28 A; A=1-229.
PDB; 5J5C; X-ray; 3.40 A; B=1-224.
PDBsum; 3LTL; -.
PDBsum; 5EE5; -.
PDBsum; 5J5C; -.
ProteinModelPortal; Q9Y6D6; -.
SMR; Q9Y6D6; -.
BioGrid; 115816; 35.
DIP; DIP-29748N; -.
IntAct; Q9Y6D6; 20.
STRING; 9606.ENSP00000262215; -.
iPTMnet; Q9Y6D6; -.
PhosphoSitePlus; Q9Y6D6; -.
BioMuta; ARFGEF1; -.
DMDM; 116241267; -.
EPD; Q9Y6D6; -.
MaxQB; Q9Y6D6; -.
PaxDb; Q9Y6D6; -.
PeptideAtlas; Q9Y6D6; -.
PRIDE; Q9Y6D6; -.
Ensembl; ENST00000262215; ENSP00000262215; ENSG00000066777.
GeneID; 10565; -.
KEGG; hsa:10565; -.
UCSC; uc003xxo.2; human.
CTD; 10565; -.
DisGeNET; 10565; -.
EuPathDB; HostDB:ENSG00000066777.8; -.
GeneCards; ARFGEF1; -.
HGNC; HGNC:15772; ARFGEF1.
HPA; HPA023399; -.
HPA; HPA023822; -.
MIM; 604141; gene.
neXtProt; NX_Q9Y6D6; -.
OpenTargets; ENSG00000066777; -.
PharmGKB; PA134908197; -.
eggNOG; KOG0929; Eukaryota.
eggNOG; COG5307; LUCA.
GeneTree; ENSGT00760000119036; -.
HOGENOM; HOG000181045; -.
HOVERGEN; HBG004846; -.
InParanoid; Q9Y6D6; -.
KO; K18442; -.
OMA; LLWNMEM; -.
OrthoDB; EOG091G00F0; -.
PhylomeDB; Q9Y6D6; -.
TreeFam; TF300714; -.
ChiTaRS; ARFGEF1; human.
EvolutionaryTrace; Q9Y6D6; -.
GeneWiki; ARFGEF1; -.
GenomeRNAi; 10565; -.
PRO; PR:Q9Y6D6; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000066777; -.
CleanEx; HS_ARFGEF1; -.
ExpressionAtlas; Q9Y6D6; baseline and differential.
Genevisible; Q9Y6D6; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IBA:GO_Central.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:UniProtKB.
GO; GO:0010256; P:endomembrane system organization; IMP:UniProtKB.
GO; GO:0006887; P:exocytosis; TAS:ProtInc.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0090284; P:positive regulation of protein glycosylation in Golgi; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0090303; P:positive regulation of wound healing; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
Gene3D; 1.10.1000.11; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032629; DCB_dom.
InterPro; IPR015403; Sec7_C.
InterPro; IPR023394; Sec7_C_sf.
InterPro; IPR000904; Sec7_dom.
InterPro; IPR035999; Sec7_dom_sf.
InterPro; IPR032691; Sec7_N.
Pfam; PF16213; DCB; 1.
Pfam; PF09324; DUF1981; 1.
Pfam; PF01369; Sec7; 1.
Pfam; PF12783; Sec7_N; 1.
SMART; SM00222; Sec7; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF48425; SSF48425; 1.
PROSITE; PS50190; SEC7; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
Nucleus; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Transport.
CHAIN 1 1849 Brefeldin A-inhibited guanine nucleotide-
exchange protein 1.
/FTId=PRO_0000120207.
DOMAIN 709 840 SEC7. {ECO:0000255|PROSITE-
ProRule:PRU00189}.
REGION 2 224 DCB; DCB:DCB domain and DCB:HUS domain
interaction.
REGION 557 577 HUS; DCB:HUS domain interaction.
MOTIF 711 715 Nuclear localization signal (NLS).
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000250|UniProtKB:G3X9K3}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:G3X9K3}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:D4A631}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1566 1566 Phosphoserine.
{ECO:0000250|UniProtKB:D4A631}.
MOD_RES 1569 1569 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 273 273 D -> Y (in dbSNP:rs4321984).
/FTId=VAR_028749.
VARIANT 316 316 G -> E (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036155.
MUTAGEN 221 221 E->K: No effect on self-association.
{ECO:0000269|PubMed:17640864}.
MUTAGEN 712 714 KPK->AAA: Inhibits nuclear localization.
{ECO:0000269|PubMed:16467138}.
MUTAGEN 883 883 S->A: Abolishes cAMP-induced nuclear
localization.
{ECO:0000269|PubMed:16467138}.
MUTAGEN 883 883 S->D: No effect on cAMP-induced nuclear
localization.
{ECO:0000269|PubMed:16467138}.
CONFLICT 233 233 Q -> P (in Ref. 1; AAD38427).
{ECO:0000305}.
CONFLICT 620 620 L -> S (in Ref. 1; AAD38427).
{ECO:0000305}.
CONFLICT 1055 1055 E -> K (in Ref. 1; AAD38427).
{ECO:0000305}.
CONFLICT 1590 1590 V -> A (in Ref. 3; BAA91912).
{ECO:0000305}.
HELIX 7 21 {ECO:0000244|PDB:5EE5}.
HELIX 23 25 {ECO:0000244|PDB:5EE5}.
HELIX 28 30 {ECO:0000244|PDB:5EE5}.
HELIX 31 48 {ECO:0000244|PDB:5EE5}.
HELIX 77 80 {ECO:0000244|PDB:5EE5}.
HELIX 81 88 {ECO:0000244|PDB:5EE5}.
HELIX 93 108 {ECO:0000244|PDB:5EE5}.
STRAND 122 124 {ECO:0000244|PDB:5J5C}.
HELIX 126 135 {ECO:0000244|PDB:5EE5}.
HELIX 145 160 {ECO:0000244|PDB:5EE5}.
HELIX 168 184 {ECO:0000244|PDB:5EE5}.
HELIX 188 194 {ECO:0000244|PDB:5EE5}.
HELIX 197 224 {ECO:0000244|PDB:5EE5}.
HELIX 698 711 {ECO:0000244|PDB:3LTL}.
HELIX 713 722 {ECO:0000244|PDB:3LTL}.
HELIX 730 739 {ECO:0000244|PDB:3LTL}.
HELIX 745 752 {ECO:0000244|PDB:3LTL}.
HELIX 757 768 {ECO:0000244|PDB:3LTL}.
HELIX 777 786 {ECO:0000244|PDB:3LTL}.
HELIX 794 810 {ECO:0000244|PDB:3LTL}.
HELIX 821 838 {ECO:0000244|PDB:3LTL}.
HELIX 849 855 {ECO:0000244|PDB:3LTL}.
STRAND 861 864 {ECO:0000244|PDB:3LTL}.
HELIX 867 879 {ECO:0000244|PDB:3LTL}.
SEQUENCE 1849 AA; 208767 MW; 1EB2547F28F63BCA CRC64;
MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKAETEK QSPPHGEAKA
GSSTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGNAPDST
TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN
IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM EKERHRQHHH LLQSPVSHHE
PESPQLRYLP PQTVDHISQE HEGDLDLHTN DVDKSLQDDT EPENGSDISS AENEQTEADQ
ATAAETLSKN EVLYDGENHD CEEKPQDIVQ NIVEEMVNIV VGDMGEGTTI NASADGNIGT
IEDGSDSENI QANGIPGTPI SVAYTPSLPD DRLSVSSNDT QESGNSSGPS PGAKFSHILQ
KDAFLVFRSL CKLSMKPLSD GPPDPKSHEL RSKILSLQLL LSILQNAGPI FRTNEMFINA
IKQYLCVALS KNGVSSVPEV FELSLSIFLT LLSNFKTHLK MQIEVFFKEI FLYILETSTS
SFDHKWMVIQ TLTRICADAQ SVVDIYVNYD CDLNAANIFE RLVNDLSKIA QGRGSQELGM
SNVQELSLRK KGLECLVSIL KCMVEWSKDQ YVNPNSQTTL GQEKPSEQEM SEIKHPETIN
RYGSLNSLES TSSSGIGSYS TQMSGTDNPE QFEVLKQQKE IIEQGIDLFN KKPKRGIQYL
QEQGMLGTTP EDIAQFLHQE ERLDSTQVGE FLGDNDKFNK EVMYAYVDQH DFSGKDFVSA
LRMFLEGFRL PGEAQKIDRL MEKFAARYLE CNQGQTLFAS ADTAYVLAYS IIMLTTDLHS
PQVKNKMTKE QYIKMNRGIN DSKDLPEEYL SAIYNEIAGK KISMKETKEL TIPTKSSKQN
VASEKQRRLL YNLEMEQMAK TAKALMEAVS HVQAPFTSAT HLEHVRPMFK LAWTPFLAAF
SVGLQDCDDT EVASLCLEGI RCAIRIACIF SIQLERDAYV QALARFTLLT VSSGITEMKQ
KNIDTIKTLI TVAHTDGNYL GNSWHEILKC ISQLELAQLI GTGVKPRYIS GTVRGREGSL
TGTKDQAPDE FVGLGLVGGN VDWKQIASIQ ESIGETSSQS VVVAVDRIFT GSTRLDGNAI
VDFVRWLCAV SMDELLSTTH PRMFSLQKIV EISYYNMGRI RLQWSRIWEV IGDHFNKVGC
NPNEDVAIFA VDSLRQLSMK FLEKGELANF RFQKDFLRPF EHIMKRNRSP TIRDMVVRCI
AQMVNSQAAN IRSGWKNIFS VFHLAASDQD ESIVELAFQT TGHIVTLVFE KHFPATIDSF
QDAVKCLSEF ACNAAFPDTS MEAIRLIRHC AKYVSDRPQA FKEYTSDDMN VAPEDRVWVR
GWFPILFELS CIINRCKLDV RTRGLTVMFE IMKTYGHTYE KHWWQDLFRI VFRIFDNMKL
PEQQTEKAEW MTTTCNHALY AICDVFTQYL EVLSDVLLDD IFAQLYWCVQ QDNEQLARSG
TNCLENVVIL NGEKFTLEIW DKTCNCTLDI FKTTIPHALL TWRPNSGETA PPPPSPVSEK
PLDTISQKSV DIHDSIQPRS VDNRPQAPLV SASAVNEEVS KIKSTAKFPE QKLFAALLIK
CVVQLELIQT IDNIVFFPAT SKKEDAENLA AAQRDAVDFD VRVDTQDQGM YRFLTSQQLF
KLLDCLLESH RFAKAFNSNN EQRTALWKAG FKGKSKPNLL KQETSSLACG LRILFRMYMD
ESRVSAWEEV QQRLLNVCSE ALSYFLTLTS ESHREAWTNL LLLFLTKVLK ISDNRFKAHA
SFYYPLLCEI MQFDLIPELR AVLRRFFLRI GVVFQISQPP EQELGINKQ


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