GBF1
entrez
8729
canonical
uniprot
Q92538
canonical
ensembl
ENSG00000107862
resolver
ensp
ENSP00000359000
resolver
ensp
ENSP00000501064
resolver
ensp
ENSP00000501233
resolver
ensp
ENSP00000502877
resolver
ensp
ENSP00000502966
resolver
ensp
ENSP00000503207
resolver
ensp
ENSP00000503428
resolver
ensp
ENSP00000503565
resolver
ensp
ENSP00000503918
resolver
ensp
ENSP00000503981
resolver
ensp
ENSP00000504214
resolver
ensp
ENSP00000541663
resolver
ensp
ENSP00000541665
resolver
ensp
ENSP00000586403
resolver
ensp
ENSP00000586404
resolver
ensp
ENSP00000635553
resolver
enst
ENST00000673650
resolver
enst
ENST00000674034
resolver
enst
ENST00000677439
resolver
enst
ENST00000677618
resolver
enst
ENST00000678351
resolver
enst
ENST00000679238
resolver
enst
ENST00000916345
resolver
genesymbol
GBF1
resolver
genesymbol_syn
KIAA0248
resolver
hgnc
HGNC:4181
resolver
uniprot
A0A669KB10
resolver
uniprot
A0A669KBG8
resolver
uniprot
A0A7I2V2L5
resolver
uniprot
A0A7I2V452
resolver
uniprot
A0A7I2V514
resolver
uniprot
A0A7I2YQ65
resolver
uniprot
A0A7P0RGV0
resolver
uniprot
Q149P0
resolver
uniprot
Q149P1
resolver
uniprot
Q5VXX3
resolver
uniprot
Q96CK6
resolver
uniprot
Q96HZ3
resolver
uniprot
Q9H473
resolver
uniprot_entry
A0A669KB10_HUMAN
resolver
uniprot_entry
A0A669KBG8_HUMAN
resolver
uniprot_entry
A0A7I2V2L5_HUMAN
resolver
uniprot_entry
A0A7I2V452_HUMAN
resolver
uniprot_entry
A0A7I2V514_HUMAN
resolver
uniprot_entry
A0A7I2YQ65_HUMAN
resolver
uniprot_entry
GBF1_HUMAN
resolver
uniprot_sec
A0A7P0RGV0
resolver
uniprot_sec
Q149P0
resolver
uniprot_sec
Q149P1
resolver
uniprot_sec
Q5VXX3
resolver
uniprot_sec
Q96CK6
resolver
uniprot_sec
Q96HZ3
resolver
uniprot_sec
Q9H473
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by brefeldin A (BFA) (PubMed:15616190). Inhibited by golgicide A (GCA) (By similarity). {ECO:0000250|UniProtKB:Q9R1D7, ECO:0000269|PubMed:15616190}.
uniprot
proteins
amino_acid_sequence
MVDKNIYIIQGEINIVVGAIKRNARWSTHTPLDEERDPLLHSFGHLKEVLNSITELSEIEPNVFLRPFLEVIRSEDTTGPITGLALTSVNKFLSYALIDPTHEGTAEGMENMADAVTHARFVGTDPASDEVVLMKILQVLRTLLLTPVGAHLTNESVCEIMQSCFRICFEMRLSELLRKSAEHTLVDMVQLLFTRLPQFKEEPKNYVGTNMKKLKMRAGGMSDSSKWKKQKRSPRPPRHMTKVTPGSELPTPNGTTLSSNLTGGMPFIDVPTPISSASSEAASAVVSPSTDSGLEFSSQTTSKEDLTDLEQPGSPGYSTATEPGSSELGVPEQPDLQQEGTHVEKSQSASVESIPEVLEECTSPADHSDSASVHDMDYVNPRGVRFTQSSQKEGTALVPYGLPCIRELFRFLISLTNPHDRHNSEVMIHMGLHLLTVALESAPVAQCQTLLGLIKDEMCRHLFQLLSIERLNLYAASLRVCFLLFESMREHLKFQMEMYIKKLMEIITVENPKMPYEMKEMALEAIVQLWRIPSFVTELYINYDCDYYCSNLFEELTKLLSKNAFPVSGQLYTTHLLSLDALLTVIDSTEAHCQAKVLNSLTQQEKKETARPSCEIVDGTREASNTERTASDGKAVGMASDIPGLHLPGGGRLPPEHGKSGCSDLEEAVDSGADKKFARKPPRFSCLLPDPRELIEIKNKKKLLITGTEQFNQKPKKGIQFLQEKGLLTIPMDNTEVAQWLRENPRLDKKMIGEFVSDRKNIDLLESFVSTFSFQGLRLDEALRLYLEAFRLPGEAPVIQRLLEAFTERWMNCNGSPFANSDACFSLAYAVIMLNTDQHNHNVRKQNAPMTLEEFRKNLKGVNGGKDFEQDILEDMYHAIKNEEIVMPEEQTGLVRENYVWNVLLHRGATPEGIFLRVPTASYDLDLFTMTWGPTIAALSYVFDKSLEETIIQKAISGFRKCAMISAHYGLSDVFDNLIISLCKFTALSSESIENLPSVFGSNPKAHIAAKTVFHLAHRHGDILREGWKNIMEAMLQLFRAQLLPKAMIEVEDFVDPNGKISLQREETPSNRGESTVLSFVSWLTLSGPEQSSVRGPSTENQEAKRVALECIKQCDPEKMITESKFLQLESLQELMKALVSVTPDEETYDEEDAAFCLEMLLRIVLENRDRVGCVWQTVRDHLYHLCVQAQDFCFLVERAVVGLLRLAIRLLRREEISAQVLLSLRILLLMKPSVLSRVSHQVAYGLHELLKTNAANIHSGDDWATLFTLLECIGSGVKPPAALQATARADAPDAGAQSDSELPSYHQNDVSLDRGYTSDSEVYTDHGRPGKIHRSATDADVVNSGWLVVGKDDVDNSKPGPSRPGPSPLINQYSLTVGLDLGPHDTKSLLKCVESLSFIVRDAAHITPDNFELCVKTLRIFVEASLNGGCKSQEKRGKSHKYDSKGNRFKKKSKEGSMLRRPRTSSQHASRGGQSDDDEDEGVPASYHTVSLQVSQDLLDLMHTLHTRAASIYSSWAEEQRHLETGGQKIEADSRTLWAHCWCPLLQGIACLCCDARRQVRMQALTYLQRALLVHDLQKLDALEWESCFNKVLFPLLTKLLENISPADVGGMEETRMRASTLLSKVFLQHLSPLLSLSTFAALWLTILDFMDKYMHAGSSDLLSEAIPESLKNMLLVMDTAEIFHSADARGGGPSALWEITWERIDCFLPHLRDELFKQTVIQDPMPMEPQGQKPLASAHLTSAAGDTRTPGHPPPPEIPSELGACDFEKPESPRAASSSSPGSPVASSPSRLSPTPDGPPPLAQPPLILQPLASPLQVGVPPMTLPIILNPALIEATSPVPLLATPRPTDPIPTSEVN
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, axonal, type 2GG (CMT2GG) [MIM:606483]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2GG is an autosomal dominant form characterized by slowly progressive distal muscle weakness and atrophy primarily affecting the lower limbs and causing difficulty walking. Some individuals may also have involvement of the hands. {ECO:0000269|PubMed:32937143}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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:12047556, PubMed:12808027, PubMed:16926190, PubMed:17956946, PubMed:18003980, 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 mitosis 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). Plays a role in maintaining mitochondrial morphology (PubMed:25190516). {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:0000269|PubMed:25190516, ECO:0000305|PubMed:19039328, ECO:0000305|PubMed:22573891}.
uniprot
proteins
mass_dalton
206574
uniprot
proteins
mutagenesis
MUTAGEN 544; /note="D->A: Increases interaction with COPG1 and PNPLA2."; /evidence="ECO:0000269|PubMed:19039328, ECO:0000269|PubMed:21789191"; MUTAGEN 795; /note="E->D: Inhibits Golgi membrane recruitment of GGA1, GGA2 and GGA3; generates misprocessing of PSAP."; /evidence="ECO:0000269|PubMed:17666033"; MUTAGEN 795; /note="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."; /evidence="ECO:0000269|PubMed:12808027"; MUTAGEN 833; /note="M->L: Confers BFA tolerance."; /evidence="ECO:0000269|PubMed:15616190"; MUTAGEN 1338; /note="T->A: Prevents 2-DG-induced Golgi disassembly."; /evidence="ECO:0000269|PubMed:18063581
uniprot
proteins
post_translational_modification
PTM: AMPK-mediated phosphorylation at Thr-1338 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}.
uniprot
proteins
pubmed
12047556
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12634853
uniprot
proteins
pubmed
12808027
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616190
uniprot
proteins
pubmed
15813748
uniprot
proteins
pubmed
16926190
uniprot
proteins
pubmed
17005635
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17429068
uniprot
proteins
pubmed
17640864
uniprot
proteins
pubmed
17666033
uniprot
proteins
pubmed
17956946
uniprot
proteins
pubmed
18003980
uniprot
proteins
pubmed
18063581
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19039328
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19461073
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21789191
uniprot
proteins
pubmed
22185782
uniprot
proteins
pubmed
22573891
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23386609
uniprot
proteins
pubmed
23418352
uniprot
proteins
pubmed
24213530
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25190516
uniprot
proteins
pubmed
31519766
uniprot
proteins
pubmed
32937143
uniprot
proteins
pubmed
9039502
uniprot
proteins
pubmed
9828135
uniprot
proteins
sequence_length
1860
uniprot
proteins
subcellular_location
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}. Golgi apparatus {ECO:0000269|PubMed:31519766}. Cytoplasm {ECO:0000269|PubMed:22573891, ECO:0000269|PubMed:31519766}. 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}.
uniprot
proteins