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Protein

Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1

Gene

GBF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 endoplasmatic 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).By similarity2 Publications14 Publications

Enzyme regulationi

Inhibited by brefeldin A (BFA) (PubMed:15616190). Inhibited by golgicide A (GCA) (By similarity).By similarity1 Publication

GO - Molecular functioni

  • ARF guanyl-nucleotide exchange factor activity Source: GO_Central
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB

GO - Biological processi

  • cell activation involved in immune response Source: UniProtKB
  • COPI coating of Golgi vesicle Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment organization Source: UniProtKB
  • establishment of monopolar cell polarity Source: UniProtKB
  • Golgi disassembly Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • Golgi to endosome transport Source: UniProtKB
  • membrane organization Source: Reactome
  • neutrophil chemotaxis Source: UniProtKB
  • organelle organization Source: Reactome
  • positive regulation of GTPase activity Source: GOC
  • post-Golgi vesicle-mediated transport Source: Reactome
  • protein localization to endoplasmic reticulum exit site Source: UniProtKB
  • protein localization to endoplasmic reticulum tubular network Source: UniProtKB
  • protein localization to Golgi apparatus Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • reactive oxygen species biosynthetic process Source: UniProtKB
  • regulation of cell adhesion Source: GO_Central
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of protein localization to cell surface Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
  • retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
REACT_19187. Clathrin derived vesicle budding.
REACT_268299. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
Short name:
BFA-resistant GEF 1
Gene namesi
Name:GBF1
Synonyms:KIAA0248
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:4181. GBF1.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: UniProtKB
  • cis-Golgi network Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • endoplasmic reticulum lumen Source: Ensembl
  • Golgi apparatus Source: HPA
  • Golgi membrane Source: Reactome
  • Golgi stack Source: Ensembl
  • lipid particle Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • peroxisome Source: Ensembl
  • plasma membrane Source: GO_Central
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Lipid droplet, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi543 – 5431D → A: Increases interaction with COPG1 and PNPLA2. 2 Publications
Mutagenesisi794 – 7941E → D: Inhibits Golgi membrane recruitment of GGA1, GGA2 and GGA3; generates misprocessing of PSAP. 1 Publication
Mutagenesisi794 – 7941E → 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. 1 Publication
Mutagenesisi832 – 8321M → L: Confers BFA tolerance. 1 Publication
Mutagenesisi1337 – 13371T → A: Prevents 2-DG-induced Golgi disassembly. 1 Publication

Organism-specific databases

PharmGKBiPA28595.

Polymorphism and mutation databases

BioMutaiGBF1.
DMDMi13124260.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18591859Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1PRO_0000120210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication
Modified residuei507 – 5071Phosphothreonine1 Publication
Modified residuei662 – 6621Phosphoserine1 Publication
Modified residuei1298 – 12981Phosphoserine4 Publications
Modified residuei1316 – 13161Phosphotyrosine1 Publication
Modified residuei1320 – 13201Phosphoserine1 Publication
Modified residuei1335 – 13351Phosphoserine1 Publication
Modified residuei1337 – 13371Phosphothreonine; by AMPK1 Publication
Modified residuei1475 – 14751Phosphoserine1 Publication
Modified residuei1773 – 17731Phosphoserine1 Publication
Modified residuei1784 – 17841Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92538.
PaxDbiQ92538.
PeptideAtlasiQ92538.
PRIDEiQ92538.

PTM databases

PhosphoSiteiQ92538.

Miscellaneous databases

PMAP-CutDBQ92538.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ92538.
CleanExiHS_GBF1.
GenevisibleiQ92538. HS.

Organism-specific databases

HPAiHPA037759.
HPA037760.

Interactioni

Subunit structurei

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).By similarity2 Publications7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COPG1P536202EBI-359050,EBI-8511600From a different organism.
COPG1Q9Y6782EBI-359050,EBI-1049127

Protein-protein interaction databases

BioGridi114268. 26 interactions.
IntActiQ92538. 8 interactions.
MINTiMINT-5006508.
STRINGi9606.ENSP00000359000.

Structurei

3D structure databases

ProteinModelPortaliQ92538.
SMRiQ92538. Positions 706-889.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini692 – 882191SEC7PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 380380Interaction with RAB1B1 PublicationAdd
BLAST
Regioni1 – 211211DCB; DCB:DCB domain and DCB:HUS domain interactionBy similarityAdd
BLAST
Regioni530 – 55021HUS; DCB:HUS domain interactionBy similarityAdd
BLAST
Regioni886 – 1370485Phosphatidylinositol-phosphate binding; required for translocation to the leading edge and for ARF1 activation upon GPCR signaling1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1751 – 1854104Pro-richAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 SEC7 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00770000120644.
HOGENOMiHOG000230678.
HOVERGENiHBG005810.
InParanoidiQ92538.
KOiK18443.
OMAiAFTERWM.
OrthoDBiEOG7Z3F3M.
PhylomeDBiQ92538.
TreeFamiTF105934.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamiPF01369. Sec7. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92538-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVDKNIYIIQ GEINIVVGAI KRNARWSTHT PLDEERDPLL HSFGHLKEVL
60 70 80 90 100
NSITELSEIE PNVFLRPFLE VIRSEDTTGP ITGLALTSVN KFLSYALIDP
110 120 130 140 150
THEGTAEGME NMADAVTHAR FVGTDPASDE VVLMKILQVL RTLLLTPVGA
160 170 180 190 200
HLTNESVCEI MQSCFRICFE MRLSELLRKS AEHTLVDMVQ LLFTRLPQFK
210 220 230 240 250
EEPKNYVGTN MKKLKMRAGG MSDSSKWKKQ KRSPRPPRHM TKVTPGSELP
260 270 280 290 300
TPNGTTLSSN LTGGMPFIDV PTPISSASSE AASAVVSPST DSGLEFSSQT
310 320 330 340 350
TSKEDLTDLE QPGSPGYSTA TEPGSSELGV PEQPDLQEGT HVEKSQSASV
360 370 380 390 400
ESIPEVLEEC TSPADHSDSA SVHDMDYVNP RGVRFTQSSQ KEGTALVPYG
410 420 430 440 450
LPCIRELFRF LISLTNPHDR HNSEVMIHMG LHLLTVALES APVAQCQTLL
460 470 480 490 500
GLIKDEMCRH LFQLLSIERL NLYAASLRVC FLLFESMREH LKFQMEMYIK
510 520 530 540 550
KLMEIITVEN PKMPYEMKEM ALEAIVQLWR IPSFVTELYI NYDCDYYCSN
560 570 580 590 600
LFEELTKLLS KNAFPVSGQL YTTHLLSLDA LLTVIDSTEA HCQAKVLNSL
610 620 630 640 650
TQQEKKETAR PSCEIVDGTR EASNTERTAS DGKAVGMASD IPGLHLPGGG
660 670 680 690 700
RLPPEHGKSG CSDLEEAVDS GADKKFARKP PRFSCLLPDP RELIEIKNKK
710 720 730 740 750
KLLITGTEQF NQKPKKGIQF LQEKGLLTIP MDNTEVAQWL RENPRLDKKM
760 770 780 790 800
IGEFVSDRKN IDLLESFVST FSFQGLRLDE ALRLYLEAFR LPGEAPVIQR
810 820 830 840 850
LLEAFTERWM NCNGSPFANS DACFSLAYAV IMLNTDQHNH NVRKQNAPMT
860 870 880 890 900
LEEFRKNLKG VNGGKDFEQD ILEDMYHAIK NEEIVMPEEQ TGLVRENYVW
910 920 930 940 950
NVLLHRGATP EGIFLRVPTA SYDLDLFTMT WGPTIAALSY VFDKSLEETI
960 970 980 990 1000
IQKAISGFRK CAMISAHYGL SDVFDNLIIS LCKFTALSSE SIENLPSVFG
1010 1020 1030 1040 1050
SNPKAHIAAK TVFHLAHRHG DILREGWKNI MEAMLQLFRA QLLPKAMIEV
1060 1070 1080 1090 1100
EDFVDPNGKI SLQREETPSN RGESTVLSFV SWLTLSGPEQ SSVRGPSTEN
1110 1120 1130 1140 1150
QEAKRVALEC IKQCDPEKMI TESKFLQLES LQELMKALVS VTPDEETYDE
1160 1170 1180 1190 1200
EDAAFCLEML LRIVLENRDR VGCVWQTVRD HLYHLCVQAQ DFCFLVERAV
1210 1220 1230 1240 1250
VGLLRLAIRL LRREEISAQV LLSLRILLLM KPSVLSRVSH QVAYGLHELL
1260 1270 1280 1290 1300
KTNAANIHSG DDWATLFTLL ECIGSGVKPP AALQATARAD APDAGAQSDS
1310 1320 1330 1340 1350
ELPSYHQNDV SLDRGYTSDS EVYTDHGRPG KIHRSATDAD VVNSGWLVVG
1360 1370 1380 1390 1400
KDDVDNSKPG PSRPGPSPLI NQYSLTVGLD LGPHDTKSLL KCVESLSFIV
1410 1420 1430 1440 1450
RDAAHITPDN FELCVKTLRI FVEASLNGGC KSQEKRGKSH KYDSKGNRFK
1460 1470 1480 1490 1500
KKSKEGSMLR RPRTSSQHAS RGGQSDDDED EGVPASYHTV SLQVSQDLLD
1510 1520 1530 1540 1550
LMHTLHTRAA SIYSSWAEEQ RHLETGGQKI EADSRTLWAH CWCPLLQGIA
1560 1570 1580 1590 1600
CLCCDARRQV RMQALTYLQR ALLVHDLQKL DALEWESCFN KVLFPLLTKL
1610 1620 1630 1640 1650
LENISPADVG GMEETRMRAS TLLSKVFLQH LSPLLSLSTF AALWLTILDF
1660 1670 1680 1690 1700
MDKYMHAGSS DLLSEAIPES LKNMLLVMDT AEIFHSADAR GGGPSALWEI
1710 1720 1730 1740 1750
TWERIDCFLP HLRDELFKQT VIQDPMPMEP QGQKPLASAH LTSAAGDTRT
1760 1770 1780 1790 1800
PGHPPPPEIP SELGACDFEK PESPRAASSS SPGSPVASSP SRLSPTPDGP
1810 1820 1830 1840 1850
PPLAQPPLIL QPLASPLQVG VPPMTLPIIL NPALIEATSP VPLLATPRPT

DPIPTSEVN
Length:1,859
Mass (Da):206,446
Last modified:August 1, 1999 - v2
Checksum:i5015D2BD70009CFA
GO
Isoform 2 (identifier: Q92538-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     337-337: Q → QQ
     1494-1497: Missing.

Show »
Length:1,856
Mass (Da):206,145
Checksum:iD860E5B3CBF664C7
GO
Isoform 3 (identifier: Q92538-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1494-1497: Missing.

Show »
Length:1,855
Mass (Da):206,016
Checksum:iF166270903224465
GO

Sequence cautioni

The sequence BAA13379.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241A → S in BAA13379 (PubMed:9039502).Curated
Sequence conflicti459 – 4591R → C in AK025330 (PubMed:14702039).Curated
Sequence conflicti530 – 5301R → C in AAI17682 (PubMed:15489334).Curated
Sequence conflicti1811 – 18111Q → R in AK025330 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1693 – 16931G → S.
Corresponds to variant rs11191274 [ dbSNP | Ensembl ].
VAR_051926

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei337 – 3371Q → QQ in isoform 2. VSP_057522
Alternative sequencei1494 – 14974Missing in isoform 2 and isoform 3. VSP_057523

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068755 mRNA. Translation: AAD15903.1.
D87435 mRNA. Translation: BAA13379.2. Different initiation.
AK025330 mRNA. No translation available.
AL356420, AL121928, AL160011 Genomic DNA. Translation: CAH72761.1.
AL121928, AL160011, AL356420 Genomic DNA. Translation: CAI12515.1.
AL160011, AL121928, AL356420 Genomic DNA. Translation: CAH71625.1.
BC007941 mRNA. Translation: AAH07941.2.
BC117681 mRNA. Translation: AAI17682.1.
BC117682 mRNA. Translation: AAI17683.1.
BC014171 mRNA. Translation: AAH14171.2.
CCDSiCCDS7533.1. [Q92538-1]
RefSeqiNP_001186307.1. NM_001199378.1. [Q92538-2]
NP_001186308.1. NM_001199379.1. [Q92538-3]
NP_004184.1. NM_004193.2. [Q92538-1]
UniGeneiHs.290243.

Genome annotation databases

EnsembliENST00000369983; ENSP00000359000; ENSG00000107862. [Q92538-1]
GeneIDi8729.
KEGGihsa:8729.
UCSCiuc001kux.2. human. [Q92538-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068755 mRNA. Translation: AAD15903.1.
D87435 mRNA. Translation: BAA13379.2. Different initiation.
AK025330 mRNA. No translation available.
AL356420, AL121928, AL160011 Genomic DNA. Translation: CAH72761.1.
AL121928, AL160011, AL356420 Genomic DNA. Translation: CAI12515.1.
AL160011, AL121928, AL356420 Genomic DNA. Translation: CAH71625.1.
BC007941 mRNA. Translation: AAH07941.2.
BC117681 mRNA. Translation: AAI17682.1.
BC117682 mRNA. Translation: AAI17683.1.
BC014171 mRNA. Translation: AAH14171.2.
CCDSiCCDS7533.1. [Q92538-1]
RefSeqiNP_001186307.1. NM_001199378.1. [Q92538-2]
NP_001186308.1. NM_001199379.1. [Q92538-3]
NP_004184.1. NM_004193.2. [Q92538-1]
UniGeneiHs.290243.

3D structure databases

ProteinModelPortaliQ92538.
SMRiQ92538. Positions 706-889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114268. 26 interactions.
IntActiQ92538. 8 interactions.
MINTiMINT-5006508.
STRINGi9606.ENSP00000359000.

PTM databases

PhosphoSiteiQ92538.

Polymorphism and mutation databases

BioMutaiGBF1.
DMDMi13124260.

Proteomic databases

MaxQBiQ92538.
PaxDbiQ92538.
PeptideAtlasiQ92538.
PRIDEiQ92538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369983; ENSP00000359000; ENSG00000107862. [Q92538-1]
GeneIDi8729.
KEGGihsa:8729.
UCSCiuc001kux.2. human. [Q92538-1]

Organism-specific databases

CTDi8729.
GeneCardsiGC10P103995.
HGNCiHGNC:4181. GBF1.
HPAiHPA037759.
HPA037760.
MIMi603698. gene.
neXtProtiNX_Q92538.
PharmGKBiPA28595.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00770000120644.
HOGENOMiHOG000230678.
HOVERGENiHBG005810.
InParanoidiQ92538.
KOiK18443.
OMAiAFTERWM.
OrthoDBiEOG7Z3F3M.
PhylomeDBiQ92538.
TreeFamiTF105934.

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
REACT_19187. Clathrin derived vesicle budding.
REACT_268299. VxPx cargo-targeting to cilium.

Miscellaneous databases

ChiTaRSiGBF1. human.
GeneWikiiGBF1.
GenomeRNAii8729.
NextBioi32749.
PMAP-CutDBQ92538.
PROiQ92538.
SOURCEiSearch...

Gene expression databases

BgeeiQ92538.
CleanExiHS_GBF1.
GenevisibleiQ92538. HS.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamiPF01369. Sec7. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human GBF1 is a ubiquitously expressed gene of the sec7 domain family mapping to 10q24."
    Mansour S.J., Herbrick J.-A., Scherer S.W., Melancon P.
    Genomics 54:323-327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    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.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Kidney and Muscle.
  7. "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."
    Kawamoto K., Yoshida Y., Tamaki H., Torii S., Shinotsuka C., Yamashina S., Nakayama K.
    Traffic 3:483-495(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor."
    Garcia-Mata R., Sztul E.
    EMBO Rep. 4:320-325(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USO1.
  9. "ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1."
    Garcia-Mata R., Szul T., Alvarez C., Sztul E.
    Mol. Biol. Cell 14:2250-2261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-794.
  10. "Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi."
    Niu T.K., Pfeifer A.C., Lippincott-Schwartz J., Jackson C.L.
    Mol. Biol. Cell 16:1213-1222(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; ARF3; ARF4 AND ARF5, ENZYME REGULATION, MUTAGENESIS OF MET-832.
  11. "Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1."
    Szul T., Garcia-Mata R., Brandon E., Shestopal S., Alvarez C., Sztul E.
    Traffic 6:374-385(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-Golgi protein traffic."
    Zhao X., Claude A., Chun J., Shields D.J., Presley J.F., Melancon P.
    J. Cell Sci. 119:3743-3753(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment."
    Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L., Melchers W.J., van Kuppeveld F.J.
    J. Virol. 80:11852-11860(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLIOVIRUS PROTEIN 3A.
  15. "Interactions between conserved domains within homodimers in the BIG1, BIG2, and GBF1 Arf guanine nucleotide exchange factors."
    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.
    J. Biol. Chem. 282:28834-28842(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  16. "Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking."
    Szul T., Grabski R., Lyons S., Morohashi Y., Shestopal S., Lowe M., Sztul E.
    J. Cell Sci. 120:3929-3940(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARF1 AND ARF4.
  17. "Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association."
    Monetta P., Slavin I., Romero N., Alvarez C.
    Mol. Biol. Cell 18:2400-2410(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB1B.
  18. "The Arf GEF GBF1 is required for GGA recruitment to Golgi membranes."
    Lefrancois S., McCormick P.J.
    Traffic 8:1440-1451(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GGA1; GGA2 AND GGA3, MUTAGENESIS OF GLU-794.
  19. "AMP-activated protein kinase phosphorylates Golgi-specific brefeldin A resistance factor 1 at Thr1337 to induce disassembly of Golgi apparatus."
    Miyamoto T., Oshiro N., Yoshino K., Nakashima A., Eguchi S., Takahashi M., Ono Y., Kikkawa U., Yonezawa K.
    J. Biol. Chem. 283:4430-4438(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-1337, MUTAGENESIS OF THR-1337.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  21. "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."
    Manolea F., Claude A., Chun J., Rosas J., Melancon P.
    Mol. Biol. Cell 19:523-535(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-1298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor."
    Deng Y., Golinelli-Cohen M.P., Smirnova E., Jackson C.L.
    EMBO Rep. 10:58-64(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COPG1, MUTAGENESIS OF ASP-543.
  26. Cited for: FUNCTION.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1298; TYR-1316; SER-1335 AND SER-1475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "GBF1-Arf-COPI-ArfGAP-mediated Golgi-to-ER transport involved in regulation of lipid homeostasis."
    Takashima K., Saitoh A., Hirose S., Nakai W., Kondo Y., Takasu Y., Kakeya H., Shin H.W., Nakayama K.
    Cell Struct. Funct. 36:223-235(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. "Interaction between the triglyceride lipase ATGL and the Arf1 activator GBF1."
    Ellong E.N., Soni K.G., Bui Q.T., Sougrat R., Golinelli-Cohen M.P., Jackson C.L.
    PLoS ONE 6:E21889-E21889(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PNPLA2, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-543.
  33. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "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."
    Mazaki Y., Nishimura Y., Sabe H.
    Mol. Biol. Cell 23:2457-2467(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL-PHOSPHATE-BINDING.
  35. "The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the trans-Golgi network (TGN)."
    Lowery J., Szul T., Styers M., Holloway Z., Oorschot V., Klumperman J., Sztul E.
    J. Biol. Chem. 288:11532-11545(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  36. "AMPK phosphorylates GBF1 for mitotic Golgi disassembly."
    Mao L., Li N., Guo Y., Xu X., Gao L., Xu Y., Zhou L., Liu W.
    J. Cell Sci. 126:1498-1505(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY AMPK.
  37. "Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1."
    Quilty D., Gray F., Summerfeldt N., Cassel D., Melancon P.
    J. Cell Sci. 127:354-364(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  38. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-352; SER-1298; SER-1773 AND SER-1784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGBF1_HUMAN
AccessioniPrimary (citable) accession number: Q92538
Secondary accession number(s): Q149P0
, Q149P1, Q5VXX3, Q96CK6, Q96HZ3, Q9H473
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1999
Last modified: June 24, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.