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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1

UniprotKB/SwissProt ID: Q92538 (Q92538)

Gene Name: GBF1

Organism: Homo sapiens (Human)

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 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). Plays a role in maintaining mitochondrial morphology (PubMed:25190516)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Golgi apparatus, cis-Golgi network. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, trans-Golgi network. Golgi apparatus. Cytoplasm. Lipid droplet. Membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR016024 ARM-type_fold
IPR056604 GBF1-like_TPR
IPR032691 Mon2/Sec7/BIG1-like_HUS
IPR023394 Sec7_C_sf
IPR000904 Sec7_dom
IPR035999 Sec7_dom_sf

The S-nitrosylation sites of Q92538

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1157 ETYDEEDAAF C LEMLLRIVLE   
2 1174 IVLENRDRVG C VWQTVRDHLY   
3 1393 GPHDTKSLLK C VESLSFIVRD   
4 1431 IFVEASLNGG C KSQEKRGKSH   
5 1589 QKLDALEWES C FNKVLFPLLT   
6 1708 LWEITWERID C FLPHLRDELF   
7 361 VESIPEVLEE C TSPADHSDSA   
8 614 QEKKETARPS C EIVDGTREAS   
9 662 RLPPEHGKSG C SDLEEAVDSG   
10 686 KFARKPPRFS C LLPDPRELIE