GEA2/YEL022W Summary Help

Standard Name GEA2 1
Systematic Name YEL022W
Feature Type ORF, Verified
Description Guanine nucleotide exchange factor for ADP ribosylation factors (ARFs); involved in vesicular transport between the Golgi and ER, Golgi organization, and actin cytoskeleton organization; GEA2 has a paralog, GEA1, that arose from the whole genome duplication (2, 3, 4, 5 and see Summary Paragraph)
Name Description Guanine nucleotide Exchange on ARF 1
Chromosomal Location
ChrV:111421 to 115800 | ORF Map | GBrowse
Gene Ontology Annotations All GEA2 GO evidence and references
  View Computational GO annotations for GEA2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Classical genetics
Large-scale survey
81 total interaction(s) for 51 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 2
  • Co-fractionation: 1
  • Co-purification: 2
  • Reconstituted Complex: 7
  • Two-hybrid: 6

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 1
  • Dosage Rescue: 4
  • Negative Genetic: 25
  • Phenotypic Enhancement: 2
  • Positive Genetic: 4
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 4

Expression Summary
Length (a.a.) 1,459
Molecular Weight (Da) 165,666
Isoelectric Point (pI) 4.88
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:111421 to 115800 | ORF Map | GBrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..4380 111421..115800 1996-07-31 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000748

GEA2 encodes a guanine nucleotide exchange factor (GEF) for ADP ribosylation factors (ARFs, encoded by ARF1, ARF2, and ARF3 in yeast) (1). ARFs are GTPases of the Ras superfamily that regulate the formation of coated vesicles in intracellular trafficking (6, 7). The process of vesicle formation in the exocytic and endocytic pathways has been recently reviewed (8), as has the role of ARF (9).

The catalytic activity of Gea2p resides in a 200 amino acid domain, called the Sec7 domain, that is similar to the catalytic domain of Sec7p, another GEF for yeast ARFs (1). The Sec7 domain is conserved in proteins from yeast (Sec7p and Gea1p; 1, 10) and many other species, including human (11, 12, 13), rat (14), mouse (15), and Arabidopsis (16). A bovine protein, p200, with a Sec7 domain has been shown to act as a GEF for rat ARF (17). ARF GEFs are targets of the drug Brefeldin A, which inhibits secretion; different Sec7 domains show differing sensitivity to Brefeldin A (reviewed in 18).

Last updated: 1999-10-29 Contact SGD

References cited on this page View Complete Literature Guide for GEA2
1) Peyroche A, et al.  (1996) Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384(6608):479-81
2) Spang A, et al.  (2001) The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum. Mol Biol Cell 12(4):1035-45
3) Peyroche A, et al.  (2001) The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast. J Cell Sci 114(Pt 12):2241-53
4) Zakrzewska E, et al.  (2003) A role for GEA1 and GEA2 in the organization of the actin cytoskeleton in Saccharomyces cerevisiae. Genetics 165(3):985-95
5) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6) Moss J and Vaughan M  (1998) Molecules in the ARF orbit. J Biol Chem 273(34):21431-4
7) Moss J and Vaughan M  (1999) Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors. Mol Cell Biochem 193(1-2):153-7
8) Springer S, et al.  (1999) A primer on vesicle budding. Cell 97(2):145-8
9) Roth MG  (1999) Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell 97(2):149-52
10) Sata M, et al.  (1998) Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors. Proc Natl Acad Sci U S A 95(8):4204-8
11) Liu L and Pohajdak B  (1992) Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7. Biochim Biophys Acta 1132(1):75-8
12) Chardin P, et al.  (1996) A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature 384(6608):481-4
13) Meacci E, et al.  (1997) Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc Natl Acad Sci U S A 94(5):1745-8
14) Telemenakis I, et al.  (1997) Rat homologues of yeast sec7p. Eur J Cell Biol 74(2):143-9
15) Klarlund JK, et al.  (1997) Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275(5308):1927-30
16) Shevell DE, et al.  (1994) EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7. Cell 77(7):1051-62
17) Morinaga N, et al.  (1997) Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc Natl Acad Sci U S A 94(24):12926-31
18) Chardin P and McCormick F  (1999) Brefeldin A: the advantage of being uncompetitive. Cell 97(2):153-5