RAPGEF1

From Wikipedia, the free encyclopedia

Rap guanine nucleotide exchange factor (GEF) 1

Identifiers

RAPGEF1; C3G; DKFZp781P1719; GRF2

External IDs

Gene ontology
Molecular Function:	• guanyl-nucleotide exchange factor activity • protein binding
Cellular Component:	• intracellular
Biological Process:	• signal transduction • transmembrane receptor protein tyrosine kinase signaling pathway • small GTPase mediated signal transduction • regulation of small GTPase mediated signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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Refseq

NM_005312 (mRNA)
NP_005303 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 9: 133.44 - 133.61 Mb

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Pubmed search

[1]

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Rap guanine nucleotide exchange factor (GEF) 1, also known as RAPGEF1, is a human gene.

The protein encoded by this gene is a human guanine nucleotide releasing protein for Ras protein. It belongs to the adaptor-type Src homology (SH)2-containing molecules. Src homology 2 domains are globular protein modules present in a large variety of functionally distinct proteins. They mediate binding events that control the activity and localization of many proteins involved in the transmission of signals from the cell surface to the nucleus. The mRNAs of these proteins are expressed ubiquitously in human adult and fetal tissues. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some variants has not been determined.^[1]

[edit] References

^ Entrez Gene: RAPGEF1 Rap guanine nucleotide exchange factor (GEF) 1.

[edit] Further reading

Pessin JE, Okada S (2002). "Insulin and EGF receptors integrate the Ras and Rap signaling pathways.". Endocr. J. 46 Suppl: S11–6. PMID 12054111.
Ehrhardt A, Ehrhardt GR, Guo X, Schrader JW (2002). "Ras and relatives--job sharing and networking keep an old family together.". Exp. Hematol. 30 (10): 1089–106. PMID 12384139.
Tanaka S, Morishita T, Hashimoto Y, et al. (1994). "C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins.". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3443–7. PMID 7512734.
Knudsen BS, Feller SM, Hanafusa H (1995). "Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk.". J. Biol. Chem. 269 (52): 32781–7. PMID 7806500.
Takai S, Tanaka M, Sugimura H, et al. (1994). "Mapping of the human C3G gene coding a guanine nucleotide releasing protein for Ras family to 9q34.3 by fluorescence in situ hybridization.". Hum. Genet. 94 (5): 549–50. PMID 7959692.
Gotoh T, Hattori S, Nakamura S, et al. (1996). "Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G.". Mol. Cell. Biol. 15 (12): 6746–53. PMID 8524240.
Smit L, van der Horst G, Borst J (1996). "Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors.". J. Biol. Chem. 271 (15): 8564–9. PMID 8621483.
Matsuda M, Ota S, Tanimura R, et al. (1996). "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins.". J. Biol. Chem. 271 (24): 14468–72. PMID 8662907.
Uemura N, Salgia R, Li JL, et al. (1997). "The BCR/ABL oncogene alters interaction of the adapter proteins CRKL and CRK with cellular proteins.". Leukemia 11 (3): 376–85. PMID 9067577.
Husson H, Mograbi B, Schmid-Antomarchi H, et al. (1997). "CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2.". Oncogene 14 (19): 2331–8. doi:10.1038/sj.onc.1201074. PMID 9178909.
Chin H, Saito T, Arai A, et al. (1997). "Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells.". Biochem. Biophys. Res. Commun. 239 (2): 412–7. doi:10.1006/bbrc.1997.7480. PMID 9344843.
Ahmad S, Alsayed YM, Druker BJ, Platanias LC (1997). "The type I interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein.". J. Biol. Chem. 272 (48): 29991–4. PMID 9374471.
Guerrero C, Fernandez-Medarde A, Rojas JM, et al. (1998). "Transformation suppressor activity of C3G is independent of its CDC25-homology domain.". Oncogene 16 (5): 613–24. doi:10.1038/sj.onc.1201569. PMID 9482107.
Ohashi Y, Tachibana K, Kamiguchi K, et al. (1998). "T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G.". J. Biol. Chem. 273 (11): 6446–51. PMID 9497377.
Astier A, Manié SN, Law SF, et al. (1998). "Association of the Cas-like molecule HEF1 with CrkL following integrin and antigen receptor signaling in human B-cells: potential relevance to neoplastic lymphohematopoietic cells.". Leuk. Lymphoma 28 (1-2): 65–72. PMID 9498705.
Yokote K, Hellman U, Ekman S, et al. (1998). "Identification of Tyr-762 in the platelet-derived growth factor alpha-receptor as the binding site for Crk proteins.". Oncogene 16 (10): 1229–39. doi:10.1038/sj.onc.1201641. PMID 9546424.
Kirsch KH, Georgescu MM, Hanafusa H (1998). "Direct binding of p130(Cas) to the guanine nucleotide exchange factor C3G.". J. Biol. Chem. 273 (40): 25673–9. PMID 9748234.
Ichiba T, Hashimoto Y, Nakaya M, et al. (1999). "Activation of C3G guanine nucleotide exchange factor for Rap1 by phosphorylation of tyrosine 504.". J. Biol. Chem. 274 (20): 14376–81. PMID 10318861.
Nosaka Y, Arai A, Miyasaka N, Miura O (1999). "CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3.". J. Biol. Chem. 274 (42): 30154–62. PMID 10514505.
Uemura N, Griffin JD (2000). "The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration.". J. Biol. Chem. 274 (53): 37525–32. PMID 10608804.