Biology:RABEP1
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
Rab GTPase-binding effector protein 1 is an enzyme that in humans is encoded by the RABEP1 gene.[1][2] It belongs to rabaptin protein family.
Interactions
RABEP1 has been shown to interact with:
References
- ↑ 1.0 1.1 "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion". Cell 83 (3): 423–32. Nov 1995. doi:10.1016/0092-8674(95)90120-5. PMID 8521472.
- ↑ "Entrez Gene: RABEP1 rabaptin, RAB GTPase binding effector protein 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9135.
- ↑ 3.0 3.1 3.2 "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". The EMBO Journal 22 (1): 78–88. Jan 2003. doi:10.1093/emboj/cdg015. PMID 12505986.
- ↑ "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain". Nature Structural Biology 9 (7): 527–31. Jul 2002. doi:10.1038/nsb808. PMID 12042876.
- ↑ 5.0 5.1 "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". The EMBO Journal 17 (7): 1941–51. Apr 1998. doi:10.1093/emboj/17.7.1941. PMID 9524117.
- ↑ "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". The Journal of Biological Chemistry 272 (10): 6097–100. Mar 1997. doi:10.1074/jbc.272.10.6097. PMID 9045618.
- ↑ "Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER". FEBS Letters 508 (2): 201–9. Nov 2001. doi:10.1016/s0014-5793(01)02993-3. PMID 11718716.
Further reading
- "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". The Journal of Biological Chemistry 272 (10): 6097–100. Mar 1997. doi:10.1074/jbc.272.10.6097. PMID 9045618.
- "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". The EMBO Journal 17 (7): 1941–51. Apr 1998. doi:10.1093/emboj/17.7.1941. PMID 9524117.
- "The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis". The Journal of Neuroscience 18 (19): 7757–67. Oct 1998. doi:10.1523/JNEUROSCI.18-19-07757.1998. PMID 9742146.
- "Human rabaptin-5 is selectively cleaved by caspase-3 during apoptosis". The Journal of Biological Chemistry 274 (53): 37583–90. Dec 1999. doi:10.1074/jbc.274.53.37583. PMID 10608812.
- "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles". The Biochemical Journal 346 (3): 593–601. Mar 2000. doi:10.1042/0264-6021:3460593. PMID 10698684.
- "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome". The Journal of Cell Biology 149 (1): 67–80. Apr 2000. doi:10.1083/jcb.149.1.67. PMID 10747088.
- "The MAK-V protein kinase regulates endocytosis in mouse". Molecular & General Genetics 264 (4): 411–8. Nov 2000. doi:10.1007/s004380000293. PMID 11129044.
- "Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor". Science 292 (5522): 1716–8. Jun 2001. doi:10.1126/science.1060896. PMID 11387476. Bibcode: 2001Sci...292.1716Z.
- "Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER". FEBS Letters 508 (2): 201–9. Nov 2001. doi:10.1016/S0014-5793(01)02993-3. PMID 11718716.
- "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes". Nature Cell Biology 4 (2): 124–33. Feb 2002. doi:10.1038/ncb744. PMID 11788822.
- "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". The EMBO Journal 22 (1): 78–88. Jan 2003. doi:10.1093/emboj/cdg015. PMID 12505986.
- "The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites". The Journal of Biological Chemistry 279 (30): 31409–18. Jul 2004. doi:10.1074/jbc.M402183200. PMID 15143060.
- "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology 14 (16): 1436–50. Aug 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. Jan 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.