RABEP1

Rab GTPase-binding effector protein 1 is an enzyme that in humans is encoded by the RABEP1 gene.[5][6] It belongs to rabaptin protein family.

RABEP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1P4U, 1TU3, 1X79, 4N3Y, 4N3Z, 4Q9U
Identifiers
Aliases	RABEP1, RAB5EP, RABPT5, rabaptin, RAB GTPase binding effector protein 1
External IDs	OMIM: 603616 MGI: 1860236 HomoloGene: 3451 GeneCards: RABEP1
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.2 Start 5,282,265 bp[1] End 5,386,340 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 B4|11 43.21 cM Start 70,844,778 bp[2] End 70,943,105 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • growth factor activity • protein homodimerization activity • GO:0001948 protein binding • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity • protein domain specific binding Cellular component • intracellular membrane-bounded organelle • cytoplasmic vesicle • endocytic vesicle • cytoplasm • recycling endosome • endosome • early endosome • early endosome membrane • macromolecular complex Biological process • Lipid bilayer fusion • apoptotic process • protein transport • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • vesicle-mediated transport • endocytosis • regulation of receptor activity • Golgi to plasma membrane transport • protein localization to ciliary membrane • signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9135	54189
Ensembl	ENSG00000029725	ENSMUSG00000020817
UniProt	Q15276	O35551
RefSeq (mRNA)	NM_001083585 NM_001291581 NM_001291582 NM_004703	NM_001291141 NM_001291142 NM_001291143 NM_019400
RefSeq (protein)	NP_001077054 NP_001278510 NP_001278511 NP_004694	NP_001278070 NP_001278071 NP_001278072 NP_062273
Location (UCSC)	Chr 17: 5.28 – 5.39 Mb	Chr 11: 70.84 – 70.94 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

RABEP1 has been shown to interact with:

• AP1G1,[7][8]
• GGA1,[7]
• GGA2,[7]
• RAB4A,[9] and
• RAB5A.[5][9][10][11]

References

1. GRCh38: Ensembl release 89: ENSG00000029725 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020817 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Stenmark H, Vitale G, Ullrich O, Zerial M (Nov 1995). "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion". Cell. 83 (3): 423–32. doi:10.1016/0092-8674(95)90120-5. PMID 8521472.
6. "Entrez Gene: RABEP1 rabaptin, RAB GTPase binding effector protein 1".
7. Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (Jan 2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". The EMBO Journal. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
8. Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S (Jul 2002). "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain". Nature Structural Biology. 9 (7): 527–31. doi:10.1038/nsb808. PMID 12042876.
9. Vitale G, Rybin V, Christoforidis S, Thornqvist P, McCaffrey M, Stenmark H, Zerial M (Apr 1998). "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". The EMBO Journal. 17 (7): 1941–51. doi:10.1093/emboj/17.7.1941. PMC 1170540. PMID 9524117.
10. Xiao GH, Shoarinejad F, Jin F, Golemis EA, Yeung RS (Mar 1997). "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. doi:10.1074/jbc.272.10.6097. PMID 9045618.
11. Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T (Nov 2001). "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. doi:10.1016/s0014-5793(01)02993-3. PMID 11718716.

Further reading

• Xiao GH, Shoarinejad F, Jin F, Golemis EA, Yeung RS (Mar 1997). "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. doi:10.1074/jbc.272.10.6097. PMID 9045618.
• Vitale G, Rybin V, Christoforidis S, Thornqvist P, McCaffrey M, Stenmark H, Zerial M (Apr 1998). "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". The EMBO Journal. 17 (7): 1941–51. doi:10.1093/emboj/17.7.1941. PMC 1170540. PMID 9524117.
• Neve RL, Coopersmith R, McPhie DL, Santeufemio C, Pratt KG, Murphy CJ, Lynn SD (Oct 1998). "The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis". The Journal of Neuroscience. 18 (19): 7757–67. doi:10.1523/JNEUROSCI.18-19-07757.1998. PMC 6793001. PMID 9742146.
• Swanton E, Bishop N, Woodman P (Dec 1999). "Human rabaptin-5 is selectively cleaved by caspase-3 during apoptosis". The Journal of Biological Chemistry. 274 (53): 37583–90. doi:10.1074/jbc.274.53.37583. PMID 10608812.
• Nagelkerken B, Van Anken E, Van Raak M, Gerez L, Mohrmann K, Van Uden N, Holthuizen J, Pelkmans L, Van Der Sluijs P (Mar 2000). "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles". The Biochemical Journal. 346 (3): 593–601. doi:10.1042/0264-6021:3460593. PMC 1220890. PMID 10698684.
• Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS (Apr 2000). "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. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088.
• Korobko IV, Korobko EV, Kiselev SL (Nov 2000). "The MAK-V protein kinase regulates endocytosis in mouse". Molecular & General Genetics. 264 (4): 411–8. doi:10.1007/s004380000293. PMID 11129044.
• Zhu Y, Doray B, Poussu A, Lehto VP, Kornfeld S (Jun 2001). "Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor". Science. 292 (5522): 1716–8. doi:10.1126/science.1060896. PMID 11387476.
• Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T (Nov 2001). "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. doi:10.1016/S0014-5793(01)02993-3. PMID 11718716.
• de Renzis S, Sönnichsen B, Zerial M (Feb 2002). "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes". Nature Cell Biology. 4 (2): 124–33. doi:10.1038/ncb744. PMID 11788822.
• Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (Jan 2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". The EMBO Journal. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
• Mattera R, Puertollano R, Smith WJ, Bonifacino JS (Jul 2004). "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. doi:10.1074/jbc.M402183200. PMID 15143060.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "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. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.