RABEP1

Rabaptin, RAB GTPase binding effector protein 1

PDB rendering based on 1tu3.

Available structures
PDB	1TU3, 1X79

Identifiers

Symbols

RABEP1; RAB5EP; RABPT5

External IDs

OMIM: 603616 MGI: 1860236 HomoloGene: 3451 GeneCards: RABEP1 Gene

Gene Ontology
Molecular function	• GTPase activator activity • protein binding • growth factor activity • protein homodimerization activity
Cellular component	• cytoplasm • early endosome • centrosome • cytoplasmic membrane-bounded vesicle • recycling endosome
Biological process	• endocytosis • apoptosis • cellular membrane fusion • protein transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
5.19 – 5.29 Mb

Chr 11:
70.66 – 70.76 Mb

PubMed search

[1]

[2]

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 GGA2,^[3] RAB4A,^[4] RAB5A,^[5]^[4]^[1]^[6] AP1G1^[7]^[3] and GGA1.^[3]

References

^ ^a ^b Stenmark H, Vitale G, Ullrich O, Zerial M (Jan 1996). "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.
^ "Entrez Gene: RABEP1 rabaptin, RAB GTPase binding effector protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9135.
^ ^a ^b ^c Mattera, Rafael; Arighi Cecilia N, Lodge Robert, Zerial Marino, Bonifacino Juan S (Jan. 2003). "Divalent interaction of the GGAs with the Rabaptin-5–Rabex-5 complex". EMBO J. (England) 22 (1): 78–88. doi:10.1093/emboj/cdg015. ISSN 0261-4189. PMC 140067. PMID 12505986. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140067.
^ ^a ^b 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". EMBO J. (ENGLAND) 17 (7): 1941–51. doi:10.1093/emboj/17.7.1941. ISSN 0261-4189. PMC 1170540. PMID 9524117. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170540.
^ Xiao, G H; Shoarinejad F, Jin F, Golemis E A, Yeung R S (Mar. 1997). "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". J. Biol. Chem. (UNITED STATES) 272 (10): 6097–100. doi:10.1074/jbc.272.10.6097. ISSN 0021-9258. PMID 9045618.
^ 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 Lett. (Netherlands) 508 (2): 201–9. doi:10.1016/S0014-5793(01)02993-3. ISSN 0014-5793. PMID 11718716.
^ Nogi, Terukazu; Shiba Yoko, Kawasaki Masato, Shiba Tomoo, Matsugaki Naohiro, Igarashi Noriyuki, Suzuki Mamoru, Kato Ryuichi, Takatsu Hiroyuki, Nakayama Kazuhisa, Wakatsuki Soichi (Jul. 2002). "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain". Nat. Struct. Biol. (United States) 9 (7): 527–31. doi:10.1038/nsb808. ISSN 1072-8368. PMID 12042876.

Xiao GH, Shoarinejad F, Jin F et al. (1997). "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". J. Biol. Chem. 272 (10): 6097–100. doi:10.1074/jbc.272.10.6097. PMID 9045618.
Vitale G, Rybin V, Christoforidis S et al. (1998). "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". EMBO J. 17 (7): 1941–51. doi:10.1093/emboj/17.7.1941. PMC 1170540. PMID 9524117. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170540.
Neve RL, Coopersmith R, McPhie DL et al. (1998). "The neuronal growth-associated protein GAP-43 interacts with rabaptin-5 and participates in endocytosis". J. Neurosci. 18 (19): 7757–67. PMID 9742146.
Swanton E, Bishop N, Woodman P (2000). "Human rabaptin-5 is selectively cleaved by caspase-3 during apoptosis". J. Biol. Chem. 274 (53): 37583–90. doi:10.1074/jbc.274.53.37583. PMID 10608812.
Nagelkerken B, Van Anken E, Van Raak M et al. (2000). "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles". Biochem. J. 346 Pt 3 (3): 593–601. doi:10.1042/0264-6021:3460593. PMC 1220890. PMID 10698684. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220890.
Hirst J, Lui WW, Bright NA et al. (2000). "A Family of Proteins with γ-Adaptin and Vhs Domains That Facilitate Trafficking between the Trans-Golgi Network and the Vacuole/Lysosome". J. Cell Biol. 149 (1): 67–80. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175106.
Korobko IV, Korobko EV, Kiselev SL (2001). "The MAK-V protein kinase regulates endocytosis in mouse". Mol. Gen. Genet. 264 (4): 411–8. PMID 11129044.
Zhu Y, Doray B, Poussu A et al. (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 et al. (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 Lett. 508 (2): 201–9. doi:10.1016/S0014-5793(01)02993-3. PMID 11718716.
de Renzis S, Sönnichsen B, Zerial M (2002). "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes". Nat. Cell Biol. 4 (2): 124–33. doi:10.1038/ncb744. PMID 11788822.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Mattera R, Arighi CN, Lodge R et al. (2003). "Divalent interaction of the GGAs with the Rabaptin-5–Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140067.
Mattera R, Puertollano R, Smith WJ, Bonifacino JS (2004). "The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites". J. Biol. Chem. 279 (30): 31409–18. doi:10.1074/jbc.M402183200. PMID 15143060.
Jin J, Smith FD, Stark C et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
Kimura K, Wakamatsu A, Suzuki Y et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
Ewing RM, Chu P, Elisma F et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.

PDB gallery

1tu3: Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain

1x79: Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5

RABEP1

Interactions

References

Further reading