RABEP1

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)
End	5,386,340 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	70,833,931 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; biceps brachii; ; sural nerve; ; postcentral gyrus; ; internal globus pallidus; ; gastrocnemius muscle; ; middle temporal gyrus; ; entorhinal cortex; ; superior frontal gyrus; ; ganglionic eminence;
	Top expressed in
	substantia nigra; ; barrel cortex; ; adrenal gland; ; superior frontal gyrus; ; sciatic nerve; ; Region I of hippocampus proper; ; cingulate gyrus; ; cerebellar cortex; ; motor neuron; ; facial motor nucleus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	growth factor activity ; protein homodimerization activity ; protein binding ; 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 ; protein-containing complex ;
Biological process	membrane fusion ; apoptotic process ; protein transport ; positive regulation of GTPase activity ; vesicle-mediated transport ; endocytosis ; regulation of signaling receptor activity ; Golgi to plasma membrane transport ; protein localization to ciliary membrane ; signal transduction ;
	Sources:Amigo / QuickGO
Orthologs
	9135
	54189
	ENSG00000029725
	ENSMUSG00000020817
	Q15276
	O35551
	NM_001083585 ; NM_001291581 ; NM_001291582 ; NM_004703
	NM_001291141 ; NM_001291142 ; NM_001291143 ; NM_019400
	NP_001077054 ; NP_001278510 ; NP_001278511 ; NP_004694
	NP_001278070 ; NP_001278071 ; NP_001278072 ; NP_062273
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 11, 2024

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.

Interactions

RABEP1 has been shown to interact with:

Related Research Articles

The Rab family of proteins is a member of the Ras superfamily of small G proteins. Approximately 70 types of Rabs have now been identified in humans. Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices. Rab GTPases regulate many steps of membrane trafficking, including vesicle formation, vesicle movement along actin and tubulin networks, and membrane fusion. These processes make up the route through which cell surface proteins are trafficked from the Golgi to the plasma membrane and are recycled. Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside the cell, such as the transferrin receptor, or serves as a means of regulating the number of a certain type of protein molecules on the surface.

In molecular biology, the Guanosine dissociation inhibitors (GDIs) constitute a family of small GTPases that serve a regulatory role in vesicular membrane traffic. GDIs bind to the GDP-bound form of Rho and Rab small GTPases and not only prevent exchange, but also prevent the small GTPase from localizing at the membrane, which is their place of action. This inhibition can be removed by the action of a GDI displacement factor. GDIs also inhibit cdc42 by binding to its tail and preventing its insertion into membranes; hence it cannot trigger WASPs and cannot lead to nucleation of F-actin.

Ras-related protein Rab-5A is a protein that in humans is encoded by the RAB5A gene.

Epidermal growth factor receptor substrate 15 is a protein that in humans is encoded by the EPS15 gene.

Ras-related protein Rab-7a is a protein that in humans is encoded by the RAB7A gene.

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.

Ras-related protein Rab-4A is a protein that in humans is encoded by the RAB4A gene.

AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene.

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.

AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.

Intersectin-1 is a protein that, in humans, is encoded by the ITSN1 gene.

ADP-ribosylation factor-binding protein GGA2 is a protein that in humans is encoded by the GGA2 gene.

Ras-related protein Rab-5B is a protein that in humans is encoded by the RAB5B gene.

AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene.

Rab5 GDP/GTP exchange factor is a protein that in humans is encoded by the RABGEF1 gene.

Adaptin ear-binding coat-associated protein 2 is a protein that in humans is encoded by the NECAP2 gene.

RalBP1-associated Eps domain-containing protein 2 is a protein that in humans is encoded by the REPS2 gene.

<span class="mw-page-title-main">Rabaptin</span>

Rabaptin is a key protein involved in regeneration of injured axons.

<span class="mw-page-title-main">TBC domain</span>

The TBC domain is an evolutionarily conserved protein domain found in all eukaryotes. It is approximately 180 to 200 amino acids long. The domain is named for its initial discovery in the proteins Tre-2, Bub2, and Cdc16.

Ras-related protein Rab-4B is a protein that in humans is encoded by the RAB4B gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000029725 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020817 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 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.
↑ "Entrez Gene: RABEP1 rabaptin, RAB GTPase binding effector protein 1".
1 2 3 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.
↑ 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. S2CID 42630285.
1 2 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.
↑ 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 . hdl: 20.500.12613/9244 . 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 Letters. 508 (2): 201–9. doi: 10.1016/s0014-5793(01)02993-3 . PMID 11718716. S2CID 21545088.

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 . hdl: 20.500.12613/9244 . 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. S2CID 21231710.
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. Bibcode:2001Sci...292.1716Z. doi:10.1126/science.1060896. PMID 11387476. S2CID 9453730.
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. S2CID 21545088.
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. S2CID 6596498.
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. Bibcode:2004CBio...14.1436J. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000029725 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid8521472-5] 1 2 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.

[entrez-6] "Entrez Gene: RABEP1 rabaptin, RAB GTPase binding effector protein 1".

[pmid12505986-7] 1 2 3 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.

[pmid12042876-8] 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. S2CID 42630285.

[pmid9524117-9] 1 2 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.

[pmid9045618-10] 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 . hdl: 20.500.12613/9244 . PMID 9045618.

[pmid11718716-11] 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. S2CID 21545088.

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RABEP1

Contents

Interactions

Related Research Articles

References

Further reading