RABEP1

RABEP1

Identifiers

RABEP1, RAB5EP, RABPT5, rabaptin, RAB GTPase binding effector protein 1

External IDs

OMIM: 603616; MGI: 1860236; GeneCards: RABEP1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1P4U, 1TU3, 1X79, 4N3Y, 4N3Z, 4Q9U

Gene location (Human)

Chr.	Chromosome 17 (human)

Band	17p13.2	Start	5,282,265 bp
Band	17p13.2	End	5,386,340 bp

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)

Band	11 B3- B4\|11 43.21 cM	Start	70,735,604 bp
Band	11 B3- B4\|11 43.21 cM	End	70,833,931 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

Skeletal muscle tissue of rectus abdominis

Achilles tendon

biceps brachii

sural nerve

postcentral gyrus

internal globus pallidus

C1 segment

Skeletal muscle tissue of biceps brachii

gastrocnemius muscle

middle temporal gyrus

Top expressed in

dentate gyrus of hippocampal formation granule cell

tail of embryo

substantia nigra

barrel cortex

adrenal gland

genital tubercle

superior frontal gyrus

sciatic nerve

Region I of hippocampus proper

primary visual cortex

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

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


9135


54189


ENSG00000029725


ENSMUSG00000020817


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: 70.74 – 70.83 Mb

PubMed search

View/Edit Human

View/Edit Mouse

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

Interactions

RABEP1 has been shown to interact with:

AP1G1,
GGA1,
GGA2,
RAB4A, and
RAB5A.

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.

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. 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.

v t e 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

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