REEP2

REEP2
Identifiers
Aliases	REEP2, C5orf19, SGC32445, SPG72, Yip2d, receptor accessory protein 2
External IDs	OMIM: 609347; MGI: 2385070; HomoloGene: 41146; GeneCards: REEP2; OMA:REEP2 - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	138,446,969 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	34,980,516 bp
RNA expression pattern
	Top expressed in
	right hemisphere of cerebellum; ; right frontal lobe; ; cingulate gyrus; ; anterior cingulate cortex; ; Brodmann area 9; ; nucleus accumbens; ; prefrontal cortex; ; amygdala; ; anterior pituitary; ; putamen;
	Top expressed in
	zygote; ; superior frontal gyrus; ; dentate gyrus of hippocampal formation granule cell; ; cerebellar cortex; ; primary visual cortex; ; neural layer of retina; ; secondary oocyte; ; supraoptic nucleus; ; spermatid; ; greater petrosal nerve;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	taste receptor binding;
Cellular component	integral component of membrane; cytoplasmic microtubule; integral component of plasma membrane; endoplasmic reticulum membrane; endoplasmic reticulum; membrane;
Biological process	endoplasmic reticulum tubular network organization; sensory perception of bitter taste; sensory perception of sweet taste; protein transport into membrane raft; regulation of intracellular transport;
	Sources:Amigo / QuickGO
Orthologs
	51308
	225362
	ENSG00000132563
	ENSMUSG00000038555
	Q9BRK0
	Q8VCD6
	NM_001271803; NM_016606
	NM_001204914; NM_144865
	NP_001258732; NP_057690
	NP_001191843; NP_659114
	Wikidata
View/Edit Human	View/Edit Mouse

Receptor expression-enhancing protein 2 is a protein that in humans is encoded by the REEP2 gene.^[5]^[6]

Function

The protein encoded by REEP2 belongs to a family of proteins with receptor enhancing expression capabilities, including possible enhancement of G protein-coupled receptors.^[7] The REEP2 protein shows a restricted mode of expression in human tissues.^[8]

Clinical significance

REEP2 mutations have been reported in families with hereditary spastic paraplegia.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000132563 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000038555 – 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.
^ Clark, Adrian J.L.; Metherell, Louise A.; Cheetham, Michael E.; Huebner, Angela (2005). "Inherited ACTH insensitivity illuminates the mechanisms of ACTH action". Trends in Endocrinology & Metabolism. 16 (10): 451–457. doi:10.1016/j.tem.2005.10.006. PMID 16271481.
^ Saito, Harumi; Kubota, Momoka; Roberts, Richard W.; Chi, Qiuyi; Matsunami, Hiroaki (2004). "RTP Family Members Induce Functional Expression of Mammalian Odorant Receptors". Cell. 119 (5): 679–691. doi:10.1016/j.cell.2004.11.021. PMID 15550249.
^ Björk, Susann; Hurt, Carl M.; Ho, Vincent K.; Angelotti, Timothy (2013-12-17). "Correction: REEPs Are Membrane Shaping Adapter Proteins That Modulate Specific G Protein-Coupled Receptor Trafficking by Affecting ER Cargo Capacity". PLOS ONE. 8 (12): 10.1371/annotation/6f86410c–63c3–4fcd-b1cb-9fd8d2ea95d0. doi:10.1371/annotation/6f86410c-63c3-4fcd-b1cb-9fd8d2ea95d0. ISSN 1932-6203. PMC 3867549.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ Uhlén, Mathias; Fagerberg, Linn; Hallström, Björn M.; Lindskog, Cecilia; Oksvold, Per; Mardinoglu, Adil; Sivertsson, Åsa; Kampf, Caroline; Sjöstedt, Evelina (2015-01-23). "Tissue-based map of the human proteome". Science. 347 (6220): 1260419. doi:10.1126/science.1260419. ISSN 0036-8075. PMID 25613900.
^ Esteves, Typhaine; Durr, Alexandra; Mundwiller, Emeline; Loureiro, José L.; Boutry, Maxime; Gonzalez, Michael A.; Gauthier, Julie; El-Hachimi, Khalid H.; Depienne, Christel (2014). "Loss of Association of REEP2 with Membranes Leads to Hereditary Spastic Paraplegia". The American Journal of Human Genetics. 94 (2): 268–277. doi:10.1016/j.ajhg.2013.12.005. PMC 3928657. PMID 24388663.

Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Lai F, Godley LA, Joslin J, Fernald AA, Liu J, Espinosa R, Zhao N, Pamintuan L, Till BG, Larson RA, Qian Z, Le Beau MM (January 2001). "Transcript map and comparative analysis of the 1.5-Mb commonly deleted segment of human 5q31 in malignant myeloid diseases with a del(5q)". Genomics. 71 (2): 235–45. doi:10.1006/geno.2000.6414. PMID 11161817.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000132563 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000038555 – 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] Clark, Adrian J.L.; Metherell, Louise A.; Cheetham, Michael E.; Huebner, Angela (2005). "Inherited ACTH insensitivity illuminates the mechanisms of ACTH action". Trends in Endocrinology & Metabolism. 16 (10): 451–457. doi:10.1016/j.tem.2005.10.006. PMID 16271481.

[6] Saito, Harumi; Kubota, Momoka; Roberts, Richard W.; Chi, Qiuyi; Matsunami, Hiroaki (2004). "RTP Family Members Induce Functional Expression of Mammalian Odorant Receptors". Cell. 119 (5): 679–691. doi:10.1016/j.cell.2004.11.021. PMID 15550249.

[7] Björk, Susann; Hurt, Carl M.; Ho, Vincent K.; Angelotti, Timothy (2013-12-17). "Correction: REEPs Are Membrane Shaping Adapter Proteins That Modulate Specific G Protein-Coupled Receptor Trafficking by Affecting ER Cargo Capacity". PLOS ONE. 8 (12): 10.1371/annotation/6f86410c–63c3–4fcd-b1cb-9fd8d2ea95d0. doi:10.1371/annotation/6f86410c-63c3-4fcd-b1cb-9fd8d2ea95d0. ISSN 1932-6203. PMC 3867549.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[8] Uhlén, Mathias; Fagerberg, Linn; Hallström, Björn M.; Lindskog, Cecilia; Oksvold, Per; Mardinoglu, Adil; Sivertsson, Åsa; Kampf, Caroline; Sjöstedt, Evelina (2015-01-23). "Tissue-based map of the human proteome". Science. 347 (6220): 1260419. doi:10.1126/science.1260419. ISSN 0036-8075. PMID 25613900.

[9] Esteves, Typhaine; Durr, Alexandra; Mundwiller, Emeline; Loureiro, José L.; Boutry, Maxime; Gonzalez, Michael A.; Gauthier, Julie; El-Hachimi, Khalid H.; Depienne, Christel (2014). "Loss of Association of REEP2 with Membranes Leads to Hereditary Spastic Paraplegia". The American Journal of Human Genetics. 94 (2): 268–277. doi:10.1016/j.ajhg.2013.12.005. PMC 3928657. PMID 24388663.

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Function

Clinical significance

References

Further reading