ARL2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3DOE, 3DOF

Identifiers

Aliases

ARL2, ARFL2, ADP ribosylation factor like GTPase 2

External IDs

MGI: 1928393 HomoloGene: 1260 GeneCards: ARL2

Gene ontology
Molecular function	• nucleotide binding • GTP binding • GTPase inhibitor activity • protein binding • GTPase activity
Cellular component	• cytoplasm • cytosol • centrosome • lateral plasma membrane • mitochondrial intermembrane space • intracellular • microtubule organizing center • mitochondrial matrix • mitochondrion • primary cilium • extracellular exosome • cytoskeleton • nucleus
Biological process	• tubulin complex assembly • centrosome organization • regulation of insulin secretion • small GTPase mediated signal transduction • negative regulation of GTPase activity • regulation of microtubule polymerization • bicellular tight junction assembly • positive regulation of microtubule polymerization • cell cycle • maintenance of protein location in nucleus • positive regulation of cell-substrate adhesion
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


402


56327

Ensembl


ENSG00000213465


ENSMUSG00000024944

UniProt


P36404


Q9D0J4

RefSeq (mRNA)


NM_001667 NM_001199745


NM_019722

RefSeq (protein)


NP_001186674.1 NP_001658.2


NP_062696.2

Location (UCSC)

Chr 11: 65.01 – 65.02 Mb

Chr 19: 6.13 – 6.14 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

ADP-ribosylation factor-like protein 2 is a protein that in humans is encoded by the ARL2 gene.^[3]^[4]^[5]

Function

The ADP-ribosylation factor (ARF) genes are small GTP-binding proteins of the RAS superfamily. ARL2 is a member of a functionally distinct group of ARF-like genes.^[5]

Interactions

ARL2 has been shown to interact with Protein unc-119 homolog,^[6] TBCD^[7]^[8] and PDE6D.^[9]^[10]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Clark J, Moore L, Krasinskas A, Way J, Battey J, Tamkun J, Kahn RA (November 1993). "Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes". Proc. Natl. Acad. Sci. U.S.A. 90 (19): 8952–6. doi:10.1073/pnas.90.19.8952. PMC 47479. PMID 8415637.
↑ Guru SC, Agarwal SK, Manickam P, Olufemi SE, Crabtree JS, Weisemann JM, Kester MB, Kim YS, Wang Y, Emmert-Buck MR, Liotta LA, Spiegel AM, Boguski MS, Roe BA, Collins FS, Marx SJ, Burns L, Chandrasekharappa SC (September 1997). "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Res. 7 (7): 725–35. doi:10.1101/gr.7.7.725. PMC 310681. PMID 9253601.
1 2 "Entrez Gene: ARL2 ADP-ribosylation factor-like 2".
↑ Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (January 2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1-3): 26–32. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357.
↑ Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (October 2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
↑ Bhamidipati A, Lewis SA, Cowan NJ (May 2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823. PMID 10831612.
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
↑ Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.

Maruyama K, Sugano S (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.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (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.
Bhamidipati A, Lewis SA, Cowan NJ (2000). "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. doi:10.1083/jcb.149.5.1087. PMC 2174823. PMID 10831612.
Sharer JD, Shern JF, Van Valkenburgh H, Wallace DC, Kahn RA (2002). "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter". Mol. Biol. Cell. 13 (1): 71–83. doi:10.1091/mbc.01-05-0245. PMC 65073. PMID 11809823.
Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (2002). "The complex of Arl2-GTP and PDE delta: from structure to function". EMBO J. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
Antoshechkin I, Han M (2002). "The C. elegans evl-20 gene is a homolog of the small GTPase ARL2 and regulates cytoskeleton dynamics during cytokinesis and morphogenesis". Dev. Cell. 2 (5): 579–91. doi:10.1016/S1534-5807(02)00146-6. PMID 12015966.
Kobayashi A, Kubota S, Mori N, McLaren MJ, Inana G (2003). "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain". FEBS Lett. 534 (1-3): 26–32. doi:10.1016/S0014-5793(02)03766-3. PMID 12527357.
Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Zhou C, Cunningham L, Marcus AI, Li Y, Kahn RA (2006). "Arl2 and Arl3 regulate different microtubule-dependent processes". Mol. Biol. Cell. 17 (5): 2476–87. doi:10.1091/mbc.E05-10-0929. PMC 1446103. PMID 16525022.
Beghin A, Honore S, Messana C, Matera EL, Aim J, Burlinchon S, Braguer D, Dumontet C (2007). "ADP ribosylation factor like 2 (Arl2) protein influences microtubule dynamics in breast cancer cells". Exp. Cell Res. 313 (3): 473–85. doi:10.1016/j.yexcr.2006.10.024. PMID 17188265.

PDB gallery

1ksg: Complex of Arl2 and PDE delta, Crystal Form 1

1ksh: Complex of Arl2 and PDE delta, Crystal Form 2 (native)

1ksj: Complex of Arl2 and PDE delta, Crystal Form 2 (SeMet)

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ARL2

Function

Interactions

References

Further reading