ARL2

ADP-ribosylation factor-like 2

PDB rendering based on 1ksg.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ARL2 ; ARFL2
External IDs OMIM: 601175 MGI: 1928393 HomoloGene: 1260 GeneCards: ARL2 Gene
Orthologs
Species Human Mouse
Entrez 402 56327
Ensembl ENSG00000213465 ENSMUSG00000024944
UniProt P36404 Q9D0J4
RefSeq (mRNA) NM_001199745 NM_019722
RefSeq (protein) NP_001186674 NP_062696
Location (UCSC) Chr 11:
65.01 – 65.02 Mb
Chr 19:
6.13 – 6.14 Mb
PubMed search

ADP-ribosylation factor-like protein 2 is a protein that in humans is encoded by the ARL2 gene.[1][2][3]

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.[3]

Interactions

ARL2 has been shown to interact with Protein unc-119 homolog,[4] TBCD[5][6] and PDE6D.[7][8]

References

  1. 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.
  2. 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.
  3. 1 2 "Entrez Gene: ARL2 ADP-ribosylation factor-like 2".
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.

Further reading


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