ARL2

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ADP-ribosylation factor-like 2
Protein ARL2 PDB 1ksg.png
PDB rendering based on 1ksg.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ARL2 ; ARFL2
External IDs OMIM601175 MGI1928393 HomoloGene1260 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:
64.78 – 64.79 Mb
Chr 19:
6.13 – 6.14 Mb
PubMed search [1] [2]

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

Function[edit]

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[edit]

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

References[edit]

  1. ^ Clark J, Moore L, Krasinskas A, Way J, Battey J, Tamkun J et al. (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 et al. (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. ^ a b "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 et al. (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 et al. (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[edit]