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Gene Review

UBA2  -  E1 ubiquitin-activating protein UBA2

Saccharomyces cerevisiae S288c

Synonyms: D9509.10, PIP2, Polymerase-interacting protein 2, SMT3-activating enzyme subunit 2, UAL1, ...
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Disease relevance of UBA2


High impact information on UBA2

  • Furthermore, UBA2 and AOS1 are both essential genes, providing additional evidence that they act in a distinct pathway whose role in cell viability is to conjugate Smt3p to other proteins [2].
  • Interestingly, the surfaces of UbL and Ub that bind to UBA1, UBA2, and PUbS2 are similar, consisting of five beta-strands and their connecting loops [3].
  • We show here that cNLS-dependent protein import is impaired in mutants with defective Ulp1 and Uba2, two enzymes involved in the SUMO conjugation reaction [4].
  • Based on these data, we propose that Fab1p is a PI(4)P 5-kinase and that the product of the Fab1p reaction, PIP2, functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole [5].
  • The EF-hand consensus and the putative PIP2-binding sites are seemingly not required for End3 protein function [6].

Biological context of UBA2


Anatomical context of UBA2

  • By use of the same technique for model membranes, it was shown that in phosphatidylcholine bilayers the collision frequency of the three fluorescent phosphoinositides decreased in the order PI greater than PIP greater than PIP2 [10].

Associations of UBA2 with chemical compounds


Regulatory relationships of UBA2

  • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer [2].

Other interactions of UBA2

  • We describe the isolation and analysis of another essential gene, termed UBA2, that encodes a 71-kDa protein with extensive sequence similarities to both the UBA1-encoded yeast E1 and E1 enzymes of other organisms [8].
  • Depletion of Uba2 from cells produces extracts which polyadenylate precursor RNA with increased efficiency compared to extracts from nondepleted cells, while depletion of Ufd1 yields extracts which are defective in processing [9].
  • The last 115 amino acids of Uba2, which contains an 82-amino acid region not present in previously characterized E1 enzymes, is sufficient for the interaction with Pap1 [9].


  1. Phosphoinositide profiling in complex lipid mixtures using electrospray ionization mass spectrometry. Wenk, M.R., Lucast, L., Di Paolo, G., Romanelli, A.J., Suchy, S.F., Nussbaum, R.L., Cline, G.W., Shulman, G.I., McMurray, W., De Camilli, P. Nat. Biotechnol. (2003) [Pubmed]
  2. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. Johnson, E.S., Schwienhorst, I., Dohmen, R.J., Blobel, G. EMBO J. (1997) [Pubmed]
  3. Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a. Ryu, K.S., Lee, K.J., Bae, S.H., Kim, B.K., Kim, K.A., Choi, B.S. J. Biol. Chem. (2003) [Pubmed]
  4. A lack of SUMO conjugation affects cNLS-dependent nuclear protein import in yeast. Stade, K., Vogel, F., Schwienhorst, I., Meusser, B., Volkwein, C., Nentwig, B., Dohmen, R.J., Sommer, T. J. Biol. Chem. (2002) [Pubmed]
  5. Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast. Yamamoto, A., DeWald, D.B., Boronenkov, I.V., Anderson, R.A., Emr, S.D., Koshland, D. Mol. Biol. Cell (1995) [Pubmed]
  6. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Bénédetti, H., Raths, S., Crausaz, F., Riezman, H. Mol. Biol. Cell (1994) [Pubmed]
  7. Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis. Hatfield, P.M., Vierstra, R.D. J. Biol. Chem. (1992) [Pubmed]
  8. An essential yeast gene encoding a homolog of ubiquitin-activating enzyme. Dohmen, R.J., Stappen, R., McGrath, J.P., Forrová, H., Kolarov, J., Goffeau, A., Varshavsky, A. J. Biol. Chem. (1995) [Pubmed]
  9. The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts. del Olmo, M., Mizrahi, N., Gross, S., Moore, C.L. Mol. Gen. Genet. (1997) [Pubmed]
  10. Enzymatic synthesis of pyrene-labeled polyphosphoinositides and their behavior in organic solvents and phosphatidylcholine bilayers. Gadella, T.W., Moritz, A., Westerman, J., Wirtz, K.W. Biochemistry (1990) [Pubmed]
  11. Reconstitution of the mammalian PI3K/PTEN/Akt pathway in yeast. Rodríguez-Escudero, I., Roelants, F.M., Thorner, J., Nombela, C., Molina, M., Cid, V.J. Biochem. J. (2005) [Pubmed]
  12. Inositol metabolism in yeasts. White, M.J., Lopes, J.M., Henry, S.A. Adv. Microb. Physiol. (1991) [Pubmed]
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