The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

POM152  -  Pom152p

Saccharomyces cerevisiae S288c

Synonyms: Nuclear pore protein POM152, Nucleoporin POM152, P150, Pore membrane protein POM152, YM9553.05, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on POM152

  • We investigate the function of the three integral membrane nucleoporins, which are Ndc1p, Pom152p, and Pom34p, in NPC assembly and transport in Saccharomyces cerevisiae [1].
  • The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function [1].
  • There, Nup188p interacts with an integral protein of the pore membrane domain, Pom152p, and another abundant nucleoporin, Nic96p [2].
  • Examination of the genetic interactions between these proteins indicate that while deletion of either POM152, NUP170, or NUP188 alone is not lethal, pairwise combinations are [3].
  • This ER pool of POM152 is likely to be involved in the duplication of nuclear pores and NPCs during S-phase [4].

Biological context of POM152


Anatomical context of POM152

  • The results of these experiments suggest that Pom152p contains a single transmembrane segment with its N terminus (amino acid residues 1-175) extending into the nuclear pore and its C terminus (amino acid residues 196-1337) positioned in the lumen of the nuclear envelope [7].
  • POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope [6].
  • When expressed in mouse 3T3 cells, POM152 was found to be localized to the pore membrane, suggesting a conserved sorting pathway between yeast and mammals [6].

Associations of POM152 with chemical compounds

  • POM152 is likely to be a type II membrane protein with its NH2-terminal region (175 residues) and its COOH-terminal region (1,142 residues) positioned on the pore side and cisternal side of the pore membrane, respectively [6].

Other interactions of POM152

  • However, truncations of the N-glycosylated, lumenal domain of Pom152p and pom152 mutants lacking N-linked glycosylation sites are viable in combination with nup1Delta, suppress nup1Delta temperature sensitivity, and partially suppress the nuclear protein import defects associated with the deletion of NUP1 [5].
  • Finally, we have found that a deletion of POM152, which encodes an abundant but nonessential nucleoporin, suppresses the SPB duplication defect associated with a mutation in the NDC1 gene [8].
  • The requirement for Pom152p in strains containing mutations allelic to the NPC protein genes NIC96 and NUP59 could be alleviated by Pom152p's N terminus, independent of its integration into the membrane [7].
  • Snl1p has a predicted molecular mass of 18.3 kDa, a putative transmembrane domain, and limited sequence similarity to Pom152p, the only previously identified yeast NPC-associated integral membrane protein [9].

Analytical, diagnostic and therapeutic context of POM152

  • Electron microscopy studies reveal that the absence of Ndc1p and Pom152p results in aberrant pores that have enlarged diameters and lack proteinaceous material, leading to an increased diffusion between the cytoplasm and the nucleus [1].
  • An inducible endo-beta-1,6-glucanase was purified from Penicillium brefeldianum by DEAE-cellulose, Bio-Gel P-150 and high-pressure liquid chromatography [10].


  1. The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function. Madrid, A.S., Mancuso, J., Cande, W.Z., Weis, K. J. Cell Biol. (2006) [Pubmed]
  2. The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. Nehrbass, U., Rout, M.P., Maguire, S., Blobel, G., Wozniak, R.W. J. Cell Biol. (1996) [Pubmed]
  3. Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. Aitchison, J.D., Rout, M.P., Marelli, M., Blobel, G., Wozniak, R.W. J. Cell Biol. (1995) [Pubmed]
  4. Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. Strambio-de-Castillia, C., Blobel, G., Rout, M.P. J. Cell Biol. (1995) [Pubmed]
  5. Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p. Belanger, K.D., Gupta, A., MacDonald, K.M., Ott, C.M., Hodge, C.A., Cole, C.M., Davis, L.I. Genetics (2005) [Pubmed]
  6. POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope. Wozniak, R.W., Blobel, G., Rout, M.P. J. Cell Biol. (1994) [Pubmed]
  7. Topology and functional domains of the yeast pore membrane protein Pom152p. Tcheperegine, S.E., Marelli, M., Wozniak, R.W. J. Biol. Chem. (1999) [Pubmed]
  8. Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. Chial, H.J., Rout, M.P., Giddings, T.H., Winey, M. J. Cell Biol. (1998) [Pubmed]
  9. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Ho, A.K., Raczniak, G.A., Ives, E.B., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
  10. Purification and properties of a beta-1,6-glucanase from Penicillium brefeldianum. Schep, G.P., Shepherd, M.G., Sullivan, P.A. Biochem. J. (1984) [Pubmed]
WikiGenes - Universities