POM152/YMR129W Summary Help

Standard Name POM152 1
Systematic Name YMR129W
Feature Type ORF, Verified
Description Glycoprotein subunit of transmembrane ring of nuclear pore complex; contributes to nucleocytoplasmic transport, nuclear pore complex (NPC) biogenesis and spindle pole body duplication; homologous to human NUP210 (1, 2, 3, 4, 5, 6 and see Summary Paragraph)
Name Description POre Membrane 1
Chromosomal Location
ChrXIII:527804 to 531817 | ORF Map | GBrowse
Gene Ontology Annotations All POM152 GO evidence and references
  View Computational GO annotations for POM152
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 72 genes
Classical genetics
Large-scale survey
163 total interaction(s) for 86 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 48
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 7
  • Biochemical Activity: 1
  • Co-fractionation: 1
  • Co-purification: 2
  • PCA: 1
  • Protein-RNA: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 56
  • Phenotypic Enhancement: 1
  • Positive Genetic: 5
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 16
  • Synthetic Rescue: 8

Expression Summary
Length (a.a.) 1,337
Molecular Weight (Da) 151,651
Isoelectric Point (pI) 6.71
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:527804 to 531817 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..4014 527804..531817 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004736

POM152 encodes a nuclear pore protein (1, 7). Transport of macromolecules between the nucleus and the cytoplasm of eukaryotic cells occurs through the nuclear pore complex (NPC), a large macromolecular complex that spans the nuclear envelope (reviewed in 7, 8, 9, 10). The structure of the vertebrate NPC has been studied extensively; recent reviews include 11, 12, 13, and 14. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate (15, 16). Many yeast nuclear pore proteins, or nucleoporins, have been identified by a variety of genetic approaches (reviewed in 7, 8, 17, 18, 19). Pom152p is an integral membrane protein (1), and is one of the most abundant yeast nucleoporins (20). Pom152p interacts physically with other abundant yeast nucleoporins, Nic96p, Nup157p, Nup170p, and Nup188p (21, 7). These abundant nucleoporins may form the structural core of the NPC (7). POM152 is not essential, but overproduction of Pom152p inhibits cell growth (1). pom152 mutations are also synthetically lethal with mutations in several nucleoporin genes (20, 21, 7, 22). Analysis of the domain structure and membrane topology of Pom152p reveals that different domains may have different functions, and show different genetic interactions with other nucleoporin genes (22). Deletion of POM152 suppresses a spindle pole body duplication defect caused by a mutation in NDC1, which encodes a shared component of the nuclear pore and the spindle pole body (23).

Last updated: 1999-11-01 Contact SGD

References cited on this page View Complete Literature Guide for POM152
1) Wozniak RW, et al.  (1994) POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope. J Cell Biol 125(1):31-42
2) Strambio-de-Castillia C, et al.  (1995) Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. J Cell Biol 131(1):19-31
3) Rout MP, et al.  (2000) The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148(4):635-51
4) Onischenko E, et al.  (2009) Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance. J Cell Biol 185(3):475-91
5) Fernandez-Martinez J and Rout MP  (2009) Nuclear pore complex biogenesis. Curr Opin Cell Biol 21(4):603-12
6) Witkin KL, et al.  (2010) Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae. Genetics 186(3):867-83
7) Fabre E and Hurt E  (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31:277-313
8) Wente SR, et al.  (1997) "The nucleus and nucleocytoplasmic transport in Saccharomyces cerevisiae." Pp. 471-546 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Cell Cycle and Cell Biology, edited by Pringle JR, Broach JR and Jones EW. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
9) Pemberton LF, et al.  (1998) Transport routes through the nuclear pore complex. Curr Opin Cell Biol 10(3):392-9
10) Izaurralde E and Adam S  (1998) Transport of macromolecules between the nucleus and the cytoplasm. RNA 4(4):351-64
11) Hinshaw JE  (1994) Architecture of the nuclear pore complex and its involvement in nucleocytoplasmic transport. Biochem Pharmacol 47(1):15-20
12) Pante N and Aebi U  (1996) Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol 31(2):153-99
13) Davis LI  (1995) The nuclear pore complex. Annu Rev Biochem 64:865-96
14) Pante N and Aebi U  (1994) Toward the molecular details of the nuclear pore complex. J Struct Biol 113(3):179-89
15) Rout MP and Blobel G  (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123(4):771-83
16) Yang Q, et al.  (1998) Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol Cell 1(2):223-34
17) Doye V and Hurt E  (1997) From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol 9(3):401-11
18) Doye V and Hurt EC  (1995) Genetic approaches to nuclear pore structure and function. Trends Genet 11(6):235-41
19) Newmeyer DD  (1993) The nuclear pore complex and nucleocytoplasmic transport. Curr Opin Cell Biol 5(3):395-407
20) Aitchison JD, et al.  (1995) 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. J Cell Biol 131(5):1133-48
21) Nehrbass U, et al.  (1996) The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. J Cell Biol 133(6):1153-62
22) Tcheperegine SE, et al.  (1999) Topology and functional domains of the yeast pore membrane protein Pom152p. J Biol Chem 274(8):5252-8
23) Chial HJ, et al.  (1998) Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. J Cell Biol 143(7):1789-800