NUP188/YML103C Summary Help

NUP188 BASIC INFORMATION

Standard Name NUP188
Systematic Name YML103C
Feature Type ORF, Verified
Description Subunit of the nuclear pore complex (NPC), involved in the structural organization of the complex and of the nuclear envelope, also involved in nuclear envelope permeability, interacts with Pom152p and Nic96p (1, 2 and see Summary Paragraph)
Name Description NUclear Pore
GO Annotations All NUP188 GO evidence and references
    View Computational GO annotations for NUP188
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All NUP188 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions NUP188 All interactions details and references
93 total interaction(s) for 76 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 7
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • Co-purification: 1
  • FRET: 8
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 2
  • Phenotypic Enhancement: 32
  • Phenotypic Suppression: 14
  • Synthetic Growth Defect: 10
  • Synthetic Lethality: 14

Sequence Information
ChrXIII:67549 to 62582 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..4968 67549..62582 1996-07-31 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000004571

NUP188 RESOURCES

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SGD ORF map
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  • Functional Analysis

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Expression Summary histogram

SUMMARY PARAGRAPH for NUP188

NUP188 encodes a nuclear pore protein (3, 4). 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 4, 5, 6, 7). The structure of the vertebrate NPC has been studied extensively; recent reviews include 8, 9, 10, and 11. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate (12, 13). Many yeast nuclear pore proteins, or nucleoporins, have been identified by a variety of genetic approaches (reviewed in 4, 5, 14, 15, 16). Nup188p is one of the most abundant yeast nucleoporins (3). Nup188p interacts physically with other abundant yeast nucleoporins, Nic96p, Pom152p, Nup157p, and Nup170p (2, 4). These abundant nucleoporins may form the structural core of the NPC (4). NUP188 is not essential, but both null and dominant alleles cause temperature sensitivity and defects in nuclear envelope morphology (2, 17). The nup188 null also causes a defect in protein import into the nucleus, which can be suppressed by overexpressing cytosolic HSP70-related chaperones (18). nup188 mutations are also synthetically lethal with mutations in several other nucleoporin genes (3, 2, 4, 19).

Last updated: 1999-08-12

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for NUP188]

1) Shulga N, et al.  (2000) Yeast nucleoporins involved in passive nuclear envelope permeability. J Cell Biol 149(5):1027-38
2) 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
3) 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
4) Fabre E and Hurt E  (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31:277-313
5) 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
6) Pemberton LF, et al.  (1998) Transport routes through the nuclear pore complex. Curr Opin Cell Biol 10(3):392-9
7) Izaurralde E and Adam S  (1998) Transport of macromolecules between the nucleus and the cytoplasm. RNA 4(4):351-64
8) Hinshaw JE  (1994) Architecture of the nuclear pore complex and its involvement in nucleocytoplasmic transport. Biochem Pharmacol 47(1):15-20
9) Pante N and Aebi U  (1996) Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol 31(2):153-99
10) Davis LI  (1995) The nuclear pore complex. Annu Rev Biochem 64:865-96
11) Pante N and Aebi U  (1994) Toward the molecular details of the nuclear pore complex. J Struct Biol 113(3):179-89
12) Rout MP and Blobel G  (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123(4):771-83
13) 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
14) Doye V and Hurt E  (1997) From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol 9(3):401-11
15) Doye V and Hurt EC  (1995) Genetic approaches to nuclear pore structure and function. Trends Genet 11(6):235-41
16) Newmeyer DD  (1993) The nuclear pore complex and nucleocytoplasmic transport. Curr Opin Cell Biol 5(3):395-407
17) Zabel U, et al.  (1996) Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. J Cell Biol 133(6):1141-52
18) Shulga N, et al.  (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7
19) Tcheperegine SE, et al.  (1999) Topology and functional domains of the yeast pore membrane protein Pom152p. J Biol Chem 274(8):5252-8