ASM4/YDL088C Summary Help

Standard Name ASM4
Systematic Name YDL088C
Alias NUP59
Feature Type ORF, Verified
Description FG-nucleoporin component of central core of nuclear pore complex (NPC); contributes directly to nucleocytoplasmic transport; induces membrane tubulation, which may contribute to nuclear pore assembly; ASM4 has a paralog, NUP53, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6, 7 and see Summary Paragraph)
Chromosomal Location
ChrIV:300003 to 298417 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ASM4 GO evidence and references
  View Computational GO annotations for ASM4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Classical genetics
Large-scale survey
132 total interaction(s) for 78 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 21
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 2
  • Biochemical Activity: 1
  • Co-purification: 1
  • PCA: 2
  • Reconstituted Complex: 7
  • Two-hybrid: 3

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 61
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 3
  • Positive Genetic: 13
  • Synthetic Growth Defect: 5
  • Synthetic Lethality: 8

Expression Summary
Length (a.a.) 528
Molecular Weight (Da) 58,793
Isoelectric Point (pI) 8.04
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:300003 to 298417 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2004-02-11 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1587 300003..298417 2004-02-11 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 SGDIDS000002246

Asm4p is a nuclear pore protein that forms a complex with two other nucleoporins, Nup53p and Nup170p (1). 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 8, 9, 10, 11). The structure of the vertebrate NPC has been studied extensively; recent reviews include 12, 13, 14, and 15. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate (16, 17). Many yeast nuclear pore proteins, or nucleoporins, have been identified by a variety of genetic approaches (reviewed in 8, 9, 18, 19, 20). The Asm4p-containing complex also interacts with the karyopherin Pse1p (1). Lopez et al. (21) report that ASM4 is essential for vegetative growth in some strain backgrounds tested. Mutations in ASM4 also show genetic interactions with mutations in other nucleoporin genes (22, 1) and with POL3, which encodes a subunit of DNA polymerase delta (23). Asm4p is structurally similar to Nup53p, and similar protein sequences are found in several eukaryotes (1).

Last updated: 1999-08-03 Contact SGD

References cited on this page View Complete Literature Guide for ASM4
1) Marelli M, et al.  (1998) Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J Cell Biol 143(7):1813-30
2) Iouk T, et al.  (2002) The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. J Cell Biol 159(5):807-19
3) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
4) Patel SS, et al.  (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129(1):83-96
5) Thomsen R, et al.  (2008) General, rapid, and transcription-dependent fragmentation of nucleolar antigens in S. cerevisiae mRNA export mutants. RNA 14(4):706-16
6) Patel SS and Rexach MF  (2008) Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium. Mol Cell Proteomics 7(1):121-31
7) Vollmer B, et al.  (2012) Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly. EMBO J 31(20):4072-84
8) Fabre E and Hurt E  (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31:277-313
9) 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
10) Pemberton LF, et al.  (1998) Transport routes through the nuclear pore complex. Curr Opin Cell Biol 10(3):392-9
11) Izaurralde E and Adam S  (1998) Transport of macromolecules between the nucleus and the cytoplasm. RNA 4(4):351-64
12) Hinshaw JE  (1994) Architecture of the nuclear pore complex and its involvement in nucleocytoplasmic transport. Biochem Pharmacol 47(1):15-20
13) Pante N and Aebi U  (1996) Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol 31(2):153-99
14) Davis LI  (1995) The nuclear pore complex. Annu Rev Biochem 64:865-96
15) Pante N and Aebi U  (1994) Toward the molecular details of the nuclear pore complex. J Struct Biol 113(3):179-89
16) Rout MP and Blobel G  (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123(4):771-83
17) 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
18) Doye V and Hurt E  (1997) From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol 9(3):401-11
19) Doye V and Hurt EC  (1995) Genetic approaches to nuclear pore structure and function. Trends Genet 11(6):235-41
20) Newmeyer DD  (1993) The nuclear pore complex and nucleocytoplasmic transport. Curr Opin Cell Biol 5(3):395-407
21) Lopez MC, et al.  (1998) Disruption of six Saccharomyces cerevisiae genes from chromosome IV and basic phenotypic analysis of deletion mutants. Yeast 14(13):1199-208
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) Giot L, et al.  (1995) Suppressors of thermosensitive mutations in the DNA polymerase delta gene of Saccharomyces cerevisiae. Mol Gen Genet 246(2):212-22