NPL3/YDR432W Summary Help

Standard Name NPL3 1
Systematic Name YDR432W
Alias MTR13 2 , MTS1 3 , NOP3 4 , NAB1 5
Feature Type ORF, Verified
Description RNA-binding protein; promotes elongation, regulates termination, and carries poly(A) mRNA from nucleus to cytoplasm; represses translation initiation by binding eIF4G; required for pre-mRNA splicing; interacts with E3 ubiquitin ligase Bre1p, linking histone ubiquitination to mRNA processing; may have role in telomere maintenance; dissociation from mRNAs promoted by Mtr10p; phosphorylated by Sky1p in cytoplasm; protein abundance increases in response to DNA replication stress (6, 7, 8, 9, 10, 11, 12, 13, 14)
Name Description Nuclear Protein Localization 1
Chromosomal Location
ChrIV:1328783 to 1330027 | ORF Map | GBrowse
Gene Ontology Annotations All NPL3 GO evidence and references
  View Computational GO annotations for NPL3
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
1335 total interaction(s) for 1103 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 103
  • Affinity Capture-RNA: 6
  • Affinity Capture-Western: 40
  • Biochemical Activity: 15
  • Co-localization: 4
  • Far Western: 1
  • PCA: 1
  • Protein-peptide: 6
  • Protein-RNA: 1
  • Reconstituted Complex: 10
  • Two-hybrid: 19

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 3
  • Negative Genetic: 68
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 9
  • Positive Genetic: 18
  • Synthetic Growth Defect: 361
  • Synthetic Lethality: 35
  • Synthetic Rescue: 633

Expression Summary
Length (a.a.) 414
Molecular Weight (Da) 45,407
Isoelectric Point (pI) 5.35
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:1328783 to 1330027 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1245 1328783..1330027 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 SGDIDS000002840
References cited on this page View Complete Literature Guide for NPL3
1) Bossie MA, et al.  (1992) A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast. Mol Biol Cell 3(8):875-93
2) Kadowaki T, et al.  (1994) Isolation and characterization of Saccharomyces cerevisiae mRNA transport-defective (mtr) mutants. J Cell Biol 126(3):649-59
3) Ellis EM and Reid GA  (1993) The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding protein involved in mitochondrial protein targeting. Gene 132(2):175-83
4) Russell ID and Tollervey D  (1992) NOP3 is an essential yeast protein which is required for pre-rRNA processing. J Cell Biol 119(4):737-47
5) Wilson SM, et al.  (1994) Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae. J Cell Biol 127(5):1173-84
6) Lee MS, et al.  (1996) A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Genes Dev 10(10):1233-46
7) Gilbert W, et al.  (2001) Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. RNA 7(2):302-13
8) Windgassen M, et al.  (2004) Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the translating mRNPs, and Npl3p can function as a translational repressor. Mol Cell Biol 24(23):10479-91
9) Dermody JL, et al.  (2008) Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation. PLoS One 3(9):e3273
10) Kress TL, et al.  (2008) A Single SR-like Protein, Npl3, Promotes Pre-mRNA Splicing in Budding Yeast. Mol Cell 32(5):727-34
11) Rajyaguru P, et al.  (2012) Scd6 Targets eIF4G to Repress Translation: RGG Motif Proteins as a Class of eIF4G-Binding Proteins. Mol Cell 45(2):244-54
12) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
13) Lee-Soety JY, et al.  (2012) Yeast hnRNP-related proteins contribute to the maintenance of telomeres. Biochem Biophys Res Commun 426(1):12-7
14) Moehle EA, et al.  (2012) The Yeast SR-Like Protein Npl3 Links Chromatin Modification to mRNA Processing. PLoS Genet 8(11):e1003101