RRD1/YIL153W Summary Help

Standard Name RRD1 1
Systematic Name YIL153W
Alias YPA1
Feature Type ORF, Verified
Description Peptidyl-prolyl cis/trans-isomerase; activator of the phosphotyrosyl phosphatase activity of PP2A; involved in G1 phase progression, microtubule dynamics, bud morphogenesis and DNA repair; required for rapid reduction of Sgs1p levels in response to rapamycin; subunit of the Tap42p-Sit4p-Rrd1p complex; protein increases in abundance and relative distribution to the nucleus increases upon DNA replication stress (1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11)
Name Description Resistant to Rapamycin Deletion 1
Chromosomal Location
ChrIX:55198 to 56379 | ORF Map | GBrowse
Gene Ontology Annotations All RRD1 GO evidence and references
  View Computational GO annotations for RRD1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Classical genetics
Large-scale survey
164 total interaction(s) for 129 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 11
  • Co-localization: 1
  • Co-purification: 1
  • Protein-peptide: 1
  • Reconstituted Complex: 4
  • Two-hybrid: 7

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 82
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 2
  • Positive Genetic: 10
  • Synthetic Growth Defect: 17
  • Synthetic Lethality: 12
  • Synthetic Rescue: 6

Expression Summary
Length (a.a.) 393
Molecular Weight (Da) 45,082
Isoelectric Point (pI) 6.83
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIX:55198 to 56379 | ORF Map | GBrowse
Last Update Coordinates: 1994-12-10 | Sequence: 1994-12-10
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1182 55198..56379 1994-12-10 1994-12-10
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001415
References cited on this page View Complete Literature Guide for RRD1
1) Rempola B, et al.  (2000) Functional analysis of RRD1 (YIL153w) and RRD2 (YPL152w), which encode two putative activators of the phosphotyrosyl phosphatase activity of PP2A in Saccharomyces cerevisiae. Mol Gen Genet 262(6):1081-92
2) Van Hoof C, et al.  (2000) The Saccharomyces cerevisiae homologue YPA1 of the mammalian phosphotyrosyl phosphatase activator of protein phosphatase 2A controls progression through the G1 phase of the yeast cell cycle. J Mol Biol 302(1):103-20
3) Mitchell DA and Sprague GF  (2001) The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae. Mol Cell Biol 21(2):488-500
4) Van Hoof C, et al.  (2001) The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations. Exp Cell Res 264(2):372-87
5) Van Hoof C, et al.  (1998) Functional analysis of conserved domains in the phosphotyrosyl phosphatase activator. Molecular cloning of the homologues from Drosophila melanogaster and Saccharomyces cerevisiae. Biochemistry 37(37):12899-908
6) Zheng Y and Jiang Y  (2005) The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes. Mol Biol Cell 16(4):2119-27
7) Douville J, et al.  (2004) The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1, interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-1-oxide and UVA. Curr Genet 46(2):72-81
8) Fellner T, et al.  (2003) A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo. Genes Dev 17(17):2138-50
9) Jordens J, et al.  (2006) The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase. J Biol Chem 281(10):6349-57
10) Marrakchi R, et al.  (2011) The isomerase Rrd1 mediates rapid loss of the Sgs1 helicase in response to rapamycin. Biochem Cell Biol 89(3):332-40
11) 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