YVH1/YIR026C Summary Help

Standard Name YVH1 1, 2
Systematic Name YIR026C
Feature Type ORF, Verified
Description Protein phosphatase; involved in vegetative growth at low temperatures, sporulation, and glycogen accumulation; mutants are defective in 60S ribosome assembly; member of the dual-specificity family of protein phosphatases (1, 3, 4, 5 and see Summary Paragraph)
Name Description Yeast vaccinia virus VH1 Homolog 1
Chromosomal Location
ChrIX:405967 to 404873 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: 31 cM
Gene Ontology Annotations All YVH1 GO evidence and references
  View Computational GO annotations for YVH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
Large-scale survey
79 total interaction(s) for 63 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 16
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 14
  • PCA: 10
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Lethality: 2
  • Dosage Rescue: 8
  • Negative Genetic: 16
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 3
  • Synthetic Growth Defect: 3
  • Synthetic Rescue: 3

Expression Summary
Length (a.a.) 364
Molecular Weight (Da) 41,185
Isoelectric Point (pI) 8.01
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIX:405967 to 404873 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: 31 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1994-12-10
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1095 405967..404873 2011-02-03 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 SGDIDS000001465

YVH1 was originally identified as an atypical dual-specificity protein phosphatase (DUSP) based on sequence similarity (1, 6). However, assays with the purified protein have to date only provided evidence for phosphotyrosine-specific protein phosphatase activity (1). YVH1 is induced by nitrogen starvation (1) and reduced temperature (7) where it clusters with genes involved in rRNA synthesis and ribosomal protein genes (8). Yvh1p associates with pre-60S ribosomes and is required for a late-step in the maturation of the 60S ribosomal subunit (9, 5, 10). Yvh1p is involved in the assembly of the ribosome stalk, a structure of the large subunit required for translation factor recruitment and ribosome activity. Specifically, Yvh1p is recruited to the pre-60S particle by Rpl12p where it facilitates the release of the Mrt4p assembly factor from the stalk of the maturing pre-60S particle (10, 9). Release of Mrt4p allows Rpp0p (an Mrt4p paralog) to gain access and load onto the pre-60S subunit, resulting in the maturation of the ribosome stalk, and subsequent release of Yvh1p (10, 9).

While YVH1 is not essential for viability, deletion results in defects in growth, glycogen accumulation, meiosis and sporulation (1, 7, 4, 3, 11). Several of these null phenotypes are similar to those associated with constitutively active protein kinase A, and altering cAMP levels partially suppresses the glycogen accumulation and spore maturation defects, implicating Yvh1p in cAMP-mediated signaling (4). Lack of YVH1 results in several ribosome assembly related defects including: altered polysome profiles, defective nuclear export of pre-60S ribosomal particles, and defects in rRNA processing (9, 5, 10). These defects are independent of the catalytic activity of the phosphatase, but instead dependent on an intact C-terminal cysteine-rich RING variant domain (4, 5, 10). In the human ortholog, this RING variant domain is capable of coordinating zinc (1, 12).

Dual-specificity phosphatases (DUSPs) exist in many different species (13). An ortholog from C. albicans (YVH1) controls growth, filamentation and virulence (14). A human ortholog, DUSP12 (OMIM), is able to functionally complement a yvh1 null mutant (12, 10). Another related human dual specificity phosphatase, DUSP7 (OMIM), regulates MAPK signaling pathways, is involved in cell crowding, and is overexpressed in leukocytes derived from AML (acute myelogenous leukemia) and ALL (acute lymphoblastic leukemia) patients (15).

Last updated: 2010-03-11 Contact SGD

References cited on this page View Complete Literature Guide for YVH1
1) Guan K, et al.  (1992) A yeast protein phosphatase related to the vaccinia virus VH1 phosphatase is induced by nitrogen starvation. Proc Natl Acad Sci U S A 89(24):12175-9
2) Cooper, T.  (1993) Personal Communication, Mortimer Map Edition 12
3) Park HD, et al.  (1996) The S. cerevisiae nitrogen starvation-induced Yvh1p and Ptp2p phosphatases play a role in control of sporulation. Yeast 12(11):1135-51
4) Beeser AE and Cooper TG  (2000) The dual-specificity protein phosphatase Yvh1p regulates sporulation, growth, and glycogen accumulation independently of catalytic activity in Saccharomyces cerevisiae via the cyclic AMP-dependent protein kinase cascade. J Bacteriol 182(12):3517-28
5) Liu Y and Chang A  (2009) A mutant plasma membrane protein is stabilized upon loss of Yvh1, a novel ribosome assembly factor. Genetics 181(3):907-15
6) Patterson KI, et al.  (2009) Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem J 418(3):475-89
7) Sakumoto N, et al.  (1999) A series of protein phosphatase gene disruptants in Saccharomyces cerevisiae. Yeast 15(15):1669-79
8) Sahara T, et al.  (2002) Comprehensive expression analysis of time-dependent genetic responses in yeast cells to low temperature. J Biol Chem 277(51):50015-21
9) Kemmler S, et al.  (2009) Yvh1 is required for a late maturation step in the 60S biogenesis pathway. J Cell Biol 186(6):863-80
10) Lo KY, et al.  (2009) Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0. J Cell Biol 186(6):849-62
11) Beeser AE and Cooper TG  (1999) The dual-specificity protein phosphatase Yvh1p acts upstream of the protein kinase mck1p in promoting spore development in Saccharomyces cerevisiae. J Bacteriol 181(17):5219-24
12) Muda M, et al.  (1999) Identification of the human YVH1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function. J Biol Chem 274(34):23991-5
13) Wang T, et al.  (1998) Isolation and identification of xylitol dehydrogenase gene from Trichoderma reesei. Chin J Biotechnol 14(3):179-85
14) Hanaoka N, et al.  (2005) A putative dual-specific protein phosphatase encoded by YVH1 controls growth, filamentation and virulence in Candida albicans. Microbiology 151(Pt 7):2223-32
15) Levy-Nissenbaum O, et al.  (2006) The Pyst2-L phosphatase is involved in cell-crowding. Immunol Lett 104(1-2):138-45