YNL134C Summary Help

Systematic Name YNL134C
Feature Type ORF, Verified
Description Protein of unknown function; similar to dehydrogenases from other model organisms; green fluorescent protein (GFP)-fusion protein localizes to both the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress (1, 2, 3, 4 and see Summary Paragraph)
Chromosomal Location
ChrXIV:373581 to 372451 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All YNL134C GO evidence and references
  View Computational GO annotations for YNL134C
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 10 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
20 total interaction(s) for 16 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 8
  • Affinity Capture-RNA: 2
  • PCA: 2

Genetic Interactions
  • Negative Genetic: 8

Resources
Expression Summary
histogram
Resources
Length (a.a.) 376
Molecular Weight (Da) 41,164
Isoelectric Point (pI) 6.14
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIV:373581 to 372451 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1131 373581..372451 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005078
SUMMARY PARAGRAPH for YNL134C

About the medium-chain dehydrogenase/reductase (MDR) family

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (5), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (6, 7). Many MDR members are basic metabolic enzymes acting on alcohols or aldehydes, and thus these enzymes may have roles in detoxifying alcohols and related compounds, protecting against environmental stresses such as osmotic shock, reduced or elevated temperatures, or oxidative stress (6). The family also includes the mammalian zeta-crystallin lens protein, which may protect the lens against oxidative damage and enzymes which produce lignocellulose in plants (6).

MDR enzymes typically have subunits of about 350 aa residues and are two-domain proteins, with a catalytic domain and a second domain for binding to the nicotinamide cofactor, either NAD(H) or NADP(H) (6, 7). They contain 0, 1, or 2 zinc atoms (8). When zinc is present, it is involved in catalysis at the active site.

Based on phylogenetic and sequence analysis, the members of the MDR superfamily can be further divided into more closely related subgroups (6, 7). In families which are widespread from prokaryotes to eukaryotes, some members appear conserved across all species, while others appear to be due to lineage specific duplications. Some subgroups are only found in certain taxa. S. cerevisiae contains fifteen (6) or twenty-one (7) members of the MDR superfamily, listed below. The difference in number is due to six sequences that were included as members of the quinone oxidoreductase family by Riveros-Rosas et al. (7) but not by Nordling et al. (6).

Zinc-containing enzyme groups:
- PDH; "polyol" dehydrogenase family - BDH1, BDH2, SOR1, SOR2, XYL2
- ADH; class III alcohol dehydrogenase family - SFA1
- Y-ADH; "yeast" alcohol dehydrogenase family - ADH1, ADH2, ADH3, ADH5
- CADH; cinnamyl alcohol dehydrogenase family - ADH6, ADH7

Non-zinc-containing enzyme groups:
- NRBP; nuclear receptor binding protein (7) or MRF; mitochondrial respiratory function (6) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (6, 7), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (7)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (7) or ACR; acyl-CoA reductase (6) family - no members in S. cerevisiae

Last updated: 2008-08-19 Contact SGD

References cited on this page View Complete Literature Guide for YNL134C
1) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
2) Balakrishnan R, et al.  (2005) Fungal BLAST and Model Organism BLASTP Best Hits: new comparison resources at the Saccharomyces Genome Database (SGD). Nucleic Acids Res 33 Database Issue:D374-7
3) Lee MW, et al.  (2007) Global protein expression profiling of budding yeast in response to DNA damage. Yeast 24(3):145-54
4) 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
5) Jornvall H, et al.  (1981) Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc Natl Acad Sci U S A 78(7):4226-30
6) Nordling E, et al.  (2002) Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-76
7) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
8) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463():373-7