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ALD4 / YOR374W Protein

Protein abundance data, domains, shared domains with other proteins, protein sequence retrieval for various strains, sequence-based physico-chemical properties, protein modification sites, and external identifiers for the protein.

Aliases
ALDH2 12 , ALD7 15
Protein Product
aldehyde dehydrogenase (NADP(+)) ALD4
Feature Type
ORF , Verified
EC Number
1.2.1.4
Summary
Ald4p is 519 amino acids long, very short-lived, low-to-moderate in abundance; contains Arg/Lys polymorphism at residue 165; sumoylated on K306, trimethylated on K345, acetylated on 6 lysines, phosphorylated on 11 residues, succinylated on 24 lysines; protein activity regulated by Cdc5p via phosphorylation on S269 and S398

AlphaFold Protein Structure

AlphaFold, developed by DeepMind, is an AI program that accurately predicts protein structures from amino acid sequences, enabling visualization of protein conformations. The predicted structures can be accessed through the Protein Data Bank (PDB) and AlphaFold Protein Structure Database.

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Model Confidence

Very high
Confident
Low
Very low

Experimental Data

Contains experimentally-derived protein half-life data obtained using stable isotope labeling by amino acids (SILAC) coupled with mass spectrometry. This section also contains protein abundance data for both untreated and treated cells obtained from over 20 studies. These data have been normalized and converted to a common unit of molecules per cell.

Protein Half Life

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ExperimentResultReference
half-life3.3 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
1172SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1345SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
11117SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
12022SD0.2 M hydroxyurea160 minconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
27656SD200 ng/ml sirolimus700 minconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 27 entries

Domains and Classification - S288C

Collection of computationally identified domains and motifs, as determined by InterProScan analysis; includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain.

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Gene Protein Coordinates Accession ID Description Source No. of Genes with Domain

Domain Locations

Visual representation of the locations of the domains within the protein, as listed in the Domains and Classification table. Each row displays the domain(s) derived from a different Source, with domains color-coded according to this Source.

Scroll over a domain to view its exact coordinates and its Description.

Shared Domains

This diagram displays domains (colored squares) shared between the given protein (yellow circle) and other proteins (gray circles); the domains are color-coded according to their source, as displayed in the Domain Locations table, above.

Reset

Click on a gene or domain name to go to its specific page within SGD; drag any of the gene or domain objects around within the visualization for easier viewing; click “Reset” to automatically redraw the diagram.

Alleles

Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.

ald4-C324A | ald4-E290K | ald4-N192D | ald4-S269A | ald4-Δ

View all ALD4 alleles in SGD search

Sequence

Protein sequence for the given gene in S288C and other strains, when available. Use the pull-down menu under "Strain" to select the sequence for a specific strain. The displayed sequence can be downloaded in FASTA format as a .txt file. Amino acids displayed in blue represent modification sites. More detailed evidence for these modification sites is presented in the Post-translational Modifications table, located just below the protein sequence. 

  1 MFSRSTLCLK TSASSIGRLQ LRYFSHLPMT VPIKLPNGLE YEQPTGLFIN NKFVPSKQNK 
 61 TFEVINPSTE EEICHIYEGR EDDVEEAVQA ADRAFSNGSW NGIDPIDRGK ALYRLAELIE 
121 QDKDVIASIE TLDNGKAISS SRGDVDLVIN YLKSSAGFAD KIDGRMIDTG RTHFSYTKRQ 
181 PLGVCGQIIP WNFPLLMWAW KIAPALVTGN TVVLKTAEST PLSALYVSKY IPQAGIPPGV 
241 INIVSGFGKI VGEAITNHPK IKKVAFTGST ATGRHIYQSA AAGLKKVTLE LGGKSPNIVF 
301 ADAELKKAVQ NIILGIYYNS GEVCCAGSRV YVEESIYDKF IEEFKAASES IKVGDPFDES 
361 TFQGAQTSQM QLNKILKYVD IGKNEGATLI TGGERLGSKG YFIKPTVFGD VKEDMRIVKE 
421 EIFGPVVTVT KFKSADEVIN MANDSEYGLA AGIHTSNINT ALKVADRVNA GTVWINTYND 
481 FHHAVPFGGF NASGLGREMS VDALQNYLQV KAVRAKLDE*

* Blue amino acids indicate modification sites. More information below.

Post-translational Modifications - S288C

Modification sites for the protein in the selected strain, based on the presence of a residue in the specific strain, as inferred from experimental evidence.

51 entries for 36 sites

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SiteModificationModifierReference
S14phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
K57succinylated residueFrankovsky J, et al. (2021) PMID: 34480900
S96phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S96phosphorylated residueHolt LJ, et al. (2009) PMID: 19779198
S96phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
S99phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
K123succinylated residueFrankovsky J, et al. (2021) PMID: 34480900
K153succinylated residueFrankovsky J, et al. (2021) PMID: 34480900
K161succinylated residueFrankovsky J, et al. (2021) PMID: 34480900
S175phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
Showing 1 to 10 of 51 entries

Sequence-Based Physico-chemical Properties - S288C

Calculated protein properties, including amino acid composition, length, coding region calculations, and atomic composition.

Amino Acid Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Amino AcidFrequencyPercentage
A438.29
C50.96
D265.01
E336.36
F234.43
G458.67
H81.54
I438.29
K387.32
L366.94
M81.54
N275.20
P214.05
Q163.08
R183.47
S377.13
T305.78
V397.51
W50.96
Y183.47

Physical Details

Length (a.a): 519
Molecular Weight (Da): 56721.1
Isoelectric Point (pl): 6.72
Formula: C2544H4006N675O766S13
Aliphatic Index: 86.62
Instability Index: 31.19

Coding Region Translation Calculations

Codon Bias: 0.4
Codon Adaptation Index: 0.28
Frequence of Optimal Codons: 0.67
Hydropathicity of Protein: -0.15
Aromaticity Score: 0.09

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 54570.0
NO Cys residues appear as half cystines: 54320.0

Atomic Composition

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Atom Frequency Percentage

Data not found or not available for  S288C

External Identifiers

List of external identifiers for the protein from various database sources.

16 entries for 9 sources

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External IDSource
4053DIP
1.2.1.4ExPASy
Z75282GenBank/EMBL/DDBJ
1420808GenBank/EMBL/DDBJ
2506349GenBank/EMBL/DDBJ
6324950GenBank/EMBL/DDBJ
CAA99705.1GenBank/EMBL/DDBJ
661LoQAtE
NM_001183794.1NCBI
DAA11133.1NCBI
Showing 1 to 10 of 16 entries

Resources

Homologs

AGD | AnalogYeast | BLASTP at NCBI | FungiDB | PhylomeDB | PomBase | YGOB | YOGY

Protein Databases

AlphaFold Protein Structure | GPMDB | ModelArchive | Pfam domains | SUPERFAMILY | TopologYeast | UniProtKB

Localization

CYCLoPs | dHITS | LoQAtE | YeastGFP | YeastRC Public Images | YeastRGB | YPL+

Post-translational Modifications

CoSMoS.c. | PhosphoGRID | PhosphoPep