Protein Help

SSB1 / YDL229W 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
YG101 20
Protein Product
Hsp70 family ATPase SSB1
Feature Type
ORF , Verified
Paralog
SSB2 8
EC Number
3.6.4.10
Summary
Ssb1p is 613 amino acids long, of moderate half-life, high in abundance; contains 9 70kDa heat shock protein signature domains; carbamoylated on C54, N-glycosylated on N504, ubiquitinylated on 20 lysines, succinylated on 18 lysines, sumoylated on 5 lysines, phosphorylated on 31 residues

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-life9.6 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
228337SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
159372SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
208438SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
85001SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
21227SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 30 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.


ssb1-Δ

View all SSB1 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 MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE RLIGDAAKNQ
61 AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD GNPVIEVQYL EETKTFSPQE
121 ISAMVLTKMK EIAEAKIGKK VEKAVITVPA YFNDAQRQAT KDAGAISGLN VLRIINEPTA
181 AAIAYGLGAG KSEKERHVLI FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL
241 LEHFKAEFKK KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
301 TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ KLLSDFFDGK
361 QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV APLSLGVGMQ GDMFGIVVPR
421 NTTVPTIKRR TFTTCADNQT TVQFPVYQGE RVNCKENTLL GEFDLKNIPM MPAGEPVLEA
481 IFEVDANGIL KVTAVEKSTG KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH
541 EARQRLESYV ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
601 GLKRVVTKAM SSR*

* 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.

125 entries for 63 sites

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SiteModificationModifierReference
K21ubiquitinylated lysineRSP5Fang NN, et al. (2014) PMID: 25344756
S26phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
S27phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
T40phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
T40phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
T40phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S42phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
S42phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S42phosphorylated residueZhou X, et al. (2021) PMID: 33481703
T47phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
Showing 1 to 10 of 125 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
A6210.11
C30.49
D386.20
E508.16
F264.24
G426.85
H50.82
I355.71
K477.67
L518.32
M101.63
N223.59
P203.26
Q243.92
R294.73
S437.01
T457.34
V518.32
W10.16
Y91.47

Physical Details

Length (a.a): 613
Molecular Weight (Da): 66590.2
Isoelectric Point (pl): 5.08
Formula: C2931H4742N804O933S13
Aliphatic Index: 85.63
Instability Index: 36.03

Coding Region Translation Calculations

Codon Bias: 0.87
Codon Adaptation Index: 0.82
Frequence of Optimal Codons: 0.93
Hydropathicity of Protein: -0.24
Aromaticity Score: 0.06

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 19035.0
NO Cys residues appear as half cystines: 18910.0

Atomic 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.

Atom Frequency Percentage

Data not found or not available for  S288C

External Identifiers

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

31 entries for 10 sources


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External IDSource
2254DIP
3.6.4.10ExPASy
1431385GenBank/EMBL/DDBJ
AAA35099.1GenBank/EMBL/DDBJ
CAA31995.1GenBank/EMBL/DDBJ
AAA34692.1GenBank/EMBL/DDBJ
CAA98807.1GenBank/EMBL/DDBJ
6319972GenBank/EMBL/DDBJ
Z74277GenBank/EMBL/DDBJ
X13713GenBank/EMBL/DDBJ
Showing 1 to 10 of 31 entries

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