Protein Help

CHS3 / YBR023C 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
CAL1 7 , CSD2 8 , DIT101 5 , KTI2 9
Protein Product
chitin synthase CHS3
Feature Type
ORF , Verified
EC Number
2.4.1.16

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-life3.7 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
2937SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
2007SD0.2 M hydroxyurea160 min0.68confocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
2132SD200 ng/ml sirolimus700 min0.73confocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
2988YEPDuntreatedflow cytometry evidenceS288CDavidson GS, et al. (2011)Ho B, et al. (2018)
3730YEPDcell quiescence7 d1.25flow cytometry evidenceS288CDavidson GS, et al. (2011)Ho B, et al. (2018)
Showing 1 to 5 of 14 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.


chs3-L24A | chs3-Δ

View all CHS3 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 MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN NPDNPHFYYA
61 QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF SGRETDSYLL QDMNTTDKKA
121 SVKISDEGVA EDEFDKDGDV DNFEESSTQP INKSIKPLRK ETNDTLSFWQ MYCYFITFWA
181 PAPILAFCGM PKKERQMAWR EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV
241 STEFVVINGK AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP
301 KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR DAFYGLKSKA
361 DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP VVFDDLKTSN LQGYDLSLVL
421 SNGHERKIAR CLSEIIKVGE VDSKTVGCIA SDVVLYVSLV FILSVVIIKF IIACYFRWTV
481 ARKQGAYIVD NKTMDKHTND IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD
541 LLKKHSSKMF QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS
601 TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP LIHTICFVTC
661 YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN DKTTPEIALG MMDDFVTPPD
721 EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD DSTIPPENQQ RVPIITIVKC GTPAEQGAAK
781 PGNRGKRDSQ IILMSFLEKI TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV
841 FPDALTHMVA EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV
901 TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL LGEDRFLSSL
961 MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST VHNLFELVLI RDLCGTFCFS
1021 MQFVIGIELI GTMVLPLAIC FTIYVIIFAI VSKPTPVITL VLLAIILGLP GLIVVITATR
1081 WSYLWWMCVY ICALPIWNFV LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI
1141 KMRTWREFER EDILNRKEES DSFVA*

* 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.

73 entries for 32 sites

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SiteModificationModifierReference
S22phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S22phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S26phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S29phosphorylated residueMacGilvray ME, et al. (2020) PMID: 32597660
S29phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S29phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
S29phosphorylated residueGohlke S, et al. (2018) PMID: 29763674
S29phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S32phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S32phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
Showing 1 to 10 of 73 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
A595.06
C221.89
D847.21
E544.64
F564.81
G625.32
H231.97
I736.27
K837.12
L1028.76
M302.58
N595.06
P554.72
Q353.00
R463.95
S1059.01
T736.27
V806.87
W231.97
Y413.52

Physical Details

Length (a.a): 1165
Molecular Weight (Da): 131593.5
Isoelectric Point (pl): 6.69
Formula: C5904H9164N1549O1755S52
Aliphatic Index: 79.35
Instability Index: 38.76

Coding Region Translation Calculations

Codon Bias: 0.11
Codon Adaptation Index: 0.17
Frequence of Optimal Codons: 0.49
Hydropathicity of Protein: -0.27
Aromaticity Score: 0.1

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 188965.0
NO Cys residues appear as half cystines: 187590.0

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.

27 entries for 10 sources


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External IDSource
AN1555AspGD
orf19.4937CGD
2482DIP
2.4.1.16ExPASy
6319497GenBank/EMBL/DDBJ
AAA34844.1GenBank/EMBL/DDBJ
CAA53680.1GenBank/EMBL/DDBJ
CAA40559.1GenBank/EMBL/DDBJ
CAA84965.1GenBank/EMBL/DDBJ
X76078GenBank/EMBL/DDBJ
Showing 1 to 10 of 27 entries

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