GSC2 / YGR032W 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.
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.
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.
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
Protein Abundance
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Abundance (molecules/cell) | Media | Treatment | Treatment time | Fold Change | Visualization | Strain background | Original Reference | Reference |
|---|---|---|---|---|---|---|---|---|
| 1891 | SD | 2 mM 1,4-dithiothreitol | 2 hr | confocal microscopy evidence | S288C | Breker M, et al. (2013) | Ho B, et al. (2018) | |
| 1596 | SD minus nitrogen | cellular response to nitrogen starvation | 15 hr | confocal microscopy evidence | S288C | Breker M, et al. (2013) | Ho B, et al. (2018) | |
| 3904 | SD | untreated | quantitative mass spectrometry evidence | S288C | de Godoy LM, et al. (2008) | Ho B, et al. (2018) | ||
| 776 | YEPD | untreated | quantitative mass spectrometry evidence | S288C | Kulak NA, et al. (2014) | Ho B, et al. (2018) | ||
| 552 | YEPD | untreated | quantitative mass spectrometry evidence | W303 | Nagaraj N, et al. (2012) | Ho B, et al. (2018) |
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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| Evidence ID | Analyze ID | Gene | Gene Systematic Name | 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.
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.
View all GSC2 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.
This locus is not translated into a protein.
1 MSYNDPNLNG QYYSNGDGTG DGNYPTYQVT QDQSAYDEYG QPIYTQNQLD DGYYDPNEQY
61 VDGTQFPQGQ DPSQDQGPYN NDASYYNQPP NMMNPSSQDG ENFSDFSSYG PPSGTYPNDQ
121 YTPSQMSYPD QDGSSGASTP YGNGVVNGNG QYYDPNAIEM ALPNDPYPAW TADPQSPLPI
181 EQIEDIFIDL TNKFGFQRDS MRNMFDHFMT LLDSRSSRMS PEQALLSLHA DYIGGDTANY
241 KKWYFAAQLD MDDEIGFRNM KLGKLSRKAR KAKKKNKKAM QEASPEDTEE TLNQIEGDNS
301 LEAADFRWKS KMNQLSPFEM VRQIALFLLC WGEANQVRFT PECLCFIYKC ASDYLDSAQC
361 QQRPDPLPEG DFLNRVITPL YRFIRSQVYE IVDGRYVKSE KDHNKVIGYD DVNQLFWYPE
421 GIAKIVMEDG TRLIDLPAEE RYLKLGEIPW DDVFFKTYKE TRSWLHLVTN FNRIWIMHIS
481 VYWMYCAYNA PTFYTHNYQQ LVDNQPLAAY KWATAALGGT VASLIQVAAT LCEWSFVPRK
541 WAGAQHLSRR FWFLCVIMGI NLGPVIFVFA YDKDTVYSTA AHVVGAVMFF VAVATLVFFS
601 VMPLGGLFTS YMKKSTRSYV ASQTFTASFA PLHGLDRWMS YLVWVTVFAA KYAESYFFLI
661 LSLRDPIRIL STTSMRCTGE YWWGNKICKV QPKIVLGLMI ATDFILFFLD TYLWYIVVNT
721 VFSVGKSFYL GISILTPWRN IFTRLPKRIY SKILATTDME IKYKPKVLIS QIWNAIIISM
781 YREHLLAIDH VQKLLYHQVP SEIEGKRTLR APTFFVSQDD NNFETEFFPR DSEAERRISF
841 FAQSLSTPIP EPLPVDNMPT FTVLTPHYAE RILLSLREII REDDQFSRVT LLEYLKQLHP
901 VEWDCFVKDT KILAEETAAY ENNEDEPEKE DALKSQIDDL PFYCIGFKSA APEYTLRTRI
961 WASLRSQTLY RTISGFMNYS RAIKLLYRVE NPEIVQMFGG NADGLERELE KMARRKFKFL
1021 VSMQRLAKFK PHELENAEFL LRAYPDLQIA YLDEEPPLNE GEEPRIYSAL IDGHCEILEN
1081 GRRRPKFRVQ LSGNPILGDG KSDNQNHALI FYRGEYIQLI DANQDNYLEE CLKIRSVLAE
1141 FEELGIEQIH PYTPGLKYED QSTNHPVAIV GAREYIFSEN SGVLGDVAAG KEQTFGTLFA
1201 RTLAQIGGKL HYGHPDFINA TFMTTRGGVS KAQKGLHLNE DIYAGMNAVL RGGRIKHCEY
1261 YQCGKGRDLG FGTILNFTTK IGAGMGEQML SREYYYLGTQ LPIDRFLTFY YAHPGFHLNN
1321 LFIQLSLQMF MLTLVNLHAL AHESILCVYD RDKPITDVLY PIGCYNFHPA IDWVRRYTLS
1381 IFIVFWIAFV PIVVQELIER GLWKATQRFF RHILSLSPMF EVFAGQIYSS ALLSDIAVGG
1441 ARYISTGRGF ATSRIPFSIL YSRFAGSAIY MGSRSMLMLL FGTVAHWQAP LLWFWASLSA
1501 LIFAPFIFNP HQFAWEDFFL DYRDYIRWLS RGNNKYHRNS WIGYVRMSRS RVTGFKRKLV
1561 GDESEKSAGD ASRAHRTNLI MAEIIPCAIY AAGCFIAFTF INAQTGVKTT DEDRVNSTLR
1621 IIICTLAPIV IDIGVLFFCM GLSCCSGPLL GMCCKKTGSV MAGIAHGIAV VVHIVFFIVM
1681 WVLEGFSFVR MLIGVVTCIQ CQRLIFHCMT VLLLTREFKN DHANTAFWTG KWYSTGLGYM
1741 AWTQPTRELT AKVIELSEFA ADFVLGHVIL IFQLPVICIP KIDKFHSIML FWLKPSRQIR
1801 PPIYSLKQAR LRKRMVRRYC SLYFLVLIIF AGCIVGPAVA SAHVPKDLGS GLTGTFHNLV
1861 QPRNVSNNDT GSQMSTYKSH YYTHTPSLKT WSTIK*
* 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.
16 entries for 14 sitesIncrease the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Site | Modification | Modifier | Reference |
|---|---|---|---|
| K278 | ubiquitinylated lysine | Swaney DL, et al. (2013) PMID: 23749301 | |
| K278 | ubiquitinylated lysine | Back S, et al. (2019) PMID: 30489083 | |
| S284 | phosphorylated residue | Lanz MC, et al. (2021) PMID: 33491328 | |
| K806 | ubiquitinylated lysine | Peng J, et al. (2003) PMID: 12872131 | |
| K806 | ubiquitinylated lysine | Swaney DL, et al. (2013) PMID: 23749301 | |
| K929 | ubiquitinylated lysine | Swaney DL, et al. (2013) PMID: 23749301 | |
| K948 | ubiquitinylated lysine | Swaney DL, et al. (2013) PMID: 23749301 | |
| S974 | phosphorylated residue | Albuquerque CP, et al. (2008) PMID: 18407956 | |
| K984 | ubiquitinylated lysine | Swaney DL, et al. (2013) PMID: 23749301 | |
| K1028 | ubiquitinylated lysine | Swaney DL, et al. (2013) PMID: 23749301 |
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 Acid | Frequency | Percentage |
|---|---|---|
| A | 128 | 6.75 |
| C | 32 | 1.69 |
| D | 98 | 5.17 |
| E | 95 | 5.01 |
| F | 116 | 6.12 |
| G | 120 | 6.33 |
| H | 43 | 2.27 |
| I | 132 | 6.97 |
| K | 83 | 4.38 |
| L | 174 | 9.18 |
| M | 53 | 2.80 |
| N | 80 | 4.22 |
| P | 94 | 4.96 |
| Q | 81 | 4.27 |
| R | 101 | 5.33 |
| S | 122 | 6.44 |
| T | 103 | 5.44 |
| V | 101 | 5.33 |
| W | 37 | 1.95 |
| Y | 102 | 5.38 |
Physical Details
| Length (a.a): | 1895 |
| Molecular Weight (Da): | 216982.7 |
| Isoelectric Point (pl): | 7.02 |
| Formula: | C9897H15018N2565O2770S85 |
| Aliphatic Index: | 79.81 |
| Instability Index: | 38.48 |
Coding Region Translation Calculations
| Codon Bias: | 0.2 |
| Codon Adaptation Index: | 0.21 |
| Frequence of Optimal Codons: | 0.55 |
| Hydropathicity of Protein: | -0.14 |
| Aromaticity Score: | 0.13 |
Extinction Coefficients at 280nm
| ALL Cys residues appear as half cystines: | 357480.0 |
| NO Cys residues appear as half cystines: | 355480.0 |
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.
29 entries for 10 sourcesIncrease the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
Resources
Homologs
AGD | AnalogYeast | BLASTP at NCBI | CGD | FungiDB | PhylomeDB | PomBase | PomBase | PomBase | PomBase | YGOB | YOGY
Protein Databases
AlphaFold Protein Structure | GPMDB | ModelArchive | Pfam domains | SUPERFAMILY | TopologYeast | UniProtKB
Localization
CYCLoPs | dHITS | LoQAtE | YeastGFP | YeastRGB | YPL+