Protein Help

MTC5 / YDR128W 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
SEA3 2
Feature Type
ORF , Verified
Summary
Relative distribution to the vacuolar membrane decreases upon DNA replication stress

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-life6.2 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
1705SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1913SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1690SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1117SDuntreatedquantitative mass spectrometry evidenceS288Cde Godoy LM, et al. (2008)Ho B, et al. (2018)
3390SD0.03% methyl methanesulfonate7 hrwide-field microscopy evidenceS288CDénervaud N, et al. (2013)Ho B, et al. (2018)
Showing 1 to 5 of 11 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.


mtc5-Δ

View all MTC5 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 MCSSINEGPY NSPTFGKSLS LKVDGGFNAV SINPSGRDIV LASRQGLYII DLDDPFTPPR
61 WLHHITPWQV ADVQWSPHPA KPYWIVSTSN QKAIIWNLAK SSSNAIEFVL HGHSRAITDI
121 NFNPQHPDVL ATCSVDTYVH AWDMRSPHRP FYSTSSWRSA ASQVKWNYKD PNVLASSHGN
181 DIFVWDLRKG STPLCSLKGH VSSVNSIDFN RFKYSEIMSS SNDGTVKFWD YSKSTTESKR
241 TVTTNFPIWR GRYLPFGEGY CIMPMVGGNN AVYLINLCDD DDSEQNKKTK LQPIYAFKGH
301 SDRVIDFLWR SRHTCDGDYD DREFQLVTWS KDCDLKLWPI SDSIYGKVNF DRGKRLEEKL
361 PDYDYCSYNK EPENRENVQK NEFRRLRENF VTTSGLKKNK TNHITWLSGI RMNSATSQED
421 LFNETKIQNL GEEVSAIGHK FPKVVFEKIS VSTRELCLTL NGPWSEENPD DYIFLRISIN
481 FPLNYPNKGD PPKFTIEENS NLTMSKRQEI LSNLATIGQK YTDSNLYCLE PCIRFVLGEK
541 VSLEDIEEGQ EPLLNFDIAD HIDFEELSSL DSSYSDSQNP ENLSSQSDIE SYKEALVFPD
601 TSNQGLDFGR NLALDTTPVP NGCGSCWTAT GELFCFFANE KKPEKKQNAI IKLSQKEAGV
661 EKHPFKIEPQ VLYDKEVDSS VITAADELKA RPKRYVDTLG LGGGTNGDSR TYFDDETSSD
721 DSFDSVADDW DDILRNDIIV RTKIPILRGN FKAFSSVHSE SGKTVESTKK NKNLVISKNF
781 SSLLSDRKEL ALEYLFMDAT PEGFARNNAL VAEKFDLDEI SHCWQILSDM LIDQSDYDPY
841 TTIWNNHPMG IKWFIKEAIV YFERQQNLQM LAMLCCVILS ARRKKIPARY YGQELENMEG
901 TIVFNDNESQ NTSFWKGSDA FSTRSRSSTV TPNFYGNHLR GKNIHGGDNS SIRSDDHHAR
961 LRTHNTLNGS SKFTEPAQKQ GSRAISSSPF HSRMPDIKVE LLHDDIIEAY EQEDLLHLEV
1021 SDIPKFQTYI YQYSKLLFRW GLPLERVKIL KVSTDFRSSY SSQGIPPNNN KKSPYNGVLT
1081 HWIENNEFGE EKFLARNCNY CDLRVTRSSF ICGNCQHVLH SSCARIWWEI GDECPSGCGC
1141 NCPEMFDA*

* 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.

60 entries for 30 sites

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SiteModificationModifierReference
K336methylated residueWang K, et al. (2015) PMID: 25109467
S414phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
S414phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S414phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
T416phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
T416phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S417phosphorylated residueHolt LJ, et al. (2009) PMID: 19779198
S417phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
S417phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
S417phosphorylated residueZhou X, et al. (2021) PMID: 33481703
Showing 1 to 10 of 60 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
A474.09
C262.26
D847.32
E726.27
F564.88
G615.31
H302.61
I726.27
K736.36
L897.75
M151.31
N796.88
P564.88
Q353.05
R554.79
S12010.45
T585.05
V544.70
W262.26
Y403.48

Physical Details

Length (a.a): 1148
Molecular Weight (Da): 130919.7
Isoelectric Point (pl): 5.76
Formula: C5809H8860N1586O1793S41
Aliphatic Index: 68.68
Instability Index: 44.13

Coding Region Translation Calculations

Codon Bias: -0.04
Codon Adaptation Index: 0.12
Frequence of Optimal Codons: 0.41
Hydropathicity of Protein: -0.59
Aromaticity Score: 0.11

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 204225.0
NO Cys residues appear as half cystines: 202600.0

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.

16 entries for 9 sources


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External IDSource
orf19.3241CGD
1825DIP
CAA88209.1GenBank/EMBL/DDBJ
Z48179GenBank/EMBL/DDBJ
398365749GenBank/EMBL/DDBJ
74676351GenBank/EMBL/DDBJ
665660GenBank/EMBL/DDBJ
2577LoQAtE
DAA11974.1NCBI
NM_001180436.3NCBI
Showing 1 to 10 of 16 entries

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