Protein Help

GAL11 / YOL051W 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
MED15 7 , RAR3 8 , SDS4 9 , SPT13 10 , ABE1
Feature Type
ORF , Verified
Summary
Gal11p is 1081 amino acids long, short-lived, and low in abundance; contains KIX domain; N-glycosylated on 3 asparagines, sumoylated on 3 lysines, phosphorylated on 41 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-life4.5 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
3095SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1931SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2756SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2860SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2179SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 23 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.


gal11-Q383stop | gal11-R84K | gal11-V27N | gal11-V76R | gal11-V76R,R84K | gal11-Δ

View all GAL11 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 MSAAPVQDKD TLSNAERAKN VNGLLQVLMD INTLNGGSSD TADKIRIHAK NFEAALFAKS
61 SSKKEYMDSM NEKVAVMRNT YNTRKNAVTA AAANNNIKPV EQHHINNLKN SGNSANNMNV
121 NMNLNPQMFL NQQAQARQQV AQQLRNQQQQ QQQQQQQQRR QLTPQQQQLV NQMKVAPIPK
181 QLLQRIPNIP PNINTWQQVT ALAQQKLLTP QDMEAAKEVY KIHQQLLFKA RLQQQQAQAQ
241 AQANNNNNGL PQNGNINNNI NIPQQQQMQP PNSSANNNPL QQQSSQNTVP NVLNQINQIF
301 SPEEQRSLLQ EAIETCKNFE KTQLGSTMTE PVKQSFIRKY INQKALRKIQ ALRDVKNNNN
361 ANNNGSNLQR AQNVPMNIIQ QQQQQNTNNN DTIATSATPN AAAFSQQQNA SSKLYQMQQQ
421 QQAQAQAQAQ AQAQAQAQAQ AQAAQAAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ
481 AHAQHQPSQQ PQQAQQQPNP LHGLTPTAKD VEVIKQLSLD ASKTNLRLTD VTNSLSNEEK
541 EKIKMKLKQG QKLFVQVSNF APQVYIITKN ENFLKEVFQL RIFVKEILEK CAEGIFVVKL
601 DTVDRLIIKY QKYWESMRIQ ILRRQAILRQ QQQMANNNGN PGTTSTGNNN NIATQQNMQQ
661 SLQQMQHLQQ LKMQQQQQQQ QQQQQQQQQQ QQQQQQHIYP SSTPGVANYS AMANAPGNNI
721 PYMNHKNTSS MDFLNSMENT PKVPVSAAAT PSLNKTINGK VNGRTKSNTI PVTSIPSTNK
781 KLSISNAASQ QPTPRSASNT AKSTPNTNPS PLKTQTKNGT PNPNNMKTVQ SPMGAQPSYN
841 SAIIENAFRK EELLLKDLEI RKLEISSRFK HRQEIFKDSP MDLFMSTLGD CLGIKDEEML
901 TSCTIPKAVV DHINGSGKRK PTKAAQRARD QDSIDISIKD NKLVMKSKFN KSNRSYSIAL
961 SNVAAIFKGI GGNFKDLSTL VHSSSPSTSS NMDVGNPRKR KASVLEISPQ DSIASVLSPD
1021 SNIMSDSKKI KVDSPDDPFM TKSGATTSEK QEVTNEAPFL TSGTSSEQFN VWDWNNWTSA
1081 T*

* 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.

149 entries for 47 sites

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SiteModificationModifierReference
S2phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
N15N-glycosylated residueJung SJ, et al. (2021) PMID: 34153287
N102N-glycosylated residueJung SJ, et al. (2021) PMID: 34153287
T163phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
T163phosphorylated residueMacGilvray ME, et al. (2020) PMID: 32597660
T163phosphorylated residueCDC28Holt LJ, et al. (2009) PMID: 19779198
T163phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
N173N-glycosylated residueJung SJ, et al. (2021) PMID: 34153287
S335phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
T505phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
Showing 1 to 10 of 149 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
A1079.90
C40.37
D343.15
E373.42
F252.31
G302.78
H131.20
I595.46
K777.12
L696.38
M333.05
N11810.92
P555.09
Q17316.00
R343.15
S888.14
T615.64
V464.26
W50.46
Y131.20

Physical Details

Length (a.a): 1081
Molecular Weight (Da): 120350.9
Isoelectric Point (pl): 10.49
Formula: C5138H8394N1582O1677S37
Aliphatic Index: 64.24
Instability Index: 51.21

Coding Region Translation Calculations

Codon Bias: 0.15
Codon Adaptation Index: 0.16
Frequence of Optimal Codons: 0.53
Hydropathicity of Protein: -0.87
Aromaticity Score: 0.04

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 47120.0
NO Cys residues appear as half cystines: 46870.0

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.

28 entries for 10 sources


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External IDSource
orf19.5105CGD
2334DIP
6324522GenBank/EMBL/DDBJ
AAA34622.1GenBank/EMBL/DDBJ
CAA99056.1GenBank/EMBL/DDBJ
CAA62537.1GenBank/EMBL/DDBJ
X91067GenBank/EMBL/DDBJ
Z74793GenBank/EMBL/DDBJ
2507028GenBank/EMBL/DDBJ
377656187GenBank/EMBL/DDBJ
Showing 1 to 10 of 28 entries

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