Protein Help

STH1 / YIL126W 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
NPS1 6
Protein Product
RSC chromatin remodeling complex ATPase subunit STH1
Feature Type
ORF , Verified
EC Number
3.6.4.12
Summary
Sth1p is 1359 nucleotides long, shorter-lived, low-to-moderate in abundance; acetylated on K944, ubiquitinylated on 3 lysines, sumoylated on 5 lysines, phosphorylated on 23 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-life7.9 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
5035SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
3988SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
5408SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
3647SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
4802SDuntreatedconfocal 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.


sth1-(nps1-105) | sth1-2 | sth1-3 | sth1-AID | sth1-D394A | sth1-DAmP | sth1-F659A | ... Show all

View all STH1 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 MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY
61 RYRAIQNHPK ENKLEIKAIE DTFRNISRDQ DIYETKLDTL RKSIDKGFQY DEDLLNKHLV
121 ALQLLEKDTD VPDYFLDLPD TKNDNTTAIE VDYSEKKPIK ISADFNAKAK SLGLESKFSN
181 ATKTALGDPD TEIRISARIS NRINELERLP ANLGTYSLDD CLEFITKDDL SSRMDTFKIK
241 ALVELKSLKL LTKQKSIRQK LINNVASQAH HNIPYLRDSP FTAAAQRSVQ IRSKVIVPQT
301 VRLAEELERQ QLLEKRKKER NLHLQKINSI IDFIKERQSE QWSRQERCFQ FGRLGASLHN
361 QMEKDEQKRI ERTAKQRLAA LKSNDEEAYL KLLDQTKDTR ITQLLRQTNS FLDSLSEAVR
421 AQQNEAKILH GEEVQPITDE EREKTDYYEV AHRIKEKIDK QPSILVGGTL KEYQLRGLEW
481 MVSLYNNHLN GILADEMGLG KTIQSISLIT YLYEVKKDIG PFLVIVPLST ITNWTLEFEK
541 WAPSLNTIIY KGTPNQRHSL QHQIRVGNFD VLLTTYEYII KDKSLLSKHD WAHMIIDEGH
601 RMKNAQSKLS FTISHYYRTR NRLILTGTPL QNNLPELWAL LNFVLPKIFN SAKTFEDWFN
661 TPFANTGTQE KLELTEEETL LIIRRLHKVL RPFLLRRLKK EVEKDLPDKV EKVIKCKLSG
721 LQQQLYQQML KHNALFVGAG TEGATKGGIK GLNNKIMQLR KICNHPFVFD EVEGVVNPSR
781 GNSDLLFRVA GKFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS
841 TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDWN PHQDLQAQDR
901 AHRIGQKNEV RILRLITTDS VEEVILERAM QKLDIDGKVI QAGKFDNKST AEEQEAFLRR
961 LIESETNRDD DDKAELDDDE LNDTLARSAD EKILFDKIDK ERMNQERADA KAQGLRVPPP
1021 RLIQLDELPK VFREDIEEHF KKEDSEPLGR IRQKKRVYYD DGLTEEQFLE AVEDDNMSLE
1081 DAIKKRREAR ERRRLRQNGT KENEIETLEN TPEASETSLI ENNSFTAAVD EETNADKETT
1141 ASRSKRRSSR KKRTISIVTA EDKENTQEES TSQENGGAKV EEEVKSSSVE IINGSESKKK
1201 KPKLTVKIKL NKTTVLENND GKRAEEKPES KSPAKKTAAK KTKTKSKSLG IFPTVEKLVE
1261 EMREQLDEVD SHPRTSIFEK LPSKRDYPDY FKVIEKPMAI DIILKNCKNG TYKTLEEVRQ
1321 ALQTMFENAR FYNEEGSWVY VDADKLNEFT DEWFKEHSS*

* 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.

58 entries for 32 sites

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SiteModificationModifierReference
S38phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S38phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
S38phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S51phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
S51phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S51phosphorylated residueMacGilvray ME, et al. (2020) PMID: 32597660
S51phosphorylated residueSoulard A, et al. (2010) PMID: 20702584
S51phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S52phosphorylated residueSoulard A, et al. (2010) PMID: 20702584
S52phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
Showing 1 to 10 of 58 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
A815.96
C60.44
D916.70
E1359.93
F493.61
G503.68
H241.77
I856.25
K1299.49
L14510.67
M241.77
N715.22
P443.24
Q674.93
R876.40
S836.11
T896.55
V594.34
W100.74
Y302.21

Physical Details

Length (a.a): 1359
Molecular Weight (Da): 156734.6
Isoelectric Point (pl): 6.68
Formula: C6900H11133N1945O2152S30
Aliphatic Index: 79.26
Instability Index: 40.61

Coding Region Translation Calculations

Codon Bias: 0.13
Codon Adaptation Index: 0.19
Frequence of Optimal Codons: 0.51
Hydropathicity of Protein: -0.73
Aromaticity Score: 0.07

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 100075.0
NO Cys residues appear as half cystines: 99700.0

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.

27 entries for 10 sources


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External IDSource
orf19.239CGD
5889DIP
3.6.4.12ExPASy
M83755GenBank/EMBL/DDBJ
D10595GenBank/EMBL/DDBJ
6322065GenBank/EMBL/DDBJ
DQ115392GenBank/EMBL/DDBJ
Z46833GenBank/EMBL/DDBJ
BAA01446.1GenBank/EMBL/DDBJ
AAZ22501.1GenBank/EMBL/DDBJ
Showing 1 to 10 of 27 entries

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