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SLH1 / YGR271W 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
RQT2 4
Protein Product
RNA helicase
Feature Type
ORF , Verified
EC Number
3.6.4.13

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.

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-life9.4 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
2167SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2214SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1732SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1522SD minus nitrogencellular response to nitrogen starvation15 hr0.7confocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2040SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 19 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.

slh1-Δ

View all SLH1 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 MSTEYSADSS KSFMIAMQSM IDTSQTFNLD RSKISLPDFD DELKKVQKDE QNQRTELTVL 
  61 SQDRNDWDDI FEEFKDISFA QLQSIIDSYK TKNAVAVYKK IGKLINEAET TLSSNVLLET 
 121 VLQMVYKHQK QELEKELLDF LGTGNIDLVS LLLQHRRMIV ATPIETTILL IKNAVNSTPE 
 181 FLTQQDIRNQ VLKSAEDAKN RKLNPATKII KYPHVFRKYE AGSTTAMAFA GQKFTLPVGT 
 241 TRMSYNTHEE IIIPAADQAS NKNYLYTKLL KISDLDHFCK TVFPYETLNQ IQSLVYPVAY 
 301 KTNENMLICA PTGAGKTDIA LLTIINTIKQ FSVVNGENEI DIQYDDFKVI YVAPLKALAA 
 361 EIVDKFSKKL APFNIQVREL TGDMQLTKAE ILATQVIVTT PEKWDVVTRK ANGDNDLVSK 
 421 VKLLIIDEVH LLHEDRGSVI ETLVARTLRQ VESSQSMIRI IGLSATLPNF MDVADFLGVN 
 481 RQIGMFYFDQ SFRPKPLEQQ LLGCRGKAGS RQSKENIDKV AYDKLSEMIQ RGYQVMVFVH 
 541 SRKETVKSAR NFIKLAESNH EVDLFAPDPI EKDKYSRSLV KNRDKDMKEI FQFGFGIHHA 
 601 GMARSDRNLT EKMFKDGAIK VLCCTATLAW GVNLPADCVI IKGTQVYDSK KGGFIDLGIS 
 661 DVIQIFGRGG RPGFGSANGT GILCTSNDRL DHYVSLITQQ HPIESRFGSK LVDNLNAEIS 
 721 LGSVTNVDEA IEWLGYTYMF VRMRKNPFTY GIDWEEIAND PQLYERRRKM IVVAARRLHA 
 781 LQMIVFDEVS MHFIAKDLGR VSSDFYLLNE SVEIFNQMCD PRATEADVLS MISMSSEFDG 
 841 IKFREEESKE LKRLSDESVE CQIGSQLDTP QGKANVLLQA YISQTRIFDS ALSSDSNYVA 
 901 QNSVRICRAL FLIGVNRRWG KFSNVMLNIC KSIEKRLWAF DHPLCQFDLP ENIIRRIRDT 
 961 KPSMEHLLEL EADELGELVH NKKAGSRLYK ILSRFPKINI EAEIFPITTN VMRIHIALGP 
1021 DFVWDSRIHG DAQFFWVFVE ESDKSQILHF EKFILNRRQL NNQHEMDFMI PLSDPLPPQV 
1081 VVKVVSDTWI GCESTHAISF QHLIRPFNET LQTKLLKLRP LPTSALQNPL IESIYPFKYF 
1141 NPMQTMTFYT LYNTNENAFV GSPTGSGKTI VAELAIWHAF KTFPGKKIVY IAPMKALVRE 
1201 RVDDWRKKIT PVTGDKVVEL TGDSLPDPKD VHDATIVITT PEKFDGISRN WQTRKFVQDV 
1261 SLIIMDEIHL LASDRGPILE MIVSRMNYIS SQTKQPVRLL GMSTAVSNAY DMAGWLGVKD 
1321 HGLYNFPSSV RPVPLKMYID GFPDNLAFCP LMKTMNKPVF MAIKQHSPDK PALIFVASRR 
1381 QTRLTALDLI HLCGMEDNPR RFLNIDDEEE LQYYLSQVTD DTLKLSLQFG IGLHHAGLVQ 
1441 KDRSISHQLF QKNKIQILIA TSTLAWGVNL PAHLVIIKGT QFFDAKIEGY RDMDLTDILQ 
1501 MMGRAGRPAY DTTGTAIVYT KESKKMFYKH FLNVGFPVES SLHKVLDDHL GAEITSGSIT 
1561 NKQEALDFLS WTFLFRRAHH NPTYYGIEDD TSTAGVSEHL SSLIDSTLEN LRESQCVLLH 
1621 GDDIVATPFL SISSYYYISH LTIRQLLKQI HDHATFQEVL RWLSLAVEYN ELPVRGGEII 
1681 MNEEMSQQSR YSVESTFTDE FELPMWDPHV KTFLLLQAHL SRVDLPIADY IQDTVSVLDQ 
1741 SLRILQAYID VASELGYFHT VLTMIKMMQC IKQGYWYEDD PVSVLPGLQL RRIKDYTFSE 
1801 QGFIEMTPQQ KKKKLLTLEE IGRFGYKKLL NVFDQLTFGM TESEDTKKRF VSVCQRLPVL 
1861 EGMKFEEQEN NEVLTFYSKH LSSKHNNGFE VYCDKFPKIQ KELWFLIGHK GDELLMIKRC 
1921 QPKQMNKEVI IHCDLFIPEE IRGEELQFSL INDALGLRYD MVHKLIS*

* 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.

6 entries for 6 sites

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SiteModificationModifierReference
T178phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
N189N-glycosylated residueZielinska DF, et al. (2012) PMID: 22633491
K193ubiquitinylated lysineBack S, et al. (2019) PMID: 30489083
S419phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
T1210phosphorylated residueZhou X, et al. (2021) PMID: 33481703
T1213phosphorylated residueZhou X, et al. (2021) PMID: 33481703
Showing 1 to 6 of 6 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
A1035.24
C211.07
D1286.51
E1236.25
F1005.08
G944.78
H522.64
I1517.68
K1346.81
L20010.17
M603.05
N834.22
P753.81
Q964.88
R934.73
S1366.91
T1135.74
V1256.35
W201.02
Y603.05

Physical Details

Length (a.a): 1967
Molecular Weight (Da): 224827.7
Isoelectric Point (pl): 6.58
Formula: C10099H15897N2683O2958S81
Aliphatic Index: 88.14
Instability Index: 42.51

Coding Region Translation Calculations

Codon Bias: 0.05
Codon Adaptation Index: 0.15
Frequence of Optimal Codons: 0.47
Hydropathicity of Protein: -0.23
Aromaticity Score: 0.09

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 200650.0
NO Cys residues appear as half cystines: 199400.0

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.

21 entries for 10 sources

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External IDSource
orf19.3980CGD
5563DIP
3.6.4.13ExPASy
AAC49699.1GenBank/EMBL/DDBJ
CAA97301.1GenBank/EMBL/DDBJ
U35242GenBank/EMBL/DDBJ
Z73056GenBank/EMBL/DDBJ
347595711GenBank/EMBL/DDBJ
398366359GenBank/EMBL/DDBJ
1723776GenBank/EMBL/DDBJ
Showing 1 to 10 of 21 entries

Resources

Homologs

AGD | AnalogYeast | BLASTP at NCBI | CGD | FungiDB | PhylomeDB | PomBase | YGOB | YOGY

Protein Databases

AlphaFold Protein Structure | GPMDB | ModelArchive | Pfam domains | SUPERFAMILY | TopologYeast | UniProtKB

Localization

CYCLoPs | dHITS | LoQAtE | YeastGFP | YeastRC Public Images | YeastRGB | YPL+

Post-translational Modifications

CoSMoS.c. | PhosphoGRID | PhosphoPep