Protein Help

USO1 / YDL058W 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
INT1
Feature Type
ORF , Verified

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.


Downloading... 1.00 MB

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-life10.2 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
2664SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2124SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2517SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2587SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
2743SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 29 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.


uso1-1 | uso1-Δ

View all USO1 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 MDIIQGLIQQ PKIQSVDETI PTLCDRVENS TLISDRRSAV LGLKAFSRQY RESVIASGLK
61 PLLNTLKRDY MDEDSVKAIL ETILILFIRG DGHDDLTRGW ISQQSRLQNG KYPSPLVMKQ
121 EKEQVDQFSL WIADALTQSE DLIHLLVEFW EIDNFHIRLY TIQLLEAVMA TRPLKARSAL
181 ISLPTSISTM VSLLDDMHEP IRDEAILLLM AVVNDSPHVQ KLVAFENIFE RLFSIIEEEG
241 GLRGSLVVND CLSLINNILK YNTSNQTLFL ETGNLPKLAH LLSEPISQDE VFFWNDQRIV
301 NINTALDIVS LTVEPGNTVT TKHQNALLDS SVLMVVLRLA FFHNIPKKVR PVALLTAANM
361 VRSNEHAQLE FSKIDVPYFD PSLPVNSTAN GGPIKLIPVV SILINWMLYA NSVHTFDTRV
421 ACSRLLKAYF MDNFDLQRDF LLKQVQLCNN STNNVGDNAK ENGGSNKSDK ESDSDKDTDG
481 KDGTEYEGSF KANLFEVLLN YDAELNLNPF KLFFTTDIFM FFFQQDHKYS EELREITRNV
541 TTGNDLEDEE PLKAIQTISE LLTTSLTAAD IRIPISYLTF LIYWLFGDFK ATNDFLSDKS
601 VIKSLLSFSY QIQDEDVTIK CLVTMLLGVA YEFSSKESPF PRKEYFEFIT KTLGKDNYAS
661 RIKQFKKDSY FSKVDMNEDS ILTPELDETG LPKVYFSTYF IQLFNENIYR IRTALSHDPD
721 EEPINKISFE EVEKLQRQCT KLKGEITSLQ TETESTHENL TEKLIALTNE HKELDEKYQI
781 LNSSHSSLKE NFSILETELK NVRDSLDEMT QLRDVLETKD KENQTALLEY KSTIHKQEDS
841 IKTLEKGLET ILSQKKKAED GINKMGKDLF ALSREMQAVE ENCKNLQKEK DKSNVNHQKE
901 TKSLKEDIAA KITEIKAINE NLEEMKIQCN NLSKEKEHIS KELVEYKSRF QSHDNLVAKL
961 TEKLKSLANN YKDMQAENES LIKAVEESKN ESSIQLSNLQ NKIDSMSQEK ENFQIERGSI
1021 EKNIEQLKKT ISDLEQTKEE IISKSDSSKD EYESQISLLK EKLETATTAN DENVNKISEL
1081 TKTREELEAE LAAYKNLKNE LETKLETSEK ALKEVKENEE HLKEEKIQLE KEATETKQQL
1141 NSLRANLESL EKEHEDLAAQ LKKYEEQIAN KERQYNEEIS QLNDEITSTQ QENESIKKKN
1201 DELEGEVKAM KSTSEEQSNL KKSEIDALNL QIKELKKKNE TNEASLLESI KSVESETVKI
1261 KELQDECNFK EKEVSELEDK LKASEDKNSK YLELQKESEK IKEELDAKTT ELKIQLEKIT
1321 NLSKAKEKSE SELSRLKKTS SEERKNAEEQ LEKLKNEIQI KNQAFEKERK LLNEGSSTIT
1381 QEYSEKINTL EDELIRLQNE NELKAKEIDN TRSELEKVSL SNDELLEEKQ NTIKSLQDEI
1441 LSYKDKITRN DEKLLSIERD NKRDLESLKE QLRAAQESKA KVEEGLKKLE EESSKEKAEL
1501 EKSKEMMKKL ESTIESNETE LKSSMETIRK SDEKLEQSKK SAEEDIKNLQ HEKSDLISRI
1561 NESEKDIEEL KSKLRIEAKS GSELETVKQE LNNAQEKIRI NAEENTVLKS KLEDIERELK
1621 DKQAEIKSNQ EEKELLTSRL KELEQELDST QQKAQKSEEE RRAEVRKFQV EKSQLDEKAM
1681 LLETKYNDLV NKEQAWKRDE DTVKKTTDSQ RQEIEKLAKE LDNLKAENSK LKEANEDRSE
1741 IDDLMLLVTD LDEKNAKYRS KLKDLGVEIS SDEEDDEEDD EEDEEEGQVA *

* 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.

24 entries for 17 sites

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SiteModificationModifierReference
S57phosphorylated residueMacGilvray ME, et al. (2020) PMID: 32597660
T65phosphorylated residueMacGilvray ME, et al. (2020) PMID: 32597660
S474phosphorylated residueMacGilvray ME, et al. (2020) PMID: 32597660
S474phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
T761phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S952phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
S952phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
K972ubiquitinylated lysineSwaney DL, et al. (2013) PMID: 23749301
S1032phosphorylated residueSmolka MB, et al. (2007) PMID: 17563356
S1032phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
Showing 1 to 10 of 24 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
A854.75
C90.50
D1126.26
E25614.30
F502.79
G362.01
H221.23
I1166.48
K20411.40
L21612.07
M261.45
N1146.37
P281.56
Q894.97
R603.35
S1588.83
T1005.59
V683.80
W70.39
Y341.90

Physical Details

Length (a.a): 1790
Molecular Weight (Da): 206349.3
Isoelectric Point (pl): 4.59
Formula: C9008H14556N2428O3022S35
Aliphatic Index: 83.41
Instability Index: 44.51

Coding Region Translation Calculations

Codon Bias: 0.09
Codon Adaptation Index: 0.17
Frequence of Optimal Codons: 0.49
Hydropathicity of Protein: -0.81
Aromaticity Score: 0.05

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 89660.0
NO Cys residues appear as half cystines: 89160.0

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.

29 entries for 10 sources


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External IDSource
AN0706AspGD
orf19.2629CGD
6815DIP
CAA98621.1GenBank/EMBL/DDBJ
AAB00143.1GenBank/EMBL/DDBJ
CAA98620.1GenBank/EMBL/DDBJ
AAB66659.1GenBank/EMBL/DDBJ
CAA38253.1GenBank/EMBL/DDBJ
L03188GenBank/EMBL/DDBJ
6320145GenBank/EMBL/DDBJ
Showing 1 to 10 of 29 entries

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