Protein Help

KAP114 / YGL241W 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.


Protein Product
karyopherin KAP114
Feature Type
ORF , Verified
Summary
Protein abundance increases in response to 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-life9.0 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
2046SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1707SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1939SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1649SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1740SDuntreatedconfocal 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.


kap114-(Δ347–371) | kap114-(Δ899–956) | kap114-Δ

View all KAP114 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 MDINELIIGA QSADKHTREV AETQLLQWCD SDASQVFKAL ANVALQHEAS LESRQFALLS
61 LRKLITMYWS PGFESYRSTS NVEIDVKDFI REVLLKLCLN DNENTKIKNG ASYCIVQISA
121 VDFPDQWPQL LTVIYDAISH QHSLNAMSLL NEIYDDVVSE EMFFEGGIGL ATMEIVFKVL
181 NTETSTLIAK IAALKLLKAC LLQMSSHNEY DEASRKSFVS QCLATSLQIL GQLLTLNFGN
241 VDVISQLKFK SIIYENLVFI KNDFSRKHFS SELQKQFKIM AIQDLENVTH INANVETTES
301 EPLLETVHDC SIYIVEFLTS VCTLQFSVEE MNKIITSLTI LCQLSSETRE IWTSDFNTFV
361 SKETGLAASY NVRDQANEFF TSLPNPQLSL IFKVVSNDIE HSTCNYSTLE SLLYLLQCIL
421 LNDDEITGEN IDQSLQILIK TLENILVSQE IPELILARAI LTIPRVLDKF IDALPDIKPL
481 TSAFLAKSLN LALKSDKELI KSATLIAFTY YCYFAELDSV LGPEVCSETQ EKVIRIINQV
541 SSDAEEDTNG ALMEVLSQVI SYNPKEPHSR KEILQAEFHL VFTISSEDPA NVQVVVQSQE
601 CLEKLLDNIN MDNYKNYIEL CLPSFINVLD SNNANNYRYS PLLSLVLEFI TVFLKKKPND
661 GFLPDEINQY LFEPLAKVLA FSTEDETLQL ATEAFSYLIF NTDTRAMEPR LMDIMKVLER
721 LLSLEVSDSA AMNVGPLVVA IFTRFSKEIQ PLIGRILEAV VVRLIKTQNI STEQNLLSVL
781 CFLTCNDPKQ TVDFLSSFQI DNTDALTLVM RKWIEAFEVI RGEKRIKENI VALSNLFFLN
841 DKRLQKVVVN GNLIPYEGDL IITRSMAKKM PDRYVQVPLY TKIIKLFVSE LSFQSKQPNP
901 EQLITSDIKQ EVVNANKDDD NDDWEDVDDV LDYDKLKEYI DDDVDEEADD DSDDITGLMD
961 VKESVVQLLV RFFKEVASKD VSGFHCIYET LSDSERKVLS EALL*

* 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.

5 entries for 5 sites

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SiteModificationModifierReference
T23phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S31phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S34phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S865phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
K909sumoylated lysineMMS21Rothenbusch U, et al. (2012) PMID: 22562154
Showing 1 to 5 of 5 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
A565.58
C171.69
D706.97
E828.17
F494.88
G201.99
H121.20
I807.97
K595.88
L13012.95
M181.79
N595.88
P282.79
Q474.68
R282.79
S878.67
T545.38
V757.47
W60.60
Y272.69

Physical Details

Length (a.a): 1004
Molecular Weight (Da): 113856.7
Isoelectric Point (pl): 4.28
Formula: C5106H8044N1283O1583S35
Aliphatic Index: 103.83
Instability Index: 35.5

Coding Region Translation Calculations

Codon Bias: 0.03
Codon Adaptation Index: 0.14
Frequence of Optimal Codons: 0.45
Hydropathicity of Protein: -0.01
Aromaticity Score: 0.08

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 74230.0
NO Cys residues appear as half cystines: 73230.0

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.

19 entries for 9 sources


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External IDSource
orf19.7086CGD
5881DIP
CAA96960.1GenBank/EMBL/DDBJ
CAA89014.1GenBank/EMBL/DDBJ
793871GenBank/EMBL/DDBJ
Z72763GenBank/EMBL/DDBJ
1322907GenBank/EMBL/DDBJ
1723977GenBank/EMBL/DDBJ
6321196GenBank/EMBL/DDBJ
Z49149GenBank/EMBL/DDBJ
Showing 1 to 10 of 19 entries

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