Protein Help

RAD50 / YNL250W 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
MRX complex DNA-binding subunit
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-life7.7 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
1832SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1414SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1724SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1356SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1551SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 16 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.


rad50-1 | rad50-10A | rad50-2TEV | rad50-E1042A | rad50-E1042K | rad50-E1042Δ | rad50-E1044Δ | ... Show all

View all RAD50 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 MSAIYKLSIQ GIRSFDSNDR ETIEFGKPLT LIVGMNGSGK TTIIECLKYA TTGDLPPNSK
61 GGVFIHDPKI TGEKDIRAQV KLAFTSANGL NMIVTRNIQL LMKKTTTTFK TLEGQLVAIN
121 NSGDRSTLST RSLELDAQVP LYLGVPKAIL EYVIFCHQED SLWPLSEPSN LKKKFDEIFQ
181 AMKFTKALDN LKSIKKDMSV DIKLLKQSVE HLKLDKDRSK AMKLNIHQLQ TKIDQYNEEV
241 SEIESQLNEI TEKSDKLFKS NQDFQKILSK VENLKNTKLS ISDQVKRLSN SIDILDLSKP
301 DLQNLLANFS KVLMDKNNQL RDLETDISSL KDRQSSLQSL SNSLIRRQGE LEAGKETYEK
361 NRNHLSSLKE AFQHKFQGLS NIENSDMAQV NHEMSQFKAF ISQDLTDTID QFAKDIQLKE
421 TNLSDLIKSI TVDSQNLEYN KKDRSKLIHD SEELAEKLKS FKSLSTQDSL NHELENLKTY
481 KEKLQSWESE NIIPKLNQKI EEKNNEMIIL ENQIEKFQDR IMKTNQQADL YAKLGLIKKS
541 INTKLDELQK ITEKLQNDSR IRQVFPLTQE FQRADLEMDF QKLFINMQKN IAINNKKMHE
601 LDRRYTNALY NLNTIEKDLQ DNQKSKEKVI QLLSENLPED CTIDEYNDVL EETELSYKTA
661 LENLKMHQTT LEFNRKALEI AERDSCCYLC SRKFENESFK SKLLQELKTK TDANFEKTLK
721 DTVQNEKEYL HSLRLLEKHI ITLNSINEKI DNSQKCLEKA KEETKTSKSK LDELEVDSTK
781 LKDEKELAES EIRPLIEKFT YLEKELKDLE NSSKTISEEL SIYNTSEDGI QTVDELRDQQ
841 RKMNDSLREL RKTISDLQME KDEKVRENSR MINLIKEKEL TVSEIESSLT QKQNIDDSIR
901 SKRENINDID SRVKELEARI ISLKNKKDEA QSVLDKVKNE RDIQVRNKQK TVADINRLID
961 RFQTIYNEVV DFEAKGFDEL QTTIKELELN KAQMLELKEQ LDLKSNEVNE EKRKLADSNN
1021 EEKNLKQNLE LIELKSQLQH IESEISRLDV QNAEAERDKY QEESLRLRTR FEKLSSENAG
1081 KLGEMKQLQN QIDSLTHQLR TDYKDIEKNY HKEWVELQTR SFVTDDIDVY SKALDSAIMK
1141 YHGLKMQDIN RIIDELWKRT YSGTDIDTIK IRSDEVSSTV KGKSYNYRVV MYKQDVELDM
1201 RGRCSAGQKV LASIIIRLAL SETFGANCGV IALDEPTTNL DEENIESLAK SLHNIINMRR
1261 HQKNFQLIVI THDEKFLGHM NAAAFTDHFF KVKRDDRQKS QIEWVDINRV TY*

* 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.

21 entries for 16 sites

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SiteModificationModifierReference
K6monoacetylated residueYe Y, et al. (2016) PMID: 27173583
K40monoacetylated residueYe Y, et al. (2016) PMID: 27173583
S199phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S245phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
K253monoacetylated residueYe Y, et al. (2016) PMID: 27173583
S434phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S460phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
T466phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
T466phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S469phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
Showing 1 to 10 of 21 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
A493.73
C90.69
D977.39
E13210.06
F392.97
G292.21
H221.68
I1017.70
K14911.36
L15311.66
M272.06
N927.01
P141.07
Q796.02
R594.50
S1088.23
T735.56
V473.58
W50.38
Y282.13

Physical Details

Length (a.a): 1312
Molecular Weight (Da): 152549.6
Isoelectric Point (pl): 5.87
Formula: C6661H10863N1858O2151S36
Aliphatic Index: 84.62
Instability Index: 43.11

Coding Region Translation Calculations

Codon Bias: 0.07
Codon Adaptation Index: 0.17
Frequence of Optimal Codons: 0.48
Hydropathicity of Protein: -0.78
Aromaticity Score: 0.05

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 69720.0
NO Cys residues appear as half cystines: 69220.0

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.

23 entries for 10 sources


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External IDSource
AN3619AspGD
orf19.1648CGD
2419DIP
1302293GenBank/EMBL/DDBJ
1255968GenBank/EMBL/DDBJ
4273GenBank/EMBL/DDBJ
CAA65494.1GenBank/EMBL/DDBJ
CAA32919.1GenBank/EMBL/DDBJ
CAA96157.1GenBank/EMBL/DDBJ
6324079GenBank/EMBL/DDBJ
Showing 1 to 10 of 23 entries

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