Protein Help

BRR2 / YER172C 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
RSS1 7 , SLT22 2 8 , SNU246 4 , PRP44
Protein Product
ATP-dependent RNA helicase BRR2
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.


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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-life7.5 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
1809SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1510SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1761SD1 mM hydrogen peroxide1 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1460SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1708SDuntreatedconfocal microscopy evidenceS288CChong YT, et al. (2015)Ho B, et al. (2018)
Showing 1 to 5 of 17 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.


brr2-5001 | brr2-5002 | brr2-5003 | brr2-5005 | brr2-5018 | brr2-5019-supp1 | brr2-5023-supp1 | ... Show all

View all BRR2 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 MTEHETKDKA KKIREIYRYD EMSNKVLKVD KRFMNTSQNP QRDAEISQPK SMSGRISAKD
61 MGQGLCNNIN KGLKENDVAV EKTGKSASLK KIQQHNTILN SSSDFRLHYY PKDPSNVETY
121 EQILQWVTEV LGNDIPHDLI IGTADIFIRQ LKENEENEDG NIEERKEKIQ HELGINIDSL
181 KFNELVKLMK NITDYETHPD NSNKQAVAIL ADDEKSDEEE VTEMSNNANV LGGEINDNED
241 DDEEYDYNDV EVNSKKKNKR ALPNIENDII KLSDSKTSNI ESVPIYSIDE FFLQRKLRSE
301 LGYKDTSVIQ DLSEKILNDI ETLEHNPVAL EQKLVDLLKF ENISLAEFIL KNRSTIFWGI
361 RLAKSTENEI PNLIEKMVAK GLNDLVEQYK FRETTHSKRE LDSGDDQPQS SEAKRTKFSN
421 PAIPPVIDLE KIKFDESSKL MTVTKVSLPE GSFKRVKPQY DEIHIPAPSK PVIDYELKEI
481 TSLPDWCQEA FPSSETTSLN PIQSKVFHAA FEGDSNMLIC APTGSGKTNI ALLTVLKALS
541 HHYNPKTKKL NLSAFKIVYI APLKALVQEQ VREFQRRLAF LGIKVAELTG DSRLSRKQID
601 ETQVLVSTPE KWDITTRNSN NLAIVELVRL LIIDEIHLLH DDRGPVLESI VARTFWASKY
661 GQEYPRIIGL SATLPNYEDV GRFLRVPKEG LFYFDSSFRP CPLSQQFCGI KERNSLKKLK
721 AMNDACYEKV LESINEGNQI IVFVHSRKET SRTATWLKNK FAEENITHKL TKNDAGSKQI
781 LKTEAANVLD PSLRKLIESG IGTHHAGLTR SDRSLSEDLF ADGLLQVLVC TATLAWGVNL
841 PAHTVIIKGT DVYSPEKGSW EQLSPQDVLQ MLGRAGRPRY DTFGEGIIIT DQSNVQYYLS
901 VLNQQLPIES QFVSKLVDNL NAEVVAGNIK CRNDAVNWLA YTYLYVRMLA SPMLYKVPDI
961 SSDGQLKKFR ESLVHSALCI LKEQELVLYD AENDVIEATD LGNIASSFYI NHASMDVYNR
1021 ELDEHTTQID LFRIFSMSEE FKYVSVRYEE KRELKQLLEK APIPIREDID DPLAKVNVLL
1081 QSYFSQLKFE GFALNSDIVF IHQNAGRLLR AMFEICLKRG WGHPTRMLLN LCKSATTKMW
1141 PTNCPLRQFK TCPVEVIKRL EASTVPWGDY LQLETPAEVG RAIRSEKYGK QVYDLLKRFP
1201 KMSVTCNAQP ITRSVMRFNI EIIADWIWDM NVHGSLEPFL LMLEDTDGDS ILYYDVLFIT
1261 PDIVGHEFTL SFTYELKQHN QNNLPPNFFL TLISENWWHS EFEIPVSFNG FKLPKKFPPP
1321 TPLLENISIS TSELGNDDFS EVFEFKTFNK IQSQVFESLY NSNDSVFVGS GKGTGKTAMA
1381 ELALLNHWRQ NKGRAVYINP SGEKIDFLLS DWNKRFSHLA GGKIINKLGN DPSLNLKLLA
1441 KSHVLLATPV QFELLSRRWR QRKNIQSLEL MIYDDAHEIS QGVYGAVYET LISRMIFIAT
1501 QLEKKIRFVC LSNCLANARD FGEWAGMTKS NIYNFSPSER IEPLEINIQS FKDVEHISFN
1561 FSMLQMAFEA SAAAAGNRNS SSVFLPSRKD CMEVASAFMK FSKAIEWDML NVEEEQIVPY
1621 IEKLTDGHLR APLKHGVGIL YKGMASNDER IVKRLYEYGA VSVLLISKDC SAFACKTDEV
1681 IILGTNLYDG AEHKYMPYTI NELLEMVGLA SGNDSMAGKV LILTSHNMKA YYKKFLIEPL
1741 PTESYLQYII HDTLNNEIAN SIIQSKQDCV DWFTYSYFYR RIHVNPSYYG VRDTSPHGIS
1801 VFLSNLVETC LNDLVESSFI EIDDTEAEVT AEVNGGDDEA TEIISTLSNG LIASHYGVSF
1861 FTIQSFVSSL SNTSTLKNML YVLSTAVEFE SVPLRKGDRA LLVKLSKRLP LRFPEHTSSG
1921 SVSFKVFLLL QAYFSRLELP VDFQNDLKDI LEKVVPLINV VVDILSANGY LNATTAMDLA
1981 QMLIQGVWDV DNPLRQIPHF NNKILEKCKE INVETVYDIM ALEDEERDEI LTLTDSQLAQ
2041 VAAFVNNYPN VELTYSLNNS DSLISGVKQK ITIQLTRDVE PENLQVTSEK YPFDKLESWW
2101 LVLGEVSKKE LYAIKKVTLN KETQQYELEF DTPTSGKHNL TIWCVCDSYL DADKELSFEI
2161 NVK*

* 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.

23 entries for 17 sites

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SiteModificationModifierReference
K12sumoylated lysineBhagwat NR, et al. (2021) PMID: 33502312
Y19phosphorylated residueBhagwat NR, et al. (2021) PMID: 33502312
K25sumoylated lysineBhagwat NR, et al. (2021) PMID: 33502312
S37phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S101phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S216phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
K304monoacetylated residueHenriksen P, et al. (2012) PMID: 22865919
S403phosphorylated residueZhou X, et al. (2021) PMID: 33481703
S403phosphorylated residueSoulard A, et al. (2010) PMID: 20702584
S403phosphorylated residueAlbuquerque CP, et al. (2008) PMID: 18407956
Showing 1 to 10 of 23 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
A1165.36
C241.11
D1285.92
E1768.14
F934.30
G924.25
H442.03
I1557.17
K1577.26
L23210.73
M411.90
N1356.24
P853.93
Q793.65
R853.93
S1778.18
T1095.04
V1366.29
W261.20
Y733.37

Physical Details

Length (a.a): 2163
Molecular Weight (Da): 246125.2
Isoelectric Point (pl): 5.18
Formula: C11026H17289N2903O3345S65
Aliphatic Index: 88.63
Instability Index: 43.57

Coding Region Translation Calculations

Codon Bias: 0.01
Codon Adaptation Index: 0.13
Frequence of Optimal Codons: 0.44
Hydropathicity of Protein: -0.32
Aromaticity Score: 0.09

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 253270.0
NO Cys residues appear as half cystines: 251770.0

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.

34 entries for 11 sources


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External IDSource
orf19.3098CGD
850DIP
3.6.4.13ExPASy
U18922GenBank/EMBL/DDBJ
731380GenBank/EMBL/DDBJ
256599941GenBank/EMBL/DDBJ
240104615GenBank/EMBL/DDBJ
603413GenBank/EMBL/DDBJ
256599942GenBank/EMBL/DDBJ
508123650GenBank/EMBL/DDBJ
Showing 1 to 10 of 34 entries

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