Protein Help

IRA1 / YBR140C 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
GLC1 22 , PPD1 23
Protein Product
GTPase-activating protein IRA1
Feature Type
ORF , Verified
Paralog
IRA2 5

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.


Parsing response... [127/127]

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-life6.5 hrChristiano R, et al. (2014)

Protein Abundance

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Abundance (molecules/cell)MediaTreatmentTreatment timeFold ChangeVisualizationStrain backgroundOriginal ReferenceReference
1512SDuntreatedconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1367SD2 mM 1,4-dithiothreitol2 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
1816SD minus nitrogencellular response to nitrogen starvation15 hrconfocal microscopy evidenceS288CBreker M, et al. (2013)Ho B, et al. (2018)
3236YEPDuntreatedflow cytometry evidenceS288CDavidson GS, et al. (2011)Ho B, et al. (2018)
4900YEPDcell quiescence7 d1.51flow cytometry evidenceS288CDavidson GS, et al. (2011)Ho B, et al. (2018)
Showing 1 to 5 of 14 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.


ira1-(GS 1-36) | ira1-(glc1-2) | ira1-(sns2) | ira1-5002 | ira1-A1259D | ira1-A1311V | ira1-D212H | ... Show all

View all IRA1 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 MNQSDPQDKK NFPMEYSLTK HLFFDRLLLV LPIESNLKTY ADVEADSVFN SCRSIILNIA
61 ITKDLNPIIE NTLGLIDLIV QDEEITSDNI TDDIAHSILV LLRLLSDVFE YYWDQNNDFK
121 KIRNDNYKPG FSSHRPNFHT SRPKHTRINP ALATMLLCKI SKLKFNTRTL KVLQNMSHHL
181 SGSATISKSS ILPDSQEFLQ KRNYPAYTEK IDLTIDYIQR FISASNHVEF TKCVKTKVVA
241 PLLISHTSTE LGVVNHLDLF GCEYLTDKNL LAYLDILQHL SSYMKRTIFH SLLLYYASKA
301 FLFWIMARPK EYVKIYNNLI SSDYNSPSSS SDNGGSNNSD KTSISQLVSL LFDDVYSTFS
361 VSSLLTNVNN DHHYHLHHSS SSSKTTNTNS PNSISKTSIK QSSVNASGNV SPSQFSTGND
421 ASPTSPMASL SSPLNTNILG YPLSPITSTL GQANTSTSTT AATTKTDADT PSTMNTNNNN
481 NNNNSANLNN IPQRIFSLDD ISSFNSSRKS LNLDDSNSLF LWDTSQHSNA SMTNTNMHAG
541 VNNSQSQNDQ SSLNYMENIM ELYSNYTGSE LSSHTAILRF LVVLTLLDSE VYDEMNSNSY
601 RKISEPIMNI NPKDSNTSSW GSASKNPSIR HLTHGLKKLT LQQGRKRNVK FLTYLIRNLN
661 GGQFVSDVSL IDSIRSILFL MTMTSSISQI DSNIASVIFS KRFYNLLGQN LEVGTNWNSA
721 TANTFISHCV ERNPLTHRRL QLEFFASGLQ LDSDLFLRHL QLEKELNHID LPKISLYTEG
781 FRVFFHLVST KKLHEDIAEK TSSVLKRLFC IIADILLKAT PYFDDNVTKI IASILDGHIL
841 DQFDAARTLS NDDHVSFDAA TSVYTEPTEI IHNSSDASLV SSLSQSPLSI NSGSNITNTR
901 TWDIQSILPT LSNRSSASDL SLSNILTNPL EAQQNNNANL LAHRLSGVPT TKRYASPNDS
961 ERSRQSPYSS PPQLQQSDLP SPLSVLSSSA GFSSNHSITA TPTILKNIKS PKPNKTKKIA
1021 DDKQLKQPSY SRVILSDNDE ARKIMMNIFS IFKRMTNWFI RPDANTEFPK TFTDIIKPLF
1081 VSILDSNQRL QVTARAFIEI PLSYIATFED IDNDLDPRVL NDHYLLCTYA VTLFASSLFD
1141 LKLENAKREM LLDIIVKFQR VRSYLSNLAE KHNLVQAIIT TERLTLPLLV GAVGSGIFIS
1201 LYCSRGNTPR LIKISCCEFL RSLRFYQKYV GALDQYSIYN IDFIDAMAQD NFTASGSVAL
1261 QRRLRNNILT YIKGSDSILL DSMDVIYKKW FYFSCSKSVT QEELVDFRSL AGILASMSGI
1321 LSDMQELEKS KSAPDNEGDS LSFESRNPAY EVHKSLKLEL TKKMNFFISK QCQWLNNPNL
1381 LTRENSRDIL SIELHPLSFN LLFNNLGLKI DELMSIDLSK SHEDSSFVLL EQIIIIIRTI
1441 LKRDDDEKIM LLFSTDLLDA VDKLIEIVEK ISIKSSKYYK GIIQMSKMFR AFEHSEKNLG
1501 ISNHFHLKNK WLKLVIGWFK LSINKDYDFE NLSRPLREMD LQKRDEDFLY IDTSIESAKA
1561 LAYLTHNVPL EIPPSSSKED WNRSSTVSFG NHFTILLKGL EKSADLNQFP VSLRHKISIL
1621 NENVIIALTN LSNANVNVSL KFTLPMGYSP NKDIRIAFLR VFIDIVTNYP VNPEKHEMDK
1681 MLAIDDFLKY IIKNPILAFF GSLACSPADV DLYAGGFLNA FDTRNASHIL VTELLKQEIK
1741 RAARSDDILR RNSCATRALS LYTRSRGNKY LIKTLRPVLQ GIVDNKESFE IDKMKPGSEN
1801 SEKMLDLFEK YMTRLIDAIT SSIDDFPIEL VDICKTIYNA ASVNFPEYAY IAVGSFVFLR
1861 FIGPALVSPD SENIIIVTHA HDRKPFITLA KVIQSLANGR ENIFKKDILV SKEEFLKTCS
1921 DKIFNFLSEL CKIPTNNFTV NVREDPTPIS FDYSFLHKFF YLNEFTIRKE IINESKLPGE
1981 FSFLKNTVML NDKILGVLGQ PSMEIKNEIP PFVVENREKY PSLYEFMSRY AFKKVDMKEE
2041 EEDNAPFVHE AMTLDGIQII VVTFTNCEYN NFVMDSLVYK VLQIYARMWC SKHYVVIDCT
2101 TFYGGKANFQ KLTTLFFSLI PEQASSNCMG CYYFNVNKSF MDQWASSYTV ENPYLVTTIP
2161 RCFINSNTDQ SLIKSLGLSG RSLEVLKDVR VTLHDITLYD KEKKKFCPVS LKIGNKYFQV
2221 LHEIPQLYKV TVSNRTFSIK FNNVYKISNL ISVDVSNTTG VSSEFTLSLD NEEKLVFCSP
2281 KYLEIVKMFY YAQLKMEEDF GTDFSNDISF STSSSAVNAS YCNVKEVGEI ISHLSLVILV
2341 GLFNEDDLVK NISYNLLVAT QEAFNLDFGT RLHKSPETYV PDDTTTFLAL IFKAFSESST
2401 ELTPYIWKYM LDGLENDVIP QEHIPTVVCS LSYWVPNLYE HVYLANDEEG PEAISRIIYS
2461 LIRLTVKEPN FTTAYLQQIW FLLALDGRLT NVIVEEIVSH ALDRDSENRD WMKAVSILTS
2521 FPTTEIACQV IEKLINMIKS FLPSLAVEAS AHSWSELTIL SKISVSIFFE SPLLSQMYLP
2581 EILFAVSLLI DVGPSEIRVS LYELLMNVCH SLTNNESLPE RNRKNLDIVC ATFARQKLNF
2641 ISGFSQEKGR VLPNFAASSF SSKFGTLDLF TKNIMLLMEY GSISEGAQWE AKYKKYLMDA
2701 IFGHRSFFSA RAMMILGIMS KSHTSLFLCK ELLVETMKVF AEPVVDDEQM FIIIAHVFTY
2761 SKIVEGLDPS SELMKELFWL ATICVESPHP LLFEGGLLFM VNCLKRLYTV HLQLGFDGKS
2821 LAKKLMESRN FAATLLAKLE SYNGCIWNED NFPHIILGFI ANGLSIPVVK GAALDCLQAL
2881 FKNTYYERKS NPKSSDYLCY LFLLHLVLSP EQLSTLLLEV GFEDELVPLN NTLKVPLTLI
2941 NWLSSDSDKS NIVLYQGALL FSCVMSDEPC KFRFALLMRY LLKVNPICVF RFYTLTRKEF
3001 RRLSTLEQSS EAVAVSFELI GMLVTHSEFN YLEEFNDEMV ELLKKRGLSV VKPLDIFDQE
3061 HIEKLKGEGE HQVAIYERKR LATMILARMS CS*

* 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.

66 entries for 37 sites

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SiteModificationModifierReference
S4phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
T62phosphorylated residueHolt LJ, et al. (2009) PMID: 19779198
S330phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
S331phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
S331phosphorylated residueSwaney DL, et al. (2013) PMID: 23749301
T388phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
T388phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S390phosphorylated residueLanz MC, et al. (2021) PMID: 33491328
S390phosphorylated residueLeutert M, et al. (2023) PMID: 37845410
S390phosphorylated residueZhou X, et al. (2021) PMID: 33481703
Showing 1 to 10 of 66 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
A1484.79
C401.29
D1725.56
E1725.56
F1735.60
G933.01
H702.26
I2367.63
K1956.31
L37512.13
M692.23
N2166.99
P1153.72
Q832.68
R1153.72
S34911.29
T1765.69
V1645.30
W230.74
Y1083.49

Physical Details

Length (a.a): 3092
Molecular Weight (Da): 350948.8
Isoelectric Point (pl): 6.54
Formula: C15796H24780N4094O4713S109
Aliphatic Index: 93.26
Instability Index: 43.77

Coding Region Translation Calculations

Codon Bias: 0.04
Codon Adaptation Index: 0.14
Frequence of Optimal Codons: 0.45
Hydropathicity of Protein: -0.12
Aromaticity Score: 0.1

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines: 289920.0
NO Cys residues appear as half cystines: 287420.0

Atomic 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.

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 7 sources


Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

External IDSource
2318DIP
AAA34709.1GenBank/EMBL/DDBJ
CAA53498.1GenBank/EMBL/DDBJ
CAA55537.1GenBank/EMBL/DDBJ
CAA85098.1GenBank/EMBL/DDBJ
X75891GenBank/EMBL/DDBJ
X78937GenBank/EMBL/DDBJ
585325GenBank/EMBL/DDBJ
Z36009GenBank/EMBL/DDBJ
M24378GenBank/EMBL/DDBJ
Showing 1 to 10 of 23 entries

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