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P38266

- AIM3_YEAST

UniProt

P38266 - AIM3_YEAST

Protein

Altered inheritance of mitochondria protein 3

Gene

AIM3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. actin cortical patch assembly Source: SGD
    2. barbed-end actin filament capping Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29070-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Altered inheritance of mitochondria protein 3
    Gene namesi
    Name:AIM3
    Ordered Locus Names:YBR108W
    ORF Names:YBR0901
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR108w.
    SGDiS000000312. AIM3.

    Subcellular locationi

    Membrane raft 1 Publication; Peripheral membrane protein 1 Publication
    Note: Localize within detergent-insoluble glycolipid-enriched membranes.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. membrane raft Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Increases frequency of mitochondrial genome loss.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 947947Altered inheritance of mitochondria protein 3PRO_0000202486Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571Phosphoserine1 Publication
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei64 – 641Phosphoserine1 Publication
    Modified residuei476 – 4761Phosphoserine1 Publication
    Modified residuei729 – 7291Phosphothreonine2 Publications
    Modified residuei861 – 8611Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38266.
    PaxDbiP38266.
    PeptideAtlasiP38266.

    Expressioni

    Gene expression databases

    GenevestigatoriP38266.

    Interactioni

    Subunit structurei

    Interacts with RVS167.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BZZ1P388222EBI-21584,EBI-3889
    LSB1P532813EBI-21584,EBI-23329
    LSB3P436034EBI-21584,EBI-22980
    RVS167P397436EBI-21584,EBI-14500
    YSC84P327935EBI-21584,EBI-24460

    Protein-protein interaction databases

    BioGridi32812. 151 interactions.
    DIPiDIP-1602N.
    IntActiP38266. 16 interactions.
    MINTiMINT-385431.
    STRINGi4932.YBR108W.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi95 – 398304Gln-richAdd
    BLAST
    Compositional biasi371 – 44777Pro-richAdd
    BLAST
    Compositional biasi862 – 90746Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AIM3 family.Curated

    Phylogenomic databases

    eggNOGiNOG12793.
    OMAiPPKPFRH.
    OrthoDBiEOG712V4W.

    Sequencei

    Sequence statusi: Complete.

    P38266-1 [UniParc]FASTAAdd to Basket

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    MGFWENNKDS ITSGLKSAGK YGYQGTKYVA KTGYKASKKH YNNSKARRER    50
    KSGKKNSSDE EYDSEDEMEY ERKPTDIRSL KDPKSFPPPP LKPGQKTYTG 100
    QQQQQMPNGQ ASYAFQGAYQ GQPGAGSTEQ SQYAQPQYNQ YPQQQLQQGV 150
    MPQQQQLQQG VVPQQPPIYG EQVPPYGSNS NATSYQSLPQ QNQPQNAIPS 200
    QVSLNSASQQ STGFVSQNLQ YGTQSSNPAP SPSFQNGLQC HQQPQYVSHG 250
    STNLGQSQFP SGQQQQPTTQ FGQQVLPSPA QPQQQQQGQP LPPPRGQVIL 300
    PAPGEPLSNG FGQQQQQQQQ QQQPLNQNNA LLPQMNVEGV SGMAAVQPVY 350
    GQAMSSTTNM QDSNPSYGAS PMQGQPPVGG QPPVPVRMQP QPPQPMQQGN 400
    IYPIEPSLDS TGSTPHFEVT PFDPDAPAPK PKIDIPTVDV SSLPPPPTHR 450
    DRGAVVHQEP APSGKIQPNT TSSAASLPAK HSRTTTADNE RNSGNKENDE 500
    STSKSSILGH YDVDVNIMPP PKPFRHGLDS VPSEHTTKNA PERAVPILPP 550
    RNNVEPPPPP SRGNFERTES VLSTNAANVQ EDPISNFLPP PKPFRHTETK 600
    QNQNSKASPV EMKGEVLPGH PSEEDRNVEP SLVPQSKPQS QSQFRRAHME 650
    TQPIQNFQPP PKPFRRSQSS NSSDSSYTID GPEANHGRGR GRIAKHHDGD 700
    EYNPKSENST ENGRLGDAPN SFIRKRAPTP PAPSRSEKLH EGTITSEVDS 750
    SKDANKYEKS IPPVTSSIQA QQSTKKAPPP VVKPKPRNFS LKANEYPKEL 800
    TREATGQDEV LNSITNELSH IKLRKTNVNL EKLGGSKKVK DSSPVPSDLD 850
    EKYVSASGSI TPPRPPPSRS SPKKVPPVVP KKNDNLKKKP PVVPKKKPLL 900
    KSLEPRPIEM ERAYSGDISA ADDNLNPFER YKRNVVPQED DRLHKLK 947
    Length:947
    Mass (Da):103,863
    Last modified:July 27, 2011 - v3
    Checksum:iCD624428B29DA272
    GO

    Sequence cautioni

    The sequence CAA55611.1 differs from that shown. Reason: Frameshift at position 841.
    The sequence CAA85063.1 differs from that shown. Reason: Frameshift at position 841.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti515 – 5151V → A in CAA55611. (PubMed:7900426)Curated
    Sequence conflicti515 – 5151V → A in CAA85063. (PubMed:7813418)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78993 Genomic DNA. Translation: CAA55611.1. Frameshift.
    Z35977 Genomic DNA. Translation: CAA85063.1. Frameshift.
    BK006936 Genomic DNA. Translation: DAA07227.2.
    PIRiS48273.
    RefSeqiNP_009666.3. NM_001178456.2.

    Genome annotation databases

    EnsemblFungiiYBR108W; YBR108W; YBR108W.
    GeneIDi852405.
    KEGGisce:YBR108W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78993 Genomic DNA. Translation: CAA55611.1 . Frameshift.
    Z35977 Genomic DNA. Translation: CAA85063.1 . Frameshift.
    BK006936 Genomic DNA. Translation: DAA07227.2 .
    PIRi S48273.
    RefSeqi NP_009666.3. NM_001178456.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32812. 151 interactions.
    DIPi DIP-1602N.
    IntActi P38266. 16 interactions.
    MINTi MINT-385431.
    STRINGi 4932.YBR108W.

    Proteomic databases

    MaxQBi P38266.
    PaxDbi P38266.
    PeptideAtlasi P38266.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR108W ; YBR108W ; YBR108W .
    GeneIDi 852405.
    KEGGi sce:YBR108W.

    Organism-specific databases

    CYGDi YBR108w.
    SGDi S000000312. AIM3.

    Phylogenomic databases

    eggNOGi NOG12793.
    OMAi PPKPFRH.
    OrthoDBi EOG712V4W.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29070-MONOMER.

    Miscellaneous databases

    NextBioi 971246.

    Gene expression databases

    Genevestigatori P38266.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Analysis of a 70 kb region on the right arm of yeast chromosome II."
      Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
      Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 515.
      Strain: ATCC 204508 / S288c.
    4. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
      Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
      Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF FRAMESHIFT.
    5. "Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p."
      Germann M., Swain E., Bergman L., Nickels J.T. Jr.
      J. Biol. Chem. 280:4270-4278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RVS167, SUBCELLULAR LOCATION.
    6. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; THR-729 AND THR-861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis."
      Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J., Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M., Troyanskaya O.G., Caudy A.A.
      PLoS Genet. 5:E1000407-E1000407(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-58 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAIM3_YEAST
    AccessioniPrimary (citable) accession number: P38266
    Secondary accession number(s): D6VQA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3