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P32357

- AAR2_YEAST

UniProt

P32357 - AAR2_YEAST

Protein

A1 cistron-splicing factor AAR2

Gene

AAR2

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 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing. Involved in splicing pre-mRNA of the A1 cistron and other genes that are important for cell growth.2 Publications

    GO - Biological processi

    1. spliceosomal tri-snRNP complex assembly Source: SGD

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28966-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A1 cistron-splicing factor AAR2
    Gene namesi
    Name:AAR2
    Ordered Locus Names:YBL074C
    ORF Names:YBL06.06, YBL0611
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL074c.
    SGDiS000000170. AAR2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: This protein lacks a nuclear localization signal, it may interact in the cytoplasm with a component of spliceosomes via the leucine-zipper and then be transported into the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. U5 snRNP Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi253 – 2531S → A: No effect on interaction with PRP8. 1 Publication
    Mutagenesisi253 – 2531S → D or E: Disrupts interaction with PRP8. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 355355A1 cistron-splicing factor AAR2PRO_0000209705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei253 – 2531Phosphoserine1 Publication
    Modified residuei274 – 2741Phosphothreonine1 Publication
    Modified residuei328 – 3281Phosphotyrosine1 Publication
    Modified residuei331 – 3311Phosphoserine1 Publication
    Modified residuei345 – 3451Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated on serine and tyrosine residues.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32357.
    PaxDbiP32357.

    Expressioni

    Gene expression databases

    GenevestigatoriP32357.

    Interactioni

    Subunit structurei

    Heterodimer Probable. Interacts with PRP8 (via RNase H homology domain and MPN domain), competing with BRR2 for the same binding site. Component of a U5 snRNP complex that contains at least the U5 snRNA, PRP8, SNU114, AAR2, SMB1, SMD1, SMD2, SMD3, SME1, SMX2 and SMX3, but is not a component of the U4/U6-U5 tri-snRNP complex.3 PublicationsCurated

    Protein-protein interaction databases

    BioGridi32628. 20 interactions.
    DIPiDIP-6642N.
    IntActiP32357. 7 interactions.
    MINTiMINT-663730.
    STRINGi4932.YBL074C.

    Structurei

    Secondary structure

    1
    355
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi13 – 175
    Beta strandi20 – 245
    Beta strandi32 – 365
    Beta strandi38 – 403
    Beta strandi42 – 487
    Beta strandi51 – 6010
    Helixi62 – 643
    Beta strandi66 – 727
    Turni73 – 764
    Beta strandi77 – 837
    Helixi86 – 9813
    Beta strandi102 – 1043
    Helixi113 – 1186
    Helixi123 – 1297
    Beta strandi136 – 1416
    Turni147 – 1493
    Beta strandi153 – 1553
    Helixi172 – 1743
    Beta strandi183 – 1853
    Turni186 – 1883
    Helixi194 – 1996
    Helixi202 – 2065
    Helixi207 – 2148
    Helixi217 – 23418
    Helixi237 – 25115
    Helixi258 – 27417
    Helixi277 – 2793
    Helixi280 – 2834
    Helixi286 – 2949
    Turni297 – 3004
    Helixi303 – 31210
    Helixi314 – 3163
    Beta strandi345 – 3539

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SBSX-ray2.10A1-355[»]
    3SBTX-ray1.80B1-355[»]
    3ZEFX-ray3.10A/D1-355[»]
    4I43X-ray2.00A1-355[»]
    4ILGX-ray2.10A1-355[»]
    4ILHX-ray1.85B1-331[»]
    4ILIX-ray3.20A/B1-318[»]
    ProteinModelPortaliP32357.
    SMRiP32357. Positions 1-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni261 – 28222Leucine-zipperAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi332 – 34110Asp/Glu-rich (acidic)

    Sequence similaritiesi

    Belongs to the AAR2 family.Curated

    Phylogenomic databases

    eggNOGiNOG331204.
    HOGENOMiHOG000033742.
    KOiK13205.
    OMAiYLDKSWY.
    OrthoDBiEOG7GTTGG.

    Family and domain databases

    InterProiIPR007946. AAR2.
    [Graphical view]
    PANTHERiPTHR12689. PTHR12689. 1 hit.
    PfamiPF05282. AAR2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32357-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTVPFTSAP IEVTIGIDQY SFNVKENQPF HGIKDIPIGH VHVIHFQHAD    50
    NSSMRYGYWF DCRMGNFYIQ YDPKDGLYKM MEERDGAKFE NIVHNFKERQ 100
    MMVSYPKIDE DDTWYNLTEF VQMDKIRKIV RKDENQFSYV DSSMTTVQEN 150
    ELLKSSLQKA GSKMEAKNED DPAHSLNYTV INFKSREAIR PGHEMEDFLD 200
    KSYYLNTVML QGIFKNSSNY FGELQFAFLN AMFFGNYGSS LQWHAMIELI 250
    CSSATVPKHM LDKLDEILYY QIKTLPEQYS DILLNERVWN ICLYSSFQKN 300
    SLHNTEKIME NKYPELLGKD NEDDALIYGI SDEERDDEDD EHNPTIVGGL 350
    YYQRP 355
    Length:355
    Mass (Da):41,688
    Last modified:October 1, 1993 - v1
    Checksum:i1F030D821D974131
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90455 Genomic DNA. Translation: BAA14421.1.
    Z26879 Genomic DNA. Translation: CAA81524.1.
    Z35835 Genomic DNA. Translation: CAA84894.1.
    M36115 Genomic DNA. No translation available.
    BK006936 Genomic DNA. Translation: DAA07048.1.
    PIRiS18510.
    RefSeqiNP_009479.1. NM_001178314.1.

    Genome annotation databases

    EnsemblFungiiYBL074C; YBL074C; YBL074C.
    GeneIDi852205.
    KEGGisce:YBL074C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90455 Genomic DNA. Translation: BAA14421.1 .
    Z26879 Genomic DNA. Translation: CAA81524.1 .
    Z35835 Genomic DNA. Translation: CAA84894.1 .
    M36115 Genomic DNA. No translation available.
    BK006936 Genomic DNA. Translation: DAA07048.1 .
    PIRi S18510.
    RefSeqi NP_009479.1. NM_001178314.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SBS X-ray 2.10 A 1-355 [» ]
    3SBT X-ray 1.80 B 1-355 [» ]
    3ZEF X-ray 3.10 A/D 1-355 [» ]
    4I43 X-ray 2.00 A 1-355 [» ]
    4ILG X-ray 2.10 A 1-355 [» ]
    4ILH X-ray 1.85 B 1-331 [» ]
    4ILI X-ray 3.20 A/B 1-318 [» ]
    ProteinModelPortali P32357.
    SMRi P32357. Positions 1-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32628. 20 interactions.
    DIPi DIP-6642N.
    IntActi P32357. 7 interactions.
    MINTi MINT-663730.
    STRINGi 4932.YBL074C.

    Proteomic databases

    MaxQBi P32357.
    PaxDbi P32357.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL074C ; YBL074C ; YBL074C .
    GeneIDi 852205.
    KEGGi sce:YBL074C.

    Organism-specific databases

    CYGDi YBL074c.
    SGDi S000000170. AAR2.

    Phylogenomic databases

    eggNOGi NOG331204.
    HOGENOMi HOG000033742.
    KOi K13205.
    OMAi YLDKSWY.
    OrthoDBi EOG7GTTGG.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28966-MONOMER.

    Miscellaneous databases

    NextBioi 970703.

    Gene expression databases

    Genevestigatori P32357.

    Family and domain databases

    InterProi IPR007946. AAR2.
    [Graphical view ]
    PANTHERi PTHR12689. PTHR12689. 1 hit.
    Pfami PF05282. AAR2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "AAR2, a gene for splicing pre-mRNA of the MATa1 cistron in cell type control of Saccharomyces cerevisiae."
      Nakazawa N., Harashima S., Oshima Y.
      Mol. Cell. Biol. 11:5693-5700(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "The two genes encoding yeast ribosomal protein S8 reside on different chromosomes, and are closely linked to the hsp70 stress protein genes SSA3 and SSA4."
      Logghe M., Molemans F., Fiers W., Contreras R.
      Yeast 10:1093-1100(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces cerevisiae."
      Boorstein W.R., Craig E.A.
      Mol. Cell. Biol. 10:3262-3267(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-355.
    6. "The yeast U5 snRNP coisolated with the U1 snRNP has an unexpected protein composition and includes the splicing factor Aar2p."
      Gottschalk A., Kastner B., Luhrmann R., Fabrizio P.
      RNA 7:1554-1565(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), INTERACTION WITH PRP8, PHOSPHORYLATION AT SER-253; THR-274; TYR-328; SER-331 AND THR-345, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-253.
    10. "Crystal structure of Prp8 reveals active site cavity of the spliceosome."
      Galej W.P., Oubridge C., Newman A.J., Nagai K.
      Nature 493:638-643(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PRP8, INTERACTION WITH PRP8.

    Entry informationi

    Entry nameiAAR2_YEAST
    AccessioniPrimary (citable) accession number: P32357
    Secondary accession number(s): D6VPS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7330 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3