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P50085

- PHB2_YEAST

UniProt

P50085 - PHB2_YEAST

Protein

Prohibitin-2

Gene

PHB2

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 118 (01 Oct 2014)
      Sequence version 2 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. mitochondrion inheritance Source: SGD
    2. negative regulation of proteolysis Source: SGD
    3. protein folding Source: SGD
    4. replicative cell aging Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30909-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prohibitin-2
    Gene namesi
    Name:PHB2
    Ordered Locus Names:YGR231C
    ORF Names:G8561
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR231c.
    SGDiS000003463. PHB2.

    Subcellular locationi

    Mitochondrion inner membrane 3 Publications; Single-pass type II membrane protein 3 Publications; Intermembrane side 3 Publications

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: SGD
    3. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 310310Prohibitin-2PRO_0000213888Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    MaxQBiP50085.
    PaxDbiP50085.
    PeptideAtlasiP50085.
    PRIDEiP50085.

    Expressioni

    Gene expression databases

    GenevestigatoriP50085.

    Interactioni

    Subunit structurei

    The mitochondrial prohibitin complex consists of two subunits (PHB1 and PHB2), assembled into a membrane-associated ring-shaped supercomplex of approximately 1 mDa.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PHB1P409613EBI-23530,EBI-13360

    Protein-protein interaction databases

    BioGridi33483. 164 interactions.
    IntActiP50085. 41 interactions.
    MINTiMINT-2734711.
    STRINGi4932.YGR231C.

    Structurei

    3D structure databases

    ProteinModelPortaliP50085.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei38 – 5821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili212 – 253421 PublicationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the prohibitin family.Curated

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0330.
    GeneTreeiENSGT00550000075076.
    HOGENOMiHOG000205692.
    KOiK17081.
    OMAiTYMTFSP.
    OrthoDBiEOG7BS4MS.

    Family and domain databases

    InterProiIPR001107. Band_7.
    IPR000163. Prohibitin.
    [Graphical view]
    PANTHERiPTHR23222. PTHR23222. 1 hit.
    PfamiPF01145. Band_7. 1 hit.
    [Graphical view]
    PRINTSiPR00679. PROHIBITIN.
    SMARTiSM00244. PHB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50085-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNRSPGEFQR YAKAFQKQLS KVQQTGGRGQ VPSPRGAFAG LGGLLLLGGG    50
    ALFINNALFN VDGGHRAIVY SRIHGVSSRI FNEGTHFIFP WLDTPIIYDV 100
    RAKPRNVASL TGTKDLQMVN ITCRVLSRPD VVQLPTIYRT LGQDYDERVL 150
    PSIVNEVLKA VVAQFNASQL ITQREKVSRL IRENLVRRAS KFNILLDDVS 200
    ITYMTFSPEF TNAVEAKQIA QQDAQRAAFV VDKARQEKQG MVVRAQGEAK 250
    SAELIGEAIK KSRDYVELKR LDTARDIAKI LASSPNRVIL DNEALLLNTV 300
    VDARIDGRGK 310
    Length:310
    Mass (Da):34,407
    Last modified:October 3, 2006 - v2
    Checksum:i3526D9690F39B493
    GO

    Sequence cautioni

    The sequence CAA61181.1 differs from that shown. Reason: Frameshift at position 310.
    The sequence CAA97259.1 differs from that shown. Reason: Frameshift at position 310.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87941 Genomic DNA. Translation: CAA61181.1. Frameshift.
    Z73016 Genomic DNA. Translation: CAA97259.1. Frameshift.
    BK006941 Genomic DNA. Translation: DAA08322.1.
    PIRiS57696.
    RefSeqiNP_011747.2. NM_001181360.1.

    Genome annotation databases

    EnsemblFungiiYGR231C; YGR231C; YGR231C.
    GeneIDi853146.
    KEGGisce:YGR231C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87941 Genomic DNA. Translation: CAA61181.1 . Frameshift.
    Z73016 Genomic DNA. Translation: CAA97259.1 . Frameshift.
    BK006941 Genomic DNA. Translation: DAA08322.1 .
    PIRi S57696.
    RefSeqi NP_011747.2. NM_001181360.1.

    3D structure databases

    ProteinModelPortali P50085.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33483. 164 interactions.
    IntActi P50085. 41 interactions.
    MINTi MINT-2734711.
    STRINGi 4932.YGR231C.

    Proteomic databases

    MaxQBi P50085.
    PaxDbi P50085.
    PeptideAtlasi P50085.
    PRIDEi P50085.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR231C ; YGR231C ; YGR231C .
    GeneIDi 853146.
    KEGGi sce:YGR231C.

    Organism-specific databases

    CYGDi YGR231c.
    SGDi S000003463. PHB2.

    Phylogenomic databases

    eggNOGi COG0330.
    GeneTreei ENSGT00550000075076.
    HOGENOMi HOG000205692.
    KOi K17081.
    OMAi TYMTFSP.
    OrthoDBi EOG7BS4MS.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30909-MONOMER.

    Miscellaneous databases

    NextBioi 973222.
    PROi P50085.

    Gene expression databases

    Genevestigatori P50085.

    Family and domain databases

    InterProi IPR001107. Band_7.
    IPR000163. Prohibitin.
    [Graphical view ]
    PANTHERi PTHR23222. PTHR23222. 1 hit.
    Pfami PF01145. Band_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00679. PROHIBITIN.
    SMARTi SM00244. PHB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII."
      van der Aart Q.J.M., Kleine K., Steensma H.Y.
      Yeast 12:385-390(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins."
      Nijtmans L.G.J., de Jong L., Artal-Sanz M., Coates P.J., Berden J.A., Back J.W., Muijsers A.O., van der Spek H., Grivell L.A.
      EMBO J. 19:2444-2451(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    5. "A structure for the yeast prohibitin complex: structure prediction and evidence from chemical crosslinking and mass spectrometry."
      Back J.W., Artal-Sanz M., De Jong L., De Koning L.J., Nijtmans L.G.J., De Koster C.G., Grivell L.A., Van Der Spek H., Muijsers A.O.
      Protein Sci. 11:2471-2478(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    6. "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.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    10. "Formation of membrane-bound ring complexes by prohibitins in mitochondria."
      Tatsuta T., Model K., Langer T.
      Mol. Biol. Cell 16:248-259(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SINGLE PARTICLE ELECTRON MICROSCOPY, COILED-COIL DOMAIN.

    Entry informationi

    Entry nameiPHB2_YEAST
    AccessioniPrimary (citable) accession number: P50085
    Secondary accession number(s): D6VV11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2850 molecules/cell in log phase SD medium.1 Publication
    Mitochondrial targeting of PHB2 is ensured by a bipartite non-cleavable presequence at the N-terminus.

    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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3