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P53196

- RPN14_YEAST

UniProt

P53196 - RPN14_YEAST

Protein

26S proteasome regulatory subunit RPN14

Gene

RPN14

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 116 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.4 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. proteasome regulatory particle assembly Source: SGD
    2. ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30528-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    26S proteasome regulatory subunit RPN14
    Alternative name(s):
    Proteasome non-ATPase subunit 14
    Gene namesi
    Name:RPN14
    Ordered Locus Names:YGL004C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL004c.
    SGDiS000002972. RPN14.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. nucleus Source: SGD
    3. proteasome complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 41741726S proteasome regulatory subunit RPN14PRO_0000051475Add
    BLAST

    Proteomic databases

    MaxQBiP53196.
    PaxDbiP53196.
    PeptideAtlasiP53196.

    Expressioni

    Gene expression databases

    GenevestigatoriP53196.

    Interactioni

    Subunit structurei

    Associates with the 19S proteasome regulatory particle (RP). Interacts directly with RPT5 and RPT6.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSM3P383486EBI-23691,EBI-21152
    NAS6P500864EBI-23691,EBI-14028
    RPT5P332974EBI-23691,EBI-13920
    RPT6Q019396EBI-23691,EBI-13914

    Protein-protein interaction databases

    BioGridi33241. 30 interactions.
    DIPiDIP-6617N.
    IntActiP53196. 23 interactions.
    MINTiMINT-675986.
    STRINGi4932.YGL004C.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi8 – 103
    Helixi14 – 196
    Beta strandi27 – 359
    Beta strandi38 – 458
    Turni49 – 513
    Beta strandi60 – 656
    Beta strandi68 – 736
    Beta strandi76 – 816
    Beta strandi84 – 863
    Turni87 – 904
    Beta strandi96 – 1027
    Beta strandi104 – 1063
    Beta strandi108 – 1136
    Beta strandi118 – 1214
    Beta strandi127 – 1315
    Beta strandi134 – 1374
    Beta strandi139 – 1446
    Beta strandi148 – 1558
    Beta strandi158 – 1647
    Turni165 – 1673
    Beta strandi172 – 1754
    Beta strandi181 – 1877
    Turni188 – 1914
    Beta strandi192 – 1976
    Beta strandi202 – 2065
    Turni207 – 2104
    Beta strandi211 – 2166
    Beta strandi226 – 2338
    Helixi240 – 2423
    Beta strandi257 – 2637
    Beta strandi268 – 2725
    Turni273 – 2753
    Beta strandi278 – 2825
    Beta strandi290 – 2956
    Beta strandi302 – 3076
    Beta strandi310 – 3167
    Beta strandi324 – 3307
    Beta strandi335 – 3417
    Beta strandi344 – 3496
    Turni350 – 3523
    Beta strandi353 – 3608
    Beta strandi366 – 3705
    Beta strandi376 – 3783
    Beta strandi387 – 3915
    Beta strandi394 – 3974
    Beta strandi399 – 4046
    Turni405 – 4073
    Beta strandi408 – 4147

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ACPX-ray2.00A1-417[»]
    3VL1X-ray1.60A/B1-417[»]
    ProteinModelPortaliP53196.
    SMRiP53196. Positions 1-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53196.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati134 – 17340WD 1Add
    BLAST
    Repeati176 – 21540WD 2Add
    BLAST
    Repeati242 – 28140WD 3Add
    BLAST
    Repeati285 – 32541WD 4Add
    BLAST
    Repeati330 – 37142WD 5Add
    BLAST
    Repeati380 – 41637WD 6Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat PAAF1/RPN14 family.Curated
    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00390000005948.
    HOGENOMiHOG000142386.
    KOiK11887.
    OMAiDESNGEV.
    OrthoDBiEOG7TBCBC.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 2 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 4 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53196-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKTITVAHI QYDFKAVLEE NDENDDEFYI NVDKNLNEIK EHKIVVLGNS    50
    RGVDAGKGNT FEKVGSHLYK ARLDGHDFLF NTIIRDGSKM LKRADYTAVD 100
    TAKLQMRRFI LGTTEGDIKV LDSNFNLQRE IDQAHVSEIT KLKFFPSGEA 150
    LISSSQDMQL KIWSVKDGSN PRTLIGHRAT VTDIAIIDRG RNVLSASLDG 200
    TIRLWECGTG TTIHTFNRKE NPHDGVNSIA LFVGTDRQLH EISTSKKNNL 250
    EFGTYGKYVI AGHVSGVITV HNVFSKEQTI QLPSKFTCSC NSLTVDGNNA 300
    NYIYAGYENG MLAQWDLRSP ECPVGEFLIN EGTPINNVYF AAGALFVSSG 350
    FDTSIKLDII SDPESERPAI EFETPTFLVS NDDEVSQFCY VSDDESNGEV 400
    LEVGKNNFCA LYNLSNP 417
    Length:417
    Mass (Da):46,383
    Last modified:October 1, 1996 - v1
    Checksum:i025CAB9A872E1AB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72526 Genomic DNA. Translation: CAA96704.1.
    AY692599 Genomic DNA. Translation: AAT92618.1.
    BK006941 Genomic DNA. Translation: DAA08095.1.
    PIRiS64006.
    RefSeqiNP_011511.3. NM_001180869.3.

    Genome annotation databases

    EnsemblFungiiYGL004C; YGL004C; YGL004C.
    GeneIDi852880.
    KEGGisce:YGL004C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72526 Genomic DNA. Translation: CAA96704.1 .
    AY692599 Genomic DNA. Translation: AAT92618.1 .
    BK006941 Genomic DNA. Translation: DAA08095.1 .
    PIRi S64006.
    RefSeqi NP_011511.3. NM_001180869.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ACP X-ray 2.00 A 1-417 [» ]
    3VL1 X-ray 1.60 A/B 1-417 [» ]
    ProteinModelPortali P53196.
    SMRi P53196. Positions 1-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33241. 30 interactions.
    DIPi DIP-6617N.
    IntActi P53196. 23 interactions.
    MINTi MINT-675986.
    STRINGi 4932.YGL004C.

    Proteomic databases

    MaxQBi P53196.
    PaxDbi P53196.
    PeptideAtlasi P53196.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL004C ; YGL004C ; YGL004C .
    GeneIDi 852880.
    KEGGi sce:YGL004C.

    Organism-specific databases

    CYGDi YGL004c.
    SGDi S000002972. RPN14.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00390000005948.
    HOGENOMi HOG000142386.
    KOi K11887.
    OMAi DESNGEV.
    OrthoDBi EOG7TBCBC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30528-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P53196.
    NextBioi 972523.

    Gene expression databases

    Genevestigatori P53196.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 2 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 4 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 2 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome."
      Seong K.M., Baek J.H., Yu M.H., Kim J.
      FEBS Lett. 581:2567-2573(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPT5.
    7. "Chaperone-mediated pathway of proteasome regulatory particle assembly."
      Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y., Lee B.H., Zhang F., Shi Y., Gygi S.P., Finley D.
      Nature 459:861-865(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE PROTEASOME REGULATORY PARTICLE.
    8. "Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base."
      Funakoshi M., Tomko R.J. Jr., Kobayashi H., Hochstrasser M.
      Cell 137:887-899(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE 19S REGULATORY PARTICLE OF THE PROTEASOME, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle."
      Saeki Y., Toh-E A., Kudo T., Kawamura H., Tanaka K.
      Cell 137:900-913(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE 19S REGULATORY PARTICLE OF THE PROTEASOME, INTERACTION WITH RPT6.

    Entry informationi

    Entry nameiRPN14_YEAST
    AccessioniPrimary (citable) accession number: P53196
    Secondary accession number(s): D6VUD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 116 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 2210 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3