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P20449

- DBP5_YEAST

UniProt

P20449 - DBP5_YEAST

Protein

ATP-dependent RNA helicase DBP5

Gene

DBP5

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 152 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription.11 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi138 – 1458ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. protein binding Source: IntAct
    4. RNA binding Source: UniProtKB-KW
    5. RNA-dependent ATPase activity Source: SGD
    6. RNA helicase activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. mRNA export from nucleus Source: SGD
    3. protein transport Source: UniProtKB-KW
    4. translational termination Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33590-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase DBP5 (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 5
    Helicase CA5/6
    Ribonucleic acid-trafficking protein 8
    Gene namesi
    Name:DBP5
    Synonyms:RAT8
    Ordered Locus Names:YOR046C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR046c.
    SGDiS000005572. DBP5.

    Subcellular locationi

    Cytoplasm. Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Nuclear pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly and reversibly in response to ethanol stress.

    GO - Cellular componenti

    1. cellular bud tip Source: SGD
    2. cytoplasm Source: SGD
    3. nuclear membrane Source: UniProtKB-SubCell
    4. nuclear pore Source: SGD
    5. nuclear pore cytoplasmic filaments Source: SGD
    6. nucleus Source: SGD
    7. polysome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701P → H in RAT8-7; accumulates poly(A)+ RNA in the nucleus at 16 degrees Celsius. 1 Publication
    Mutagenesisi171 – 1711S → P in DBP5-2; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with L-236 and F-245. 1 Publication
    Mutagenesisi220 – 2201L → P in DBP5-1; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with S-466. 1 Publication
    Mutagenesisi236 – 2361F → L in DBP5-2; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with P-171 and F-245. 1 Publication
    Mutagenesisi267 – 2671L → P in RAT8-2; accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. 1 Publication
    Mutagenesisi345 – 3451V → F in DBP5-2; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with P-171 and L-236. 1 Publication
    Mutagenesisi385 – 3851I → D in RAT8-3; accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. 1 Publication
    Mutagenesisi466 – 4661T → S in DBP5-1; accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius; when associated with P-220. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482ATP-dependent RNA helicase DBP5PRO_0000055019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861Phosphoserine2 Publications
    Modified residuei93 – 931Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP20449.
    PaxDbiP20449.
    PeptideAtlasiP20449.

    Expressioni

    Gene expression databases

    GenevestigatoriP20449.

    Interactioni

    Subunit structurei

    Associates with the nuclear pore complex. Interacts with NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary for the association to the nuclear pore complex. Interacts also with the TFIIH complex subunits TFB1, TFB2 and RAD3.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GFD1Q048392EBI-5617,EBI-27549
    ZDS1P501113EBI-5617,EBI-29626

    Protein-protein interaction databases

    BioGridi34447. 181 interactions.
    DIPiDIP-2352N.
    IntActiP20449. 7 interactions.
    MINTiMINT-488024.
    STRINGi4932.YOR046C.

    Structurei

    Secondary structure

    1
    482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi78 – 803
    Helixi83 – 853
    Helixi87 – 904
    Helixi94 – 974
    Helixi101 – 1099
    Beta strandi110 – 1134
    Helixi117 – 12711
    Beta strandi128 – 1303
    Beta strandi134 – 1374
    Helixi144 – 15512
    Beta strandi165 – 1684
    Helixi172 – 18514
    Turni186 – 1883
    Beta strandi193 – 1975
    Beta strandi210 – 2145
    Helixi216 – 2249
    Beta strandi235 – 2395
    Helixi241 – 2466
    Helixi250 – 25910
    Turni261 – 2644
    Beta strandi266 – 2727
    Helixi276 – 28510
    Beta strandi290 – 2923
    Helixi296 – 2983
    Turni301 – 3033
    Beta strandi304 – 3107
    Helixi314 – 32512
    Turni326 – 3294
    Beta strandi330 – 3367
    Helixi340 – 35213
    Beta strandi358 – 3603
    Beta strandi362 – 3643
    Helixi366 – 37712
    Turni378 – 3803
    Beta strandi383 – 3864
    Helixi388 – 3903
    Beta strandi391 – 3933
    Beta strandi399 – 4068
    Beta strandi413 – 4153
    Helixi417 – 4248
    Helixi425 – 4273
    Beta strandi434 – 4407
    Helixi443 – 45513
    Turni456 – 4583
    Beta strandi462 – 4654
    Helixi469 – 48012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KBENMR-A71-296[»]
    2KBFNMR-A296-482[»]
    3GFPX-ray1.80A296-482[»]
    3PEUX-ray2.60A297-482[»]
    3PEVX-ray2.50A297-482[»]
    3PEWX-ray1.50A91-482[»]
    3PEYX-ray1.40A91-482[»]
    3RRMX-ray2.88A91-482[»]
    3RRNX-ray4.00A91-482[»]
    ProteinModelPortaliP20449.
    SMRiP20449. Positions 71-481.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20449.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 292168Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini303 – 480178Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi92 – 12029Q motifAdd
    BLAST
    Motifi239 – 2424DEAD box

    Domaini

    The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    GeneTreeiENSGT00530000063236.
    HOGENOMiHOG000268797.
    KOiK01529.
    OMAiDQCLRVK.
    OrthoDBiEOG7FNCJ0.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20449-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDTKRDPAD LLASLKIDNE KEDTSEVSTK ETVKSQPEKT ADSIKPAEKL    50
    VPKVEEKKTK QEDSNLISSE YEVKVKLADI QADPNSPLYS AKSFDELGLA 100
    PELLKGIYAM KFQKPSKIQE RALPLLLHNP PRNMIAQSQS GTGKTAAFSL 150
    TMLTRVNPED ASPQAICLAP SRELARQTLE VVQEMGKFTK ITSQLIVPDS 200
    FEKNKQINAQ VIVGTPGTVL DLMRRKLMQL QKIKIFVLDE ADNMLDQQGL 250
    GDQCIRVKRF LPKDTQLVLF SATFADAVRQ YAKKIVPNAN TLELQTNEVN 300
    VDAIKQLYMD CKNEADKFDV LTELYGLMTI GSSIIFVATK KTANVLYGKL 350
    KSEGHEVSIL HGDLQTQERD RLIDDFREGR SKVLITTNVL ARGIDIPTVS 400
    MVVNYDLPTL ANGQADPATY IHRIGRTGRF GRKGVAISFV HDKNSFNILS 450
    AIQKYFGDIE MTRVPTDDWD EVEKIVKKVL KD 482
    Length:482
    Mass (Da):53,874
    Last modified:October 1, 1996 - v2
    Checksum:iC50CAFE8C060D46B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28135 Genomic DNA. Translation: AAB01679.1.
    Z74954 Genomic DNA. Translation: CAA99237.1.
    Z74955 Genomic DNA. Translation: CAA99239.1.
    BK006948 Genomic DNA. Translation: DAA10828.1.
    PIRiS66920.
    RefSeqiNP_014689.1. NM_001183465.1.

    Genome annotation databases

    EnsemblFungiiYOR046C; YOR046C; YOR046C.
    GeneIDi854211.
    KEGGisce:YOR046C.

    Cross-referencesi

    Web resourcesi

    RNA helicases from the baker's yeast Saccharomyces cerevisiae

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28135 Genomic DNA. Translation: AAB01679.1 .
    Z74954 Genomic DNA. Translation: CAA99237.1 .
    Z74955 Genomic DNA. Translation: CAA99239.1 .
    BK006948 Genomic DNA. Translation: DAA10828.1 .
    PIRi S66920.
    RefSeqi NP_014689.1. NM_001183465.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KBE NMR - A 71-296 [» ]
    2KBF NMR - A 296-482 [» ]
    3GFP X-ray 1.80 A 296-482 [» ]
    3PEU X-ray 2.60 A 297-482 [» ]
    3PEV X-ray 2.50 A 297-482 [» ]
    3PEW X-ray 1.50 A 91-482 [» ]
    3PEY X-ray 1.40 A 91-482 [» ]
    3RRM X-ray 2.88 A 91-482 [» ]
    3RRN X-ray 4.00 A 91-482 [» ]
    ProteinModelPortali P20449.
    SMRi P20449. Positions 71-481.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34447. 181 interactions.
    DIPi DIP-2352N.
    IntActi P20449. 7 interactions.
    MINTi MINT-488024.
    STRINGi 4932.YOR046C.

    Proteomic databases

    MaxQBi P20449.
    PaxDbi P20449.
    PeptideAtlasi P20449.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR046C ; YOR046C ; YOR046C .
    GeneIDi 854211.
    KEGGi sce:YOR046C.

    Organism-specific databases

    CYGDi YOR046c.
    SGDi S000005572. DBP5.

    Phylogenomic databases

    eggNOGi COG0513.
    GeneTreei ENSGT00530000063236.
    HOGENOMi HOG000268797.
    KOi K01529.
    OMAi DQCLRVK.
    OrthoDBi EOG7FNCJ0.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33590-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P20449.
    NextBioi 976065.

    Gene expression databases

    Genevestigatori P20449.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Chang T.-H.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(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. "Identification of five putative yeast RNA helicase genes."
      Chang T.-H., Arenas J., Abelson J.
      Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-425.
    5. "Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export."
      Tseng S.S.-I., Weaver P.L., Liu Y., Hitomi M., Tartakoff A.M., Chang T.-H.
      EMBO J. 17:2651-2662(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-171; LEU-220; PHE-236; VAL-345 AND THR-466.
    6. "Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export."
      Snay-Hodge C.A., Colot H.V., Goldstein A.L., Cole C.N.
      EMBO J. 17:2663-2676(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-170; LEU-267 AND ILE-385.
    7. "Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p."
      Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P., Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., Izaurralde E.
      EMBO J. 18:4332-4347(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NUP159, ASSOCIATION WITH THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
    8. "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr255p."
      Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., Stutz F.
      EMBO J. 18:5761-5777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GLE1, SUBCELLULAR LOCATION, ASSOCIATION WITH THE NUCLEAR PORE COMPLEX.
    9. "Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells."
      Hodge C.A., Colot H.V., Stafford P., Cole C.N.
      EMBO J. 18:5778-5788(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NUP159 AND GLE1, ASSOCIATION WITH THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
    10. "Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause hyperadenylation during 3'-end formation of nascent transcripts."
      Hilleren P., Parker R.
      RNA 7:753-764(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: FUNCTION.
    12. "An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components."
      Estruch F., Cole C.N.
      Mol. Biol. Cell 14:1664-1676(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TFB1; TFB2 AND RAD3.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    15. "Stress response in yeast mRNA export factor: reversible changes in Rat8p localization are caused by ethanol stress but not heat shock."
      Takemura R., Inoue Y., Izawa S.
      J. Cell Sci. 117:4189-4197(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore."
      Weirich C.S., Erzberger J.P., Berger J.M., Weis K.
      Mol. Cell 16:749-760(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NUP159, SUBCELLULAR LOCATION.
    17. "Physical and genetic interactions link the yeast protein Zds1p with mRNA nuclear export."
      Estruch F., Hodge C.A., Rodriguez-Navarro S., Cole C.N.
      J. Biol. Chem. 280:9691-9697(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GFD1 AND ZDS1.
    18. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    19. "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-86 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDBP5_YEAST
    AccessioniPrimary (citable) accession number: P20449
    Secondary accession number(s): D6W2B2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 152 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 14900 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3