Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20449

- DBP5_YEAST

UniProt

P20449 - DBP5_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. RNA binding Source: UniProtKB-KW
  4. RNA-dependent ATPase activity Source: SGD
  5. 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
Complete GO annotation...

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 pore Source: SGD
  4. nuclear pore cytoplasmic filaments Source: SGD
  5. nucleus Source: SGD
  6. polysome Source: SGD
Complete GO annotation...

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.
InParanoidiP20449.
KOiK01529.
OMAiDQCLRVK.
OrthoDBiEOG7FNCJ0.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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

        10         20         30         40         50
MSDTKRDPAD LLASLKIDNE KEDTSEVSTK ETVKSQPEKT ADSIKPAEKL
60 70 80 90 100
VPKVEEKKTK QEDSNLISSE YEVKVKLADI QADPNSPLYS AKSFDELGLA
110 120 130 140 150
PELLKGIYAM KFQKPSKIQE RALPLLLHNP PRNMIAQSQS GTGKTAAFSL
160 170 180 190 200
TMLTRVNPED ASPQAICLAP SRELARQTLE VVQEMGKFTK ITSQLIVPDS
210 220 230 240 250
FEKNKQINAQ VIVGTPGTVL DLMRRKLMQL QKIKIFVLDE ADNMLDQQGL
260 270 280 290 300
GDQCIRVKRF LPKDTQLVLF SATFADAVRQ YAKKIVPNAN TLELQTNEVN
310 320 330 340 350
VDAIKQLYMD CKNEADKFDV LTELYGLMTI GSSIIFVATK KTANVLYGKL
360 370 380 390 400
KSEGHEVSIL HGDLQTQERD RLIDDFREGR SKVLITTNVL ARGIDIPTVS
410 420 430 440 450
MVVNYDLPTL ANGQADPATY IHRIGRTGRF GRKGVAISFV HDKNSFNILS
460 470 480
AIQKYFGDIE MTRVPTDDWD EVEKIVKKVL KD
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.
InParanoidi P20449.
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. DEAD/DEAH_box_helicase_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 153 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