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P53550

- DCP2_YEAST

UniProt

P53550 - DCP2_YEAST

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Protein

mRNA-decapping enzyme subunit 2

Gene
DCP2, PSU1, YNL118C, N1917
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.4 Publications

Cofactori

Manganese By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi149 – 1491Manganese By similarity
Metal bindingi153 – 1531Manganese By similarity

GO - Molecular functioni

  1. chromatin binding Source: SGD
  2. hydrolase activity Source: SGD
  3. m7G(5')pppN diphosphatase activity Source: SGD
  4. manganese ion binding Source: InterPro
  5. mRNA binding Source: SGD
  6. protein binding Source: IntAct

GO - Biological processi

  1. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  2. deadenylation-independent decapping of nuclear-transcribed mRNA Source: SGD
  3. mRNA processing Source: UniProtKB-KW
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  5. positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
  6. stress granule assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing, Nonsense-mediated mRNA decay

Keywords - Ligandi

Manganese, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33140-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme subunit 2 (EC:3.-.-.-)
Alternative name(s):
Protein PSU1
Gene namesi
Name:DCP2
Synonyms:PSU1
Ordered Locus Names:YNL118C
ORF Names:N1917
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL118c.
SGDiS000005062. DCP2.

Subcellular locationi

CytoplasmP-body
Note: Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. cytoplasmic mRNA processing body Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. 1 Publication
Mutagenesisi68 – 681I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. 1 Publication
Mutagenesisi142 – 1421D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 970970mRNA-decapping enzyme subunit 2PRO_0000057054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161Phosphoserine1 Publication
Modified residuei439 – 4391Phosphoserine1 Publication
Modified residuei677 – 6771Phosphothreonine1 Publication
Modified residuei679 – 6791Phosphoserine2 Publications
Modified residuei682 – 6821Phosphoserine2 Publications
Modified residuei751 – 7511Phosphoserine3 Publications
Modified residuei771 – 7711Phosphoserine1 Publication
Modified residuei773 – 7731Phosphoserine1 Publication
Modified residuei778 – 7781Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53550.
PeptideAtlasiP53550.

Expressioni

Gene expression databases

GenevestigatoriP53550.

Interactioni

Subunit structurei

Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNA, LSM2, LSM4 and LSM8. Interacts with EDC3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP1Q125175EBI-270,EBI-38519
EDC3P399987EBI-270,EBI-22300

Protein-protein interaction databases

BioGridi35708. 153 interactions.
DIPiDIP-969N.
IntActiP53550. 43 interactions.
MINTiMINT-385102.

Structurei

Secondary structure

1
970
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 1128
Beta strandi117 – 1259
Beta strandi132 – 1354
Beta strandi138 – 1403
Helixi142 – 15413
Turni159 – 1613
Beta strandi167 – 1726
Beta strandi175 – 18511
Beta strandi187 – 1893
Beta strandi194 – 20613
Helixi207 – 2137
Helixi214 – 2163
Beta strandi221 – 2233
Helixi224 – 2274
Helixi228 – 23710
Helixi242 – 2443

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JVBNMR-A100-245[»]
4K6EX-ray2.10A102-245[»]
4KG3X-ray1.70A/B/C100-245[»]
4KG4X-ray1.80A/B100-245[»]
ProteinModelPortaliP53550.
SMRiP53550. Positions 14-245.

Miscellaneous databases

EvolutionaryTraceiP53550.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 228128Nudix hydrolaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi134 – 15522Nudix boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi345 – 43086Pro-richAdd
BLAST
Compositional biasi436 – 4394Poly-Ser

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000018878.
KOiK12613.
OMAiPRNDASK.
OrthoDBiEOG7P5TBG.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53550-1 [UniParc]FASTAAdd to Basket

« Hide

MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW    50
FYTDFIKLMN PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK 100
KSIPVRGAAI FNENLSKILL VQGTESDSWS FPRGKISKDE NDIDCCIREV 150
KEEIGFDLTD YIDDNQFIER NIQGKNYKIF LISGVSEVFN FKPQVRNEID 200
KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ IKNEDQLKSY 250
AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE 300
LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM 350
ANVFMSNPQL FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP 400
NPMAFGVPNM HNLSGPAVSQ PFSLPPAPLP RDSGYSSSSP GQLLDILNSK 450
KPDSNVQSSK KPKLKILQRG TDLNSIKQNN NDETAHSNSQ ALLDLLKKPT 500
SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE TARDERNSLN 550
VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS 600
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD 650
NSKLISQDIL KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP 700
KVKILKRGET FASLANDKKA FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ 750
SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE NASTSSINDA NASELLGMLK 800
QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP RTEGGPSSEM 850
STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI 900
LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF 950
DVRSNGTSGS NELLSILHRK 970
Length:970
Mass (Da):108,667
Last modified:October 1, 1996 - v1
Checksum:iD53CA2C5A546FA4A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881V → A in strain: YJM339. 1 Publication
Natural varianti288 – 2881Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. 1 Publication
Natural varianti301 – 3011L → H in strain: YJM280, YJM 20 and YJM339. 1 Publication
Natural varianti319 – 3191S → P in strain: YJM627. 1 Publication
Natural varianti494 – 4941D → N in strain: YJM339. 1 Publication
Natural varianti505 – 5051I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. 1 Publication
Natural varianti522 – 5221G → D in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
Natural varianti547 – 5471N → T in strain: YJM280 and YJM320. 1 Publication
Natural varianti567 – 5671S → R in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
Natural varianti574 – 5741N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication
Natural varianti577 – 5771S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. 1 Publication
Natural varianti622 – 6221G → S in strain: V1-09 and YJM339. 1 Publication
Natural varianti650 – 6501D → G in strain: YJM280 and YJM320. 1 Publication
Natural varianti740 – 7401P → S in strain: YJM269 and YJM270. 1 Publication
Natural varianti807 – 8071T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. 1 Publication
Natural varianti823 – 8231S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication
Natural varianti835 – 8351D → N in strain: YJM280 and YJM320. 1 Publication
Natural varianti844 – 8441G → V in strain: V1-09. 1 Publication
Natural varianti851 – 8511S → P in strain: YJM280, YJM320 and YJM627. 1 Publication
Natural varianti854 – 8541M → I in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
Natural varianti864 – 8641E → Q in strain: YJM269 and YJM270. 1 Publication
Natural varianti865 – 8651L → S in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication
Natural varianti866 – 8661D → A in strain: YJM627.
Natural varianti909 – 9091A → T in strain: YJM280 and YJM320. 1 Publication
Natural varianti945 – 9451I → L in strain: YJM627. 1 Publication
Natural varianti951 – 9511D → E in strain: V1-09. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti425 – 4251P → L in AAA68866. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31377 Genomic DNA. Translation: AAC99860.1.
L43065 Genomic DNA. Translation: AAA68866.1.
EF125216 Genomic DNA. Translation: ABN58539.1.
EF125217 Genomic DNA. Translation: ABN58548.1.
EF125218 Genomic DNA. Translation: ABN58557.1.
EF125219 Genomic DNA. Translation: ABN58566.1.
EF125220 Genomic DNA. Translation: ABN58578.1.
EF125221 Genomic DNA. Translation: ABN58584.1.
EF125222 Genomic DNA. Translation: ABN58593.1.
EF125223 Genomic DNA. Translation: ABN58602.1.
EF125224 Genomic DNA. Translation: ABN58611.1.
EF125225 Genomic DNA. Translation: ABN58620.1.
EF125226 Genomic DNA. Translation: ABN58629.1.
EF125228 Genomic DNA. Translation: ABN58647.1.
Z69382 Genomic DNA. Translation: CAA93389.1.
Z71394 Genomic DNA. Translation: CAA95998.1.
BK006947 Genomic DNA. Translation: DAA10430.1.
PIRiS63059.
RefSeqiNP_014281.1. NM_001182956.1.

Genome annotation databases

EnsemblFungiiYNL118C; YNL118C; YNL118C.
GeneIDi855605.
KEGGisce:YNL118C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31377 Genomic DNA. Translation: AAC99860.1 .
L43065 Genomic DNA. Translation: AAA68866.1 .
EF125216 Genomic DNA. Translation: ABN58539.1 .
EF125217 Genomic DNA. Translation: ABN58548.1 .
EF125218 Genomic DNA. Translation: ABN58557.1 .
EF125219 Genomic DNA. Translation: ABN58566.1 .
EF125220 Genomic DNA. Translation: ABN58578.1 .
EF125221 Genomic DNA. Translation: ABN58584.1 .
EF125222 Genomic DNA. Translation: ABN58593.1 .
EF125223 Genomic DNA. Translation: ABN58602.1 .
EF125224 Genomic DNA. Translation: ABN58611.1 .
EF125225 Genomic DNA. Translation: ABN58620.1 .
EF125226 Genomic DNA. Translation: ABN58629.1 .
EF125228 Genomic DNA. Translation: ABN58647.1 .
Z69382 Genomic DNA. Translation: CAA93389.1 .
Z71394 Genomic DNA. Translation: CAA95998.1 .
BK006947 Genomic DNA. Translation: DAA10430.1 .
PIRi S63059.
RefSeqi NP_014281.1. NM_001182956.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JVB NMR - A 100-245 [» ]
4K6E X-ray 2.10 A 102-245 [» ]
4KG3 X-ray 1.70 A/B/C 100-245 [» ]
4KG4 X-ray 1.80 A/B 100-245 [» ]
ProteinModelPortali P53550.
SMRi P53550. Positions 14-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35708. 153 interactions.
DIPi DIP-969N.
IntActi P53550. 43 interactions.
MINTi MINT-385102.

Proteomic databases

MaxQBi P53550.
PeptideAtlasi P53550.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL118C ; YNL118C ; YNL118C .
GeneIDi 855605.
KEGGi sce:YNL118C.

Organism-specific databases

CYGDi YNL118c.
SGDi S000005062. DCP2.

Phylogenomic databases

GeneTreei ENSGT00390000018878.
KOi K12613.
OMAi PRNDASK.
OrthoDBi EOG7P5TBG.

Enzyme and pathway databases

BioCyci YEAST:G3O-33140-MONOMER.

Miscellaneous databases

EvolutionaryTracei P53550.
NextBioi 979774.

Gene expression databases

Genevestigatori P53550.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
Pfami PF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view ]
SUPFAMi SSF55811. SSF55811. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen."
    He F., Jacobson A.
    Genes Dev. 9:437-454(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Tzagoloff A.A.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24657 / D273-10B.
  3. "Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast."
    Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M.
    Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-188; ASN-288 DEL; HIS-301; PRO-319; ASN-494; THR-505; ASP-522; THR-547; ARG-567; SER-574; ASN-577; SER-622; GLY-650; SER-740; ALA-807; PRO-823; ASN-835; VAL-844; PRO-851; ILE-854; GLN-864; SER-865; THR-909; LEU-945 AND GLU-951.
    Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230.
  4. "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames."
    de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G.
    Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "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-679 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Crystal structure of human Edc3 and its functional implications."
    Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.
    Mol. Cell. Biol. 28:5965-5976(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDC3.
  8. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  9. "The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif."
    Dunckley T., Parker R.
    EMBO J. 18:5411-5422(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCP1.
  10. "Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins."
    Fromont-Racine M., Mayes A.E., Brunet-Simon A., Rain J.-C., Colley A., Dix I., Decourty L., Joly N., Ricard F., Beggs J.D., Legrain P.
    Yeast 17:95-110(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSM2; LSM4 AND LSM8.
  11. "Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae."
    Dunckley T., Tucker M., Parker R.
    Genetics 157:27-37(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-60; ILE-68 AND ASP-142, INTERACTION WITH EDC1.
  12. "Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
    Tharun S., Parker R.
    Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MRNA, FUNCTION OF THE DCP1-DCP2 COMPLEX.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. Cited for: FUNCTION OF THE DCP1-DCP2 COMPLEX.
  15. "Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
    Sheth U., Parker R.
    Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Crystal structure of Dcp1p and its functional implications in mRNA decapping."
    She M., Decker C.J., Sundramurthy K., Liu Y., Chen N., Parker R., Song H.
    Nat. Struct. Mol. Biol. 11:249-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCP1.
  17. "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-116; SER-682 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-439; THR-677; SER-679; SER-682; SER-751; SER-771; SER-773 AND SER-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: STRUCTURE BY NMR OF 100-245.

Entry informationi

Entry nameiDCP2_YEAST
AccessioniPrimary (citable) accession number: P53550
Secondary accession number(s): B0KZS6
, B0KZU4, B0KZW2, B0KZY0, B0KZY9, B0KZZ8, B0L007, D6W164, Q6LCS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 137 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 8530 molecules/cell in log phase SD medium.

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

External Data

Dasty 3

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