UniProtKB - P53550 (DCP2_YEAST)
m7GpppN-mRNA hydrolase
DCP2
Functioni
Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:10508173, PubMed:11139489, PubMed:11741542).
Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12554866).
Decapping is the major pathway of mRNA degradation in yeast and occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body (PubMed:10508173, PubMed:11139489, PubMed:11741542).
Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts (PubMed:19779198).
4 PublicationsMiscellaneous
Catalytic activityi
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H+ + N7-methyl-GDP1 PublicationEC:3.6.1.621 PublicationThis reaction proceeds in the forward1 Publication direction.
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 149 | ManganeseBy similarity | 1 | |
Metal bindingi | 153 | ManganeseBy similarity | 1 |
GO - Molecular functioni
- chromatin binding Source: SGD
- hydrolase activity Source: SGD
- m7G(5')pppN diphosphatase activity Source: SGD
- manganese ion binding Source: InterPro
- mRNA binding Source: SGD
GO - Biological processi
- deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
- deadenylation-independent decapping of nuclear-transcribed mRNA Source: ComplexPortal
- mRNA processing Source: UniProtKB-KW
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
- positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
- stress granule assembly Source: SGD
Keywordsi
Molecular function | Hydrolase, RNA-binding |
Biological process | mRNA processing, Nonsense-mediated mRNA decay |
Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.6.1.62, 984 |
Reactomei | R-SCE-430039, mRNA decay by 5' to 3' exoribonuclease R-SCE-450385, Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA R-SCE-450513, Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA |
Names & Taxonomyi
Protein namesi | Recommended name: m7GpppN-mRNA hydrolaseCurated (EC:3.6.1.621 Publication)Alternative name(s): Protein PSU1 mRNA-decapping enzyme subunit 21 Publication |
Gene namesi | Ordered Locus Names:YNL118CImported ORF Names:N1917 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000005062, DCP2 |
VEuPathDBi | FungiDB:YNL118C |
Subcellular locationi
Other locations
- P-body 1 Publication
Nucleus
- nucleus Source: SGD
Other locations
- cytoplasm Source: SGD
- cytoplasmic side of membrane Source: SGD
- Dcp1-Dcp2 complex Source: SGD
- P-body Source: SGD
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 60 | N → D in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with V-68 and V-142. 1 Publication | 1 | |
Mutagenesisi | 68 | I → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-142. 1 Publication | 1 | |
Mutagenesisi | 142 | D → V in DCP2-7; impairs mRNA decay at 37 degrees Celsius; when associated with D-60 and V-68. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000057054 | 1 – 970 | m7GpppN-mRNA hydrolaseAdd BLAST | 970 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 116 | PhosphoserineCombined sources | 1 | |
Modified residuei | 439 | PhosphoserineCombined sources | 1 | |
Modified residuei | 677 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 679 | PhosphoserineCombined sources | 1 | |
Modified residuei | 682 | PhosphoserineCombined sources | 1 | |
Modified residuei | 751 | PhosphoserineCombined sources | 1 | |
Modified residuei | 771 | PhosphoserineCombined sources | 1 | |
Modified residuei | 773 | PhosphoserineCombined sources | 1 | |
Modified residuei | 778 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | P53550 |
PaxDbi | P53550 |
PRIDEi | P53550 |
PTM databases
iPTMneti | P53550 |
Interactioni
Subunit structurei
Binary interactionsi
P53550
With | #Exp. | IntAct |
---|---|---|
DCP1 [Q12517] | 5 | EBI-270,EBI-38519 |
EDC3 [P39998] | 6 | EBI-270,EBI-22300 |
PAT1 [P25644] | 3 | EBI-270,EBI-204 |
Protein-protein interaction databases
BioGRIDi | 35708, 662 interactors |
ComplexPortali | CPX-1628, Decapping complex, DCP1-DCP2 |
DIPi | DIP-969N |
IntActi | P53550, 45 interactors |
MINTi | P53550 |
STRINGi | 4932.YNL118C |
Miscellaneous databases
RNActi | P53550, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P53550 |
BMRBi | P53550 |
SMRi | P53550 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P53550 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 101 – 228 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 128 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 302 – 341 | DisorderedSequence analysisAdd BLAST | 40 | |
Regioni | 417 – 465 | DisorderedSequence analysisAdd BLAST | 49 | |
Regioni | 501 – 520 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 528 – 692 | DisorderedSequence analysisAdd BLAST | 165 | |
Regioni | 831 – 867 | DisorderedSequence analysisAdd BLAST | 37 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 134 – 155 | Nudix boxAdd BLAST | 22 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 313 – 341 | Polar residuesSequence analysisAdd BLAST | 29 | |
Compositional biasi | 432 – 464 | Polar residuesSequence analysisAdd BLAST | 33 | |
Compositional biasi | 562 – 576 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 577 – 614 | Polar residuesSequence analysisAdd BLAST | 38 | |
Compositional biasi | 633 – 648 | Basic and acidic residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 649 – 663 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 665 – 679 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 840 – 867 | Polar residuesSequence analysisAdd BLAST | 28 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2937, Eukaryota |
GeneTreei | ENSGT00390000018878 |
HOGENOMi | CLU_009571_0_0_1 |
InParanoidi | P53550 |
OMAi | EPFANNK |
Family and domain databases
CDDi | cd03672, Dcp2p, 1 hit |
Gene3Di | 1.10.10.1050, 1 hit |
InterProi | View protein in InterPro IPR007722, DCP2_BoxA IPR036189, DCP2_BoxA_sf IPR044099, Dcp2_NUDIX IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF05026, DCP2, 1 hit PF00293, NUDIX, 1 hit |
SMARTi | View protein in SMART SM01125, DCP2, 1 hit |
SUPFAMi | SSF140586, SSF140586, 1 hit SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MSLPLRHALE NVTSVDRILE DLLVRFIINC PNEDLSSVER ELFHFEEASW
60 70 80 90 100
FYTDFIKLMN PTLPSLKIKS FAQLIIKLCP LVWKWDIRVD EALQQFSKYK
110 120 130 140 150
KSIPVRGAAI FNENLSKILL VQGTESDSWS FPRGKISKDE NDIDCCIREV
160 170 180 190 200
KEEIGFDLTD YIDDNQFIER NIQGKNYKIF LISGVSEVFN FKPQVRNEID
210 220 230 240 250
KIEWFDFKKI SKTMYKSNIK YYLINSMMRP LSMWLRHQRQ IKNEDQLKSY
260 270 280 290 300
AEEQLKLLLG ITKEEQIDPG RELLNMLHTA VQANSNNNAV SNGQVPSSQE
310 320 330 340 350
LQHLKEQSGE HNQQKDQQSS FSSQQQPSIF PSLSEPFANN KNVIPPTMPM
360 370 380 390 400
ANVFMSNPQL FATMNGQPFA PFPFMLPLTN NSNSANPIPT PVPPNFNAPP
410 420 430 440 450
NPMAFGVPNM HNLSGPAVSQ PFSLPPAPLP RDSGYSSSSP GQLLDILNSK
460 470 480 490 500
KPDSNVQSSK KPKLKILQRG TDLNSIKQNN NDETAHSNSQ ALLDLLKKPT
510 520 530 540 550
SSQKIHASKP DTSFLPNDSV SGIQDAEYED FESSSDEEVE TARDERNSLN
560 570 580 590 600
VDIGVNVMPS EKDSRRSQKE KPRNDASKTN LNASAESNSV EWGPGKSSPS
610 620 630 640 650
TQSKQNSSVG MQNKYRQEIH IGDSDAYEVF ESSSDEEDGK KLEELEQTQD
660 670 680 690 700
NSKLISQDIL KENNFQDGEV PHRDMPTESN KSINETVGLS STTNTVKKVP
710 720 730 740 750
KVKILKRGET FASLANDKKA FDSSSNVSSS KDLLQMLRNP ISSTVSSNQQ
760 770 780 790 800
SPKSQHLSGD EEIMMMLKRN SVSKPQNSEE NASTSSINDA NASELLGMLK
810 820 830 840 850
QKEKDITAPK QPYNVDSYSQ KNSAKGLLNI LKKNDSTGYP RTEGGPSSEM
860 870 880 890 900
STSMKRNDAT NNQELDKNST ELLNYLKPKP LNDGYENISN KDSSHELLNI
910 920 930 940 950
LHGNKNSSAF NNNVYATDGY SLASDNNENS SNKLLNMLQN RSSAINEPNF
960 970
DVRSNGTSGS NELLSILHRK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 425 | P → L in AAA68866 (Ref. 2) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 188 | V → A in strain: YJM339. 1 Publication | 1 | |
Natural varianti | 288 | Missing in strain: V1-09, YJM269, YJM270, YJM326, YJM339, YJM627 and YJM1129. 1 Publication | 1 | |
Natural varianti | 301 | L → H in strain: YJM280, YJM 20 and YJM339. 1 Publication | 1 | |
Natural varianti | 319 | S → P in strain: YJM627. 1 Publication | 1 | |
Natural varianti | 494 | D → N in strain: YJM339. 1 Publication | 1 | |
Natural varianti | 505 | I → T in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129. 1 Publication | 1 | |
Natural varianti | 522 | G → D in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 547 | N → T in strain: YJM280 and YJM320. 1 Publication | 1 | |
Natural varianti | 567 | S → R in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 574 | N → S in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 577 | S → N in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129. 1 Publication | 1 | |
Natural varianti | 622 | G → S in strain: V1-09 and YJM339. 1 Publication | 1 | |
Natural varianti | 650 | D → G in strain: YJM280 and YJM320. 1 Publication | 1 | |
Natural varianti | 740 | P → S in strain: YJM269 and YJM270. 1 Publication | 1 | |
Natural varianti | 807 | T → A in strain: YJM 69, YJM270, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 823 | S → P in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 835 | D → N in strain: YJM280 and YJM320. 1 Publication | 1 | |
Natural varianti | 844 | G → V in strain: V1-09. 1 Publication | 1 | |
Natural varianti | 851 | S → P in strain: YJM280, YJM320 and YJM627. 1 Publication | 1 | |
Natural varianti | 854 | M → I in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 864 | E → Q in strain: YJM269 and YJM270. 1 Publication | 1 | |
Natural varianti | 865 | L → S in strain: YJM269, YJM270, YJM326 and YJM1129. 1 Publication | 1 | |
Natural varianti | 866 | D → A in strain: YJM627. | 1 | |
Natural varianti | 909 | A → T in strain: YJM280 and YJM320. 1 Publication | 1 | |
Natural varianti | 945 | I → L in strain: YJM627. 1 Publication | 1 | |
Natural varianti | 951 | D → E in strain: V1-09. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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 |
Genome annotation databases
EnsemblFungii | YNL118C_mRNA; YNL118C; YNL118C |
GeneIDi | 855605 |
KEGGi | sce:YNL118C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
5LM5 | X-ray | 2.60 | C/D | 437-450 | [»] | |
5LMF | X-ray | 2.15 | C/D | 484-500 | [»] | |
5LMG | X-ray | 1.89 | C/D | 957-970 | [»] | |
6Y3Z | X-ray | 3.49 | A | 1-271 | [»] | |
AlphaFoldDBi | P53550 | |||||
BMRBi | P53550 | |||||
SMRi | P53550 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 35708, 662 interactors |
ComplexPortali | CPX-1628, Decapping complex, DCP1-DCP2 |
DIPi | DIP-969N |
IntActi | P53550, 45 interactors |
MINTi | P53550 |
STRINGi | 4932.YNL118C |
PTM databases
iPTMneti | P53550 |
Proteomic databases
MaxQBi | P53550 |
PaxDbi | P53550 |
PRIDEi | P53550 |
Genome annotation databases
EnsemblFungii | YNL118C_mRNA; YNL118C; YNL118C |
GeneIDi | 855605 |
KEGGi | sce:YNL118C |
Organism-specific databases
SGDi | S000005062, DCP2 |
VEuPathDBi | FungiDB:YNL118C |
Phylogenomic databases
eggNOGi | KOG2937, Eukaryota |
GeneTreei | ENSGT00390000018878 |
HOGENOMi | CLU_009571_0_0_1 |
InParanoidi | P53550 |
OMAi | EPFANNK |
Enzyme and pathway databases
BRENDAi | 3.6.1.62, 984 |
Reactomei | R-SCE-430039, mRNA decay by 5' to 3' exoribonuclease R-SCE-450385, Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA R-SCE-450513, Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA |
Miscellaneous databases
ChiTaRSi | DCP2, yeast |
EvolutionaryTracei | P53550 |
PROi | PR:P53550 |
RNActi | P53550, protein |
Family and domain databases
CDDi | cd03672, Dcp2p, 1 hit |
Gene3Di | 1.10.10.1050, 1 hit |
InterProi | View protein in InterPro IPR007722, DCP2_BoxA IPR036189, DCP2_BoxA_sf IPR044099, Dcp2_NUDIX IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF05026, DCP2, 1 hit PF00293, NUDIX, 1 hit |
SMARTi | View protein in SMART SM01125, DCP2, 1 hit |
SUPFAMi | SSF140586, SSF140586, 1 hit SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DCP2_YEAST | |
Accessioni | P53550Primary (citable) accession number: P53550 Secondary accession number(s): B0KZS6 Q6LCS6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | May 25, 2022 | |
This is version 194 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XIV
Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families