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Protein

mRNA-decapping enzyme subunit 1

Gene

DCP1

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

Functioni

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. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA.16 Publications

GO - Molecular functioni

  • enzyme activator activity Source: SGD
  • mRNA binding Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33539-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-decapping enzyme subunit 1
Gene namesi
Name:DCP1
Ordered Locus Names:YOL149W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL149W.
SGDiS000005509. DCP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • cytoplasmic side of membrane Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16 – 20EFYRK → AFYAA in DCP1-17; partial loss of mRNA-decapping activity. 1 Publication5
Mutagenesisi29 – 31RYD → AYA in DCP1-2; strong loss of mRNA decapping activity at 36 degrees Celsius. 2 Publications3
Mutagenesisi32 – 34PKI → AKA: Partial loss of mRNA-decapping activity. 1 Publication3
Mutagenesisi37 – 38LL → AA: Strong loss of mRNA-decapping activity; when associated with A-217 and A-221. 1 Publication2
Mutagenesisi47Y → A in DCP1-32; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi47Y → F in DCP1-35; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi48 – 50KWD → AWA in DCP1-4; partial loss of mRNA decapping activity. In DCP1-43; strong loss of mRNA-decapping activity; when associated with A-187 and A-188. In DCP1-44; strong loss of mRNA-decapping activity; when associated with A-216 and A-219. 1 Publication3
Mutagenesisi56W → A in DCP1-31; partial loss of mRNA decapping activity. 3 Publications1
Mutagenesisi70R → A in DCP1-33; strong loss of mRNA decapping activity. 2 Publications1
Mutagenesisi156G → D in DCP1-1; strong loss of mRNA decapping activity. 1 Publication1
Mutagenesisi187 – 188KD → AA in DCP1-19; partial loss of mRNA decapping activity. In DCP1-43; strong loss of mRNA-decapping activity; when associated with A-48 and A-50. 1 Publication2
Mutagenesisi204W → A in DCP1-33; partial loss of mRNA decapping activity. 1 Publication1
Mutagenesisi216 – 219ELIK → ALIA in DCP1-25; partial loss of mRNA-decapping activity. In DCP1-44; strong loss of mRNA-decapping activity; when associated with A-48 and A-50. 1 Publication4
Mutagenesisi217L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-221. 1 Publication1
Mutagenesisi221L → A: Strong loss of mRNA-decapping activity; when associated with A-37; A-38 and A-217. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002329981 – 231mRNA-decapping enzyme subunit 1Add BLAST231

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12517.
PRIDEiQ12517.

Interactioni

Subunit structurei

Component of the decapping complex composed of DCP1 and DCP2. Interacts with mRNAs, DHH1, LSM1, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, and the cap-binding proteins PAB1 and TIF4632/eIF-4G.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP2P535505EBI-38519,EBI-270
EDC3P399985EBI-38519,EBI-22300
RPS28BP0C0X03EBI-38519,EBI-16112

Protein-protein interaction databases

BioGridi34268. 67 interactors.
DIPiDIP-1288N.
IntActiQ12517. 24 interactors.
MINTiMINT-390330.

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 30Combined sources7
Beta strandi34 – 50Combined sources17
Turni51 – 54Combined sources4
Beta strandi55 – 70Combined sources16
Beta strandi139 – 150Combined sources12
Beta strandi152 – 157Combined sources6
Helixi160 – 169Combined sources10
Helixi171 – 176Combined sources6
Beta strandi183 – 187Combined sources5
Beta strandi190 – 194Combined sources5
Beta strandi200 – 207Combined sources8
Helixi208 – 223Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q67X-ray2.30A/B1-231[»]
ProteinModelPortaliQ12517.
SMRiQ12517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12517.

Family & Domainsi

Sequence similaritiesi

Belongs to the DCP1 family.Curated

Phylogenomic databases

HOGENOMiHOG000246588.
InParanoidiQ12517.
KOiK12612.
OMAiKQLLFHT.
OrthoDBiEOG092C4W9A.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR010334. Dcp1.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 3 hits.
PfamiPF06058. DCP1. 2 hits.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGAATAAEN SATQLEFYRK ALNFNVIGRY DPKIKQLLFH TPHASLYKWD
60 70 80 90 100
FKKDEWNKLE YQGVLAIYLR DVSQNTNLLP VSPQEVDIFD SQNGSNNIQV
110 120 130 140 150
NNGSDNSNRN SSGNGNSYKS NDSLTYNCGK TLSGKDIYNY GLIILNRINP
160 170 180 190 200
DNFSMGIVPN SVVNKRKVFN AEEDTLNPLE CMGVEVKDEL VIIKNLKHEV
210 220 230
YGIWIHTVSD RQNIYELIKY LLENEPKDSF A
Length:231
Mass (Da):26,266
Last modified:November 1, 1996 - v1
Checksum:i8456B1C96C121C4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48239 Genomic DNA. Translation: CAA88278.1.
Z74891 Genomic DNA. Translation: CAA99170.1.
AY558431 Genomic DNA. Translation: AAS56757.1.
BK006948 Genomic DNA. Translation: DAA10636.1.
PIRiS60387.
RefSeqiNP_014492.1. NM_001183403.1.

Genome annotation databases

EnsemblFungiiYOL149W; YOL149W; YOL149W.
GeneIDi854016.
KEGGisce:YOL149W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48239 Genomic DNA. Translation: CAA88278.1.
Z74891 Genomic DNA. Translation: CAA99170.1.
AY558431 Genomic DNA. Translation: AAS56757.1.
BK006948 Genomic DNA. Translation: DAA10636.1.
PIRiS60387.
RefSeqiNP_014492.1. NM_001183403.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q67X-ray2.30A/B1-231[»]
ProteinModelPortaliQ12517.
SMRiQ12517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34268. 67 interactors.
DIPiDIP-1288N.
IntActiQ12517. 24 interactors.
MINTiMINT-390330.

Proteomic databases

MaxQBiQ12517.
PRIDEiQ12517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL149W; YOL149W; YOL149W.
GeneIDi854016.
KEGGisce:YOL149W.

Organism-specific databases

EuPathDBiFungiDB:YOL149W.
SGDiS000005509. DCP1.

Phylogenomic databases

HOGENOMiHOG000246588.
InParanoidiQ12517.
KOiK12612.
OMAiKQLLFHT.
OrthoDBiEOG092C4W9A.

Enzyme and pathway databases

BioCyciYEAST:G3O-33539-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12517.
PROiQ12517.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR010334. Dcp1.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16290. PTHR16290. 3 hits.
PfamiPF06058. DCP1. 2 hits.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCP1_YEAST
AccessioniPrimary (citable) accession number: Q12517
Secondary accession number(s): D6W1S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 126 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 2880 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.