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Protein

m7GpppN-mRNA hydrolase

Gene

Dcp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety.1 Publication

Catalytic activityi

5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA) + H2O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).

Cofactori

Mn2+By similarity, Mg2+By similarityNote: Mn2+ ion is required for highest activity. Can also utilize magnesium ions.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi144 – 1441ManganeseBy similarity
Metal bindingi148 – 1481ManganeseBy similarity

GO - Molecular functioni

  1. m7G(5')pppN diphosphatase activity Source: UniProtKB
  2. manganese ion binding Source: InterPro
  3. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. histone mRNA catabolic process Source: UniProtKB
  2. mRNA catabolic process Source: UniProtKB
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nonsense-mediated mRNA decay

Keywords - Ligandi

Manganese, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.
REACT_261877. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
m7GpppN-mRNA hydrolase (EC:3.6.1.62)
Alternative name(s):
mRNA-decapping enzyme 2
Gene namesi
Name:Dcp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1917890. Dcp2.

Subcellular locationi

CytoplasmP-body By similarity. Nucleus By similarity
Note: Predominantly cytoplasmic, in processing bodies (PB). A minor amount is nuclear (By similarity).By similarity

GO - Cellular componenti

  1. cell junction Source: MGI
  2. cytoplasmic mRNA processing body Source: MGI
  3. intracellular membrane-bounded organelle Source: MGI
  4. nucleoplasm Source: MGI
  5. RISC complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422m7GpppN-mRNA hydrolasePRO_0000057052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei276 – 2761PhosphoserineBy similarity
Modified residuei284 – 2841PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CYC6.
PaxDbiQ9CYC6.
PRIDEiQ9CYC6.

PTM databases

PhosphoSiteiQ9CYC6.

Expressioni

Tissue specificityi

Strongly expressed in brain and testis. Weakly expressed in lung. Not detected in heart, liver, kidney and muscle (at protein level).1 Publication

Developmental stagei

Strongly expressed in brain, heart, liver at 14.5 and 16.5 dpc. Strongly expressed in brain at 20 dpc. Weakly expressed in heart and liver at 20 dpc (at protein level).1 Publication

Gene expression databases

BgeeiQ9CYC6.
CleanExiMM_DCP2.
GenevestigatoriQ9CYC6.

Interactioni

Subunit structurei

Found in a mRNA decay complex with LSM1, LSM3, LSM4, EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B. Forms a complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex directly interacts with EDC4/HEDLS. Interacts with DPC1B, UPF1, UPF2 and UPF3B. Associates with polysomes. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus) (By similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with DDX17 in an RNA-dependent manner (By similarity). Interacts with ZC3HAV1 (By similarity). Interacts with APOBEC3G in an RNA-dependent manner (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025350.

Structurei

3D structure databases

ProteinModelPortaliQ9CYC6.
SMRiQ9CYC6. Positions 12-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 226132Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi129 – 15022Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family. DCP2 subfamily.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00390000018878.
HOGENOMiHOG000005974.
HOVERGENiHBG051321.
InParanoidiQ9CYC6.
KOiK12613.
OMAiVHSQPAK.
OrthoDBiEOG7XM2XP.
TreeFamiTF314180.

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.

Q9CYC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPKRLEIPG SVLDDLCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY
60 70 80 90 100
MQNTPGLPQC GIRDFAKAVF SHCPFLLPQG EDVEKILDEW KEYKMGVPTY
110 120 130 140 150
GAIILDETLE NVLLVQGYLA KSGWGFPKGK VNKEEAPHDC AAREVFEETG
160 170 180 190 200
FDIKDYICKD DYIELRINDQ LARLYIIPGV PKDTKFNPKT RREIRNIEWF
210 220 230 240 250
SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS RRFGDSSDSD
260 270 280 290 300
NGFSSAGSTP ARPTVEKLSR TKFRHSQQLF PEGSPSDQWV KHRQPLQQKS
310 320 330 340 350
HSNHGEVSDL LKAKNQNMRG NGRKQYQDSP NQKKRANGVH GQPAKQQNPL
360 370 380 390 400
VKCEKKLHPR KLQDNFETDA TCDLPCSGEE PSVEHAEGHS VACNGHCKFP
410 420
FSSRAFLSFK FDQNAIMKIL DL
Length:422
Mass (Da):48,380
Last modified:July 27, 2011 - v2
Checksum:i80FE791B05E4C8FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261F → Y in BAB30946 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017809 mRNA. Translation: BAB30946.1.
AK166560 mRNA. Translation: BAE38853.1.
CCDSiCCDS50275.1.
RefSeqiNP_081766.1. NM_027490.1.
UniGeneiMm.87629.

Genome annotation databases

EnsembliENSMUST00000025350; ENSMUSP00000025350; ENSMUSG00000024472.
GeneIDi70640.
KEGGimmu:70640.
UCSCiuc008eux.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017809 mRNA. Translation: BAB30946.1.
AK166560 mRNA. Translation: BAE38853.1.
CCDSiCCDS50275.1.
RefSeqiNP_081766.1. NM_027490.1.
UniGeneiMm.87629.

3D structure databases

ProteinModelPortaliQ9CYC6.
SMRiQ9CYC6. Positions 12-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025350.

PTM databases

PhosphoSiteiQ9CYC6.

Proteomic databases

MaxQBiQ9CYC6.
PaxDbiQ9CYC6.
PRIDEiQ9CYC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025350; ENSMUSP00000025350; ENSMUSG00000024472.
GeneIDi70640.
KEGGimmu:70640.
UCSCiuc008eux.2. mouse.

Organism-specific databases

CTDi167227.
MGIiMGI:1917890. Dcp2.

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00390000018878.
HOGENOMiHOG000005974.
HOVERGENiHBG051321.
InParanoidiQ9CYC6.
KOiK12613.
OMAiVHSQPAK.
OrthoDBiEOG7XM2XP.
TreeFamiTF314180.

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.
REACT_261877. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

NextBioi332021.
PROiQ9CYC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CYC6.
CleanExiMM_DCP2.
GenevestigatoriQ9CYC6.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. "Multiple mRNA decapping enzymes in mammalian cells."
    Song M.G., Li Y., Kiledjian M.
    Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A DECAPPING ENZYME, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiDCP2_MOUSE
AccessioniPrimary (citable) accession number: Q9CYC6
Secondary accession number(s): Q3TLD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.