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Q8IU60 (DCP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
m7GpppN-mRNA hydrolase

EC=3.6.1.62
Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 20
Short name=Nudix motif 20
mRNA-decapping enzyme 2
Short name=hDpc
Gene names
Name:DCP2
Synonyms:NUDT20
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.6 Ref.8 Ref.9 Ref.17 Ref.20

Catalytic activity

5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA) + H2O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA). Ref.6 Ref.20

Cofactor

Manganese. Required for highest activity. Can also utilize magnesium ions. Ref.9

Subunit structure

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. Interacts (via N-terminus and C-terminus) with TRIM21 (via N-terminus and C-terminus). Associates with polysomes. Interacts with LIMD1, WTIP and AJUBA. Interacts with DDX17 in an RNA-dependent manner. Interacts with ZC3HAV1. Interacts with APOBEC3G in an RNA-dependent manner. Ref.1 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.21 Ref.23

Subcellular location

CytoplasmP-body. Nucleus. Note: Predominantly cytoplasmic, in processing bodies (PB). A minor amount is nuclear. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.21

Tissue specificity

Expressed in brain and testis. Not detected in heart (at protein level). Ref.20

Sequence similarities

Belongs to the Nudix hydrolase family. DCP2 subfamily.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandManganese
Metal-binding
RNA-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, exonucleolytic

Traceable author statement. Source: GOC

exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histone mRNA catabolic process

Inferred from mutant phenotype Ref.17. Source: UniProtKB

mRNA catabolic process

Inferred from direct assay Ref.20. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype PubMed 22890540. Source: UniProtKB

   Cellular_componentRISC complex

Inferred from direct assay Ref.21. Source: MGI

cytoplasmic mRNA processing body

Inferred from direct assay Ref.21. Source: MGI

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

exoribonuclease activity, producing 5'-phosphomonoesters

Traceable author statement. Source: Reactome

m7G(5')pppN diphosphatase activity

Inferred from direct assay Ref.20. Source: UniProtKB

manganese ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.14PubMed 20543818PubMed 20584987Ref.21Ref.23. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IU60-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8IU60-2)

The sequence of this isoform differs from the canonical sequence as follows:
     315-349: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420m7GpppN-mRNA hydrolase
PRO_0000057051

Regions

Domain95 – 226132Nudix hydrolase
Motif129 – 15022Nudix box

Sites

Metal binding1441Manganese By similarity
Metal binding1481Manganese By similarity

Amino acid modifications

Modified residue2461Phosphoserine Ref.18 Ref.24
Modified residue2471Phosphoserine Ref.18 Ref.24
Modified residue2491Phosphoserine Ref.18 Ref.24
Modified residue2761Phosphoserine Ref.15
Modified residue2841Phosphoserine Ref.15 Ref.18 Ref.19 Ref.22

Natural variations

Alternative sequence315 – 34935Missing in isoform 2.
VSP_012908
Natural variant161F → L. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs33555 [ dbSNP | Ensembl ].
VAR_059528

Experimental info

Mutagenesis1471E → Q: Loss of decapping activity; when associated with Q-148. Ref.2
Mutagenesis1481E → Q: Strongly reduced decapping activity. Ref.1 Ref.2
Sequence conflict1031I → V in BAC03479. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 78925E9E4FF0F6C8

FASTA42048,457
        10         20         30         40         50         60 
METKRVEIPG SVLDDFCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY MQNTPGLPQC 

        70         80         90        100        110        120 
GIRDFAKAVF SHCPFLLPQG EDVEKVLDEW KEYKMGVPTY GAIILDETLE NVLLVQGYLA 

       130        140        150        160        170        180 
KSGWGFPKGK VNKEEAPHDC AAREVFEETG FDIKDYICKD DYIELRINDQ LARLYIIPGI 

       190        200        210        220        230        240 
PKDTKFNPKT RREIRNIEWF SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS 

       250        260        270        280        290        300 
RRFGDSSDSD NGFSSTGSTP AKPTVEKLSR TKFRHSQQLF PDGSPGDQWV KHRQPLQQKP 

       310        320        330        340        350        360 
YNNHSEMSDL LKGKNQSMRG NGRKQYQDSP NQKKRTNGLQ PAKQQNSLMK CEKKLHPRKL 

       370        380        390        400        410        420 
QDNFETDAVY DLPSSSEDQL LEHAEGQPVA CNGHCKFPFS SRAFLSFKFD HNAIMKILDL 

« Hide

Isoform 2 [UniParc].

Checksum: 07D9868EE38D2363
Show »

FASTA38544,443

References

« Hide 'large scale' references
[1]"Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay."
Lykke-Andersen J.
Mol. Cell. Biol. 22:8114-8121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF GLU-148, SUBCELLULAR LOCATION, INTERACTION WITH DCP1A AND UPF1, VARIANT LEU-16.
[2]"The hDcp2 protein is a mammalian mRNA decapping enzyme."
Wang Z., Jiao X., Carr-Schmid A., Kiledjian M.
Proc. Natl. Acad. Sci. U.S.A. 99:12663-12668(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF 147-GLU-GLU-148, SUBCELLULAR LOCATION, ASSOCIATION WITH POLYSOMES, VARIANT LEU-16.
Tissue: Erythroleukemia.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-16.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT LEU-16.
Tissue: Blood and Uterus.
[6]"Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures."
van Dijk E., Cougot N., Meyer S., Babajko S., Wahle E., Seraphin B.
EMBO J. 21:6915-6924(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[7]"The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH A COMPLEX CONTAINING ENZYMES INVOLVED IN MRNA DECAY.
[8]"Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
Lejeune F., Li X., Maquat L.E.
Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A MRNA DECAY COMPLEX WITH UPF1; UPF2 AND UPF3B, SUBCELLULAR LOCATION.
[9]"Functional characterization of the mammalian mRNA decapping enzyme hDcp2."
Piccirillo C., Khanna R., Kiledjian M.
RNA 9:1138-1147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, COFACTOR.
[10]"A protein interaction framework for human mRNA degradation."
Lehner B., Sanderson C.M.
Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCP1A AND DCP1B.
[11]"Cytoplasmic foci are sites of mRNA decay in human cells."
Cougot N., Babajko S., Seraphin B.
J. Cell Biol. 165:31-40(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCP1A.
[12]"Functional analysis of mRNA scavenger decapping enzymes."
Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M.
RNA 10:1412-1422(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCP1A; EDC3; EDC4 AND DDX6, SUBCELLULAR LOCATION.
[14]"Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
Wichroski M.J., Robb G.B., Rana T.M.
PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APOBEC3G.
[15]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[16]"SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity."
Yamochi T., Ohnuma K., Hosono O., Tanaka H., Kanai Y., Morimoto C.
Biochem. Biophys. Res. Commun. 370:195-199(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM21.
[17]"Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
Mullen T.E., Marzluff W.F.
Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247; SER-249 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[21]"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing."
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M., Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J., Longmore G.D., Bushell M., Sharp T.V.
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMD1; WTIP AND AJUBA.
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3HAV1 AND DDX17.
[24]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY146650 mRNA. Translation: AAN62762.1.
AY135173 mRNA. Translation: AAN08884.1.
AK090564 mRNA. Translation: BAC03479.1.
AC008536 Genomic DNA. No translation available.
BC045596 mRNA. Translation: AAH45596.1.
BC064593 mRNA. Translation: AAH64593.1.
CCDSCCDS34210.1. [Q8IU60-1]
CCDS56377.1. [Q8IU60-2]
RefSeqNP_001229306.1. NM_001242377.1.
NP_689837.2. NM_152624.5.
UniGeneHs.443875.

3D structure databases

ProteinModelPortalQ8IU60.
SMRQ8IU60. Positions 12-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127944. 16 interactions.
DIPDIP-31126N.
IntActQ8IU60. 11 interactions.
STRING9606.ENSP00000373715.

PTM databases

PhosphoSiteQ8IU60.

Polymorphism databases

DMDM269849560.

Proteomic databases

MaxQBQ8IU60.
PaxDbQ8IU60.
PRIDEQ8IU60.

Protocols and materials databases

DNASU167227.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389063; ENSP00000373715; ENSG00000172795. [Q8IU60-1]
ENST00000515408; ENSP00000425770; ENSG00000172795. [Q8IU60-2]
GeneID167227.
KEGGhsa:167227.
UCSCuc003kqh.3. human. [Q8IU60-1]
uc010jcc.3. human. [Q8IU60-2]

Organism-specific databases

CTD167227.
GeneCardsGC05P112340.
HGNCHGNC:24452. DCP2.
HPACAB011677.
HPA050694.
MIM609844. gene.
neXtProtNX_Q8IU60.
PharmGKBPA134898646.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0494.
HOGENOMHOG000005974.
HOVERGENHBG051321.
InParanoidQ8IU60.
KOK12613.
OMAHSQPAKQ.
OrthoDBEOG7XM2XP.
PhylomeDBQ8IU60.
TreeFamTF314180.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ8IU60.
BgeeQ8IU60.
CleanExHS_DCP2.
GenevestigatorQ8IU60.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. SSF55811. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCP2. human.
GeneWikiDCP2.
GenomeRNAi167227.
NextBio88663.
PROQ8IU60.
SOURCESearch...

Entry information

Entry nameDCP2_HUMAN
AccessionPrimary (citable) accession number: Q8IU60
Secondary accession number(s): C9J778 expand/collapse secondary AC list , Q6P2D4, Q7Z5W5, Q8NBG5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 24, 2009
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM