Q8IU60 (DCP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence 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 a RNA moiety. Ref.1 Ref.2 Ref.6 Ref.8 Ref.9 Ref.17 Ref.20
Catalytic activity	M7G5'ppp5'-mRNA + H2O = m7GDP + 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	Cytoplasm › P-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 process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Manganese Metal-binding RNA-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype PubMed 22890540. Source: UniProtKB
Cellular_component	RNA-induced silencing 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 electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DCP1A	Q9NPI6	6	EBI-521577,EBI-374238
DCP1B	Q8IZD4	3	EBI-521577,EBI-521595
EDC4	Q6P2E9	4	EBI-521577,EBI-1006038
UPF1	Q92900	3	EBI-521577,EBI-373471

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	m7GpppN-mRNA hydrolase		PRO_0000057051
Regions
	Domain	95 – 226	132	Nudix hydrolase
	Motif	129 – 150	22	Nudix box
Sites
	Metal binding	144	1	Manganese By similarity
	Metal binding	148	1	Manganese By similarity
Amino acid modifications
	Modified residue	246	1	Phosphoserine Ref.18 Ref.24
	Modified residue	247	1	Phosphoserine Ref.18 Ref.24
	Modified residue	249	1	Phosphoserine Ref.18 Ref.24
	Modified residue	276	1	Phosphoserine Ref.15
	Modified residue	284	1	Phosphoserine Ref.15 Ref.18 Ref.19 Ref.22
Natural variations
	Alternative sequence	315 – 349	35	Missing in isoform 2.		VSP_012908
	Natural variant	16	1	F → L. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs33555 [ dbSNP | Ensembl ].		VAR_059528
Experimental info
	Mutagenesis	147	1	E → Q: Loss of decapping activity; when associated with Q-148. Ref.2
	Mutagenesis	148	1	E → Q: Strongly reduced decapping activity. Ref.1 Ref.2
	Sequence conflict	103	1	I → V in BAC03479. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 24, 2009. Version 2. Checksum: 78925E9E4FF0F6C8	FASTA	420	48,457
	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
	Isoform 2 [UniParc]. Checksum: 07D9868EE38D2363	FASTA	385	44,443
	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 LKGKKCEKKL HPRKLQDNFE TDAVYDLPSS SEDQLLEHAE GQPVACNGHC 370 380 KFPFSSRAFL SFKFDHNAIM KILDL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00292382. IPI00440151.
RefSeq	NP_001229306.1. NM_001242377.1. NP_689837.2. NM_152624.5.
UniGene	Hs.443875.
3D structure databases
ProteinModelPortal	Q8IU60.
SMR	Q8IU60. Positions 12-242.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31126N.
IntAct	Q8IU60. 11 interactions.
STRING	9606.ENSP00000373715.
PTM databases
PhosphoSite	Q8IU60.
Polymorphism databases
DMDM	269849560.
Proteomic databases
PaxDb	Q8IU60.
PRIDE	Q8IU60.
Protocols and materials databases
DNASU	167227.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389063; ENSP00000373715; ENSG00000172795. ENST00000515408; ENSP00000425770; ENSG00000172795.
GeneID	167227.
KEGG	hsa:167227.
UCSC	uc003kqh.3. human. uc010jcc.3. human.
Organism-specific databases
CTD	167227.
GeneCards	GC05P112340.
HGNC	HGNC:24452. DCP2.
HPA	CAB011677.
MIM	609844. gene.
neXtProt	NX_Q8IU60.
PharmGKB	PA134898646.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0494.
HOGENOM	HOG000005974.
HOVERGEN	HBG051321.
InParanoid	Q8IU60.
KO	K12613.
OMA	PGVPKDT.
Enzyme and pathway databases
Reactome	REACT_21257. Metabolism of RNA. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q8IU60.
Bgee	Q8IU60.
CleanEx	HS_DCP2.
Genevestigator	Q8IU60.
GermOnline	ENSG00000172795. Homo sapiens.
Family and domain databases
Gene3D	3.90.79.10. 1 hit.
InterPro	IPR007722. mRNA_decapping_BoxA. IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
Pfam	PF05026. DCP2. 1 hit. PF00293. NUDIX. 1 hit. [Graphical view]
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DCP2. human.
GenomeRNAi	167227.
NextBio	88663.
SOURCE	Search...

Entry information

Entry name

DCP2_HUMAN

Accession

Primary (citable) accession number: Q8IU60
Secondary accession number(s): C9J778 , Q6P2D4, Q7Z5W5, Q8NBG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.