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Q8IU60

- DCP2_HUMAN

UniProt

Q8IU60 - DCP2_HUMAN

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Protein

m7GpppN-mRNA hydrolase

Gene
DCP2, NUDT20
Organism
Homo sapiens (Human)
Status
Reviewed - 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.7 Publications

Catalytic activityi

5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA) + H2O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).2 Publications

Cofactori

Manganese. Required for highest activity. Can also utilize magnesium ions.1 Publication

Sites

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

GO - Molecular functioni

  1. exoribonuclease activity, producing 5'-phosphomonoesters Source: Reactome
  2. m7G(5')pppN diphosphatase activity Source: UniProtKB
  3. manganese ion binding Source: InterPro
  4. protein binding Source: UniProtKB
  5. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. histone mRNA catabolic process Source: UniProtKB
  4. mRNA catabolic process Source: UniProtKB
  5. mRNA metabolic process Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  8. RNA metabolic process Source: Reactome
  9. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
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_18355. ATF4 activates genes.
REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DCP2
Synonyms:NUDT20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:24452. DCP2.

Subcellular locationi

CytoplasmP-body. Nucleus
Note: Predominantly cytoplasmic, in processing bodies (PB). A minor amount is nuclear.9 Publications

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: MGI
  2. cytosol Source: Reactome
  3. nucleus Source: HPA
  4. RISC complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1471E → Q: Loss of decapping activity; when associated with Q-148. 1 Publication
Mutagenesisi148 – 1481E → Q: Strongly reduced decapping activity. 2 Publications

Organism-specific databases

PharmGKBiPA134898646.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420m7GpppN-mRNA hydrolasePRO_0000057051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461Phosphoserine2 Publications
Modified residuei247 – 2471Phosphoserine2 Publications
Modified residuei249 – 2491Phosphoserine2 Publications
Modified residuei276 – 2761Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IU60.
PaxDbiQ8IU60.
PRIDEiQ8IU60.

PTM databases

PhosphoSiteiQ8IU60.

Expressioni

Tissue specificityi

Expressed in brain and testis. Not detected in heart (at protein level).1 Publication

Gene expression databases

ArrayExpressiQ8IU60.
BgeeiQ8IU60.
CleanExiHS_DCP2.
GenevestigatoriQ8IU60.

Organism-specific databases

HPAiCAB011677.
HPA050694.

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. 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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP1AQ9NPI66EBI-521577,EBI-374238
DCP1BQ8IZD43EBI-521577,EBI-521595
EDC4Q6P2E94EBI-521577,EBI-1006038
UPF1Q929003EBI-521577,EBI-373471

Protein-protein interaction databases

BioGridi127944. 47 interactions.
DIPiDIP-31126N.
IntActiQ8IU60. 11 interactions.
STRINGi9606.ENSP00000373715.

Structurei

3D structure databases

ProteinModelPortaliQ8IU60.
SMRiQ8IU60. Positions 12-242.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 226132Nudix hydrolaseAdd
BLAST

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0494.
HOGENOMiHOG000005974.
HOVERGENiHBG051321.
InParanoidiQ8IU60.
KOiK12613.
OMAiHSQPAKQ.
OrthoDBiEOG7XM2XP.
PhylomeDBiQ8IU60.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IU60-1) [UniParc]FASTAAdd to Basket

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.

« Hide

METKRVEIPG SVLDDFCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY    50
MQNTPGLPQC GIRDFAKAVF SHCPFLLPQG EDVEKVLDEW KEYKMGVPTY 100
GAIILDETLE NVLLVQGYLA KSGWGFPKGK VNKEEAPHDC AAREVFEETG 150
FDIKDYICKD DYIELRINDQ LARLYIIPGI PKDTKFNPKT RREIRNIEWF 200
SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS RRFGDSSDSD 250
NGFSSTGSTP AKPTVEKLSR TKFRHSQQLF PDGSPGDQWV KHRQPLQQKP 300
YNNHSEMSDL LKGKNQSMRG NGRKQYQDSP NQKKRTNGLQ PAKQQNSLMK 350
CEKKLHPRKL QDNFETDAVY DLPSSSEDQL LEHAEGQPVA CNGHCKFPFS 400
SRAFLSFKFD HNAIMKILDL 420
Length:420
Mass (Da):48,457
Last modified:November 24, 2009 - v2
Checksum:i78925E9E4FF0F6C8
GO
Isoform 2 (identifier: Q8IU60-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-349: Missing.

Note: No experimental confirmation available.

Show »
Length:385
Mass (Da):44,443
Checksum:i07D9868EE38D2363
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161F → L.4 Publications
Corresponds to variant rs33555 [ dbSNP | Ensembl ].
VAR_059528

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei315 – 34935Missing in isoform 2. VSP_012908Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031I → V in BAC03479. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34210.1. [Q8IU60-1]
CCDS56377.1. [Q8IU60-2]
RefSeqiNP_001229306.1. NM_001242377.1.
NP_689837.2. NM_152624.5.
UniGeneiHs.443875.

Genome annotation databases

EnsembliENST00000389063; ENSP00000373715; ENSG00000172795. [Q8IU60-1]
ENST00000515408; ENSP00000425770; ENSG00000172795. [Q8IU60-2]
GeneIDi167227.
KEGGihsa:167227.
UCSCiuc003kqh.3. human. [Q8IU60-1]
uc010jcc.3. human. [Q8IU60-2]

Polymorphism databases

DMDMi269849560.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34210.1. [Q8IU60-1 ]
CCDS56377.1. [Q8IU60-2 ]
RefSeqi NP_001229306.1. NM_001242377.1.
NP_689837.2. NM_152624.5.
UniGenei Hs.443875.

3D structure databases

ProteinModelPortali Q8IU60.
SMRi Q8IU60. Positions 12-242.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127944. 47 interactions.
DIPi DIP-31126N.
IntActi Q8IU60. 11 interactions.
STRINGi 9606.ENSP00000373715.

PTM databases

PhosphoSitei Q8IU60.

Polymorphism databases

DMDMi 269849560.

Proteomic databases

MaxQBi Q8IU60.
PaxDbi Q8IU60.
PRIDEi Q8IU60.

Protocols and materials databases

DNASUi 167227.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389063 ; ENSP00000373715 ; ENSG00000172795 . [Q8IU60-1 ]
ENST00000515408 ; ENSP00000425770 ; ENSG00000172795 . [Q8IU60-2 ]
GeneIDi 167227.
KEGGi hsa:167227.
UCSCi uc003kqh.3. human. [Q8IU60-1 ]
uc010jcc.3. human. [Q8IU60-2 ]

Organism-specific databases

CTDi 167227.
GeneCardsi GC05P112340.
HGNCi HGNC:24452. DCP2.
HPAi CAB011677.
HPA050694.
MIMi 609844. gene.
neXtProti NX_Q8IU60.
PharmGKBi PA134898646.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0494.
HOGENOMi HOG000005974.
HOVERGENi HBG051321.
InParanoidi Q8IU60.
KOi K12613.
OMAi HSQPAKQ.
OrthoDBi EOG7XM2XP.
PhylomeDBi Q8IU60.
TreeFami TF314180.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.
REACT_20518. mRNA decay by 5' to 3' exoribonuclease.
REACT_24915. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_25042. KSRP destabilizes mRNA.
REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

Miscellaneous databases

ChiTaRSi DCP2. human.
GeneWikii DCP2.
GenomeRNAii 167227.
NextBioi 88663.
PROi Q8IU60.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IU60.
Bgeei Q8IU60.
CleanExi HS_DCP2.
Genevestigatori Q8IU60.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR007722. mRNA_decapping_BoxA.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
Pfami PF05026. DCP2. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view ]
SUPFAMi SSF55811. SSF55811. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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].

Entry informationi

Entry nameiDCP2_HUMAN
AccessioniPrimary (citable) accession number: Q8IU60
Secondary accession number(s): C9J778
, Q6P2D4, Q7Z5W5, Q8NBG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 24, 2009
Last modified: September 3, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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