Overview
| Uniprot ID | Q8IU60 |
|---|
| Protein Name | m7GpppN-mRNA hydrolase |
|---|
| Gene Name | DCP2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 334 |
QDSPNQKKRTNGLQP |
Function
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:12218187, PubMed:12417715, PubMed:12923261, PubMed:21070968, PubMed:28002401, PubMed:31875550). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12486012, PubMed:12923261, PubMed:21070968, PubMed:28002401, PubMed:31875550). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:14527413). Plays a role in replication-dependent histone mRNA degradation (PubMed:18172165). Has higher activity towards mRNAs that lack a poly(A) tail (PubMed:21070968). Has no activity towards a cap structure lacking an RNA moiety (PubMed:21070968). The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping (PubMed:28002401). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts (PubMed:26098573)
Protein Sequence
10
METKRVEIPG
20
SVLDDLCSRF
30
ILHIPSEERD
40
NAIRVCFQIE
50
LAHWFYLDFY
60
MQNTPGLPQC
70
GIRDFAKAVF
80
SHCPFLLPQG
90
EDVEKVLDEW
100
KEYKMGVPTY
110
GAIILDETLE
120
NVLLVQGYLA
130
KSGWGFPKGK
140
VNKEEAPHDC
150
AAREVFEETG
160
FDIKDYICKD
170
DYIELRINDQ
180
LARLYIIPGI
190
PKDTKFNPKT
200
RREIRNIEWF
210
SIEKLPCHRN
220
DMTPKSKLGL
230
APNKFFMAIP
240
FIRPLRDWLS
250
RRFGDSSDSD
260
NGFSSTGSTP
270
AKPTVEKLSR
280
TKFRHSQQLF
290
PDGSPGDQWV
300
KHRQPLQQKP
310
YNNHSEMSDL
320
LKGKNQSMRG
330
NGRKQYQDSP
340
NQKKRTNGLQ
350
PAKQQNSLMK
360
CEKKLHPRKL
370
QDNFETDAVY
380
DLPSSSEDQL
390
LEHAEGQPVA
400
CNGHCKFPFS
410
SRAFLSFKFD
420
HNAIMKILDL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0036464 |
cytoplasmic ribonucleoprotein granule |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0000932 |
P-body |
| Cellular Component |
GO:0016442 |
RISC complex |
| Molecular Function |
GO:0140933 |
5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity |
| Molecular Function |
GO:0004534 |
5'-3' RNA exonuclease activity |
| Molecular Function |
GO:0030145 |
manganese ion binding |
| Molecular Function |
GO:0016896 |
RNA exonuclease activity, producing 5'-phosphomonoesters |
| Molecular Function |
GO:0070034 |
telomerase RNA binding |
| Biological Process |
GO:0000290 |
deadenylation-dependent decapping of nuclear-transcribed mRNA |
| Biological Process |
GO:0071044 |
histone mRNA catabolic process |
| Biological Process |
GO:0006402 |
mRNA catabolic process |
| Biological Process |
GO:0032211 |
negative regulation of telomere maintenance via telomerase |
| Biological Process |
GO:0000288 |
nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay |
| Biological Process |
GO:0000184 |
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process |
GO:0043488 |
regulation of mRNA stability |
| Biological Process |
GO:1904872 |
regulation of telomerase RNA localization to Cajal body |
Reference
[1] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.