Overview
| Uniprot ID | Q7L2J0 |
|---|
| Protein Name | 7SK snRNA methylphosphate capping enzyme |
|---|
| Gene Name | MEPCE |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 163 |
GGGGGGFKHPAFKRR |
| 257 |
VVLASPLKTGRKRHR |
Function
S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA (7SK RNA), leading to stabilize it (PubMed:17643375, PubMed:19906723, PubMed:30559425). Also has a non-enzymatic function as part of the 7SK RNP complex: the 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:17643375). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (PubMed:28254838). In the 7SK RNP complex, MEPCE is required to stabilize 7SK RNA and facilitate the assembly of 7SK RNP complex (PubMed:19906723, PubMed:38100593). MEPCE has a non-enzymatic function in the 7SK RNP complex; interaction with LARP7 within the 7SK RNP complex occluding its catalytic center (PubMed:19906723). Also required for stability of U6 snRNAs (PubMed:38100593)
Protein Sequence
10
MIEMAAEKEP
20
FLVPAPPPPL
30
KDESGGGGGP
40
TVPPHQEAAS
50
GELRGGTERG
60
PGRCAPSAGS
70
PAAAVGRESP
80
GAAATSSSGP
90
QAQQHRGGGP
100
QAQSHGEARL
110
SDPPGRAAPP
120
DVGEERRGGG
130
GTELGPPAPP
140
RPRNGYQPHR
150
PPGGGGGKRR
160
NSCNVGGGGG
170
GFKHPAFKRR
180
RRVNSDCDSV
190
LPSNFLLGGN
200
IFDPLNLNSL
210
LDEEVSRTLN
220
AETPKSSPLP
230
AKGRDPVEIL
240
IPKDITDPLS
250
LNTCTDEGHV
260
VLASPLKTGR
270
KRHRHRGQHH
280
QQQQAAGGSE
290
SHPVPPTAPL
300
TPLLHGEGAS
310
QQPRHRGQNR
320
DAPQPYELNT
330
AINCRDEVVS
340
PLPSALQGPS
350
GSLSAPPAAS
360
VISAPPSSSS
370
RHRKRRRTSS
380
KSEAGARGGG
390
QGSKEKGRGS
400
WGGRHHHHHP
410
LPAAGFKKQQ
420
RKFQYGNYCK
430
YYGYRNPSCE
440
DGRLRVLKPE
450
WFRGRDVLDL
460
GCNVGHLTLS
470
IACKWGPSRM
480
VGLDIDSRLI
490
HSARQNIRHY
500
LSEELRLPPQ
510
TLEGDPGAEG
520
EEGTTTVRKR
530
SCFPASLTAS
540
RGPIAAPQVP
550
LDGADTSVFP
560
NNVVFVTGNY
570
VLDRDDLVEA
580
QTPEYDVVLC
590
LSLTKWVHLN
600
WGDEGLKRMF
610
RRIYRHLRPG
620
GILVLEPQPW
630
SSYGKRKTLT
640
ETIYKNYYRI
650
QLKPEQFSSY
660
LTSPDVGFSS
670
YELVATPHNT
680
SKGFQRPVYL
FHKARSPSH
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0120259 |
7SK snRNP |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:1990904 |
ribonucleoprotein complex |
| Molecular Function |
GO:0097322 |
7SK snRNA binding |
| Molecular Function |
GO:0008171 |
O-methyltransferase activity |
| Molecular Function |
GO:1990276 |
RNA 5'-gamma-phosphate methyltransferase activity |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0008173 |
RNA methyltransferase activity |
| Molecular Function |
GO:0008757 |
S-adenosylmethionine-dependent methyltransferase activity |
| Molecular Function |
GO:0017069 |
snRNA binding |
| Biological Process |
GO:1904871 |
positive regulation of protein localization to Cajal body |
| Biological Process |
GO:1905382 |
positive regulation of snRNA transcription by RNA polymerase II |
| Biological Process |
GO:0001510 |
RNA methylation |
| Biological Process |
GO:0016073 |
snRNA metabolic process |
| Biological Process |
GO:0040031 |
snRNA modification |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.