Q7L2J0 · MEPCE_HUMAN
- Protein7SK snRNA methylphosphate capping enzyme
- GeneMEPCE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids689 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
Catalytic activity
- a 5'-end triphospho-guanosine-ribonucleotide-snRNA + S-adenosyl-L-methionine = a 5'-end methyltriphosphate-guanosine-ribonucleotide-snRNA + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 422 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 433 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 451-453 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GCN | ||||||
Binding site | 474-475 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DI | ||||||
Binding site | 559-560 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 581 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 7SK snRNP | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | 7SK snRNA binding | |
Molecular Function | O-methyltransferase activity | |
Molecular Function | RNA 5'-gamma-phosphate methyltransferase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA methyltransferase activity | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Molecular Function | snRNA binding | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of G1/S transition of mitotic cell cycle | |
Biological Process | positive regulation of protein localization to Cajal body | |
Biological Process | positive regulation of snRNA transcription by RNA polymerase II | |
Biological Process | RNA methylation | |
Biological Process | snRNA metabolic process | |
Biological Process | snRNA modification |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name7SK snRNA methylphosphate capping enzyme
- EC number
- Short namesMePCE
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7L2J0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 421 | Nearly abolished methyltransferase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 447-449 | Abolished methyltransferase activity and reduced interaction with LARP7, without affecting interaction with P-TEFb. | ||||
Sequence: VLD → AAA | ||||||
Mutagenesis | 585 | Decreased methyltransferase activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 674 | Strongly reduced methyltransferase activity. | ||||
Sequence: F → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 698 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000289262 | 1-689 | UniProt | 7SK snRNA methylphosphate capping enzyme | |||
Sequence: MIEMAAEKEPFLVPAPPPPLKDESGGGGGPTVPPHQEAASGELRGGTERGPGRCAPSAGSPAAAVGRESPGAAATSSSGPQAQQHRGGGPQAQSHGEARLSDPPGRAAPPDVGEERRGGGGTELGPPAPPRPRNGYQPHRPPGGGGGKRRNSCNVGGGGGGFKHPAFKRRRRVNSDCDSVLPSNFLLGGNIFDPLNLNSLLDEEVSRTLNAETPKSSPLPAKGRDPVEILIPKDITDPLSLNTCTDEGHVVLASPLKTGRKRHRHRGQHHQQQQAAGGSESHPVPPTAPLTPLLHGEGASQQPRHRGQNRDAPQPYELNTAINCRDEVVSPLPSALQGPSGSLSAPPAASVISAPPSSSSRHRKRRRTSSKSEAGARGGGQGSKEKGRGSWGGRHHHHHPLPAAGFKKQQRKFQYGNYCKYYGYRNPSCEDGRLRVLKPEWFRGRDVLDLGCNVGHLTLSIACKWGPSRMVGLDIDSRLIHSARQNIRHYLSEELRLPPQTLEGDPGAEGEEGTTTVRKRSCFPASLTASRGPIAAPQVPLDGADTSVFPNNVVFVTGNYVLDRDDLVEAQTPEYDVVLCLSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYGKRKTLTETIYKNYYRIQLKPEQFSSYLTSPDVGFSSYELVATPHNTSKGFQRPVYLFHKARSPSH | |||||||
Modified residue | 57 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 60 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 69 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 69 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 94 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 101 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 117 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 152 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 175 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 179 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 213 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 216 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 217 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 217 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 243 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 245 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 254 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 254 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 291 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 330 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 340 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 344 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 643 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 666 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with METTL16 (PubMed:29051200).
Interacts with RBM7; upon genotoxic stress this interaction is enhanced, triggering the release of inactive P-TEFb complex from the core, yielding to P-TEFb complex activation (PubMed:30824372).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-167 | Disordered | ||||
Sequence: MIEMAAEKEPFLVPAPPPPLKDESGGGGGPTVPPHQEAASGELRGGTERGPGRCAPSAGSPAAAVGRESPGAAATSSSGPQAQQHRGGGPQAQSHGEARLSDPPGRAAPPDVGEERRGGGGTELGPPAPPRPRNGYQPHRPPGGGGGKRRNSCNVGGGGGGFKHPAF | ||||||
Compositional bias | 71-90 | Polar residues | ||||
Sequence: GAAATSSSGPQAQQHRGGGP | ||||||
Region | 258-314 | Disordered | ||||
Sequence: TGRKRHRHRGQHHQQQQAAGGSESHPVPPTAPLTPLLHGEGASQQPRHRGQNRDAPQ | ||||||
Region | 332-407 | Disordered | ||||
Sequence: LPSALQGPSGSLSAPPAASVISAPPSSSSRHRKRRRTSSKSEAGARGGGQGSKEKGRGSWGGRHHHHHPLPAAGFK | ||||||
Compositional bias | 335-358 | Polar residues | ||||
Sequence: ALQGPSGSLSAPPAASVISAPPSS | ||||||
Compositional bias | 390-405 | Basic residues | ||||
Sequence: SWGGRHHHHHPLPAAG | ||||||
Domain | 431-686 | Bin3-type SAM | ||||
Sequence: DGRLRVLKPEWFRGRDVLDLGCNVGHLTLSIACKWGPSRMVGLDIDSRLIHSARQNIRHYLSEELRLPPQTLEGDPGAEGEEGTTTVRKRSCFPASLTASRGPIAAPQVPLDGADTSVFPNNVVFVTGNYVLDRDDLVEAQTPEYDVVLCLSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYGKRKTLTETIYKNYYRIQLKPEQFSSYLTSPDVGFSSYELVATPHNTSKGFQRPVYLFHKARS |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q7L2J0-1
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.
- Name1
- Length689
- Mass (Da)74,355
- Last updated2004-07-05 v1
- ChecksumCBB1D6BF144C923A
Q7L2J0-2
- Name2
- Differences from canonical
- 1-469: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8Q3WKJ6 | A0A8Q3WKJ6_HUMAN | MEPCE | 346 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_044512 | 1-469 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 71-90 | Polar residues | ||||
Sequence: GAAATSSSGPQAQQHRGGGP | ||||||
Compositional bias | 335-358 | Polar residues | ||||
Sequence: ALQGPSGSLSAPPAASVISAPPSS | ||||||
Compositional bias | 390-405 | Basic residues | ||||
Sequence: SWGGRHHHHHPLPAAG | ||||||
Sequence conflict | 661 | in Ref. 1; BAG51598 | ||||
Sequence: Y → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK055964 EMBL· GenBank· DDBJ | BAG51598.1 EMBL· GenBank· DDBJ | mRNA | ||
AC092849 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471091 EMBL· GenBank· DDBJ | EAW76534.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76535.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76536.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236956 EMBL· GenBank· DDBJ | EAL23834.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000556 EMBL· GenBank· DDBJ | AAH00556.2 EMBL· GenBank· DDBJ | mRNA | ||
BC016396 EMBL· GenBank· DDBJ | AAH16396.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC018935 EMBL· GenBank· DDBJ | AAH18935.2 EMBL· GenBank· DDBJ | mRNA | ||
AF264752 EMBL· GenBank· DDBJ | AAF74767.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AK000264 EMBL· GenBank· DDBJ | BAA91040.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |