Q8IXW5 · RPAP2_HUMAN
- ProteinPutative RNA polymerase II subunit B1 CTD phosphatase RPAP2
- GeneRPAP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids612 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes (PubMed:17643375, PubMed:22137580, PubMed:24997600).
Downstream of EIF2AK3/PERK, dephosphorylates ERN1, a sensor for the endoplasmic reticulum unfolded protein response (UPR), to abort failed ER-stress adaptation and trigger apoptosis (PubMed:30118681).
Downstream of EIF2AK3/PERK, dephosphorylates ERN1, a sensor for the endoplasmic reticulum unfolded protein response (UPR), to abort failed ER-stress adaptation and trigger apoptosis (PubMed:30118681).
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | transcription preinitiation complex | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Molecular Function | RNA polymerase core enzyme binding | |
Molecular Function | RNA polymerase II CTD heptapeptide repeat phosphatase activity | |
Biological Process | PERK-mediated unfolded protein response | |
Biological Process | snRNA transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative RNA polymerase II subunit B1 CTD phosphatase RPAP2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8IXW5
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2-32 | Abolishes dephosphorylation of ERN1; when associated with 275-G--E-612 DEL. | ||||
Sequence: Missing | ||||||
Mutagenesis | 100 | Abolishes interaction with RNA polymerase II complex subunits; when associated with A-105. | ||||
Sequence: C → A | ||||||
Mutagenesis | 105 | Abolishes interaction with RNA polymerase II complex subunits; when associated with A-100. | ||||
Sequence: C → A | ||||||
Mutagenesis | 136 | Abolishes interaction with RNA polymerase II complex subunits; when associated with A-140. | ||||
Sequence: C → A | ||||||
Mutagenesis | 140 | Abolishes interaction with RNA polymerase II complex subunits; when associated with A-136. | ||||
Sequence: C → A | ||||||
Mutagenesis | 275-612 | Abolishes dephosphorylation of ERN1; when associated with 2-A--L-32 DEL. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 610 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000250648 | 2-612 | UniProt | Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 | |||
Sequence: ADFAGPSSAGRKAGAPRCSRKAAGTKQTSTLKQEDASKRKAELEAAVRKKIEFERKALHIVEQLLEENITEEFLMECGRFITPAHYSDVVDERSIVKLCGYPLCQKKLGIVPKQKYKISTKTNKVYDITERKSFCSNFCYQASKFFEAQIPKTPVWVREEERHPDFQLLKEEQSGHSGEEVQLCSKAIKTSDIDNPSHFEKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLHQKSIMKKKAGHKANSKHKDKEQTVVDVTEQLGDCKLDSQEKDATCELPLQKVNTQSSSNSTLPERLKASENSESEYSRSEITLVGISKKSAEHFKRKFAKSNQVSRSVSSSVQVCPEVGKRNLLKVLKETLIEWKTEETLRFLYGQNYASVCLKPEASLVKEELDEDDIISDPDSHFPAWRESQNSLDESLPFRGSGTAIKPLPSYENLKKETEKLNLRIREFYRGRYVLGEETTKSQDSEEHDSTFPLIDSSSQNQIRKRIVLEKLSKVLPGLLVPLQITLGDIYTQLKNLVRTFRLTNRNIIHKPAEWTLIAMVLLSLLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNEDLESLTIIFRTSCLPE | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 216 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 350 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 414 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 426 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 429 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 433 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 480 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 480 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Associates with the RNA polymerase II complex. Interacts with transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8IXW5 | GPN1 Q9HCN4 | 9 | EBI-395878, EBI-745137 | |
BINARY | Q8IXW5 | PIH1D1 Q9NWS0 | 8 | EBI-395878, EBI-357318 | |
BINARY | Q8IXW5 | PLEKHF2 Q9H8W4 | 3 | EBI-395878, EBI-742388 | |
BINARY | Q8IXW5 | RPRD1A Q96P16-1 | 3 | EBI-395878, EBI-16112633 | |
BINARY | Q8IXW5 | RPRD1B Q9NQG5 | 6 | EBI-395878, EBI-747925 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-38 | Disordered | ||||
Sequence: MADFAGPSSAGRKAGAPRCSRKAAGTKQTSTLKQEDAS | ||||||
Coiled coil | 33-68 | |||||
Sequence: KQEDASKRKAELEAAVRKKIEFERKALHIVEQLLEE | ||||||
Zinc finger | 77-160 | RTR1-type | ||||
Sequence: ECGRFITPAHYSDVVDERSIVKLCGYPLCQKKLGIVPKQKYKISTKTNKVYDITERKSFCSNFCYQASKFFEAQIPKTPVWVRE | ||||||
Region | 193-267 | Disordered | ||||
Sequence: DIDNPSHFEKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLHQKSIMKKKAGHKANSKHKDKEQTV | ||||||
Compositional bias | 201-243 | Polar residues | ||||
Sequence: EKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLH | ||||||
Compositional bias | 295-310 | Polar residues | ||||
Sequence: VNTQSSSNSTLPERLK | ||||||
Region | 295-317 | Disordered | ||||
Sequence: VNTQSSSNSTLPERLKASENSES |
Domain
The RTR1-type zinc finger mediates interactions with RNA polymerase II complex subunits.
Sequence similarities
Belongs to the RPAP2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8IXW5-1
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
- Length612
- Mass (Da)69,509
- Last updated2003-03-01 v1
- Checksum43D6DE7C30BB5C96
Q8IXW5-2
- Name2
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 201-243 | Polar residues | ||||
Sequence: EKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLH | ||||||
Compositional bias | 295-310 | Polar residues | ||||
Sequence: VNTQSSSNSTLPERLK | ||||||
Sequence conflict | 421 | in Ref. 3; AAH31070 | ||||
Sequence: P → R | ||||||
Sequence conflict | 467 | in Ref. 1; BAB14465 | ||||
Sequence: Y → C | ||||||
Alternative sequence | VSP_020680 | 563-596 | in isoform 2 | |||
Sequence: LLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNE → FLLNVKTRIKTFMMIYFHLMNS | ||||||
Sequence conflict | 584 | In isoform Q8IXW5-2; in Ref. 3; AAH31070 | ||||
Sequence: S → N | ||||||
Alternative sequence | VSP_020681 | 597-612 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK023212 EMBL· GenBank· DDBJ | BAB14465.1 EMBL· GenBank· DDBJ | mRNA | ||
AL451010 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC031070 EMBL· GenBank· DDBJ | AAH31070.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039014 EMBL· GenBank· DDBJ | AAH39014.1 EMBL· GenBank· DDBJ | mRNA |