Q8IXW5 · RPAP2_HUMAN

  • Protein
    Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
  • Gene
    RPAP2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site100Zn2+ (UniProtKB | ChEBI)
Binding site105Zn2+ (UniProtKB | ChEBI)
Binding site136Zn2+ (UniProtKB | ChEBI)
Binding site140Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componenttranscription preinitiation complex
Molecular Functionmetal ion binding
Molecular Functionmyosin phosphatase activity
Molecular Functionprotein serine/threonine phosphatase activity
Molecular FunctionRNA polymerase core enzyme binding
Molecular FunctionRNA polymerase II CTD heptapeptide repeat phosphatase activity
Biological ProcessPERK-mediated unfolded protein response
Biological ProcesssnRNA transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
  • EC number
  • Alternative names
    • RNA polymerase II-associated protein 2

Gene names

    • Name
      RPAP2
    • Synonyms
      C1orf82

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q8IXW5
  • Secondary accessions
    • C9JKB5
    • Q49AS7
    • Q9H8Y2

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner.

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis2-32Abolishes dephosphorylation of ERN1; when associated with 275-G--E-612 DEL.
Mutagenesis100Abolishes interaction with RNA polymerase II complex subunits; when associated with A-105.
Mutagenesis105Abolishes interaction with RNA polymerase II complex subunits; when associated with A-100.
Mutagenesis136Abolishes interaction with RNA polymerase II complex subunits; when associated with A-140.
Mutagenesis140Abolishes interaction with RNA polymerase II complex subunits; when associated with A-136.
Mutagenesis275-612Abolishes dephosphorylation of ERN1; when associated with 2-A--L-32 DEL.

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00002506482-612UniProtPutative RNA polymerase II subunit B1 CTD phosphatase RPAP2
Modified residue (large scale data)8PRIDEPhosphoserine
Modified residue9UniProtPhosphoserine
Modified residue (large scale data)9PRIDEPhosphoserine
Modified residue (large scale data)175PRIDEPhosphoserine
Modified residue (large scale data)178PRIDEPhosphoserine
Modified residue216UniProtPhosphoserine
Modified residue (large scale data)350PRIDEPhosphoserine
Modified residue (large scale data)352PRIDEPhosphoserine
Modified residue (large scale data)414PRIDEPhosphoserine
Modified residue (large scale data)426PRIDEPhosphoserine
Modified residue (large scale data)429PRIDEPhosphoserine
Modified residue433UniProtPhosphoserine
Modified residue (large scale data)433PRIDEPhosphoserine
Modified residue480UniProtPhosphoserine
Modified residue (large scale data)480PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Associates with the RNA polymerase II complex. Interacts with transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, coiled coil, zinc finger, compositional bias.

TypeIDPosition(s)Description
Region1-38Disordered
Coiled coil33-68
Zinc finger77-160RTR1-type
Region193-267Disordered
Compositional bias201-243Polar residues
Compositional bias295-310Polar residues
Region295-317Disordered

Domain

The RTR1-type zinc finger mediates interactions with RNA polymerase II complex subunits.

Sequence similarities

Belongs to the RPAP2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    612
  • Mass (Da)
    69,509
  • Last updated
    2003-03-01 v1
  • Checksum
    43D6DE7C30BB5C96
MADFAGPSSAGRKAGAPRCSRKAAGTKQTSTLKQEDASKRKAELEAAVRKKIEFERKALHIVEQLLEENITEEFLMECGRFITPAHYSDVVDERSIVKLCGYPLCQKKLGIVPKQKYKISTKTNKVYDITERKSFCSNFCYQASKFFEAQIPKTPVWVREEERHPDFQLLKEEQSGHSGEEVQLCSKAIKTSDIDNPSHFEKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLHQKSIMKKKAGHKANSKHKDKEQTVVDVTEQLGDCKLDSQEKDATCELPLQKVNTQSSSNSTLPERLKASENSESEYSRSEITLVGISKKSAEHFKRKFAKSNQVSRSVSSSVQVCPEVGKRNLLKVLKETLIEWKTEETLRFLYGQNYASVCLKPEASLVKEELDEDDIISDPDSHFPAWRESQNSLDESLPFRGSGTAIKPLPSYENLKKETEKLNLRIREFYRGRYVLGEETTKSQDSEEHDSTFPLIDSSSQNQIRKRIVLEKLSKVLPGLLVPLQITLGDIYTQLKNLVRTFRLTNRNIIHKPAEWTLIAMVLLSLLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNEDLESLTIIFRTSCLPE

Q8IXW5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 563-596: LLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNE → FLLNVKTRIKTFMMIYFHLMNS
    • 597-612: Missing

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias201-243Polar residues
Compositional bias295-310Polar residues
Sequence conflict421in Ref. 3; AAH31070
Sequence conflict467in Ref. 1; BAB14465
Alternative sequenceVSP_020680563-596in isoform 2
Sequence conflict584In isoform Q8IXW5-2; in Ref. 3; AAH31070
Alternative sequenceVSP_020681597-612in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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