Q8CFF0 · PAR11_MOUSE

  • Protein
    Protein mono-ADP-ribosyltransferase PARP11
  • Gene
    Parp11
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins (By similarity).
Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (PubMed:25673562).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnuclear body
Cellular Componentnuclear envelope
Cellular Componentnuclear pore
Molecular FunctionNAD+-histone H2BE18 glutamate ADP-ribosyltransferase activity
Molecular FunctionNAD+-histone H2BE2 glutamate ADP-ribosyltransferase activity
Molecular FunctionNAD+-histone H2BE35 glutamate ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein poly-ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-aspartate ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-cysteine ADP-ribosyltransferase activity
Molecular FunctionNAD+-protein-lysine ADP-ribosyltransferase activity
Molecular Functionnucleotidyltransferase activity
Biological Processcell differentiation
Biological ProcessmRNA transport
Biological Processnuclear envelope organization
Biological Processprotein auto-ADP-ribosylation
Biological Processprotein transport
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein mono-ADP-ribosyltransferase PARP11
  • EC number
  • Alternative names
    • ADP-ribosyltransferase diphtheria toxin-like 11 (ARTD11)
    • Poly [ADP-ribose] polymerase 11 (PARP-11)

Gene names

    • Name
      Parp11

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8CFF0
  • Secondary accessions
    • Q3UAF2
    • Q3UZR7

Proteomes

Organism-specific databases

Subcellular Location

Note: Colocalizes with NUP153 at nuclear pores.

Keywords

Phenotypes & Variants

Disruption phenotype

Knockout mice are viable and are born in normal Mendelian ratios. Knockout males, but not females, exhibit a striking fertility defect, with the majority of males being sterile and a minority producing infrequent and small litters. Sperm from mutant mice exhibits mild to severe teratozoospermia, with structural defects in elongating spermatid nuclear envelope and chromatin detachment associated with abnormal nuclear shaping.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002734201-331Protein mono-ADP-ribosyltransferase PARP11
Modified residue11N6-(ADP-ribosyl)lysine
Modified residue49ADP-ribosylcysteine
Modified residue65ADP-ribosylcysteine
Modified residue80ADP-ribosyl aspartic acid

Post-translational modification

Auto-mono-ADP-ribosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Predominantly expressed in testis, preferentially in postmeiotic germ cells. Also detectable in other tissues, including liver, lung, spleen, thymus and brain.

Developmental stage

Undetectable in testis until postnatal day 18. Sharply up-regulated from postnatal days 18 to 21. This timeframe corresponds to the appearance of the first spermatids of the first wave of spermatogenesis just before initiation of elongation. Remains elevated in adult animals.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-99WWE
Domain116-331PARP catalytic

Sequence similarities

Belongs to the ARTD/PARP family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q8CFF0-1

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
    331
  • Mass (Da)
    38,737
  • Last updated
    2003-03-01 v1
  • MD5 Checksum
    4358B9B12A8F749BF76378DE67992659
MFHKTEEFFPKKTDSDVDDMDTSDTQWGWFYLAECGKWHMFQPDTNIQCSVSSEDIEKSFKTNPCGSISFTTSKFSYKIDFAEMKQMNLVTGKQRLIKRAPFSISAFSYICENEAIPMPTHWENVNPDVPYQLVSLQNQTHEYNEVASLFGKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDFH

Q8CFF0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8CFF0-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0J9YVC5A0A0J9YVC5_MOUSEParp1143

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0225571-83in isoform 2
Alternative sequenceVSP_022558177-331in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK133697
EMBL· GenBank· DDBJ
BAE21788.1
EMBL· GenBank· DDBJ
mRNA
AK151393
EMBL· GenBank· DDBJ
BAE30362.1
EMBL· GenBank· DDBJ
mRNA
BC040269
EMBL· GenBank· DDBJ
AAH40269.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help