Q460N3 · PAR15_HUMAN
- ProteinProtein mono-ADP-ribosyltransferase PARP15
- GenePARP15
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids678 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins (PubMed:16061477, PubMed:25043379, PubMed:25635049).
Acts as a negative regulator of transcription (PubMed:16061477).
Acts as a negative regulator of transcription (PubMed:16061477).
Catalytic activity
- L-aspartyl-[protein] + NAD+ = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
- L-glutamyl-[protein] + NAD+ = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 312-313 | substrate | ||||
Sequence: DI | ||||||
Binding site | 324-325 | substrate | ||||
Sequence: ST | ||||||
Binding site | 331 | substrate | ||||
Sequence: R | ||||||
Binding site | 335 | substrate | ||||
Sequence: V | ||||||
Binding site | 409-413 | substrate | ||||
Sequence: GTGNA | ||||||
Binding site | 449 | substrate | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | NAD+ ADP-ribosyltransferase activity | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD+-protein ADP-ribosyltransferase activity | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | transcription corepressor activity | |
Biological Process | negative regulation of gene expression | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | protein poly-ADP-ribosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein mono-ADP-ribosyltransferase PARP15
- 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 accessionQ460N3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_027862 | 337 | in dbSNP:rs6793271 | |||
Sequence: R → K | ||||||
Natural variant | VAR_056658 | 521 | in dbSNP:rs34383355 | |||
Sequence: A → T | ||||||
Mutagenesis | 559 | Abolishes catalytic activity. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 560 | Slightly reduces catalytic activity. Abolishes activity; when associated with Y-559 and C-604. | ||||
Sequence: G → A | ||||||
Mutagenesis | 604 | Reduces catalytic activity 20-fold. Abolishes activity; when associated with Y-559 and A-560. | ||||
Sequence: Y → C | ||||||
Natural variant | VAR_027863 | 628 | in dbSNP:rs12489170 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 758 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000252436 | 1-678 | Protein mono-ADP-ribosyltransferase PARP15 | |||
Sequence: MAAPGPLPAAALSPGAPTPRELMHGVAGVTSRAGRDREAGSVLPAGNRGARKASRRSSSRSMSRDNKFSKKDCLSIRNVVASIQTKEGLNLKLISGDVLYIWADVIVNSVPMNLQLGGGPLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITSPLQEVHFLVYTNDDEGCQAFLDEFTNWSRINPNKARIPMAGDTQGVVGTVSKPCFTAYEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNIFYDSMKKRDLSASLNFQSTFSMTTCNLPEHWTDMNHQLFCMVQLEPGQSEYNTIKDKFTRTCSSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTPPPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITFTA |
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q460N3-2 | NRM Q8IXM6 | 3 | EBI-17287327, EBI-10262547 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-67 | Disordered | ||||
Sequence: MAAPGPLPAAALSPGAPTPRELMHGVAGVTSRAGRDREAGSVLPAGNRGARKASRRSSSRSMSRDNK | ||||||
Domain | 78-267 | Macro 1 | ||||
Sequence: NVVASIQTKEGLNLKLISGDVLYIWADVIVNSVPMNLQLGGGPLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITSPLQEVHFLVYTNDDEGCQAFLDEFTNWS | ||||||
Domain | 293-464 | Macro 2 | ||||
Sequence: CFTAYEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNIFYDSMKKRD | ||||||
Domain | 482-678 | PARP catalytic | ||||
Sequence: LPEHWTDMNHQLFCMVQLEPGQSEYNTIKDKFTRTCSSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTPPPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITFTA |
Sequence similarities
Belongs to the ARTD/PARP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q460N3-1
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
- Length678
- Mass (Da)74,576
- Last updated2014-04-16 v2
- ChecksumE299386DA4B2BF8C
Q460N3-2
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK097916 EMBL· GenBank· DDBJ | BAC05197.1 EMBL· GenBank· DDBJ | mRNA | ||
BC101703 EMBL· GenBank· DDBJ | AAI01704.1 EMBL· GenBank· DDBJ | mRNA | ||
BC101701 EMBL· GenBank· DDBJ | AAI01702.1 EMBL· GenBank· DDBJ | mRNA | ||
AC092908 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
DQ063586 EMBL· GenBank· DDBJ | AAY64451.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |