Q7Z3E1 · PARPT_HUMAN
- ProteinProtein mono-ADP-ribosyltransferase TIPARP
- GeneTIPARP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids657 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate, aspartate and cysteine residues on target proteins (PubMed:23275542, PubMed:25043379, PubMed:30373764).
Acts as a negative regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to inhibit transcription activator activity of AHR (PubMed:23275542, PubMed:30373764).
Acts as a negative regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to inhibit transcription activator activity of AHR (PubMed:23275542, PubMed:30373764).
Catalytic activity
- L-aspartyl-[protein] + NAD+ = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide
- L-glutamyl-[protein] + NAD+ = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide
- L-cysteinyl-[protein] + NAD+ = H+ + nicotinamide + S-(ADP-D-ribosyl)-L-cysteinyl-[protein]
Activity regulation
ADP-ribosyltransferase activity is inhibited by PJ34; inhibition is however not specific to TIPARP and other PARP-domain containing proteins are also inhibited by PJ34 (PubMed:30373764).
Partially inhibited by KU0058948 (PubMed:30373764).
Partially inhibited by KU0058948 (PubMed:30373764).
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein mono-ADP-ribosyltransferase TIPARP
- 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 accessionQ7Z3E1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 39 | Slight reduction of auto-mono-ADP-ribosylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 41 | Partial relocalization to the cytoplasm. | ||||
Sequence: K → A | ||||||
Mutagenesis | 243 | Relocalization to the cytosol. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_027155 | 406 | in dbSNP:rs17854621 | |||
Sequence: R → S | ||||||
Mutagenesis | 532 | Abolishes ADP-ribosyltransferase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 564 | Abolishes ADP-ribosyltransferase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 631 | Does not affect ADP-ribosyltransferase activity. | ||||
Sequence: I → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 671 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, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000247835 | 1-657 | Protein mono-ADP-ribosyltransferase TIPARP | |||
Sequence: MEMETTEPEPDCVVQPPSPPDDFSCQMRLSEKITPLKTCFKKKDQKRLGTGTLRSLRPILNTLLESGSLDGVFRSRNQSTDENSLHEPMMKKAMEINSSCPPAENNMSVLIPDRTNVGDQIPEAHPSTEAPERVVPIQDHSFPSETLSGTVADSTPAHFQTDLLHPVSSDVPTSPDCLDKVIDYVPGIFQENSFTIQYILDTSDKLSTELFQDKSEEASLDLVFELVNQLQYHTHQENGIEICMDFLQGTCIYGRDCLKHHTVLPYHWQIKRTTTQKWQSVFNDSQEHLERFYCNPENDRMRMKYGGQEFWADLNAMNVYETTEFDQLRRLSTPPSSNVNSIYHTVWKFFCRDHFGWREYPESVIRLIEEANSRGLKEVRFMMWNNHYILHNSFFRREIKRRPLFRSCFILLPYLQTLGGVPTQAPPPLEATSSSQIICPDGVTSANFYPETWVYMHPSQDFIQVPVSAEDKSYRIIYNLFHKTVPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMFGRDRIINERHLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSKGVHFMFLAKVLTGRYTMGSHGMRRPPPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQYEEVSNTVSI | ||||||
Modified residue | 39 | ADP-ribosylcysteine | ||||
Sequence: C |
Post-translational modification
Auto-mono-ADP-ribosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, motif, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MEMETTEPEPDCVVQPPSPPD | ||||||
Motif | 41-47 | Nuclear localization signal | ||||
Sequence: KKKDQKR | ||||||
Zinc finger | 237-264 | C3H1-type | ||||
Sequence: ENGIEICMDFLQGTCIYGRDCLKHHTVL | ||||||
Domain | 332-410 | WWE | ||||
Sequence: STPPSSNVNSIYHTVWKFFCRDHFGWREYPESVIRLIEEANSRGLKEVRFMMWNNHYILHNSFFRREIKRRPLFRSCFI | ||||||
Domain | 449-657 | PARP catalytic | ||||
Sequence: YPETWVYMHPSQDFIQVPVSAEDKSYRIIYNLFHKTVPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMFGRDRIINERHLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSKGVHFMFLAKVLTGRYTMGSHGMRRPPPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQYEEVSNTVSI |
Sequence similarities
Belongs to the ARTD/PARP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length657
- Mass (Da)76,227
- Last updated2003-10-01 v1
- Checksum1E63E311F1B36CEB
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 43 | in Ref. 1; CAH18441 | ||||
Sequence: K → E | ||||||
Sequence conflict | 582 | in Ref. 1; CAH18441 | ||||
Sequence: G → R | ||||||
Sequence conflict | 633 | in Ref. 1; CAH18441 | ||||
Sequence: V → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL080156 EMBL· GenBank· DDBJ | CAB45747.2 EMBL· GenBank· DDBJ | mRNA | ||
BX537965 EMBL· GenBank· DDBJ | CAD97929.1 EMBL· GenBank· DDBJ | mRNA | ||
CR749647 EMBL· GenBank· DDBJ | CAH18441.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78725.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78728.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC050350 EMBL· GenBank· DDBJ | AAH50350.2 EMBL· GenBank· DDBJ | mRNA |