PARP11
entrez
57097
canonical
uniprot
Q9NR21
canonical
ensembl
ENSG00000111224
resolver
ensp
ENSP00000228820
resolver
ensp
ENSP00000395062
resolver
ensp
ENSP00000397058
resolver
ensp
ENSP00000405385
resolver
ensp
ENSP00000666621
resolver
enst
ENST00000453942
resolver
genesymbol
PARP11
resolver
genesymbol_syn
C12orf6
resolver
hgnc
HGNC:1186
resolver
uniprot
B4DRQ0
resolver
uniprot
F8WBZ7
resolver
uniprot
G3V0I3
resolver
uniprot
Q68DS1
resolver
uniprot
Q8N5Y9
resolver
uniprot_entry
G3V0I3_HUMAN
resolver
uniprot_entry
PAR11_HUMAN
resolver
uniprot_sec
B4DRQ0
resolver
uniprot_sec
F8WBZ7
resolver
uniprot_sec
Q68DS1
resolver
uniprot_sec
Q8N5Y9
resolver
amino_acid_sequence
MWEANPEMFHKAEELFSKTTNNEVDDMDTSDTQWGWFYLAECGKWHMFQPDTNSQCSVSSEDIEKSFKTNPCGSISFTTSKFSYKIDFAEMKQMNLTTGKQRLIKRAPFSISAFSYICENEAIPMPPHWENVNTQVPYQLIPLHNQTHEYNEVANLFGKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGIHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDFH
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
function
FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins (PubMed:25043379, PubMed:25673562). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity). Inhibits the type I interferon activated signaling pathway (PubMed:30988430). Mechanistically, mono-ADP-ribosylates beta-TrCP/BTRC to promote IFNAR1 ubiquitination and protect BTRC from ubiquitin-proteasome degradation. Additionally, acts as an antiviral factor by cooperating with PARP12 to suppress Zika virus replication, independent of IFNAR1 regulation or intrinsic PARP enzymatic activity (PubMed:34187568). Instead, facilitates the degradation of viral NS1 and NS3 proteins, potentially disrupting viral replication (PubMed:34187568). {ECO:0000250|UniProtKB:Q8CFF0, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25673562, ECO:0000269|PubMed:30988430, ECO:0000269|PubMed:34187568}.
uniprot
proteins
mass_dalton
39597
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="Y->A: No effect on subcellular location at the nuclear envelope."; /evidence="ECO:0000269|PubMed:25673562"; MUTAGEN 48; /note="F->A: No effect on subcellular location at the nuclear envelope."; /evidence="ECO:0000269|PubMed:25673562"; MUTAGEN 84; /note="Y->A: Loss of subcellular location at the nuclear envelope."; /evidence="ECO:0000269|PubMed:25673562"; MUTAGEN 93; /note="Q->A: Loss of subcellular location at the nuclear envelope."; /evidence="ECO:0000269|PubMed:25673562"; MUTAGEN 102; /note="R->A: Loss of subcellular location at the nuclear envelope."; /evidence="ECO:0000269|PubMed:25673562"; MUTAGEN 204; /note="H->S: Catalytically inactive mutant; when associated with S-236."; /evidence="ECO:0000269|PubMed:30988430"; MUTAGEN 205; /note="G->A: Catalytically inactive mutant."; /evidence="ECO:0000269|PubMed:34187568"; MUTAGEN 205; /note="G->W: No effect on subcellular location at the nuclear envelope."; /evidence="ECO:0000269|PubMed:25673562"; MUTAGEN 236; /note="Y->S: Catalytically inactive mutant; when associated with S-204."; /evidence="ECO:0000269|PubMed:30988430
uniprot
proteins
post_translational_modification
PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25673562}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
20106667
uniprot
proteins
pubmed
25043379
uniprot
proteins
pubmed
25673562
uniprot
proteins
pubmed
30988430
uniprot
proteins
pubmed
34187568
uniprot
proteins
sequence_length
338
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25673562}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000269|PubMed:25673562}.
uniprot
proteins