PARP10
entrez
84875
canonical
uniprot
Q53GL7
canonical
ensembl
ENSG00000178685
resolver
ensp
ENSP00000325618
resolver
ensp
ENSP00000431620
resolver
ensp
ENSP00000432733
resolver
ensp
ENSP00000434776
resolver
ensp
ENSP00000527457
resolver
ensp
ENSP00000527458
resolver
ensp
ENSP00000527459
resolver
ensp
ENSP00000527460
resolver
ensp
ENSP00000584273
resolver
ensp
ENSP00000636800
resolver
ensp
ENSP00000636801
resolver
ensp
ENSP00000636802
resolver
ensp
ENSP00000636803
resolver
enst
ENST00000313028
resolver
enst
ENST00000524918
resolver
enst
ENST00000525773
resolver
enst
ENST00000527262
resolver
enst
ENST00000857398
resolver
enst
ENST00000857399
resolver
enst
ENST00000857400
resolver
enst
ENST00000857401
resolver
enst
ENST00000914214
resolver
enst
ENST00000966741
resolver
enst
ENST00000966742
resolver
enst
ENST00000966743
resolver
enst
ENST00000966744
resolver
genesymbol
PARP10
resolver
hgnc
HGNC:25895
resolver
uniprot
B4E0C4
resolver
uniprot
E9PK67
resolver
uniprot
E9PNI7
resolver
uniprot
E9PPE7
resolver
uniprot
Q8N2I0
resolver
uniprot
Q8WV05
resolver
uniprot
Q96CH7
resolver
uniprot
Q96K72
resolver
uniprot_entry
B4E0C4_HUMAN
resolver
uniprot_entry
E9PK67_HUMAN
resolver
uniprot_entry
E9PNI7_HUMAN
resolver
uniprot_entry
E9PPE7_HUMAN
resolver
uniprot_entry
PAR10_HUMAN
resolver
uniprot_sec
Q8N2I0
resolver
uniprot_sec
Q8WV05
resolver
uniprot_sec
Q96CH7
resolver
uniprot_sec
Q96K72
resolver
amino_acid_sequence
MVAMAEAEAGVAVEVRGLPPAVPDELLTLYFENRRRSGGGPVLSWQRLGCGGVLTFREPADAERVLAQADHELHGAQLSLRPAPPRAPARLLLQGLPPGTTPQRLEQHVQALLRASGLPVQPCCALASPRPDRALVQLPKPLSEADVRVLEEQAQNLGLEGTLVSLARVPQARAVRVVGDGASVDLLLLELYLENERRSGGGPLEDLQRLPGPLGTVASFQQWQVAERVLQQEHRLQGSELSLVPHYDILEPEELAENTSGGDHPSTQGPRATKHALLRTGGLVTALQGAGTVTMGSGEEPGQSGASLRTGPMVQGRGIMTTGSGQEPGQSGTSLRTGPMGSLGQAEQVSSMPMGSLEHEGLVSLRPVGLQEQEGPMSLGPVGSAGPVETSKGLLGQEGLVEIAMDSPEQEGLVGPMEITMGSLEKAGPVSPGCVKLAGQEGLVEMVLLMEPGAMRFLQLYHEDLLAGLGDVALLPLEGPDMTGFRLCGAQASCQAAEEFLRSLLGSISCHVLCLEHPGSARFLLGPEGQHLLQGLEAQFQCVFGTERLATATLDTGLEEVDPTEALPVLPGNAHTLWTPDSTGGDQEDVSLEEVRELLATLEGLDLDGEDWLPRELEEEGPQEQPEEEVTPGHEEEEPVAPSTVAPRWLEEEAALQLALHRSLEPQGQVAEQEEAAALRQALTLSLLEQPPLEAEEPPDGGTDGKAQLVVHSAFEQDVEELDRALRAALEVHVQEETVGPWRRTLPAELRARLERCHGVSVALRGDCTILRGFGAHPARAARHLVALLAGPWDQSLAFPLAASGPTLAGQTLKGPWNNLERLAENTGEFQEVVRAFYDTLDAARSSIRVVRVERVSHPLLQQQYELYRERLLQRCERRPVEQVLYHGTTAPAVPDICAHGFNRSFCGRNATVYGKGVYFARRASLSVQDRYSPPNADGHKAVFVARVLTGDYGQGRRGLRAPPLRGPGHVLLRYDSAVDCICQPSIFVIFHDTQALPTHLITCEHVPRASPDDPSGLPGRSPDT
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
function
FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate and aspartate residues on target proteins (PubMed:18851833, PubMed:23332125, PubMed:23474714, PubMed:25043379). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:18851833). Catalyzes mono-ADP-ribosylation of GSK3B, leading to negatively regulate GSK3B kinase activity (PubMed:23332125). Involved in translesion DNA synthesis in response to DNA damage via its interaction with PCNA (PubMed:24695737). {ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:23332125, ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:24695737, ECO:0000269|PubMed:25043379}.
uniprot
proteins
mass_dalton
109998
uniprot
proteins
mutagenesis
MUTAGEN 650..690; /note="Missing: Decreased interaction with PCNA."; /evidence="ECO:0000269|PubMed:24695737"; MUTAGEN 831..838; /note="QEVVRAFY->AEVARAAA: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:24695737"; MUTAGEN 882; /note="E->A: Decreased auto-mono-ADP-ribosylation."; /evidence="ECO:0000269|PubMed:18851833"; MUTAGEN 888; /note="G->W: Abolishes catalytic activity; abolishes interaction with PARP14."; /evidence="ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:23473667, ECO:0000269|PubMed:24695737"; MUTAGEN 980..982; /note="DCI->ACA: Strongly decreased catalytic activity."; /evidence="ECO:0000269|PubMed:18851833"; MUTAGEN 985; /note="P->A: Strongly decreased catalytic activity."; /evidence="ECO:0000269|PubMed:18851833"; MUTAGEN 987; /note="I->E: Decreased catalytic activity."; /evidence="ECO:0000269|PubMed:18851833"; MUTAGEN 999; /note="T->A: Does not affect catalytic activity."; /evidence="ECO:0000269|PubMed:18851833
uniprot
proteins
post_translational_modification
PTM: Stimulated through its phosphorylation by CDK2 (PubMed:16455663). Acquires CDK-dependent phosphorylation through late-G1 to S phase, and from prometaphase to cytokinesis in the nucleolar organizing regions (PubMed:16455663). Phosphorylation is suppressed in growth-arrested cells (PubMed:16455663). {ECO:0000269|PubMed:16455663}.; PTM: Auto-mono-ADP-ribosylated on glutamate and lysine residues. {ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:25043379}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15674325
uniprot
proteins
pubmed
16455663
uniprot
proteins
pubmed
18851833
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20106667
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23332125
uniprot
proteins
pubmed
23473667
uniprot
proteins
pubmed
23474714
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24695737
uniprot
proteins
pubmed
25043379
uniprot
proteins
sequence_length
1025
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15674325}. Cytoplasm {ECO:0000269|PubMed:15674325}. Note=Shuttles between the nuclear and cytoplasmic compartment (PubMed:15674325). A subpopulation concentrates in the nucleolus during late G1/S phase (PubMed:15674325). {ECO:0000269|PubMed:15674325}.
uniprot
proteins