PIDD1
entrez
55367
canonical
uniprot
Q9HB75
canonical
ensembl
ENSG00000177595
resolver
ensp
ENSP00000337797
resolver
ensp
ENSP00000652838
resolver
ensp
ENSP00000722738
resolver
genesymbol
PIDD1
resolver
genesymbol_syn
LRDD
resolver
genesymbol_syn
PIDD
resolver
hgnc
HGNC:16491
resolver
uniprot
Q59FD1
resolver
uniprot
Q59H10
resolver
uniprot
Q59HC7
resolver
uniprot
Q7Z4P8
resolver
uniprot
Q8NC89
resolver
uniprot
Q8NDL2
resolver
uniprot
Q96C25
resolver
uniprot
Q9NRE6
resolver
uniprot_entry
PIDD1_HUMAN
resolver
uniprot_sec
Q59FD1
resolver
uniprot_sec
Q59H10
resolver
uniprot_sec
Q59HC7
resolver
uniprot_sec
Q7Z4P8
resolver
uniprot_sec
Q8NC89
resolver
uniprot_sec
Q8NDL2
resolver
uniprot_sec
Q96C25
resolver
uniprot_sec
Q9NRE6
resolver
amino_acid_sequence
MAATVEGPELEAAAAAGDASEDSDAGSRALPFLGGNRLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHEDPQLLEATLAQLPQSLSCLRSLVLKGGQRRDTLGACLRGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDAPSSPVAALIPEMPRLFLTSDLDSFPVTPQGCSVTLACGVRLQFPAGATATPITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFTPPQARRCREVVVRTRNDNSWGDLETYLEEEAPQRLWAHCQVPHFSWFLVVSRPVSNACLVPPEGTLLCSSGHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGPPSFLQPVTVQLPLPSGITGLSLDRSRLHLLYWAPPAATWDDITAQVVLELTHLYARFQVTHFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLPRNKVDATLRRLLERYRGPEPSDTVEMFEGEEFFAAFERGIDVDADRPDCVEGRICFVFYSHLKNVKEVYVTTTLDREAQAVRGQVSFYRGAVPVRVPEEAEAARQRKGADALWMATLPIKLPRLRGSEGPRRGAGLSLAPLNLGDAETGFLTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVRAVLELGRRKYQDSIRRMGLAPKDPALPGSSAPQPPEPAQA
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal recessive 75, with neuropsychiatric features and variant lissencephaly (MRT75) [MIM:619827]: An autosomal recessive disorder characterized by global developmental delay apparent from infancy or early childhood, impaired intellectual development, and behavioral and psychiatric abnormalities. Some patients present seizures and facial dysmorphism. Brain imaging often shows cortical anomalies. {ECO:0000269|PubMed:28397838, ECO:0000269|PubMed:29302074, ECO:0000269|PubMed:33414379, ECO:0000269|PubMed:34163010}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis (PubMed:10973264, PubMed:15073321, PubMed:16360037, PubMed:17159900). Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis (PubMed:15073321, PubMed:17159900). Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B (PubMed:16360037, PubMed:17159900). {ECO:0000269|PubMed:10973264, ECO:0000269|PubMed:15073321, ECO:0000269|PubMed:16360037, ECO:0000269|PubMed:17159900}.
uniprot
proteins
mass_dalton
99712
uniprot
proteins
mutagenesis
MUTAGEN 444; /note="H->Q: Loss of the proteolytic cleavage producing PIDD-C."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 445; /note="F->H,W: Loss of the proteolytic cleavage producing PIDD-C."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 446; /note="S->A: Loss of the proteolytic cleavage producing PIDD-C. Unable to translocate to the nucleus upon DNA damage. No effect on the ability to activate CASP2. Complete loss of proteolytic cleavage; when associated with A-588."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 446; /note="S->C: No effect on the proteolytic cleavage producing PIDD-C."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 582; /note="F->A: Loss of the proteolytic cleavage producing PIDD-CC."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 587; /note="F->H: Loss of the proteolytic cleavage producing PIDD-CC."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 588; /note="S->A: Loss of the proteolytic cleavage producing PIDD-CC. Loss of interaction with CRADD and of the ability to activate CASP2. No effect on translocation to the nucleus upon DNA damage. Complete loss of proteolytic cleavage; when associated with A-446."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 588; /note="S->C: No effect on the proteolytic cleavage producing PIDD-CC."; /evidence="ECO:0000269|PubMed:17159900"; MUTAGEN 801; /note="L->A: No effect on complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 814; /note="Y->A: Loss of complex assembly with CRADD. Loss of PIDDosome assembly. Loss of CASP2 activation."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 815; /note="R->A: Partial loss of complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 815; /note="R->E: Loss of complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 825; /note="R->A: Partial loss of complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 825; /note="R->E: Partial loss of complex assembly with CRADD. Decreased PIDDosome assembly. Decreased CASP2 activation."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 826; /note="D->K: Partial loss of complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 828; /note="L->E: Loss of complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 830; /note="E->K: No effect on complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 837; /note="F->D: Loss of complex assembly with CRADD. Loss of PIDDosome assembly. Loss of CASP2 activation."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 862; /note="R->A: Loss of complex assembly with CRADD. Loss of PIDDosome assembly. Loss of CASP2 activation."; /evidence="ECO:0000269|PubMed:17289572"; MUTAGEN 863; /note="Q->A: Partial loss of complex assembly with CRADD."; /evidence="ECO:0000269|PubMed:17289572
uniprot
proteins
post_translational_modification
PTM: Undergoes autoproteolytic processing whose extent either directs cells towards survival or apoptotic pathways (PubMed:17159900). Autoproteolytically cleaved into two main fragments PIDD-N and PIDD-C (PubMed:17159900). PIDD-C can be further processed into PIDD-CC, a processing which is enhanced by DNA damage (PubMed:17159900). The cleavage producing PIDD-C is required for translocation of PIDD1 to the nucleus upon DNA damage and activation of NF-kappa-B (PubMed:17159900). PIDD-CC mediates the interaction with CRADD and the cleavage producing PIDD-CC is required for the activation of CASP2 (PubMed:17159900). PIDD-N remains associated with PIDD-C and PIDD-CC after cleavage (PubMed:17159900). {ECO:0000269|PubMed:17159900}.
uniprot
proteins
pubmed
10825539
uniprot
proteins
pubmed
10973264
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15073321
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16360037
uniprot
proteins
pubmed
16652156
uniprot
proteins
pubmed
17159900
uniprot
proteins
pubmed
17289572
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
28397838
uniprot
proteins
pubmed
29302074
uniprot
proteins
pubmed
33414379
uniprot
proteins
pubmed
34163010
uniprot
proteins
pubmed
39532532
uniprot
proteins
sequence_length
910
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16360037, ECO:0000269|PubMed:17159900, ECO:0000269|PubMed:39532532}. Nucleus {ECO:0000269|PubMed:16360037, ECO:0000269|PubMed:17159900}. Note=Enriched in the nucleus upon DNA damage. {ECO:0000269|PubMed:17159900}.
uniprot
proteins