PIDD1_HUMAN - dbPTM
PIDD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIDD1_HUMAN
UniProt AC Q9HB75
Protein Name p53-induced death domain-containing protein 1
Gene Name PIDD1
Organism Homo sapiens (Human).
Sequence Length 910
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways..
Protein Sequence MAATVEGPELEAAAAAGDASEDSDAGSRALPFLGGNRLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHEDPQLLEATLAQLPQSLSCLRSLVLKGGQRRDTLGACLRGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDAPSSPVAALIPEMPRLFLTSDLDSFPVTPQGCSVTLACGVRLQFPAGATATPITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFTPPQARRCREVVVRTRNDNSWGDLETYLEEEAPQRLWAHCQVPHFSWFLVVSRPVSNACLVPPEGTLLCSSGHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGPPSFLQPVTVQLPLPSGITGLSLDRSRLHLLYWAPPAATWDDITAQVVLELTHLYARFQVTHFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLPRNKVDATLRRLLERYRGPEPSDTVEMFEGEEFFAAFERGIDVDADRPDCVEGRICFVFYSHLKNVKEVYVTTTLDREAQAVRGQVSFYRGAVPVRVPEEAEAARQRKGADALWMATLPIKLPRLRGSEGPRRGAGLSLAPLNLGDAETGFLTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVRAVLELGRRKYQDSIRRMGLAPKDPALPGSSAPQPPEPAQA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAATVEGPE
------CCCEECCHH
-
4Phosphorylation----MAATVEGPELE
----CCCEECCHHHH
-
90PhosphorylationAQLPQSLSCLRSLVL
HHHCHHHHHHHHHHH
24719451
98UbiquitinationCLRSLVLKGGQRRDT
HHHHHHHCCCCCCCH
-
299PhosphorylationGNPLGEASPDAPSSP
CCCCCCCCCCCCCCC
27080861
304PhosphorylationEASPDAPSSPVAALI
CCCCCCCCCCHHHHC
27080861
305PhosphorylationASPDAPSSPVAALIP
CCCCCCCCCHHHHCC
27080861
452PhosphorylationFSWFLVVSRPVSNAC
CEEEEEEECCCCCCE
24719451
485PhosphorylationVIFPPGATEEPRRVS
EEECCCCCCCCCHHH
19664995
639UbiquitinationLQCLPRNKVDATLRR
HHHCCCCCHHHHHHH
-
743UbiquitinationAEAARQRKGADALWM
HHHHHHHCCCCCEEE
-
788PhosphorylationDAETGFLTQSNLLSV
CCCCCCCCHHHHHHH
-
814PhosphorylationALHLGVSYREVQRIR
HHHHCCCHHHHHHHH
-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
788TPhosphorylationKinaseATMQ13315
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIDD1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PIDD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRADD_HUMANCRADDphysical
15073321
FADD_HUMANFADDphysical
10825539
MADD_HUMANMADDphysical
10825539
CASP2_HUMANCASP2physical
16360037
RIPK1_HUMANRIPK1physical
16360037
NEMO_HUMANIKBKGphysical
16360037
FADD_HUMANFADDphysical
16360037
CRADD_HUMANCRADDphysical
16360037
CRADD_HUMANCRADDphysical
21415862
CASP2_HUMANCASP2physical
21415862
PCNA_HUMANPCNAphysical
21415862
RFC5_HUMANRFC5physical
21415862
DPOD1_HUMANPOLD1physical
21415862
TELO2_HUMANTELO2physical
21415862
MCM7_HUMANMCM7physical
21415862
RPB2_HUMANPOLR2Bphysical
21415862
RPAP3_HUMANRPAP3physical
21415862
PPP6_HUMANPPP6Cphysical
21415862
DDB1_HUMANDDB1physical
21415862
FANCI_HUMANFANCIphysical
21415862
PRKDC_HUMANPRKDCphysical
21415862
ERCC2_HUMANERCC2physical
21415862
ERCC5_HUMANERCC5physical
21415862
AN32B_HUMANANP32Bphysical
21415862
HAX1_HUMANHAX1physical
21415862
AIFM1_HUMANAIFM1physical
21415862
TRI32_HUMANTRIM32physical
21415862
SENP3_HUMANSENP3physical
21415862
NUP93_HUMANNUP93physical
21415862
PRDX1_HUMANPRDX1physical
21415862
RFC4_HUMANRFC4physical
21415862
MDFI_HUMANMDFIphysical
19060904
TEAD3_HUMANTEAD3physical
21988832
MAFG_HUMANMAFGphysical
21988832
SOX8_HUMANSOX8physical
21988832
CRADD_HUMANCRADDphysical
23049853
CRYAB_HUMANCRYABphysical
23049853

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIDD1_HUMAN

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Related Literatures of Post-Translational Modification

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