PELI1
entrez
57162
canonical
uniprot
Q96FA3
canonical
ensembl
ENSG00000197329
resolver
ensp
ENSP00000351789
resolver
ensp
ENSP00000573289
resolver
ensp
ENSP00000573290
resolver
ensp
ENSP00000595047
resolver
ensp
ENSP00000595048
resolver
ensp
ENSP00000612911
resolver
ensp
ENSP00000612912
resolver
enst
ENST00000358912
resolver
enst
ENST00000903230
resolver
enst
ENST00000903231
resolver
enst
ENST00000924988
resolver
enst
ENST00000924989
resolver
enst
ENST00000942852
resolver
enst
ENST00000942853
resolver
genesymbol
PELI1
resolver
genesymbol_syn
PRISM
resolver
hgnc
HGNC:8827
resolver
uniprot
D6W5E7
resolver
uniprot
Q53T26
resolver
uniprot
Q96SM0
resolver
uniprot
Q9GZY5
resolver
uniprot
Q9HCX0
resolver
uniprot_entry
PELI1_HUMAN
resolver
uniprot_entry
Q53T26_HUMAN
resolver
uniprot_sec
D6W5E7
resolver
uniprot_sec
Q96SM0
resolver
uniprot_sec
Q9GZY5
resolver
uniprot_sec
Q9HCX0
resolver
amino_acid_sequence
MFSPDQENHPSKAPVKYGELIVLGYNGSLPNGDRGRRKSRFALFKRPKANGVKPSTVHIACTPQAAKAISNKDQHSISYTLSRAQTVVVEYTHDSNTDMFQIGRSTESPIDFVVTDTVPGSQSNSDTQSVQSTISRFACRIICERNPPFTARIYAAGFDSSKNIFLGEKAAKWKTSDGQMDGLTTNGVLVMHPRNGFTEDSKPGIWREISVCGNVFSLRETRSAQQRGKMVEIETNQLQDGSLIDLCGATLLWRTAEGLSHTPTVKHLEALRQEINAARPQCPVGFNTLAFPSMKRKDVVDEKQPWVYLNCGHVHGYHNWGNKEERDGKDRECPMCRSVGPYVPLWLGCEAGFYVDAGPPTHAFSPCGHVCSEKTTAYWSQIPLPHGTHTFHAACPFCAHQLAGEQGYIRLIFQGPLD
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:12496252, PubMed:17675297, PubMed:29883609, PubMed:30952868). Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6 (PubMed:12496252, PubMed:17675297). Acts as a positive regulator of inflammatory response in microglia through activation of NF-kappa-B and MAP kinase (By similarity). Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation (PubMed:12496252, PubMed:17675297). Conjugates 'Lys-63'-linked ubiquitin chains to the adapter protein ASC/PYCARD, which in turn is crucial for NLRP3 inflammasome activation (PubMed:34706239). Mediates 'Lys-48'-linked polyubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation; preferentially recognizes and mediates the degradation of the 'Thr-182' phosphorylated form of RIPK3 (PubMed:29883609). Negatively regulates necroptosis by reducing RIPK3 expression (PubMed:29883609). Mediates 'Lys-63'-linked ubiquitination of RIPK1 (PubMed:29883609). Following phosphorylation by ATM, catalyzes 'Lys-63'-linked ubiquitination of NBN, promoting DNA repair via homologous recombination (PubMed:30952868). Negatively regulates activation of the metabolic mTORC1 signaling pathway by mediating 'Lys-63'-linked ubiquitination of mTORC1-inhibitory protein TSC1 and thereby promoting TSC1/TSC2 complex stability (PubMed:33215753). {ECO:0000250|UniProtKB:Q8C669, ECO:0000269|PubMed:12496252, ECO:0000269|PubMed:17675297, ECO:0000269|PubMed:29883609, ECO:0000269|PubMed:30952868, ECO:0000269|PubMed:33215753}.
uniprot
proteins
mass_dalton
46286
uniprot
proteins
mutagenesis
MUTAGEN 104; /note="R->A: Loss of ability to ubiquitinate RIPK3. Loss of interaction with RIPK1, IRAK1 and RIPK3."; /evidence="ECO:0000269|PubMed:29883609"; MUTAGEN 121; /note="S->A: Decreased phosphorylation by ATM in response to DNA damage; when associated with A-127."; /evidence="ECO:0000269|PubMed:30952868"; MUTAGEN 127; /note="T->A: Decreased phosphorylation by ATM in response to DNA damage; when associated with A-121."; /evidence="ECO:0000269|PubMed:30952868"; MUTAGEN 313; /note="H->A: Loss of ability to ubiquitinate RIPK3 and NBN. No loss of interaction with RIPK3."; /evidence="ECO:0000269|PubMed:29883609, ECO:0000269|PubMed:30952868"; MUTAGEN 336; /note="C->A: Loss of ability to ubiquitinate RIPK3 and NBN. No loss of interaction with RIPK3."; /evidence="ECO:0000269|PubMed:29883609, ECO:0000269|PubMed:30952868
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:30952868}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by IRAK1 and IRAK4 enhances its E3 ligase activity (PubMed:17997719). Phosphorylated by ATM in response to DNA damage, promoting localization to DNA double-strand breaks (DSBs) and ability to mediate 'Lys-63'-linked ubiquitination of NBN (PubMed:30952868). {ECO:0000269|PubMed:17997719, ECO:0000269|PubMed:30952868}.; PTM: Sumoylated. {ECO:0000269|PubMed:21120624}.
uniprot
proteins
protein_family
Pellino family
uniprot
proteins
pubmed
11132151
uniprot
proteins
pubmed
11306823
uniprot
proteins
pubmed
12496252
uniprot
proteins
pubmed
12804775
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16951688
uniprot
proteins
pubmed
17675297
uniprot
proteins
pubmed
17997719
uniprot
proteins
pubmed
21120624
uniprot
proteins
pubmed
29883609
uniprot
proteins
pubmed
30952868
uniprot
proteins
pubmed
33215753
uniprot
proteins
pubmed
34706239
uniprot
proteins
sequence_length
418
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:17997719}. Note=Localizes to DNA double-strand breaks (DSBs) in response to DNA damage. {ECO:0000269|PubMed:17997719}.
uniprot
proteins