RBCK1
entrez
10616
canonical
uniprot
Q9BYM8
canonical
ensembl
ENSG00000125826
resolver
ensp
ENSP00000254960
resolver
ensp
ENSP00000348632
resolver
ensp
ENSP00000417173
resolver
ensp
ENSP00000513446
resolver
ensp
ENSP00000622232
resolver
ensp
ENSP00000622235
resolver
ensp
ENSP00000725829
resolver
ensp
ENSP00000755601
resolver
enst
ENST00000475269
resolver
enst
ENST00000697805
resolver
genesymbol
RBCK1
resolver
genesymbol_syn
C20orf18
resolver
genesymbol_syn
RNF54
resolver
genesymbol_syn
UBCE7IP3
resolver
genesymbol_syn
XAP3
resolver
genesymbol_syn
XAP4
resolver
hgnc
HGNC:15864
resolver
uniprot
A0A8V8TMZ2
resolver
uniprot
A6PVJ6
resolver
uniprot
O95623
resolver
uniprot
Q86SL2
resolver
uniprot
Q96BS3
resolver
uniprot
Q9BYM9
resolver
uniprot_entry
A0A8V8TMZ2_HUMAN
resolver
uniprot_entry
A6PVJ6_HUMAN
resolver
uniprot_entry
HOIL1_HUMAN
resolver
uniprot_sec
O95623
resolver
uniprot_sec
Q86SL2
resolver
uniprot_sec
Q96BS3
resolver
uniprot_sec
Q9BYM9
resolver
amino_acid_sequence
MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDIRLWVSVEDAQMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPVLQQWVIGQRLARDQETLHSHGVRQNGDSAYLYLLSARNTSLNPQELQRERQLRMLEDLGFKDLTLQPRGPLEPGPPKPGVPQEPGRGQPDAVPEPPPVGWQCPGCTFINKPTRPGCEMCCRARPEAYQVPASYQPDEEERARLAGEEEALRQYQQRKQQQQEGNYLQHVQLDQRSLVLNTEPAECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVSCPFIDNTYSCSGKLLEREIKALLTPEDYQRFLDLGISIAENRSAFSYHCKTPDCKGWCFFEDDVNEFTCPVCFHVNCLLCKAIHEQMNCKEYQEDLALRAQNDVAARQTTEMLKVMLQQGEAMRCPQCQIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH
uniprot
proteins
disease_involvement
DISEASE: Polyglucosan body myopathy 1 with or without immunodeficiency (PGBM1) [MIM:615895]: A disease characterized by polyglucosan storage myopathy associated with early-onset progressive muscle weakness and progressive dilated cardiomyopathy, which may necessitate cardiac transplant in severe cases. Some patients present with severe immunodeficiency, invasive bacterial infections and chronic autoinflammation. {ECO:0000269|PubMed:23104095, ECO:0000269|PubMed:23798481}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.31
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates (PubMed:12629548, PubMed:17449468, PubMed:18711448). Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination (PubMed:12629548). Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome (PubMed:17449468, PubMed:18711448). Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:17006537, PubMed:19136968, PubMed:21455173, PubMed:21455180, PubMed:21455181). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:21455173, PubMed:21455180, PubMed:21455181). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:17006537, PubMed:19136968, PubMed:21455173, PubMed:21455180, PubMed:21455181). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998). Binds polyubiquitin of different linkage types (PubMed:20005846, PubMed:21455181). {ECO:0000269|PubMed:12629548, ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:17449468, ECO:0000269|PubMed:18711448, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:28481331}.
uniprot
proteins
mass_dalton
57572
uniprot
proteins
mutagenesis
MUTAGEN 282; /note="C->S: Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-285."; /evidence="ECO:0000269|PubMed:12629548"; MUTAGEN 285; /note="C->S: Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-282."; /evidence="ECO:0000269|PubMed:12629548
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:12629548, ECO:0000269|PubMed:28481331}.
uniprot
proteins
post_translational_modification
PTM: Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q62921}.; PTM: Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity (By similarity). {ECO:0000250|UniProtKB:Q62921}.; PTM: (Microbial infection) Ubiquitinated by S.flexneri E3 ubiquitin-protein ligases IpaH1.4 and IpaH2.5, leading to its degradation by the proteasome, thereby preventing formation of the bacterial ubiquitin coat and activation of innate immunity (PubMed:27572974, PubMed:35294289). {ECO:0000269|PubMed:35294289, ECO:0000305|PubMed:27572974}.
uniprot
proteins
protein_family
RBR family
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12629548
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15951569
uniprot
proteins
pubmed
17006537
uniprot
proteins
pubmed
17449468
uniprot
proteins
pubmed
18711448
uniprot
proteins
pubmed
19136968
uniprot
proteins
pubmed
20005846
uniprot
proteins
pubmed
21455173
uniprot
proteins
pubmed
21455180
uniprot
proteins
pubmed
21455181
uniprot
proteins
pubmed
22430200
uniprot
proteins
pubmed
22517668
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23104095
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23708998
uniprot
proteins
pubmed
23798481
uniprot
proteins
pubmed
27572974
uniprot
proteins
pubmed
28481331
uniprot
proteins
pubmed
35294289
uniprot
proteins
pubmed
9195957
uniprot
proteins
sequence_length
510
uniprot
proteins