RNF31
entrez
55072
canonical
uniprot
Q96EP0
canonical
ensembl
ENSG00000092098
resolver
ensembl
ENSG00000259529
resolver
ensembl
ENSG00000284845
resolver
ensembl
ENSG00000285152
resolver
ensp
ENSP00000315112
resolver
ensp
ENSP00000453574
resolver
genesymbol
RNF31
resolver
genesymbol_syn
ZIBRA
resolver
hgnc
HGNC:16031
resolver
uniprot
A0A962
resolver
uniprot
Q86VI2
resolver
uniprot
Q8TEI0
resolver
uniprot
Q96GB4
resolver
uniprot
Q96NF1
resolver
uniprot
Q9H5F1
resolver
uniprot
Q9NWD2
resolver
uniprot_entry
RNF31_HUMAN
resolver
uniprot_sec
A0A962
resolver
uniprot_sec
Q86VI2
resolver
uniprot_sec
Q8TEI0
resolver
uniprot_sec
Q96GB4
resolver
uniprot_sec
Q96NF1
resolver
uniprot_sec
Q9H5F1
resolver
uniprot_sec
Q9NWD2
resolver
amino_acid_sequence
MPGEEEERAFLVAREELASALRRDSGQAFSLEQLRPLLASSLPLAARYLQLDAARLVRCNAHGEPRNYLNTLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGGRDVLRLYGYTEEQPDGLSFPEGQEEPDEHQVATVTLEVLLLRTELSLLLQNTHPRQQALEQLLEDKVEDDMLQLSEFDPLLREIAPGPLTTPSVPGSTPGPCFLCGSAPGTLHCPSCKQALCPACDHLFHGHPSRAHHLRQTLPGVLQGTHLSPSLPASAQPRPQSTSLLALGDSSLSSPNPASAHLPWHCAACAMLNEPWAVLCVACDRPRGCKGLGLGTEGPQGTGGLEPDLARGRWACQSCTFENEAAAVLCSICERPRLAQPPSLVVDSRDAGICLQPLQQGDALLASAQSQVWYCIHCTFCNSSPGWVCVMCNRTSSPIPAQHAPRPYASSLEKGPPKPGPPRRLSAPLPSSCGDPEKQRQDKMREEGLQLVSMIREGEAAGACPEEIFSALQYSGTEVPLQWLRSELPYVLEMVAELAGQQDPGLGAFSCQEARRAWLDRHGNLDEAVEECVRTRRRKVQELQSLGFGPEEGSLQALFQHGGDVSRALTELQRQRLEPFRQRLWDSGPEPTPSWDGPDKQSLVRRLLAVYALPSWGRAELALSLLQETPRNYELGDVVEAVRHSQDRAFLRRLLAQECAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGRPDLTDDTQLLSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRDPKFLWCAQCSFGFIYEREQLEATCPQCHQTFCVRCKRQWEEQHRGRSCEDFQNWKRMNDPEYQAQGLAMYLQENGIDCPKCKFSYALARGGCMHFHCTQCRHQFCSGCYNAFYAKNKCPEPNCRVKKSLHGHHPRDCLFYLRDWTALRLQKLLQDNNVMFNTEPPAGARAVPGGGCRVIEQKEVPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINAHSLDPATLYEVEELETATERYLHVRPQPLAGEDPPAYQARLLQKLTEEVPLGQSIPRRRK
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 115 with autoinflammation (IMD115) [MIM:620632]: An autosomal recessive immunologic disorder manifesting in early infancy and characterized by combined immunodeficiency, recurrent bacterial, viral, and fungal infections, as well as autoinflammatory features, including arthritis and dermatitis. {ECO:0000269|PubMed:26008899, ECO:0000269|PubMed:30936877}. Note=The disease is caused by variants affecting the gene represented in this entry. The genetic variation producing the missense variant p.Q399H, associated with IMD115, has been shown to predominantly affect splicing, leading to in-frame skipping of exon 9 and lack of 84 amino acids from residue 496 to 579. {ECO:0000269|PubMed:30936877}.
uniprot
proteins
ec_number
2.3.2.31
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase 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:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684, PubMed:28481331). 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:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:28189684). 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:20005846, PubMed:27458237). 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, PubMed:34012115). 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). Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed:34012115). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331, PubMed:34012115). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998). RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (PubMed:27777308). Binds polyubiquitin of different linkage types (PubMed:23708998). {ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:22863777, ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27777308, ECO:0000269|PubMed:28189684, ECO:0000269|PubMed:28481331, ECO:0000269|PubMed:34012115}.
uniprot
proteins
mass_dalton
119652
uniprot
proteins
mutagenesis
MUTAGEN 82; /note="Y->A: Abolished interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 82; /note="Y->F: Reduced interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 85; /note="N->A: Reduced interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 99; /note="K->E: Reduced interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 101; /note="N->R: Does not affect interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 102; /note="N->A: Abolished interaction with SPATA2."; /evidence="ECO:0000269|PubMed:27458237"; MUTAGEN 102; /note="N->D: Abolished interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 104; /note="V->A: Reduced interaction with OTULIN."; /evidence="ECO:0000269|PubMed:24726323"; MUTAGEN 360; /note="T->A: Decreased ubiquitin-binding and ability to promote formation of the bacterial ubiquitin coat."; /evidence="ECO:0000269|PubMed:28481331"; MUTAGEN 390; /note="D->A: Abolishes cleavage by caspase."; /evidence="ECO:0000269|PubMed:28189684"; MUTAGEN 699; /note="C->S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702."; /evidence="ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:21455181"; MUTAGEN 702; /note="C->S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699."; /evidence="ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:21455181"; MUTAGEN 735; /note="K->R: Reduced ubiquitination; when associated with R-783 and R-875."; /evidence="ECO:0000269|PubMed:27572974"; MUTAGEN 783; /note="K->R: Reduced ubiquitination; when associated with R-735 and R-875."; /evidence="ECO:0000269|PubMed:27572974"; MUTAGEN 871; /note="C->S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874."; /evidence="ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:21455181"; MUTAGEN 874; /note="C->S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871."; /evidence="ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:21455181"; MUTAGEN 875; /note="K->R: Reduced ubiquitination; when associated with R-735 and R-783."; /evidence="ECO:0000269|PubMed:27572974"; MUTAGEN 885; /note="C->A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-935 and A-983."; /evidence="ECO:0000269|PubMed:28481331"; MUTAGEN 935; /note="R->A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-983."; /evidence="ECO:0000269|PubMed:28481331"; MUTAGEN 983; /note="D->A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-935."; /evidence="ECO:0000269|PubMed:28481331
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:28481331}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated (PubMed:24726323). Interaction with OTULIN is required to suppress formation of 'Met-1'-linked polyubiquitin chains and prevent subsequent inactivation of the LUBAC complex (PubMed:24726323). {ECO:0000269|PubMed:24726323}.; PTM: Cleaved by caspase during apoptosis. {ECO:0000269|PubMed:28189684}.; 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. {ECO:0000269|PubMed:27572974, ECO:0000269|PubMed:28481331, ECO:0000269|PubMed:35294289}.
uniprot
proteins
protein_family
RBR family
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12693554
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15093743
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17006537
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
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
22863777
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23708998
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24726323
uniprot
proteins
pubmed
24726327
uniprot
proteins
pubmed
26008899
uniprot
proteins
pubmed
26997266
uniprot
proteins
pubmed
27458237
uniprot
proteins
pubmed
27545878
uniprot
proteins
pubmed
27572974
uniprot
proteins
pubmed
27591049
uniprot
proteins
pubmed
27777308
uniprot
proteins
pubmed
28189684
uniprot
proteins
pubmed
28481331
uniprot
proteins
pubmed
30936877
uniprot
proteins
pubmed
34012115
uniprot
proteins
pubmed
35294289
uniprot
proteins
sequence_length
1072
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q924T7}.
uniprot
proteins