MYD88
entrez
4615
canonical
uniprot
Q99836
canonical
ensembl
ENSG00000172936
resolver
ensp
ENSP00000391753
resolver
ensp
ENSP00000401399
resolver
ensp
ENSP00000497991
resolver
ensp
ENSP00000498360
resolver
ensp
ENSP00000498576
resolver
ensp
ENSP00000499012
resolver
ensp
ENSP00000514121
resolver
ensp
ENSP00000655683
resolver
enst
ENST00000417037
resolver
enst
ENST00000650112
resolver
enst
ENST00000651800
resolver
enst
ENST00000652213
resolver
genesymbol
MYD88
resolver
hgnc
HGNC:7562
resolver
uniprot
A0A0A0MSI9
resolver
uniprot
A0A0A0MST0
resolver
uniprot
A0A3B3ITY3
resolver
uniprot
A0A3F2YP85
resolver
uniprot
A0A494C0J8
resolver
uniprot
B4DKH8
resolver
uniprot
B4DKU4
resolver
uniprot
B4DQ60
resolver
uniprot
B4DQ72
resolver
uniprot
J3KPU4
resolver
uniprot
J3KQ87
resolver
uniprot
J3KQJ6
resolver
uniprot
P78397
resolver
uniprot
Q53XS7
resolver
uniprot_entry
A0A0A0MSI9_HUMAN
resolver
uniprot_entry
A0A3B3ITY3_HUMAN
resolver
uniprot_entry
A0A3F2YP85_HUMAN
resolver
uniprot_entry
A0A494C0J8_HUMAN
resolver
uniprot_entry
MYD88_HUMAN
resolver
uniprot_sec
A0A0A0MST0
resolver
uniprot_sec
B4DKH8
resolver
uniprot_sec
B4DKU4
resolver
uniprot_sec
B4DQ60
resolver
uniprot_sec
B4DQ72
resolver
uniprot_sec
J3KPU4
resolver
uniprot_sec
J3KQ87
resolver
uniprot_sec
J3KQJ6
resolver
uniprot_sec
P78397
resolver
uniprot_sec
Q53XS7
resolver
amino_acid_sequence
MAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYILKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTNPCTKSWFWTRLAKALSLP
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 68 (IMD68) [MIM:612260]: An autosomal recessive primary immunodeficiency characterized by life-threatening, often recurrent, pyogenic bacterial infections, including invasive pneumococcal disease, beginning in infancy or early childhood. {ECO:0000269|PubMed:18669862, ECO:0000269|PubMed:19506249, ECO:0000269|PubMed:21057262, ECO:0000269|PubMed:24316379}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Macroglobulinemia, Waldenstrom, 1 (WM1) [MIM:153600]: A malignant B-cell neoplasm characterized by lymphoplasmacytic infiltration of the bone marrow and hypersecretion of monoclonal immunoglobulin M (IgM) protein. Clinical features are variable and include anemia, thrombocytopenia, hepatosplenomegaly, and lymphadenopathy. Many patients have asymptomatic or indolent disease. {ECO:0000269|PubMed:21179087, ECO:0000269|PubMed:22931316, ECO:0000269|PubMed:24366360}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in MYD88 are frequently found in many hematological malignancies, such as activated B-cell type diffuse large B-cell lymphoma (ABC-DLBCL), cutaneous diffuse large B cell lymphoma (CBCL) and primary central nervous system lymphoma (PCNSL). {ECO:0000269|PubMed:21179087, ECO:0000269|PubMed:22931316}.
uniprot
proteins
function
FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response (PubMed:15361868, PubMed:18292575, PubMed:33718825, PubMed:37971847). Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:15361868, PubMed:19506249, PubMed:24316379, PubMed:40638072). Increases IL-8 transcription (PubMed:9013863). Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses such as SARS-CoV-2, SARS-CoV and HIV-1, induces IL1B release through NLRP3 inflammasome activation (PubMed:33718825). MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine (By similarity). {ECO:0000250|UniProtKB:P22366, ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:19506249, ECO:0000269|PubMed:20855887, ECO:0000269|PubMed:24316379, ECO:0000269|PubMed:33718825, ECO:0000269|PubMed:37971847, ECO:0000269|PubMed:40638072, ECO:0000269|PubMed:9013863}.
uniprot
proteins
mass_dalton
33233
uniprot
proteins
mutagenesis
MUTAGEN 179; /note="I->N: In Pococurante (Poc); abolished MYD88-dependent sensing of most Toll-like receptor (TLR) ligands."; /evidence="ECO:0000269|PubMed:23569230"; MUTAGEN 196; /note="R->A: Reduced interaction with TIRAP, and strongly reduced activity. Strongly reduced interaction with TIRAP; when associated with A-288."; /evidence="ECO:0000269|PubMed:19506249"; MUTAGEN 197; /note="D->A: Slightly reduced activity."; /evidence="ECO:0000269|PubMed:19506249"; MUTAGEN 203; /note="C->S: Abolished interaction with E.coli TcpC without affecting ability to promote Toll-like receptor (TLR)-mediated cytokine production; when associated with S-280."; /evidence="ECO:0000269|PubMed:23569230"; MUTAGEN 217; /note="R->A: Strongly reduced activity."; /evidence="ECO:0000269|PubMed:19506249"; MUTAGEN 280; /note="C->S: Abolished interaction with E.coli TcpC without affecting ability to promote Toll-like receptor (TLR)-mediated cytokine production; when associated with S-203."; /evidence="ECO:0000269|PubMed:23569230"; MUTAGEN 282; /note="K->A: Slightly reduced activity."; /evidence="ECO:0000269|PubMed:19506249"; MUTAGEN 288; /note="R->A: Slightly reduced activity, and reduced interaction with TIRAP. Strongly reduced interaction with TIRAP; when associated with A-196."; /evidence="ECO:0000269|PubMed:19506249
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination. OTUD4 specifically hydrolyzes 'Lys-63'-linked polyubiquitinated MYD88 (PubMed:29395066). Deubiquitinated by USP3 that cleaves 'Lys-63'-linked ubiquitin chains leading to inhibition of MYD88-induced NF-kappa-B signaling (PubMed:37971847). Ubiquitinated by the complex made of the adapter SMAD6 and the E3 ligase SMURF1, leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P22366, ECO:0000269|PubMed:29395066, ECO:0000269|PubMed:37971847}.; PTM: (Microbial infection) Ubiquitinated by human herpesvirus 8 (KSHV) protein RTA/ORF50, leading to proteasomal degradation and suppression of TLR4 signaling pathway. {ECO:0000269|PubMed:25320320}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15361868
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492225
uniprot
proteins
pubmed
16286016
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16951688
uniprot
proteins
pubmed
17322885
uniprot
proteins
pubmed
18292575
uniprot
proteins
pubmed
18669862
uniprot
proteins
pubmed
18810425
uniprot
proteins
pubmed
19265123
uniprot
proteins
pubmed
19506249
uniprot
proteins
pubmed
19948740
uniprot
proteins
pubmed
20696886
uniprot
proteins
pubmed
20855887
uniprot
proteins
pubmed
20966070
uniprot
proteins
pubmed
21057262
uniprot
proteins
pubmed
21179087
uniprot
proteins
pubmed
22155231
uniprot
proteins
pubmed
22931316
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23453969
uniprot
proteins
pubmed
23569230
uniprot
proteins
pubmed
24265315
uniprot
proteins
pubmed
24316379
uniprot
proteins
pubmed
24366360
uniprot
proteins
pubmed
24618691
uniprot
proteins
pubmed
25320320
uniprot
proteins
pubmed
25369374
uniprot
proteins
pubmed
29395066
uniprot
proteins
pubmed
33718825
uniprot
proteins
pubmed
36232715
uniprot
proteins
pubmed
37971847
uniprot
proteins
pubmed
40638072
uniprot
proteins
pubmed
8957090
uniprot
proteins
pubmed
9013863
uniprot
proteins
sequence_length
296
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15492225, ECO:0000269|PubMed:37971847}. Nucleus {ECO:0000269|PubMed:21057262}.
uniprot
proteins