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Q99836

- MYD88_HUMAN

UniProt

Q99836 - MYD88_HUMAN

Protein

Myeloid differentiation primary response protein MyD88

Gene

MYD88

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. 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. 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.4 Publications

    GO - Molecular functioni

    1. death receptor binding Source: ProtInc
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. TIR domain binding Source: BHF-UCL

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: BHF-UCL
    2. cell surface receptor signaling pathway Source: ProtInc
    3. cellular response to mechanical stimulus Source: UniProtKB
    4. defense response to Gram-positive bacterium Source: UniProtKB
    5. inflammatory response Source: UniProtKB-KW
    6. innate immune response Source: Reactome
    7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    8. negative regulation of apoptotic process Source: Reactome
    9. neurotrophin TRK receptor signaling pathway Source: Reactome
    10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    11. positive regulation of interleukin-17 production Source: BHF-UCL
    12. positive regulation of interleukin-23 production Source: BHF-UCL
    13. positive regulation of interleukin-6 production Source: BHF-UCL
    14. positive regulation of type I interferon production Source: Reactome
    15. regulation of inflammatory response Source: BHF-UCL
    16. response to interleukin-1 Source: BHF-UCL
    17. signal transduction Source: ProtInc
    18. toll-like receptor 10 signaling pathway Source: Reactome
    19. toll-like receptor 2 signaling pathway Source: Reactome
    20. toll-like receptor 4 signaling pathway Source: Reactome
    21. toll-like receptor 5 signaling pathway Source: Reactome
    22. toll-like receptor 9 signaling pathway Source: Reactome
    23. toll-like receptor signaling pathway Source: Reactome
    24. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    25. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_13415. p75NTR recruits signalling complexes.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_22442. Interleukin-1 signaling.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    SignaLinkiQ99836.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myeloid differentiation primary response protein MyD88
    Gene namesi
    Name:MYD88
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:7562. MYD88.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome membrane Source: Reactome
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    MYD88 deficiency (MYD88D) [MIM:612260]: Patients suffer from autosomal recessive, life-threatening, often recurrent pyogenic bacterial infections, including invasive pneumococcal disease, and die between 1 and 11 months of age. Surviving patients are otherwise healthy, with normal resistance to other microbes, and their clinical status improved with age.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931L → P in MYD88D; results in a loss of function. 1 Publication
    VAR_047953
    Natural varianti196 – 1961R → C in MYD88D; results in a loss of function. 1 Publication
    VAR_047954

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi196 – 1961R → A: Reduced interaction with TIRAP, and strongly reduced activity. Strongly reduced interaction with TIRAP; when associated with A-288. 1 Publication
    Mutagenesisi197 – 1971D → A: Slightly reduced activity. 1 Publication
    Mutagenesisi217 – 2171R → A: Strongly reduced activity. 1 Publication
    Mutagenesisi282 – 2821K → A: Slightly reduced activity. 1 Publication
    Mutagenesisi288 – 2881R → A: Slightly reduced activity, and reduced interaction with TIRAP. Strongly reduced interaction with TIRAP; when associated with A-196. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612260. phenotype.
    Orphaneti183713. Pyogenic bacterial infections due to MyD88 deficiency.
    33226. Waldenstrom macroglobulinemia.
    PharmGKBiPA31361.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296Myeloid differentiation primary response protein MyD88PRO_0000096666Add
    BLAST

    Proteomic databases

    MaxQBiQ99836.
    PaxDbiQ99836.
    PRIDEiQ99836.

    PTM databases

    PhosphoSiteiQ99836.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ99836.
    BgeeiQ99836.
    CleanExiHS_MYD88.
    GenevestigatoriQ99836.

    Organism-specific databases

    HPAiCAB009104.
    HPA042919.

    Interactioni

    Subunit structurei

    Homodimer. Also forms heterodimers with TIRAP. Binds to TLR2, TLR4, IRAK1, IRAK2 and IRAK4 via their respective TIR domains. Interacts with IL18R1. Interacts with BMX, IL1RL1, IKBKE and IRF7. Interacts with LRRFIP1 and LRRFIP2; this interaction positively regulates Toll-like receptor (TLR) signaling in response to agonist. Interacts with FLII. LRRFIP1 and LRRFIP2 compete with FLII for MYD88-binding. Interacts with IRF1. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and TRAF6; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. May interact with PIK3AP1.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-447677,EBI-447677
    Q034633EBI-447677,EBI-8803426From a different organism.
    DOCK8Q8NF503EBI-447677,EBI-2548605
    FADDQ131583EBI-447677,EBI-494804
    IRAK1P516172EBI-447677,EBI-358664
    SIAH1Q8IUQ43EBI-447677,EBI-747107
    SMAD3P840223EBI-447677,EBI-347161
    SPOPO437916EBI-447677,EBI-743549
    STAP2Q9UGK33EBI-447677,EBI-1553984
    TIRAPP587536EBI-447677,EBI-528644
    TNFRSF13BO1483612EBI-447677,EBI-519160
    TXNP105994EBI-447677,EBI-594644
    USP7Q930093EBI-447677,EBI-302474

    Protein-protein interaction databases

    BioGridi110700. 57 interactions.
    DIPiDIP-31349N.
    IntActiQ99836. 33 interactions.
    MINTiMINT-97233.
    STRINGi9606.ENSP00000379625.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Helixi27 – 3711
    Beta strandi42 – 443
    Helixi47 – 515
    Turni52 – 554
    Helixi58 – 647
    Beta strandi66 – 694
    Helixi70 – 7910
    Beta strandi80 – 834
    Helixi86 – 9611
    Helixi99 – 1024
    Helixi106 – 1127
    Turni114 – 1163
    Beta strandi159 – 1668
    Helixi169 – 1713
    Helixi172 – 18312
    Beta strandi185 – 1873
    Beta strandi191 – 1944
    Helixi196 – 1983
    Helixi209 – 2113
    Helixi212 – 2154
    Beta strandi216 – 2238
    Helixi227 – 2293
    Helixi231 – 24212
    Helixi247 – 2515
    Beta strandi252 – 2565
    Helixi266 – 2683
    Beta strandi269 – 2713
    Helixi279 – 2813
    Helixi285 – 29410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JS7NMR-A146-296[»]
    2Z5VNMR-A148-296[»]
    3MOPX-ray3.40A/B/C/D/E/F20-117[»]
    4DOMX-ray1.80A157-296[»]
    4EO7X-ray1.45A157-296[»]
    ProteinModelPortaliQ99836.
    SMRiQ99836. Positions 20-117, 146-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99836.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 10956DeathPROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 296138TIRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 15546Intermediate domainBy similarityAdd
    BLAST

    Domaini

    The intermediate domain (ID) is required for the phosphorylation and activation of IRAK.By similarity

    Sequence similaritiesi

    Contains 1 death domain.PROSITE-ProRule annotation
    Contains 1 TIR domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG70664.
    HOGENOMiHOG000070050.
    HOVERGENiHBG052547.
    InParanoidiQ99836.
    KOiK04729.
    OMAiRCKRMVV.
    OrthoDBiEOG7H792K.
    PhylomeDBiQ99836.

    Family and domain databases

    Gene3Di1.10.533.10. 1 hit.
    3.40.50.10140. 1 hit.
    InterProiIPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR017281. Myelin_different_resp_MyD88.
    IPR000157. TIR_dom.
    [Graphical view]
    PfamiPF00531. Death. 1 hit.
    PF01582. TIR. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037756. MyD88. 1 hit.
    SMARTiSM00005. DEATH. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF52200. SSF52200. 1 hit.
    PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99836-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAGGPGAGS AAPVSSTSSL PLAALNMRVR RRLSLFLNVR TQVAADWTAL    50
    AEEMDFEYLE IRQLETQADP TGRLLDAWQG RPGASVGRLL ELLTKLGRDD 100
    VLLELGPSIE EDCQKYILKQ QQEEAEKPLQ VAAVDSSVPR TAELAGITTL 150
    DDPLGHMPER FDAFICYCPS DIQFVQEMIR QLEQTNYRLK LCVSDRDVLP 200
    GTCVWSIASE LIEKRCRRMV VVVSDDYLQS KECDFQTKFA LSLSPGAHQK 250
    RLIPIKYKAM KKEFPSILRF ITVCDYTNPC TKSWFWTRLA KALSLP 296
    Length:296
    Mass (Da):33,233
    Last modified:May 1, 1997 - v1
    Checksum:iCEAE3F6B99524333
    GO
    Isoform 2 (identifier: Q99836-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         110-154: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:251
    Mass (Da):28,280
    Checksum:i1841504370960C90
    GO
    Isoform 3 (identifier: Q99836-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         156-296: HMPERFDAFI...TRLAKALSLP → AAGWWWLSLM...ASLQVPIRSD

    Note: No experimental confirmation available.

    Show »
    Length:191
    Mass (Da):20,777
    Checksum:i5995DBBBA11780B8
    GO
    Isoform 4 (identifier: Q99836-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         110-110: E → G
         111-155: Missing.
         156-296: HMPERFDAFI...TRLAKALSLP → AAGWWWLSLM...ASLQVPIRSD

    Note: No experimental confirmation available.

    Show »
    Length:146
    Mass (Da):15,823
    Checksum:i6791101414C872CA
    GO
    Isoform 5 (identifier: Q99836-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MAAGGPGAGSAAPVSSTSSLPL → M

    Show »
    Length:275
    Mass (Da):31,496
    Checksum:i06D06EECD46F5E2F
    GO
    Isoform 6 (identifier: Q99836-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-215: R → RLARRPRGG

    Show »
    Length:304
    Mass (Da):34,097
    Checksum:iC6CE78108FE60498
    GO

    Sequence cautioni

    The sequence BAG60822.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAG60834.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAW64521.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981R → C in AAB49967. (PubMed:8957090)Curated
    Sequence conflicti190 – 1901K → T in BI524129. (PubMed:15489334)Curated
    Sequence conflicti223 – 2242VS → WL in BI524129. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931L → P in MYD88D; results in a loss of function. 1 Publication
    VAR_047953
    Natural varianti196 – 1961R → C in MYD88D; results in a loss of function. 1 Publication
    VAR_047954

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222MAAGG…SSLPL → M in isoform 5. 1 PublicationVSP_053764Add
    BLAST
    Alternative sequencei110 – 15445Missing in isoform 2. 1 PublicationVSP_038887Add
    BLAST
    Alternative sequencei110 – 1101E → G in isoform 4. 1 PublicationVSP_043498
    Alternative sequencei111 – 15545Missing in isoform 4. 1 PublicationVSP_043499Add
    BLAST
    Alternative sequencei156 – 296141HMPER…ALSLP → AAGWWWLSLMITCRARNVTS RPNLHSASLQVPIRSD in isoform 3 and isoform 4. 1 PublicationVSP_043500Add
    BLAST
    Alternative sequencei215 – 2151R → RLARRPRGG in isoform 6. 1 PublicationVSP_053765

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70451 mRNA. Translation: AAB49967.1.
    U84408 mRNA. Translation: AAC50954.1.
    AB446470 mRNA. Translation: BAG55247.1.
    BT007376 mRNA. Translation: AAP36040.1.
    AK296570 mRNA. Translation: BAG59190.1.
    AK296716 mRNA. Translation: BAG59306.1.
    AK298650 mRNA. Translation: BAG60822.1. Different initiation.
    AK298666 mRNA. Translation: BAG60834.1. Different initiation.
    AP006309 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64521.1. Sequence problems.
    BC013589 mRNA. Translation: AAH13589.1.
    BI524129 mRNA. No translation available.
    RefSeqiNP_001166037.1. NM_001172566.1.
    NP_001166039.1. NM_001172568.1.
    NP_001166040.1. NM_001172569.1.
    NP_002459.2. NM_002468.4.
    UniGeneiHs.82116.

    Genome annotation databases

    EnsembliENST00000443433; ENSP00000390565; ENSG00000172936. [Q99836-3]
    ENST00000495303; ENSP00000417848; ENSG00000172936. [Q99836-4]
    GeneIDi4615.
    KEGGihsa:4615.
    UCSCiuc011ayi.2. human.
    uc011ayj.2. human. [Q99836-3]
    uc011ayk.2. human. [Q99836-4]

    Polymorphism databases

    DMDMi18202671.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70451 mRNA. Translation: AAB49967.1 .
    U84408 mRNA. Translation: AAC50954.1 .
    AB446470 mRNA. Translation: BAG55247.1 .
    BT007376 mRNA. Translation: AAP36040.1 .
    AK296570 mRNA. Translation: BAG59190.1 .
    AK296716 mRNA. Translation: BAG59306.1 .
    AK298650 mRNA. Translation: BAG60822.1 . Different initiation.
    AK298666 mRNA. Translation: BAG60834.1 . Different initiation.
    AP006309 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64521.1 . Sequence problems.
    BC013589 mRNA. Translation: AAH13589.1 .
    BI524129 mRNA. No translation available.
    RefSeqi NP_001166037.1. NM_001172566.1.
    NP_001166039.1. NM_001172568.1.
    NP_001166040.1. NM_001172569.1.
    NP_002459.2. NM_002468.4.
    UniGenei Hs.82116.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JS7 NMR - A 146-296 [» ]
    2Z5V NMR - A 148-296 [» ]
    3MOP X-ray 3.40 A/B/C/D/E/F 20-117 [» ]
    4DOM X-ray 1.80 A 157-296 [» ]
    4EO7 X-ray 1.45 A 157-296 [» ]
    ProteinModelPortali Q99836.
    SMRi Q99836. Positions 20-117, 146-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110700. 57 interactions.
    DIPi DIP-31349N.
    IntActi Q99836. 33 interactions.
    MINTi MINT-97233.
    STRINGi 9606.ENSP00000379625.

    Chemistry

    ChEMBLi CHEMBL5919.

    PTM databases

    PhosphoSitei Q99836.

    Polymorphism databases

    DMDMi 18202671.

    Proteomic databases

    MaxQBi Q99836.
    PaxDbi Q99836.
    PRIDEi Q99836.

    Protocols and materials databases

    DNASUi 4615.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000443433 ; ENSP00000390565 ; ENSG00000172936 . [Q99836-3 ]
    ENST00000495303 ; ENSP00000417848 ; ENSG00000172936 . [Q99836-4 ]
    GeneIDi 4615.
    KEGGi hsa:4615.
    UCSCi uc011ayi.2. human.
    uc011ayj.2. human. [Q99836-3 ]
    uc011ayk.2. human. [Q99836-4 ]

    Organism-specific databases

    CTDi 4615.
    GeneCardsi GC03P038179.
    HGNCi HGNC:7562. MYD88.
    HPAi CAB009104.
    HPA042919.
    MIMi 602170. gene.
    612260. phenotype.
    neXtProti NX_Q99836.
    Orphaneti 183713. Pyogenic bacterial infections due to MyD88 deficiency.
    33226. Waldenstrom macroglobulinemia.
    PharmGKBi PA31361.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70664.
    HOGENOMi HOG000070050.
    HOVERGENi HBG052547.
    InParanoidi Q99836.
    KOi K04729.
    OMAi RCKRMVV.
    OrthoDBi EOG7H792K.
    PhylomeDBi Q99836.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_13415. p75NTR recruits signalling complexes.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_22442. Interleukin-1 signaling.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    SignaLinki Q99836.

    Miscellaneous databases

    ChiTaRSi MYD88. human.
    EvolutionaryTracei Q99836.
    GeneWikii MYD88.
    GenomeRNAii 4615.
    NextBioi 17764.
    PROi Q99836.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99836.
    Bgeei Q99836.
    CleanExi HS_MYD88.
    Genevestigatori Q99836.

    Family and domain databases

    Gene3Di 1.10.533.10. 1 hit.
    3.40.50.10140. 1 hit.
    InterProi IPR011029. DEATH-like_dom.
    IPR000488. Death_domain.
    IPR017281. Myelin_different_resp_MyD88.
    IPR000157. TIR_dom.
    [Graphical view ]
    Pfami PF00531. Death. 1 hit.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037756. MyD88. 1 hit.
    SMARTi SM00005. DEATH. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF52200. SSF52200. 1 hit.
    PROSITEi PS50017. DEATH_DOMAIN. 1 hit.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization and modular analysis of human MyD88."
      Hardiman G., Rock F.L., Balasubramanian S., Kastelein R.A., Bazan J.F.
      Oncogene 13:2467-2475(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Dendritic cell.
    2. "The cloning and characterization of human MyD88: a member of an IL-1 receptor related family."
      Bonnert T.P., Garka K.E., Parnet P., Sonoda G., Testa J.R., Sims J.E.
      FEBS Lett. 402:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Epidermal carcinoma.
    3. "Natural selection in the TLR-related genes in the course of primate evolution."
      Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.
      Immunogenetics 60:727-735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
      Tissue: Umbilical cord blood.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 190-224 (ISOFORM 6).
      Tissue: Pancreas.
    9. "Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6."
      Kawai T., Sato S., Ishii K.J., Coban C., Hemmi H., Yamamoto M., Terai K., Matsuda M., Inoue J., Uematsu S., Takeuchi O., Akira S.
      Nat. Immunol. 5:1061-1068(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IRF7.
    10. "Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling."
      Honda K., Yanai H., Mizutani T., Negishi H., Shimada N., Suzuki N., Ohba Y., Takaoka A., Yeh W.C., Taniguchi T.
      Proc. Natl. Acad. Sci. U.S.A. 101:15416-15421(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IRF7.
    11. "IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST 2 and induces T helper type 2-associated cytokines."
      Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K., Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F., Kastelein R.A.
      Immunity 23:479-490(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL1RL1.
    12. "Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1."
      Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S., Kim I.H., Kim S.J., Park S.H.
      Nat. Immunol. 7:1057-1065(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH IRAK1; IRAK4; TRAF6 AND PELI1.
    13. "Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
      Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
      J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BMX.
    14. "Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins."
      Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.
      J. Immunol. 182:3450-3460(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLII; LRRFIP1 AND LRRFIP2.
    15. "AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling."
      Wan T., Liu T., Zhang H., Tang S., Min W.
      J. Biol. Chem. 285:3750-3757(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIRAP.
    16. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
      Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
      Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKBKE.
    17. "Structural basis for the multiple interactions of the MyD88 TIR domain in TLR4 signaling."
      Ohnishi H., Tochio H., Kato Z., Orii K.E., Li A., Kimura T., Hiroaki H., Kondo N., Shirakawa M.
      Proc. Natl. Acad. Sci. U.S.A. 106:10260-10265(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 148-296, FUNCTION, INTERACTION WITH TIRAP AND IRAK4, MUTAGENESIS OF ARG-196; ASP-197; ARG-217; LYS-282 AND ARG-288, CHARACTERIZATION OF VARIANT MYD88D CYS-196.
    18. "Solution NMR structure of human myeloid differentiation primary response (MYD88)."
      Northeast structural genomics consortium (NESG)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 146-296.
    19. Cited for: VARIANTS MYD88D PRO-93 AND CYS-196, CHARACTERIZATION OF VARIANTS MYD88D PRO-93 AND CYS-196.

    Entry informationi

    Entry nameiMYD88_HUMAN
    AccessioniPrimary (citable) accession number: Q99836
    Secondary accession number(s): B4DKH8
    , B4DKU4, B4DQ60, B4DQ72, J3KPU4, J3KQ87, J3KQJ6, P78397, Q53XS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3