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Q99836

- MYD88_HUMAN

UniProt

Q99836 - MYD88_HUMAN

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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

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

GO - Biological processi

  1. 3'-UTR-mediated mRNA stabilization Source: BHF-UCL
  2. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  3. cell surface receptor signaling pathway Source: ProtInc
  4. cellular response to mechanical stimulus Source: UniProtKB
  5. defense response to Gram-positive bacterium Source: UniProtKB
  6. inflammatory response Source: UniProtKB-KW
  7. innate immune response 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 TLR1:TLR2 signaling pathway Source: Reactome
  24. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  25. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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. 2 Publications
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 MyD88
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ99836.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 10956Death
Add
BLAST
Domaini159 – 296138TIR
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 15546Intermediate domain By similarity
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 death domain.
Contains 1 TIR domain.

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.

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. 2 Publications
VAR_047954

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222MAAGG…SSLPL → M in isoform 5.
VSP_053764Add
BLAST
Alternative sequencei110 – 15445Missing in isoform 2.
VSP_038887Add
BLAST
Alternative sequencei110 – 1101E → G in isoform 4.
VSP_043498
Alternative sequencei111 – 15545Missing in isoform 4.
VSP_043499Add
BLAST
Alternative sequencei156 – 296141HMPER…ALSLP → AAGWWWLSLMITCRARNVTS RPNLHSASLQVPIRSD in isoform 3 and isoform 4.
VSP_043500Add
BLAST
Alternative sequencei215 – 2151R → RLARRPRGG in isoform 6.
VSP_053765

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981R → C in AAB49967. 1 Publication
Sequence conflicti190 – 1901K → T in BI524129. 1 Publication
Sequence conflicti223 – 2242VS → WL in BI524129. 1 Publication

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

EnsembliENST00000396334; ENSP00000379625; ENSG00000172936.
ENST00000417037; ENSP00000401399; ENSG00000172936.
ENST00000424893; ENSP00000389979; ENSG00000172936.
ENST00000443433; 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 ENST00000396334 ; ENSP00000379625 ; ENSG00000172936 .
ENST00000417037 ; ENSP00000401399 ; ENSG00000172936 .
ENST00000424893 ; ENSP00000389979 ; ENSG00000172936 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 147 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

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