Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myeloid differentiation primary response protein MyD88

Gene

MYD88

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. death receptor binding Source: ProtInc
  2. identical protein binding Source: IntAct
  3. 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
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_163773. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
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 Componenti: 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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionPatients 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.

See also OMIM:612260
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 MyD88PRO_0000096666Add
BLAST

Proteomic databases

MaxQBiQ99836.
PaxDbiQ99836.
PRIDEiQ99836.

PTM databases

PhosphoSiteiQ99836.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ99836.
CleanExiHS_MYD88.
ExpressionAtlasiQ99836. baseline and differential.
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 – 243Combined sources
Helixi27 – 3711Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 515Combined sources
Turni52 – 554Combined sources
Helixi58 – 647Combined sources
Beta strandi66 – 694Combined sources
Helixi70 – 7910Combined sources
Beta strandi80 – 834Combined sources
Helixi86 – 9611Combined sources
Helixi99 – 1024Combined sources
Helixi106 – 1127Combined sources
Turni114 – 1163Combined sources
Beta strandi159 – 1668Combined sources
Helixi169 – 1713Combined sources
Helixi172 – 18312Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi191 – 1944Combined sources
Helixi196 – 1983Combined sources
Helixi209 – 2113Combined sources
Helixi212 – 2154Combined sources
Beta strandi216 – 2238Combined sources
Helixi227 – 2293Combined sources
Helixi231 – 24212Combined sources
Helixi247 – 2515Combined sources
Beta strandi252 – 2565Combined sources
Helixi266 – 2683Combined sources
Beta strandi269 – 2713Combined sources
Helixi279 – 2813Combined sources
Helixi285 – 29410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
HOGENOMiHOG000068971.
HOVERGENiHBG052547.
InParanoidiQ99836.
KOiK04729.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAGGPGAGS AAPVSSTSSL PLAALNMRVR RRLSLFLNVR TQVAADWTAL
60 70 80 90 100
AEEMDFEYLE IRQLETQADP TGRLLDAWQG RPGASVGRLL ELLTKLGRDD
110 120 130 140 150
VLLELGPSIE EDCQKYILKQ QQEEAEKPLQ VAAVDSSVPR TAELAGITTL
160 170 180 190 200
DDPLGHMPER FDAFICYCPS DIQFVQEMIR QLEQTNYRLK LCVSDRDVLP
210 220 230 240 250
GTCVWSIASE LIEKRCRRMV VVVSDDYLQS KECDFQTKFA LSLSPGAHQK
260 270 280 290
RLIPIKYKAM KKEFPSILRF ITVCDYTNPC TKSWFWTRLA KALSLP
Length:296
Mass (Da):33,233
Last modified:April 30, 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.Curated
The sequence BAG60834.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAW64521.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000495303; ENSP00000417848; ENSG00000172936.
GeneIDi4615.
KEGGihsa:4615.
UCSCiuc003chx.3. human.
uc011ayi.2. human.
uc011ayj.2. human. [Q99836-3]
uc011ayk.2. human. [Q99836-4]
uc011ayl.2. human.

Polymorphism databases

DMDMi18202671.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL5919.

PTM databases

PhosphoSiteiQ99836.

Polymorphism databases

DMDMi18202671.

Proteomic databases

MaxQBiQ99836.
PaxDbiQ99836.
PRIDEiQ99836.

Protocols and materials databases

DNASUi4615.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000443433; ENSP00000390565; ENSG00000172936.
ENST00000495303; ENSP00000417848; ENSG00000172936.
GeneIDi4615.
KEGGihsa:4615.
UCSCiuc003chx.3. human.
uc011ayi.2. human.
uc011ayj.2. human. [Q99836-3]
uc011ayk.2. human. [Q99836-4]
uc011ayl.2. human.

Organism-specific databases

CTDi4615.
GeneCardsiGC03P038179.
HGNCiHGNC:7562. MYD88.
HPAiCAB009104.
HPA042919.
MIMi602170. gene.
612260. phenotype.
neXtProtiNX_Q99836.
Orphaneti183713. Pyogenic bacterial infections due to MyD88 deficiency.
33226. Waldenstrom macroglobulinemia.
PharmGKBiPA31361.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG70664.
HOGENOMiHOG000068971.
HOVERGENiHBG052547.
InParanoidiQ99836.
KOiK04729.
OrthoDBiEOG7H792K.
PhylomeDBiQ99836.

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_13415. p75NTR recruits signalling complexes.
REACT_163773. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
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.

Miscellaneous databases

ChiTaRSiMYD88. human.
EvolutionaryTraceiQ99836.
GeneWikiiMYD88.
GenomeRNAii4615.
NextBioi17764.
PROiQ99836.
SOURCEiSearch...

Gene expression databases

BgeeiQ99836.
CleanExiHS_MYD88.
ExpressionAtlasiQ99836. baseline and differential.
GenevestigatoriQ99836.

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]
ProtoNetiSearch...

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(1995) [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(1996) [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(2007) [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 (APR-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(2003) [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(2005) [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(2003) [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(2003) [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(2003) [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(2004) [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(2005) [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(2007) [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(2008) [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(2009) [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(2012) [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(2008) [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 (JAN-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 17, 2001
Last sequence update: April 30, 1997
Last modified: March 31, 2015
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.