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Q99836 (MYD88_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myeloid differentiation primary response protein MyD88
Gene names
Name:MYD88
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.9 Ref.13 Ref.17

Subunit structure

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subcellular location

Cytoplasm Ref.9 Ref.10.

Tissue specificity

Ubiquitous. Ref.1

Domain

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

Involvement in disease

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. Ref.17 Ref.19

Sequence similarities

Contains 1 death domain.

Contains 1 TIR domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process3'-UTR-mediated mRNA stabilization

Inferred from direct assay PubMed 15294994. Source: BHF-UCL

JNK cascade

Inferred from electronic annotation. Source: Ensembl

MyD88-dependent toll-like receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

Toll signaling pathway

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 9374458. Source: ProtInc

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

immunoglobulin mediated immune response

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: InterPro

positive regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-17 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-23 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-6 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of lymphocyte proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of inflammatory response

Inferred from sequence or structural similarity. Source: BHF-UCL

response to interleukin-1

Inferred from mutant phenotype PubMed 19281832. Source: BHF-UCL

response to molecule of fungal origin

Inferred from electronic annotation. Source: Ensembl

response to peptidoglycan

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement Ref.2. Source: ProtInc

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

type I interferon biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionTIR domain binding

Inferred from physical interaction PubMed 19509286. Source: BHF-UCL

death receptor binding

Traceable author statement PubMed 9374458. Source: ProtInc

identical protein binding

Inferred from physical interaction PubMed 11544529PubMed 21516116PubMed 21988832. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99836-1)

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.
Isoform 2 (identifier: Q99836-2)

The sequence of this isoform differs from the canonical sequence as follows:
     110-154: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q99836-3)

The sequence of this isoform differs from the canonical sequence as follows:
     156-296: HMPERFDAFI...TRLAKALSLP → AAGWWWLSLM...ASLQVPIRSD
Note: No experimental confirmation available.
Isoform 4 (identifier: Q99836-4)

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.
Isoform 5 (identifier: Q99836-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MAAGGPGAGSAAPVSSTSSLPL → M
Isoform 6 (identifier: Q99836-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Myeloid differentiation primary response protein MyD88
PRO_0000096666

Regions

Domain54 – 10956Death
Domain159 – 296138TIR
Region110 – 15546Intermediate domain By similarity

Natural variations

Alternative sequence1 – 2222MAAGG…SSLPL → M in isoform 5.
VSP_053764
Alternative sequence110 – 15445Missing in isoform 2.
VSP_038887
Alternative sequence1101E → G in isoform 4.
VSP_043498
Alternative sequence111 – 15545Missing in isoform 4.
VSP_043499
Alternative sequence156 – 296141HMPER…ALSLP → AAGWWWLSLMITCRARNVTS RPNLHSASLQVPIRSD in isoform 3 and isoform 4.
VSP_043500
Alternative sequence2151R → RLARRPRGG in isoform 6.
VSP_053765
Natural variant931L → P in MYD88D; results in a loss of function. Ref.19
VAR_047953
Natural variant1961R → C in MYD88D; results in a loss of function. Ref.17 Ref.19
VAR_047954

Experimental info

Mutagenesis1961R → A: Reduced interaction with TIRAP, and strongly reduced activity. Strongly reduced interaction with TIRAP; when associated with A-288. Ref.17
Mutagenesis1971D → A: Slightly reduced activity. Ref.17
Mutagenesis2171R → A: Strongly reduced activity. Ref.17
Mutagenesis2821K → A: Slightly reduced activity. Ref.17
Mutagenesis2881R → A: Slightly reduced activity, and reduced interaction with TIRAP. Strongly reduced interaction with TIRAP; when associated with A-196. Ref.17
Sequence conflict981R → C in AAB49967. Ref.1
Sequence conflict1901K → T in BI524129. Ref.8
Sequence conflict223 – 2242VS → WL in BI524129. Ref.8

Secondary structure

..................................................... 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: CEAE3F6B99524333

FASTA29633,233
        10         20         30         40         50         60 
MAAGGPGAGS AAPVSSTSSL PLAALNMRVR RRLSLFLNVR TQVAADWTAL AEEMDFEYLE 

        70         80         90        100        110        120 
IRQLETQADP TGRLLDAWQG RPGASVGRLL ELLTKLGRDD VLLELGPSIE EDCQKYILKQ 

       130        140        150        160        170        180 
QQEEAEKPLQ VAAVDSSVPR TAELAGITTL DDPLGHMPER FDAFICYCPS DIQFVQEMIR 

       190        200        210        220        230        240 
QLEQTNYRLK LCVSDRDVLP GTCVWSIASE LIEKRCRRMV VVVSDDYLQS KECDFQTKFA 

       250        260        270        280        290 
LSLSPGAHQK RLIPIKYKAM KKEFPSILRF ITVCDYTNPC TKSWFWTRLA KALSLP 

« Hide

Isoform 2 [UniParc].

Checksum: 1841504370960C90
Show »

FASTA25128,280
Isoform 3 [UniParc].

Checksum: 5995DBBBA11780B8
Show »

FASTA19120,777
Isoform 4 [UniParc].

Checksum: 6791101414C872CA
Show »

FASTA14615,823
Isoform 5 [UniParc].

Checksum: 06D06EECD46F5E2F
Show »

FASTA27531,496
Isoform 6 [UniParc].

Checksum: C6CE78108FE60498
Show »

FASTA30434,097

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Pyogenic bacterial infections in humans with MyD88 deficiency."
von Bernuth H., Picard C., Jin Z., Pankla R., Xiao H., Ku C.-L., Chrabieh M., Mustapha I.B., Ghandil P., Camcioglu Y., Vasconcelos J., Sirvent N., Guedes M., Vitor A.B., Herrero-Mata M.J., Arostegui J.I., Rodrigo C., Alsina L. expand/collapse author list , Ruiz-Ortiz E., Juan M., Fortuny C., Yaguee J., Anton J., Pascal M., Chang H.-H., Janniere L., Rose Y., Garty B.-Z., Chapel H., Issekutz A., Marodi L., Rodriguez-Gallego C., Banchereau J., Abel L., Li X., Chaussabel D., Puel A., Casanova J.-L.
Science 321:691-696(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MYD88D PRO-93 AND CYS-196, CHARACTERIZATION OF VARIANTS MYD88D PRO-93 AND CYS-196.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001166037.1. NM_001172566.1.
NP_001166039.1. NM_001172568.1.
NP_001166040.1. NM_001172569.1.
NP_002459.2. NM_002468.4.
UniGeneHs.82116.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ99836.
SMRQ99836. Positions 20-117, 146-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110700. 57 interactions.
DIPDIP-31349N.
IntActQ99836. 33 interactions.
MINTMINT-97233.
STRING9606.ENSP00000379625.

Chemistry

ChEMBLCHEMBL5919.

PTM databases

PhosphoSiteQ99836.

Polymorphism databases

DMDM18202671.

Proteomic databases

PaxDbQ99836.
PRIDEQ99836.

Protocols and materials databases

DNASU4615.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396334; ENSP00000379625; ENSG00000172936.
ENST00000417037; ENSP00000401399; ENSG00000172936.
ENST00000424893; ENSP00000389979; ENSG00000172936.
ENST00000443433; ENSP00000390565; ENSG00000172936. [Q99836-3]
ENST00000495303; ENSP00000417848; ENSG00000172936. [Q99836-4]
GeneID4615.
KEGGhsa:4615.
UCSCuc011ayj.2. human. [Q99836-3]
uc011ayk.2. human. [Q99836-4]

Organism-specific databases

CTD4615.
GeneCardsGC03P038179.
HGNCHGNC:7562. MYD88.
HPACAB009104.
HPA042919.
MIM602170. gene.
612260. phenotype.
neXtProtNX_Q99836.
Orphanet183713. Pyogenic bacterial infections due to MyD88 deficiency.
33226. Waldenstrom macroglobulinemia.
PharmGKBPA31361.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70664.
HOGENOMHOG000070050.
HOVERGENHBG052547.
InParanoidQ99836.
KOK04729.
OMARCKRMVV.
OrthoDBEOG7H792K.
PhylomeDBQ99836.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkQ99836.

Gene expression databases

ArrayExpressQ99836.
BgeeQ99836.
CleanExHS_MYD88.
GenevestigatorQ99836.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
3.40.50.10140. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR017281. Myelin_different_resp_MyD88.
IPR000157. TIR_dom.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFPIRSF037756. MyD88. 1 hit.
SMARTSM00005. DEATH. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF52200. SSF52200. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYD88. human.
EvolutionaryTraceQ99836.
GeneWikiMYD88.
GenomeRNAi4615.
NextBio17764.
PROQ99836.
SOURCESearch...

Entry information

Entry nameMYD88_HUMAN
AccessionPrimary (citable) accession number: Q99836
Secondary accession number(s): B4DKH8 expand/collapse secondary AC list , B4DKU4, B4DQ60, B4DQ72, J3KPU4, J3KQ87, J3KQJ6, P78397, Q53XS7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM