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Myeloid differentiation primary response protein MyD88

 MYD88_HUMAN             Reviewed;         296 AA.
Q99836; B4DKH8; B4DKU4; B4DQ60; B4DQ72; J3KPU4; J3KQ87; J3KQJ6;
P78397; Q53XS7;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
18-JUL-2018, entry version 187.
RecName: Full=Myeloid differentiation primary response protein MyD88;
Name=MYD88 {ECO:0000312|HGNC:HGNC:7562};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT CYS-98.
TISSUE=Dendritic cell;
PubMed=8957090;
Hardiman G., Rock F.L., Balasubramanian S., Kastelein R.A.,
Bazan J.F.;
"Molecular characterization and modular analysis of human MyD88.";
Oncogene 13:2467-2475(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Epidermal carcinoma;
PubMed=9013863; DOI=10.1016/S0014-5793(96)01506-2;
Bonnert T.P., Garka K.E., Parnet P., Sonoda G., Testa J.R., Sims J.E.;
"The cloning and characterization of human MyD88: a member of an IL-1
receptor related family.";
FEBS Lett. 402:81-84(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 190-224 (ISOFORM 6).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IRF7.
PubMed=15361868; DOI=10.1038/ni1118;
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.;
"Interferon-alpha induction through Toll-like receptors involves a
direct interaction of IRF7 with MyD88 and TRAF6.";
Nat. Immunol. 5:1061-1068(2004).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH IRF7.
PubMed=15492225; DOI=10.1073/pnas.0406933101;
Honda K., Yanai H., Mizutani T., Negishi H., Shimada N., Suzuki N.,
Ohba Y., Takaoka A., Yeh W.C., Taniguchi T.;
"Role of a transductional-transcriptional processor complex involving
MyD88 and IRF-7 in Toll-like receptor signaling.";
Proc. Natl. Acad. Sci. U.S.A. 101:15416-15421(2004).
[11]
INTERACTION WITH IL1RL1.
PubMed=16286016; DOI=10.1016/j.immuni.2005.09.015;
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.;
"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.";
Immunity 23:479-490(2005).
[12]
IDENTIFICATION IN COMPLEX WITH IRAK1; IRAK4; TRAF6 AND PELI1.
PubMed=16951688; DOI=10.1038/ni1383;
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.;
"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor
signaling through direct interaction with the adaptor Pellino-1.";
Nat. Immunol. 7:1057-1065(2006).
[13]
FUNCTION, AND INTERACTION WITH BMX.
PubMed=18292575; DOI=10.4049/jimmunol.180.5.3485;
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.;
"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the
cross-talk between MyD88 and FAK pathways.";
J. Immunol. 180:3485-3491(2008).
[14]
INTERACTION WITH FLII; LRRFIP1 AND LRRFIP2.
PubMed=19265123; DOI=10.4049/jimmunol.0802260;
Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.;
"Modulation of TLR signaling by multiple MyD88-interacting partners
including leucine-rich repeat Fli-I-interacting proteins.";
J. Immunol. 182:3450-3460(2009).
[15]
INTERACTION WITH TIRAP.
PubMed=19948740; DOI=10.1074/jbc.M109.069385;
Wan T., Liu T., Zhang H., Tang S., Min W.;
"AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.";
J. Biol. Chem. 285:3750-3757(2010).
[16]
INTERACTION WITH DHX9.
PubMed=20696886; DOI=10.1073/pnas.1006539107;
Kim T., Pazhoor S., Bao M., Zhang Z., Hanabuchi S., Facchinetti V.,
Bover L., Plumas J., Chaperot L., Qin J., Liu Y.J.;
"Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A
helicases sense microbial DNA in human plasmacytoid dendritic cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:15181-15186(2010).
[17]
INTERACTION WITH IRAK4, AND CHARACTERIZATION OF VARIANTS TYR-34;
CYS-98 AND ILE-178.
PubMed=20966070; DOI=10.1074/jbc.M110.159996;
George J., Motshwene P.G., Wang H., Kubarenko A.V., Rautanen A.,
Mills T.C., Hill A.V., Gay N.J., Weber A.N.;
"Two human MYD88 variants, S34Y and R98C, interfere with MyD88-IRAK4-
myddosome assembly.";
J. Biol. Chem. 286:1341-1353(2011).
[18]
INTERACTION WITH IRAK4, VARIANTS MET-39; GLY-136; ILE-136; PHE-204;
ARG-205; CYS-206; THR-207; ARG-209; THR-219; ASN-230; PRO-252 AND
PRO-281, AND CHARACTERIZATION OF VARIANTS ARG-209; THR-219; ASN-230;
PRO-252 AND PRO-281.
PubMed=21179087; DOI=10.1038/nature09671;
Ngo V.N., Young R.M., Schmitz R., Jhavar S., Xiao W., Lim K.H.,
Kohlhammer H., Xu W., Yang Y., Zhao H., Shaffer A.L., Romesser P.,
Wright G., Powell J., Rosenwald A., Muller-Hermelink H.K., Ott G.,
Gascoyne R.D., Connors J.M., Rimsza L.M., Campo E., Jaffe E.S.,
Delabie J., Smeland E.B., Fisher R.I., Braziel R.M., Tubbs R.R.,
Cook J.R., Weisenburger D.D., Chan W.C., Staudt L.M.;
"Oncogenically active MYD88 mutations in human lymphoma.";
Nature 470:115-119(2011).
[19]
INTERACTION WITH IKBKE.
PubMed=23453969; DOI=10.1016/j.celrep.2013.01.031;
Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.;
"IKKepsilon-mediated tumorigenesis requires K63-linked
polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase
complex.";
Cell Rep. 3:724-733(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
FUNCTION, INTERACTION WITH IRAK4, CHARACTERIZATION OF VARIANTS TYR-34;
CYS-98 AND ILE-178, AND CHARACTERIZATION OF VARIANTS MYD88D GLU-52
DEL; PRO-93 AND CYS-196.
PubMed=24316379; DOI=10.1016/j.molimm.2013.11.008;
Yamamoto T., Tsutsumi N., Tochio H., Ohnishi H., Kubota K., Kato Z.,
Shirakawa M., Kondo N.;
"Functional assessment of the mutational effects of human IRAK4 and
MyD88 genes.";
Mol. Immunol. 58:66-76(2014).
[22]
INTERACTION WITH OTUD4, AND UBIQUITINATION.
PubMed=29395066; DOI=10.1016/j.molcel.2018.01.009;
Zhao Y., Mudge M.C., Soll J.M., Rodrigues R.B., Byrum A.K.,
Schwarzkopf E.A., Bradstreet T.R., Gygi S.P., Edelson B.T.,
Mosammaparast N.;
"OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-
Dependent Signaling.";
Mol. Cell 69:505-516(2018).
[23]
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,
AND CHARACTERIZATION OF VARIANT MYD88D CYS-196.
PubMed=19506249; DOI=10.1073/pnas.0812956106;
Ohnishi H., Tochio H., Kato Z., Orii K.E., Li A., Kimura T.,
Hiroaki H., Kondo N., Shirakawa M.;
"Structural basis for the multiple interactions of the MyD88 TIR
domain in TLR4 signaling.";
Proc. Natl. Acad. Sci. U.S.A. 106:10260-10265(2009).
[24]
STRUCTURE BY NMR OF 146-296.
Northeast structural genomics consortium (NESG);
"Solution NMR structure of human myeloid differentiation primary
response (MYD88).";
Submitted (FEB-2009) to the PDB data bank.
[25]
VARIANTS MYD88D PRO-93 AND CYS-196, AND CHARACTERIZATION OF VARIANTS
MYD88D PRO-93 AND CYS-196.
PubMed=18669862; DOI=10.1126/science.1158298;
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., 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.;
"Pyogenic bacterial infections in humans with MyD88 deficiency.";
Science 321:691-696(2008).
[26]
INVOLVEMENT IN MYD88D, AND VARIANTS MYD88D GLU-52 DEL; PRO-93 AND
CYS-196.
PubMed=21057262; DOI=10.1097/MD.0b013e3181fd8ec3;
Picard C., von Bernuth H., Ghandil P., Chrabieh M., Levy O.,
Arkwright P.D., McDonald D., Geha R.S., Takada H., Krause J.C.,
Creech C.B., Ku C.L., Ehl S., Marodi L., Al-Muhsen S., Al-Hajjar S.,
Al-Ghonaium A., Day-Good N.K., Holland S.M., Gallin J.I., Chapel H.,
Speert D.P., Rodriguez-Gallego C., Colino E., Garty B.Z., Roifman C.,
Hara T., Yoshikawa H., Nonoyama S., Domachowske J., Issekutz A.C.,
Tang M., Smart J., Zitnik S.E., Hoarau C., Kumararatne D.S.,
Thrasher A.J., Davies E.G., Bethune C., Sirvent N., de Ricaud D.,
Camcioglu Y., Vasconcelos J., Guedes M., Vitor A.B., Rodrigo C.,
Almazan F., Mendez M., Arostegui J.I., Alsina L., Fortuny C.,
Reichenbach J., Verbsky J.W., Bossuyt X., Doffinger R., Abel L.,
Puel A., Casanova J.L.;
"Clinical features and outcome of patients with IRAK-4 and MyD88
deficiency.";
Medicine (Baltimore) 89:403-425(2010).
[27]
VARIANT PRO-252.
PubMed=22931316; DOI=10.1056/NEJMoa1200710;
Treon S.P., Xu L., Yang G., Zhou Y., Liu X., Cao Y., Sheehy P.,
Manning R.J., Patterson C.J., Tripsas C., Arcaini L., Pinkus G.S.,
Rodig S.J., Sohani A.R., Harris N.L., Laramie J.M., Skifter D.A.,
Lincoln S.E., Hunter Z.R.;
"MYD88 L265P somatic mutation in Waldenstrom's macroglobulinemia.";
N. Engl. J. Med. 367:826-833(2012).
-!- FUNCTION: Adapter protein involved in the Toll-like receptor and
IL-1 receptor signaling pathway in the innate immune response
(PubMed:15361868, PubMed:18292575). Acts via IRAK1, IRAK2, IRF7
and TRAF6, leading to NF-kappa-B activation, cytokine secretion
and the inflammatory response (PubMed:15361868, PubMed:24316379,
PubMed:19506249). Increases IL-8 transcription (PubMed:9013863).
Involved in IL-18-mediated signaling pathway. Activates IRF1
resulting in its rapid migration into the nucleus to mediate an
efficient induction of IFN-beta, NOS2/INOS, and IL12A genes.
MyD88-mediated signaling in intestinal epithelial cells is crucial
for maintenance of gut homeostasis and controls the expression of
the antimicrobial lectin REG3G in the small intestine (By
similarity). {ECO:0000250|UniProtKB:P22366,
ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:18292575,
ECO:0000269|PubMed:19506249, ECO:0000269|PubMed:24316379,
ECO:0000269|PubMed:9013863}.
-!- SUBUNIT: 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. Interacts (via TIR domain) with DHX9 (via
H2A and OB-fold regions); this interaction is direct
(PubMed:20696886). Interacts with OTUD4 deubiquitinase; the
interaction is direct (PubMed:29395066).
{ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15492225,
ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:16951688,
ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:19265123,
ECO:0000269|PubMed:19506249, ECO:0000269|PubMed:19948740,
ECO:0000269|PubMed:20696886, ECO:0000269|PubMed:20966070,
ECO:0000269|PubMed:21179087, ECO:0000269|PubMed:23453969,
ECO:0000269|PubMed:24316379, ECO:0000269|PubMed:29395066}.
-!- INTERACTION:
Self; NbExp=38; IntAct=EBI-447677, EBI-447677;
Q03463:- (xeno); NbExp=3; IntAct=EBI-447677, EBI-8803426;
Q8YF33:BMEI1694 (xeno); NbExp=4; IntAct=EBI-447677, EBI-11616155;
Q99418:CYTH2; NbExp=3; IntAct=EBI-15855480, EBI-448974;
Q8NF50:DOCK8; NbExp=3; IntAct=EBI-447677, EBI-2548605;
Q13158:FADD; NbExp=3; IntAct=EBI-447677, EBI-494804;
P51617:IRAK1; NbExp=3; IntAct=EBI-447677, EBI-358664;
Q69FE3:IRAK4; NbExp=5; IntAct=EBI-447677, EBI-10249217;
Q9NWZ3:IRAK4; NbExp=12; IntAct=EBI-447677, EBI-448378;
Q6SZW1:SARM1; NbExp=5; IntAct=EBI-447677, EBI-11693532;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-447677, EBI-747107;
P84022:SMAD3; NbExp=3; IntAct=EBI-447677, EBI-347161;
O43791:SPOP; NbExp=6; IntAct=EBI-447677, EBI-743549;
Q9UGK3:STAP2; NbExp=3; IntAct=EBI-447677, EBI-1553984;
P38340:TAE1 (xeno); NbExp=3; IntAct=EBI-447677, EBI-21116;
P58753:TIRAP; NbExp=8; IntAct=EBI-447677, EBI-528644;
O00206:TLR4; NbExp=2; IntAct=EBI-447677, EBI-528701;
O14836:TNFRSF13B; NbExp=12; IntAct=EBI-447677, EBI-519160;
P10599:TXN; NbExp=4; IntAct=EBI-447677, EBI-594644;
Q93009:USP7; NbExp=3; IntAct=EBI-447677, EBI-302474;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15361868,
ECO:0000269|PubMed:15492225}. Nucleus
{ECO:0000269|PubMed:21057262}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q99836-1; Sequence=Displayed;
Name=2;
IsoId=Q99836-2; Sequence=VSP_038887;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q99836-3; Sequence=VSP_043500;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q99836-4; Sequence=VSP_043498, VSP_043499, VSP_043500;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q99836-5; Sequence=VSP_053764;
Name=6;
IsoId=Q99836-6; Sequence=VSP_053765;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8957090}.
-!- DOMAIN: The intermediate domain (ID) is required for the
phosphorylation and activation of IRAK.
{ECO:0000250|UniProtKB:P22366}.
-!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination.
OTUD4 specifically hydrolyzes 'Lys-63'-linked polyubiquitinated
MYD88. {ECO:0000269|PubMed:29395066}.
-!- 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.
{ECO:0000269|PubMed:18669862, ECO:0000269|PubMed:19506249,
ECO:0000269|PubMed:21057262, ECO:0000269|PubMed:24316379}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Defects in MYD88 are frequently found in many
hematological malignancies, such as activated B-cell type diffuse
large B-cell lymphoma (ABC-DLBCL), Waldenstroem's
macroglobulinemia, cutaneous diffuse large B cell lymphoma (CBCL)
and primary central nervous system lymphoma (PCNSL).
{ECO:0000269|PubMed:21179087, ECO:0000269|PubMed:22931316}.
-!- SEQUENCE CAUTION:
Sequence=BAG60822.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG60834.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=EAW64521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U70451; AAB49967.1; -; mRNA.
EMBL; U84408; AAC50954.1; -; mRNA.
EMBL; AB446470; BAG55247.1; -; mRNA.
EMBL; BT007376; AAP36040.1; -; mRNA.
EMBL; AK296570; BAG59190.1; -; mRNA.
EMBL; AK296716; BAG59306.1; -; mRNA.
EMBL; AK298650; BAG60822.1; ALT_INIT; mRNA.
EMBL; AK298666; BAG60834.1; ALT_INIT; mRNA.
EMBL; AP006309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64521.1; ALT_SEQ; Genomic_DNA.
EMBL; BC013589; AAH13589.1; -; mRNA.
EMBL; BI524129; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; NP_001166037.1; NM_001172566.1.
RefSeq; NP_001166039.1; NM_001172568.1.
RefSeq; NP_001166040.1; NM_001172569.1.
RefSeq; NP_002459.2; NM_002468.4.
UniGene; Hs.82116; -.
PDB; 2JS7; NMR; -; A=146-296.
PDB; 2Z5V; NMR; -; A=148-296.
PDB; 3MOP; X-ray; 3.40 A; A/B/C/D/E/F=20-117.
PDB; 4DOM; X-ray; 1.80 A; A=157-296.
PDB; 4EO7; X-ray; 1.45 A; A=157-296.
PDBsum; 2JS7; -.
PDBsum; 2Z5V; -.
PDBsum; 3MOP; -.
PDBsum; 4DOM; -.
PDBsum; 4EO7; -.
ProteinModelPortal; Q99836; -.
SMR; Q99836; -.
BioGrid; 110700; 60.
DIP; DIP-31349N; -.
IntAct; Q99836; 45.
MINT; Q99836; -.
STRING; 9606.ENSP00000401399; -.
ChEMBL; CHEMBL5919; -.
iPTMnet; Q99836; -.
PhosphoSitePlus; Q99836; -.
BioMuta; MYD88; -.
DMDM; 18202671; -.
EPD; Q99836; -.
MaxQB; Q99836; -.
PaxDb; Q99836; -.
PeptideAtlas; Q99836; -.
PRIDE; Q99836; -.
ProteomicsDB; 78500; -.
ProteomicsDB; 78501; -. [Q99836-2]
ProteomicsDB; 78502; -. [Q99836-3]
ProteomicsDB; 78503; -. [Q99836-4]
TopDownProteomics; Q99836-4; -. [Q99836-4]
DNASU; 4615; -.
Ensembl; ENST00000443433; ENSP00000390565; ENSG00000172936.
Ensembl; ENST00000495303; ENSP00000417848; ENSG00000172936.
GeneID; 4615; -.
KEGG; hsa:4615; -.
UCSC; uc011ayj.3; human. [Q99836-1]
CTD; 4615; -.
DisGeNET; 4615; -.
EuPathDB; HostDB:ENSG00000172936.12; -.
GeneCards; MYD88; -.
HGNC; HGNC:7562; MYD88.
HPA; CAB009104; -.
MalaCards; MYD88; -.
MIM; 602170; gene.
MIM; 612260; phenotype.
neXtProt; NX_Q99836; -.
Orphanet; 183713; Pyogenic bacterial infections due to MyD88 deficiency.
Orphanet; 33226; Waldenstrom macroglobulinemia.
PharmGKB; PA31361; -.
eggNOG; ENOG410IIN8; Eukaryota.
eggNOG; ENOG410ZIY0; LUCA.
HOGENOM; HOG000068971; -.
HOVERGEN; HBG052547; -.
InParanoid; Q99836; -.
KO; K04729; -.
PhylomeDB; Q99836; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
Reactome; R-HSA-5602680; MyD88 deficiency (TLR5).
Reactome; R-HSA-5603037; IRAK4 deficiency (TLR5).
Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane.
SignaLink; Q99836; -.
SIGNOR; Q99836; -.
ChiTaRS; MYD88; human.
EvolutionaryTrace; Q99836; -.
GeneWiki; MYD88; -.
GenomeRNAi; 4615; -.
PRO; PR:Q99836; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000172936; -.
CleanEx; HS_MYD88; -.
ExpressionAtlas; Q99836; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005123; F:death receptor binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043621; F:protein self-association; IDA:AgBase.
GO; GO:0070976; F:TIR domain binding; IPI:BHF-UCL.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IMP:AgBase.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISS:ARUK-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISS:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:BHF-UCL.
GO; GO:0032747; P:positive regulation of interleukin-23 production; ISS:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:AgBase.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:BHF-UCL.
GO; GO:0050727; P:regulation of inflammatory response; ISS:BHF-UCL.
GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; IMP:BHF-UCL.
CDD; cd08312; Death_MyD88; 1.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR034249; MyD88_Death.
InterPro; IPR017281; Myelin_different_resp_MyD88.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR15079; PTHR15079; 1.
Pfam; PF00531; Death; 1.
Pfam; PF01582; TIR; 1.
PIRSF; PIRSF037756; MyD88; 1.
SMART; SM00005; DEATH; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; Immunity; Inflammatory response; Innate immunity;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 296 Myeloid differentiation primary response
protein MyD88.
/FTId=PRO_0000096666.
DOMAIN 54 109 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
DOMAIN 159 296 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 110 155 Intermediate domain. {ECO:0000250}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 22 MAAGGPGAGSAAPVSSTSSLPL -> M (in isoform
5). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_053764.
VAR_SEQ 110 154 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038887.
VAR_SEQ 110 110 E -> G (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043498.
VAR_SEQ 111 155 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043499.
VAR_SEQ 156 296 HMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDR
DVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQT
KFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTN
PCTKSWFWTRLAKALSLP -> AAGWWWLSLMITCRARNVT
SRPNLHSASLQVPIRSD (in isoform 3 and
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043500.
VAR_SEQ 215 215 R -> RLARRPRGG (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_053765.
VARIANT 34 34 S -> Y (rare functional polymorphism;
loss of NF-kappa-B complex activation;
loss of interaction with IRAK4; reduces
homooligomerization).
{ECO:0000269|PubMed:20966070,
ECO:0000269|PubMed:24316379}.
/FTId=VAR_072893.
VARIANT 39 39 V -> M (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073252.
VARIANT 52 52 Missing (in MYD88D; loss of NF-kappa-B
complex activation).
{ECO:0000269|PubMed:21057262,
ECO:0000269|PubMed:24316379}.
/FTId=VAR_072894.
VARIANT 93 93 L -> P (in MYD88D; results in a loss of
function; loss of NF-kappa-B complex
activation).
{ECO:0000269|PubMed:18669862,
ECO:0000269|PubMed:21057262,
ECO:0000269|PubMed:24316379}.
/FTId=VAR_047953.
VARIANT 98 98 R -> C (found in hematological
malignancies; somatic mutation; unknown
pathological significance; loss of NF-
kappa-B complex activation; loss of
interaction with IRAK4; reduces
homooligomerization).
{ECO:0000269|PubMed:20966070,
ECO:0000269|PubMed:24316379,
ECO:0000269|PubMed:8957090}.
/FTId=VAR_072895.
VARIANT 136 136 S -> G (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073253.
VARIANT 136 136 S -> I (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073254.
VARIANT 178 178 M -> I (found in hematological
malignancies; somatic mutation; unknown
pathological significance; no effect on
NF-kappaB complex activation).
{ECO:0000269|PubMed:20966070,
ECO:0000269|PubMed:24316379}.
/FTId=VAR_072896.
VARIANT 196 196 R -> C (in MYD88D; results in a loss of
function; decreases NF-kappa-B complex
activation).
{ECO:0000269|PubMed:18669862,
ECO:0000269|PubMed:19506249,
ECO:0000269|PubMed:21057262,
ECO:0000269|PubMed:24316379}.
/FTId=VAR_047954.
VARIANT 204 204 V -> F (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073255.
VARIANT 205 205 W -> R (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073256.
VARIANT 206 206 S -> C (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073257.
VARIANT 207 207 I -> T (found in hematological
malignancies; somatic mutation; unknown
pathological significance).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073258.
VARIANT 209 209 S -> R (found in hematological
malignancies; somatic mutation; unknown
pathological significance; constitutively
activates NF-kappaB complex activation).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073259.
VARIANT 219 219 M -> T (found in hematological
malignancies; somatic mutation; unknown
pathological significance; constitutively
activates NF-kappaB complex activation).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073260.
VARIANT 230 230 S -> N (found in hematological
malignancies; somatic mutation; unknown
pathological significance; constitutively
activates NF-kappaB complex activation).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073261.
VARIANT 252 252 L -> P (found in hematological
malignancies; somatic mutation; unknown
pathological significance; constitutively
activates NF-kappaB complex activation;
gain-of-function mutation; does not
affect interaction with IRAK4).
{ECO:0000269|PubMed:21179087,
ECO:0000269|PubMed:22931316}.
/FTId=VAR_073262.
VARIANT 281 281 T -> P (found in hematological
malignancies; somatic mutation; unknown
pathological significance; no effect on
NF-kappaB complex activation).
{ECO:0000269|PubMed:21179087}.
/FTId=VAR_073263.
MUTAGEN 196 196 R->A: Reduced interaction with TIRAP, and
strongly reduced activity. Strongly
reduced interaction with TIRAP; when
associated with A-288.
{ECO:0000269|PubMed:19506249}.
MUTAGEN 197 197 D->A: Slightly reduced activity.
{ECO:0000269|PubMed:19506249}.
MUTAGEN 217 217 R->A: Strongly reduced activity.
{ECO:0000269|PubMed:19506249}.
MUTAGEN 282 282 K->A: Slightly reduced activity.
{ECO:0000269|PubMed:19506249}.
MUTAGEN 288 288 R->A: Slightly reduced activity, and
reduced interaction with TIRAP. Strongly
reduced interaction with TIRAP; when
associated with A-196.
{ECO:0000269|PubMed:19506249}.
CONFLICT 190 190 K -> T (in Ref. 8; BI524129).
{ECO:0000305}.
CONFLICT 223 224 VS -> WL (in Ref. 8; BI524129).
{ECO:0000305}.
HELIX 22 24 {ECO:0000244|PDB:3MOP}.
HELIX 27 37 {ECO:0000244|PDB:3MOP}.
STRAND 42 44 {ECO:0000244|PDB:3MOP}.
HELIX 47 51 {ECO:0000244|PDB:3MOP}.
TURN 52 55 {ECO:0000244|PDB:3MOP}.
HELIX 58 64 {ECO:0000244|PDB:3MOP}.
STRAND 66 69 {ECO:0000244|PDB:3MOP}.
HELIX 70 79 {ECO:0000244|PDB:3MOP}.
STRAND 80 83 {ECO:0000244|PDB:3MOP}.
HELIX 86 96 {ECO:0000244|PDB:3MOP}.
HELIX 99 102 {ECO:0000244|PDB:3MOP}.
HELIX 106 112 {ECO:0000244|PDB:3MOP}.
TURN 114 116 {ECO:0000244|PDB:3MOP}.
STRAND 159 166 {ECO:0000244|PDB:4EO7}.
HELIX 169 171 {ECO:0000244|PDB:4EO7}.
HELIX 172 183 {ECO:0000244|PDB:4EO7}.
STRAND 185 187 {ECO:0000244|PDB:4EO7}.
STRAND 191 194 {ECO:0000244|PDB:4EO7}.
HELIX 196 198 {ECO:0000244|PDB:4EO7}.
HELIX 209 211 {ECO:0000244|PDB:4EO7}.
HELIX 212 215 {ECO:0000244|PDB:4EO7}.
STRAND 216 223 {ECO:0000244|PDB:4EO7}.
HELIX 227 229 {ECO:0000244|PDB:4EO7}.
HELIX 231 242 {ECO:0000244|PDB:4EO7}.
HELIX 247 251 {ECO:0000244|PDB:4EO7}.
STRAND 252 256 {ECO:0000244|PDB:4EO7}.
HELIX 266 268 {ECO:0000244|PDB:4EO7}.
STRAND 269 271 {ECO:0000244|PDB:4DOM}.
HELIX 279 281 {ECO:0000244|PDB:4EO7}.
HELIX 285 294 {ECO:0000244|PDB:4EO7}.
SEQUENCE 296 AA; 33233 MW; CEAE3F6B99524333 CRC64;
MAAGGPGAGS AAPVSSTSSL PLAALNMRVR RRLSLFLNVR TQVAADWTAL AEEMDFEYLE
IRQLETQADP TGRLLDAWQG RPGASVGRLL ELLTKLGRDD VLLELGPSIE EDCQKYILKQ
QQEEAEKPLQ VAAVDSSVPR TAELAGITTL DDPLGHMPER FDAFICYCPS DIQFVQEMIR
QLEQTNYRLK LCVSDRDVLP GTCVWSIASE LIEKRCRRMV VVVSDDYLQS KECDFQTKFA
LSLSPGAHQK RLIPIKYKAM KKEFPSILRF ITVCDYTNPC TKSWFWTRLA KALSLP


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