Q99836 (MYD88_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myeloid differentiation primary response protein MyD88

Gene names

Name:

MYD88

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Ref.2 Ref.8 Ref.12 Ref.14
Subunit structure	Homodimer. Also forms heterodimers with TIRAP. Binds to TLR2, TLR4, IRAK1, IRAK2 and IRAK4 via their respective TIR domains. Interacts with IL18R1 By similarity. Interacts with BMX, IL1RL1 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 By similarity. 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Cytoplasm Ref.8 Ref.9.
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.14 Ref.16
Sequence similarities	Contains 1 death domain. Contains 1 TIR domain.

Ontologies

Keywords
Biological process	Immunity Inflammatory response Innate immunity
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3'-UTR-mediated mRNA stabilization Inferred from direct assay PubMed 15294994. Source: BHF-UCL MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB 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 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 toll-like receptor 1 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
Cellular_component	cytosol Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	death receptor binding Traceable author statement PubMed 9374458. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-447677,EBI-447677
FADD	Q13158	3	EBI-447677,EBI-494804
SIAH1	Q8IUQ4	3	EBI-447677,EBI-747107
SMAD3	P84022	3	EBI-447677,EBI-347161
SPOP	O43791	6	EBI-447677,EBI-743549
STAP2	Q9UGK3	3	EBI-447677,EBI-1553984
TIRAP	P58753	4	EBI-447677,EBI-528644
TNFRSF13B	O14836	12	EBI-447677,EBI-519160
TXN	P10599	4	EBI-447677,EBI-594644
USP7	Q93009	3	EBI-447677,EBI-302474

Alternative products

This entry describes 4 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:
     1-1: M → MRPDRAEAPGPPAM
     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:
     1-1: M → MRPDRAEAPGPPAM
     110-110: E → G
     111-155: Missing.
     156-296: HMPERFDAFI...TRLAKALSLP → AAGWWWLSLM...ASLQVPIRSD

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

Myeloid differentiation primary response protein MyD88

PRO_0000096666

Regions

Domain

54 – 109

56

Death

Domain

159 – 296

138

TIR

Region

110 – 155

46

Intermediate domain By similarity

Natural variations

Alternative sequence

1

1

M → MRPDRAEAPGPPAM in isoform 3 and isoform 4.

VSP_043497

Alternative sequence

110 – 154

45

Missing in isoform 2.

VSP_038887

Alternative sequence

110

1

E → G in isoform 4.

VSP_043498

Alternative sequence

111 – 155

45

Missing in isoform 4.

VSP_043499

Alternative sequence

156 – 296

141

HMPER…ALSLP → AAGWWWLSLMITCRARNVTS RPNLHSASLQVPIRSD in isoform 3 and isoform 4.

VSP_043500

Natural variant

93

1

L → P in MYD88D; results in a loss of function. Ref.16

VAR_047953

Natural variant

196

1

R → C in MYD88D; results in a loss of function. Ref.14 Ref.16

VAR_047954

Experimental info

Mutagenesis

196

1

R → A: Reduced interaction with TIRAP, and strongly reduced activity. Strongly reduced interaction with TIRAP; when associated with A-288. Ref.14

Mutagenesis

197

1

D → A: Slightly reduced activity. Ref.14

Mutagenesis

217

1

R → A: Strongly reduced activity. Ref.14

Mutagenesis

282

1

K → A: Slightly reduced activity. Ref.14

Mutagenesis

288

1

R → A: Slightly reduced activity, and reduced interaction with TIRAP. Strongly reduced interaction with TIRAP; when associated with A-196. Ref.14

Sequence conflict

98

1

R → C in AAB49967. Ref.1

Secondary structure

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296

Helix Strand Turn

Details...

Helix

22 – 24

3

Helix

27 – 37

11

Beta strand

42 – 44

3

Helix

47 – 51

5

Turn

52 – 55

4

Helix

58 – 64

7

Beta strand

66 – 69

4

Helix

70 – 79

10

Beta strand

80 – 83

4

Helix

86 – 96

11

Helix

99 – 102

4

Helix

106 – 112

7

Turn

114 – 116

3

Beta strand

161 – 166

6

Helix

169 – 171

3

Helix

172 – 183

12

Beta strand

185 – 187

3

Beta strand

192 – 194

3

Beta strand

197 – 201

5

Helix

209 – 211

3

Helix

212 – 215

4

Beta strand

216 – 222

7

Helix

225 – 229

5

Helix

231 – 243

13

Helix

247 – 250

4

Beta strand

252 – 258

7

Turn

266 – 268

3

Turn

279 – 281

3

Helix

285 – 294

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: CEAE3F6B99524333	FASTA	296	33,233
	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
	Isoform 2 [UniParc]. Checksum: 1841504370960C90	FASTA	251	28,280
	10 20 30 40 50 60 MAAGGPGAGS AAPVSSTSSL PLAALNMRVR RRLSLFLNVR TQVAADWTAL AEEMDFEYLE 70 80 90 100 110 120 IRQLETQADP TGRLLDAWQG RPGASVGRLL ELLTKLGRDD VLLELGPSIG HMPERFDAFI 130 140 150 160 170 180 CYCPSDIQFV QEMIRQLEQT NYRLKLCVSD RDVLPGTCVW SIASELIEKR CRRMVVVVSD 190 200 210 220 230 240 DYLQSKECDF QTKFALSLSP GAHQKRLIPI KYKAMKKEFP SILRFITVCD YTNPCTKSWF 250 WTRLAKALSL P
	Isoform 3 [UniParc]. Checksum: 0C472D3E48E2CD4C	FASTA	204	22,123
	10 20 30 40 50 60 MRPDRAEAPG PPAMAAGGPG AGSAAPVSST SSLPLAALNM RVRRRLSLFL NVRTQVAADW 70 80 90 100 110 120 TALAEEMDFE YLEIRQLETQ ADPTGRLLDA WQGRPGASVG RLLELLTKLG RDDVLLELGP 130 140 150 160 170 180 SIEEDCQKYI LKQQQEEAEK PLQVAAVDSS VPRTAELAGI TTLDDPLGAA GWWWLSLMIT 190 200 CRARNVTSRP NLHSASLQVP IRSD
	Isoform 4 [UniParc]. Checksum: 5A82F38248B67102	FASTA	159	17,170
	10 20 30 40 50 60 MRPDRAEAPG PPAMAAGGPG AGSAAPVSST SSLPLAALNM RVRRRLSLFL NVRTQVAADW 70 80 90 100 110 120 TALAEEMDFE YLEIRQLETQ ADPTGRLLDA WQGRPGASVG RLLELLTKLG RDDVLLELGP 130 140 150 SIGAAGWWWL SLMITCRARN VTSRPNLHSA SLQVPIRSD

References

	« Hide 'large scale' referencesShow '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. , 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 AND 3). Tissue: Umbilical cord blood.
[6]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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). Tissue: Pancreas.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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. , 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.
AK298650 mRNA. Translation: BAG60822.1.
AK298666 mRNA. Translation: BAG60834.1.
AP006309 Genomic DNA. No translation available.
BC013589 mRNA. Translation: AAH13589.1.

IPI

IPI00878858.
IPI00909842.
IPI00925056.

RefSeq

NP_001166037.1. NM_001172566.1.
NP_001166039.1. NM_001172568.1.
NP_001166040.1. NM_001172569.1.
NP_002459.2. NM_002468.4.

UniGene

Hs.82116.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JS7	NMR	-	A	146-296	[»]
2Z5V	NMR	-	A	148-296	[»]
3MOP	X-ray	3.40	A/B/C/D/E/F	20-117	[»]

ProteinModelPortal

Q99836.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31349N.

IntAct

Q99836. 28 interactions.

MINT

MINT-97233.

STRING

9606.ENSP00000379625.

PTM databases

PhosphoSite

Q99836.

Polymorphism databases

DMDM

18202671.

Proteomic databases

PaxDb

Q99836.

PRIDE

Q99836.

Protocols and materials databases

DNASU

4615.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000443433; ENSP00000390565; ENSG00000172936.
ENST00000495303; ENSP00000417848; ENSG00000172936.

GeneID

4615.

KEGG

hsa:4615.

UCSC

uc003chx.3. human.
uc011ayl.2. human.

Organism-specific databases

CTD

4615.

GeneCards

GC03P038179.

HGNC

HGNC:7562. MYD88.

HPA

CAB009104.

MIM

602170. gene.
612260. phenotype.

neXtProt

NX_Q99836.

Orphanet

183713. Pyogenic bacterial infections due to MyD88 deficiency.

PharmGKB

PA31361.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG70664.

HOGENOM

HOG000070050.

HOVERGEN

HBG052547.

InParanoid

Q99836.

KO

K04729.

OrthoDB

EOG4GXFNH.

PhylomeDB

Q99836.

Enzyme and pathway databases

Pathway_Interaction_DB

il1pathway. IL1-mediated signaling events.
p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q99836.

Bgee

Q99836.

CleanEx

HS_MYD88.

Genevestigator

Q99836.

GermOnline

ENSG00000172936. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.

InterPro

IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR017281. Myelin_different_resp_MyD88.
IPR000157. TIR_dom.
[Graphical view]

Pfam

PF00531. Death. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]

PIRSF

PIRSF037756. MyD88. 1 hit.

SMART

SM00005. DEATH. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.
SSF52200. TIR. 1 hit.

PROSITE

PS50017. DEATH_DOMAIN. 1 hit.
PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL5919.

ChiTaRS

MYD88. human.

EvolutionaryTrace

Q99836.

GenomeRNAi

4615.

NextBio

17764.

SOURCE

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Entry information

Entry name

MYD88_HUMAN

Accession

Primary (citable) accession number: Q99836
Secondary accession number(s): B4DKH8 , B4DQ60, B4DQ72, P78397, Q53XS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.