Toll-like receptor 3 precursor - Homo sapiens (Human)

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Names and origin

Protein names

Recommended name:
Toll-like receptor 3
Alternative name(s):
CD_antigen=CD283

Gene names

Name:

TLR3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Participates in the innate immune response to microbial agents. Mediates the innate immune response to ds-RNA, a sign of viral infection. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15
Subunit structure	Binds MYD88 via their respective TIR domains By similarity. Interacts with TICAM1. Homodimer formation is triggered by ligand binding and is required for TLR3 signaling. Binding of ds-RNA is required for the interaction with SRC. Ref.9 Ref.10 Ref.13 Ref.15 Ref.7 Ref.8
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane Ref.10.
Tissue specificity	Expressed at high level in placenta and pancreas. Also detected in CD11c+ immature dendritic cells. Only expressed in dendritic cells and not in other leukocytes, including monocyte precursors. TLR3 is the TLR that is expressed most strongly in the brain, especially in astrocytes, glia, and neurons. Ref.2
Domain	ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18 By similarity.
Post-translational modification	Heavily N-glycosylated, except on that part of the surface of the ectodomain that is involved in ligand binding. Ref.15 Ref.14 Ref.16
Involvement in disease	Defects in TLR3 are the cause of TLR3-deficient herpes simplex encephalitis (HSE) [MIM:603029]. HSE is a rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome. Ref.17 Genetic variation in TLR3 is associated with susceptibility to progression to geographic atrophy in age-related macular degeneration [MIM:612479]. Age-related macular degeneration (ARMD) is the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch's membrane. ARMD is likely to be a mechanistically heterogeneous group of disorders, and the specific disease mechanisms that underlie the vast majority of cases are currently unknown. However, a number of studies have suggested that both genetic and environmental factors are likely to play a role. Geographic atrophy (extensive atrophy of the retinal pigment epithelium and overlying photoreceptors) is an advanced form of 'dry' (nonneovascular or nonexudative) ARMD. Ref.18
Sequence similarities	Belongs to the Toll-like receptor family. Contains 22 LRR (leucine-rich) repeats. Contains 1 TIR domain.

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Ontologies

Keywords
Biological process	Immune response Inflammatory response Innate immunity
Cellular component	Endoplasmic reticulum Endosome Membrane
Coding sequence diversity	Polymorphism
Disease	Age-related macular degeneration
Domain	Leucine-rich repeat Repeat Signal Transmembrane
Ligand	RNA-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	I-kappaB phosphorylation Inferred from direct assay. Source: UniProtKB activation of NF-kappaB-inducing kinase activity Non-traceable author statement. Source: UniProtKB defense response to bacterium Traceable author statement. Source: ProtInc detection of virus Non-traceable author statement. Source: UniProtKB hyperosmotic response Non-traceable author statement. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of osteoclast differentiation Non-traceable author statement. Source: UniProtKB positive regulation of NF-kappaB import into nucleus Inferred from direct assay. Source: UniProtKB positive regulation of chemokine production Inferred from direct assay. Source: UniProtKB positive regulation of inflammatory response Inferred by curator. Source: UniProtKB positive regulation of interferon-alpha biosynthetic process Inferred from direct assay. Source: UniProtKB positive regulation of interferon-beta biosynthetic process Inferred from direct assay. Source: UniProtKB positive regulation of interferon-gamma biosynthetic process Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-6 production Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-8 production Inferred from direct assay. Source: UniProtKB positive regulation of toll-like receptor signaling pathway Inferred from direct assay. Source: UniProtKB
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endosome membrane Inferred from Experiment. Source: Reactome integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	double-stranded RNA binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from electronic annotation. Source: InterPro transmembrane receptor activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.6

Chain

24 – 904

881

Toll-like receptor 3

PRO_0000034715

Regions

Topological domain

24 – 704

681

Lumenal Potential

Transmembrane

705 – 725

21

Potential

Topological domain

726 – 904

179

Cytoplasmic Potential

Repeat

50 – 73

24

LRR 1

Repeat

75 – 97

23

LRR 2

Repeat

98 – 121

24

LRR 3

Repeat

123 – 145

23

LRR 4

Repeat

147 – 169

23

LRR 5

Repeat

170 – 193

24

LRR 6

Repeat

196 – 219

24

LRR 7

Repeat

247 – 270

24

LRR 8

Repeat

273 – 296

24

LRR 9

Repeat

298 – 320

23

LRR 10

Repeat

354 – 377

24

LRR 11

Repeat

379 – 403

25

LRR 12

Repeat

406 – 429

24

LRR 13

Repeat

431 – 454

24

LRR 14

Repeat

455 – 478

24

LRR 15

Repeat

480 – 504

25

LRR 16

Repeat

505 – 528

24

LRR 17

Repeat

530 – 552

23

LRR 18

Repeat

561 – 584

24

LRR 19

Repeat

586 – 608

23

LRR 20

Repeat

610 – 632

23

LRR 21

Repeat

634 – 659

26

LRR 22

Domain

754 – 896

143

TIR

Amino acid modifications

Modified residue

759

1

Phosphotyrosine Ref.12

Modified residue

858

1

Phosphotyrosine Ref.12

Glycosylation

52

1

N-linked (GlcNAc...) Ref.15 Ref.14

Glycosylation

57

1

N-linked (GlcNAc...) Ref.14

Glycosylation

70

1

N-linked (GlcNAc...) Ref.15

Glycosylation

124

1

N-linked (GlcNAc...) Ref.16

Glycosylation

196

1

N-linked (GlcNAc...) Ref.15

Glycosylation

247

1

N-linked (GlcNAc...) Potential

Glycosylation

252

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

265

1

N-linked (GlcNAc...) Ref.15

Glycosylation

275

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

291

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

398

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

413

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

507

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

636

1

N-linked (GlcNAc...) Ref.15

Glycosylation

662

1

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

284

1

N → I: dbSNP rs5743316.

VAR_052361

Natural variant

307

1

Y → D: dbSNP rs5743317.

VAR_052362

Natural variant

412

1

L → F Confers protection against progression to geographic atrophy in age-related macular degeneration. dbSNP rs3775291. Ref.18

VAR_021976

Natural variant

554

1

P → S in HSE; TLR3-deficient HSE. Ref.17

VAR_054887

Natural variant

737

1

S → T: dbSNP rs5743318.

VAR_024664

Experimental info

Mutagenesis

95

1

C → A: Reduced response to ds-RNA. Ref.9

Mutagenesis

122

1

C → A: Reduced response to ds-RNA. Ref.9

Mutagenesis

196

1

N → G: Reduced expression levels; when associated with R-247. Ref.9

Mutagenesis

247

1

N → R: Reduced response to ds-RNA. Reduced expression levels; when associated with G-196. Ref.9

Mutagenesis

539

1

H → A: No effect. Ref.11

Mutagenesis

539

1

H → E: Loss of RNA binding. Constitutive activation of NF-kappa-B. Ref.11

Mutagenesis

541

1

N → A: Loss of RNA binding. Abolishes activation of NF-kappa-B. Ref.11

Mutagenesis

759

1

Y → F: Reduced activation of NF-kappa-B in response to ds-RNA. Reduced induction of IL-8 in response to ds-RNA. Ref.12

Secondary structure

1

.

904

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O15455-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 034E05ECA7A4D2F7
Show »

FASTA

904

103,829

        10         20         30         40         50         60 
MRQTLPCIYF WGGLLPFGML CASSTTKCTV SHEVADCSHL KLTQVPDDLP TNITVLNLTH 

        70         80         90        100        110        120 
NQLRRLPAAN FTRYSQLTSL DVGFNTISKL EPELCQKLPM LKVLNLQHNE LSQLSDKTFA 

       130        140        150        160        170        180 
FCTNLTELHL MSNSIQKIKN NPFVKQKNLI TLDLSHNGLS STKLGTQVQL ENLQELLLSN 

       190        200        210        220        230        240 
NKIQALKSEE LDIFANSSLK KLELSSNQIK EFSPGCFHAI GRLFGLFLNN VQLGPSLTEK 

       250        260        270        280        290        300 
LCLELANTSI RNLSLSNSQL STTSNTTFLG LKWTNLTMLD LSYNNLNVVG NDSFAWLPQL 

       310        320        330        340        350        360 
EYFFLEYNNI QHLFSHSLHG LFNVRYLNLK RSFTKQSISL ASLPKIDDFS FQWLKCLEHL 

       370        380        390        400        410        420 
NMEDNDIPGI KSNMFTGLIN LKYLSLSNSF TSLRTLTNET FVSLAHSPLH ILNLTKNKIS 

       430        440        450        460        470        480 
KIESDAFSWL GHLEVLDLGL NEIGQELTGQ EWRGLENIFE IYLSYNKYLQ LTRNSFALVP 

       490        500        510        520        530        540 
SLQRLMLRRV ALKNVDSSPS PFQPLRNLTI LDLSNNNIAN INDDMLEGLE KLEILDLQHN 

       550        560        570        580        590        600 
NLARLWKHAN PGGPIYFLKG LSHLHILNLE SNGFDEIPVE VFKDLFELKI IDLGLNNLNT 

       610        620        630        640        650        660 
LPASVFNNQV SLKSLNLQKN LITSVEKKVF GPAFRNLTEL DMRFNPFDCT CESIAWFVNW 

       670        680        690        700        710        720 
INETHTNIPE LSSHYLCNTP PHYHGFPVRL FDTSSCKDSA PFELFFMINT SILLIFIFIV 

       730        740        750        760        770        780 
LLIHFEGWRI SFYWNVSVHR VLGFKEIDRQ TEQFEYAAYI IHAYKDKDWV WEHFSSMEKE 

       790        800        810        820        830        840 
DQSLKFCLEE RDFEAGVFEL EAIVNSIKRS RKIIFVITHH LLKDPLCKRF KVHHAVQQAI 

       850        860        870        880        890        900 
EQNLDSIILV FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERIGAFR HKLQVALGSK 


NSVH

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of human receptors structurally related to Drosophila Toll." Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F. Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998) [PubMed: 9435236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The innate immune facet of brain: human neurons express TLR-3 and sense viral dsRNA." Lafon M., Megret F., Lafage M., Prehaud C. J. Mol. Neurosci. 29:185-194(2006) [PubMed: 17085778] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Neuron.
[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: 18810425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-38.
[7]	"A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling." Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S. J. Immunol. 169:6668-6672(2002) [PubMed: 12471095] [Abstract] Cited for: INTERACTION WITH TICAM1.
[8]	"TICAM-1, an adapter molecule that participates in Toll-like receptor 3 mediated interferon-beta induction." Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T. Nat. Immunol. 4:161-167(2003) [PubMed: 12539043] [Abstract] Cited for: INTERACTION WITH TICAM1. Tissue: Lung.
[9]	"Recognition of double-stranded RNA by human toll-like receptor 3 and downstream receptor signaling requires multimerization and an acidic pH." de Bouteiller O., Merck E., Hasan U.A., Hubac S., Benguigui B., Trinchieri G., Bates E.E., Caux C. J. Biol. Chem. 280:38133-38145(2005) [PubMed: 16144834] [Abstract] Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-95; CYS-122; ASN-196 AND ASN-247.
[10]	"Toll-like receptor 3 associates with c-Src tyrosine kinase on endosomes to initiate antiviral signaling." Johnsen I.B., Nguyen T.T., Ringdal M., Tryggestad A.M., Bakke O., Lien E., Espevik T., Anthonsen M.W. EMBO J. 25:3335-3346(2006) [PubMed: 16858407] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRC.
[11]	"The dsRNA binding site of human Toll-like receptor 3." Bell J.K., Askins J., Hall P.R., Davies D.R., Segal D.M. Proc. Natl. Acad. Sci. U.S.A. 103:8792-8797(2006) [PubMed: 16720699] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-539 AND ASN-541.
[12]	"Two tyrosine residues of Toll-like receptor 3 trigger different steps of NF-kappa B activation." Sarkar S.N., Elco C.P., Peters K.L., Chattopadhyay S., Sen G.C. J. Biol. Chem. 282:3423-3427(2007) [PubMed: 17178723] [Abstract] Cited for: PHOSPHORYLATION AT TYR-759 AND TYR-858, FUNCTION, MUTAGENESIS OF TYR-759.
[13]	"The TLR3 signaling complex forms by cooperative receptor dimerization." Leonard J.N., Ghirlando R., Askins J., Bell J.K., Margulies D.H., Davies D.R., Segal D.M. Proc. Natl. Acad. Sci. U.S.A. 105:258-263(2008) [PubMed: 18172197] [Abstract] Cited for: FUNCTION, SUBUNIT.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52 AND ASN-57, MASS SPECTROMETRY. Tissue: Liver.
[15]	"The molecular structure of the Toll-like receptor 3 ligand-binding domain." Bell J.K., Botos I., Hall P.R., Askins J., Shiloach J., Segal D.M., Davies D.R. Proc. Natl. Acad. Sci. U.S.A. 102:10976-10980(2005) [PubMed: 16043704] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-703, FUNCTION, MASS SPECTROMETRY, DISULFIDE BONDS, SUBUNIT, GLYCOSYLATION AT ASN-52; ASN-70; ASN-196; ASN-252; ASN-265; ASN-275; ASN-291; ASN-398; ASN-413; ASN-507 AND ASN-636.
[16]	"Crystal structure of human toll-like receptor 3 (TLR3) ectodomain." Choe J., Kelker M.S., Wilson I.A. Science 309:581-585(2005) [PubMed: 15961631] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-700, DISULFIDE BONDS, GLYCOSYLATION AT ASN-124; ASN-252; ASN-275; ASN-291; ASN-398; ASN-413 AND ASN-507.
[17]	"TLR3 deficiency in patients with herpes simplex encephalitis." Zhang S.-Y., Jouanguy E., Ugolini S., Smahi A., Elain G., Romero P., Segal D., Sancho-Shimizu V., Lorenzo L., Puel A., Picard C., Chapgier A., Plancoulaine S., Titeux M., Cognet C., von Bernuth H., Ku C.-L., Casrouge A. Casanova J.-L. Science 317:1522-1527(2007) [PubMed: 17872438] [Abstract] Cited for: VARIANT HSE SER-554.
[18]	"Toll-like receptor 3 and geographic atrophy in age-related macular degeneration." Yang Z., Stratton C., Francis P.J., Kleinman M.E., Tan P.L., Gibbs D., Tong Z., Chen H., Constantine R., Yang X., Chen Y., Zeng J., Davey L., Ma X., Hau V.S., Wang C., Harmon J., Buehler J. Zhang K. N. Engl. J. Med. 359:1456-1463(2008) [PubMed: 18753640] [Abstract] Cited for: VARIANT PHE-412, PROTECTION AGAINST PROGRESSION TO GEOGRAPHIC ATROPHY IN ARMD.
[19]	Erratum Yang Z., Stratton C., Francis P.J., Kleinman M.E., Tan P.L., Gibbs D., Tong Z., Chen H., Constantine R., Yang X., Chen Y., Zeng J., Davey L., Ma X., Hau V.S., Wang C., Harmon J., Buehler J. Zhang K. N. Engl. J. Med. 359:1859-1859(2008)
+	Additional computationally mapped references.

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Web resources

TLR3base

TLR3 mutation db

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U88879 mRNA. Translation: AAC34134.1.
DQ445682 mRNA. Translation: ABE01399.1.
AB445631 mRNA. Translation: BAG55028.1.
CH471056 Genomic DNA. Translation: EAX04628.1.
BC096333 mRNA. Translation: AAH96333.1.
BC096334 mRNA. Translation: AAH96334.1.
BC096335 mRNA. Translation: AAH96335.1.

IPI

IPI00019007.

RefSeq

NP_003256.1.

UniGene

Hs.657724

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZIW	X-ray	2.10	A	27-700	[»]
2A0Z	X-ray	2.40	A	22-703	[»]

SMR

O15455. Positions 747-902.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29660N.

STRING

O15455.

PTM databases

PhosphoSite

O15455.

Proteomic databases

PRIDE

O15455.

Genome annotation databases

Ensembl

ENST00000296795; ENSP00000296795; ENSG00000164342; Homo sapiens. [Genome view]

GeneID

7098.

KEGG

hsa:7098.

UCSC

uc003iyq.1. human.

Organism-specific databases

CTD

7098.

GeneCards

GC04P187227.

H-InvDB

HIX0031434.

HGNC

HGNC:11849. TLR3.

MIM

603029. gene+phenotype.
612479. phenotype.

Orphanet

1930. Herpetic encephalitis.

PharmGKB

PA36551.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09052.

HOGENOM

HBG714435.

HOVERGEN

O15455.

InParanoid

O15455.

OMA

FQWLKCL.

OrthoDB

EOG92VC1H.

PhylomeDB

O15455.

Enzyme and pathway databases

Reactome

REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

O15455.

Bgee

O15455.

CleanEx

HS_TLR3.

Genevestigator

O15455.

GermOnline

ENSG00000164342. Homo sapiens.

Family and domain databases

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. Toll-Interleukin_rcpt.
IPR020474. Toll-like_rcpt_LRR-contain.
[Graphical view]

Pfam

PF00560. LRR_1. 2 hits.
PF01582. TIR. 1 hit.
[Graphical view]

PRINTS

PR00019. LEURICHRPT.

SMART

SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]

PROSITE

PS51450. LRR. 19 hits.
PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

27769.

SOURCE

Search...

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Entry information

Entry name

TLR3_HUMAN

Accession

Primary (citable) accession number: O15455
Secondary accession number(s): Q4VAL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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