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CLEC1B (C-Type Lectin Domain Family 1, Member B)

Written2013-11Katsue Suzuki-Inoue
Department of Clinical, Laboratory Medicine, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, 409-3898 Chuo, Yamanashi, Japan

(Note : for Links provided by Atlas : click)


Alias (NCBI)1810061I13Rik
HGNC Alias symbCLEC2
HGNC Previous name"C-type lectin domain family 1, member B"
LocusID (NCBI) 51266
Atlas_Id 49856
Location 12p13.2  [Link to chromosome band 12p13]
Location_base_pair Starts at 9993061 and ends at 9999300 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping CLEC1B.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


Description The gene is 982 bp in length and contains six exons.
Transcription In human, mouse, rabbit, rat, and bovine species, transcription produces 2-4 different mRNAs, including alternatively spliced variants and 1 unspliced form.
Pseudogene No known pseudogenes.


  Schematic representation of the domain structure of CLEC-2 (Colonna et al., 2000; Watson et al., 2007; Wang et al., 2012). TM represents transmembrane region. Neck represents neck region. CTLD represents C-type lectin-like domain.
Description CLEC-2 is a 32-kDa (229 amino acids) type II trans-membrane receptor that belongs to C-type lectin superfamily. CLEC-2 has 1 C-type lectin-like domain (CTLD) and belongs to the non-classical C-type lectins, which contain a CTLD homologous to a carbohydrate recognition domain but lack the consensus sequence for binding sugars and calcium (Colonna et al., 2000). CLEC-2 has a YxxL motif in its cytoplasmic tail, which is crucial for CLEC-2-mediated signal transduction. This sequence is called hemi-ITAM, since it resembles the immunoreceptor tyrosine-based activation motif (ITAM, YxxL-(X)10-12-YxxL), which includes 2 YxxL motifs. CLEC-2 was first identified through a bioinformatic screen for C-type lectin-like molecules with immune functions. The gene encoding human CLEC-2 is located in the natural killer complex on chromosome 12 along with other C-type lectin-like receptors, including NKG2D, LOX-1, and Dectin-1 (Sobanov et al., 2001).
Expression Organ: Highly expressed in bone marrow and slightly expressed in liver.
Cell types: CLEC-2 protein is expressed at high levels in platelets/megakaryocytes and at low levels in sinusoidal endothelial cells (Chaipan et al., 2006) and Kupffer cells (Tang et al., 2010) in humans. In mice, CLEC-2 protein is highly expressed in platelets/megakaryocytes, and is slightly expressed in other blood cells, including neutrophils, monocytes, dendritic cells, NK cells, B cells (Chang et al., 2010; Mourao-Sa et al., 2011), and Kupffer cells (Tang et al., 2010).
Localisation Plasma membrane.
Function Separation of blood and lymphatic vessels during development
Podoplanin is also expressed on the surface of lymphatic endothelial cells, but not vascular endothelial cells. During organ development, a cluster of endothelial cells in the cardinal vein is committed to the lymphatic phenotype, and sprouts to form the primary lymphatic sacs from which a portion of the peripheral lymphatic vasculature is generated by further centrifugal growth (Tammela and Alitalo, 2010). At this stage, platelets are activated by an association between CLEC-2 in the platelets and podoplanin in the lymphatic endothelial cells, which inhibits the growth and migration of lymphatic endothelial cells and facilitates the separation of blood and lymphatic vessels.
CLEC-2-deficient mice show blood-filled lymphatic vessels and severe edema due to lymphatic dysfunction (Bertozzi et al., 2010; Suzuki-Inoue et al., 2010; Finney et al., 2011). One controversial theory proposes that granule contents released from activated platelets inhibit the function of lymphatic endothelial cells (Osada et al., 2012).
Thrombus formation
Thrombus formation under flow conditions has been reported to be impaired in CLEC-2-deficient blood. In vivo thrombus formation is also inhibited in antibody-induced CLEC-2-deficient mice (May et al., 2009) or bone marrow chimeric mice deficient in CLEC-2 (Suzuki-Inoue et al., 2010). These findings suggest that CLEC-2 is involved in the stabilization of thrombus formation under flow conditions, although the precise mechanism by which this occurs has not yet been elucidated. Combined in vivo depletion of CLEC-2 and glycoprotein VI (GPVI), a collagen receptor in platelets, severely compromises haemostasis and abrogates arterial thrombosis in mice (Bender et al., 2013). CLEC-2 and GPVI, both of which generate activation signals depending on ITAMs and tyrosine kinases, play a complementary role in thrombosis and haemostasis.
Maintenance of vascular integrity
CLEC-2 is involved in maintaining vascular integrity in inflammation (Boulaftali et al., 2013) and high endothelial venules (HEVs) in lymph nodes upon lymphocyte transmigration (Herzog et al., 2013). Podoplanin is expressed on fibroblastic reticular cells, which surround HEVs. Upon lymphocyte transmigration, platelets extravasate to the perivenular space of HEVs and interact with podoplanin. Local release of sphingosine-1-phosphate after CLEC-2-podoplanin-mediated platelet activation is critical for HEV integrity during immune responses.
Antigen presentation
CLEC-2 is also expressed in dendritic cells (DCs) in mice. Associations between CLEC-2 in DCs and podoplanin in lymphatic endothelial and fibroblastic reticular cells in the lymph nodes facilitates DC entry into the lymphatics as well as movement to and within the lymph nodes, thereby reducing T cell priming. CLEC-2 engagement of podoplanin was found to be necessary for DCs to spread and migrate along stromal surfaces, and was sufficient to induce membrane protrusions through Vav and Rac1 activation (Acton et al., 2012).
HIV transmission
Previous reports indicate that platelets capture and transfer infectious HIV-1 via DC-SIGN and CLEC-2, possibly facilitated HIV-1 dissemination in infected patients (Suzuki-Inoue et al., 2011). CLEC-2 does not directly bind to the viral envelope proteins, but to podoplanin incorporated into the HIV particles released from HEK-293T cells (Chaipan et al., 2010). This mechanism does not seem to be important for viral dispersion in vivo since podoplanin is not expressed on T cells, which are the major HIV target.
Phagocytosis and cytokine production
CLEC-2 is expressed in dendritic cells, NK cells, B cells, neutrophils, and monocytes, in addition to platelets (Kerrigan et al., 2009; Chang et al., 2010; Mourao-Sa et al., 2011). Murine CLEC-2 in neutrophils mediates the phagocytosis of anti-CLEC-2 antibody-coated beads. Moreover, neutrophils stimulated by rhodocytin produce proinflammatory cytokines such as TNF-α depending on CLEC-2, but not respiratory burst (Kerrigan et al., 2009). CLEC-2 ligation in macrophages and DCs selectively up-regulates production of IL-10, an anti-inflammatory cytokine, by Toll-like receptor stimulation. Although the physiological relevance of these phenomena has not been determined, CLEC-2 is expressed in myeloid cells and may be able to modulate the inflammatory response in vivo.
Homology Among 226-229 amino acids of 5 species' (human, mouse, rat, rabbit, and bovine) CLEC-2, there are 129 positions with 100% sequence conservation, 36 positions with 80% sequence conservation, and 44 positions with 60% sequence conservation. Human CLEC-2 is 62% identical to mouse CLEC-2, and 70% to rabbit CLEC-2.


Note No known mutations.

Implicated in

Entity Haematogenous tumour metastasis
Note CLEC-2 has been identified as a receptor for a platelet activating snake venom, rhodocytin (Suzuki-Inoue et al., 2006). Podoplanin is a type I transmembrane sialomucin-like glycoprotein, and is identified as the endogenous ligand for CLEC-2 (Suzuki-Inoue et al., 2007; Christou et al., 2008). It is expressed on the surface of certain types of tumour cells, where it causes aggregation of platelets in the blood stream, facilitating haematogenous tumour metastasis. Platelet aggregation surrounding tumour cells is considered to protect the tumour cells from shear stress and NK cells (Nieswandt et al., 1999) in the blood stream and provide scaffolding for tumour cell nests. Growth factors released from activated platelets stimulate angiogenesis and/or tumour growth. In an experimental model of metastasis in mice, an anti-podoplanin blocking antibody significantly inhibited the number of tumour-cell containing metastatic lung nodules that expressed podoplanin, implying that CLEC-2/podoplanin may be a promising target protein for anti-metastatic drugs (Kato et al., 2008).
Entity Various diseases
Note No implication in any specific diseases in human has been reported.


Podoplanin-rich stromal networks induce dendritic cell motility via activation of the C-type lectin receptor CLEC-2.
Acton SE, Astarita JL, Malhotra D, Lukacs-Kornek V, Franz B, Hess PR, Jakus Z, Kuligowski M, Fletcher AL, Elpek KG, Bellemare-Pelletier A, Sceats L, Reynoso ED, Gonzalez SF, Graham DB, Chang J, Peters A, Woodruff M, Kim YA, Swat W, Morita T, Kuchroo V, Carroll MC, Kahn ML, Wucherpfennig KW, Turley SJ.
Immunity. 2012 Aug 24;37(2):276-89. doi: 10.1016/j.immuni.2012.05.022. Epub 2012 Aug 9.
PMID 22884313
Combined in vivo depletion of glycoprotein VI and C-type lectin-like receptor 2 severely compromises hemostasis and abrogates arterial thrombosis in mice.
Bender M, May F, Lorenz V, Thielmann I, Hagedorn I, Finney BA, Vogtle T, Remer K, Braun A, Bosl M, Watson SP, Nieswandt B.
Arterioscler Thromb Vasc Biol. 2013 May;33(5):926-34. doi: 10.1161/ATVBAHA.112.300672. Epub 2013 Feb 28.
PMID 23448972
Platelets regulate lymphatic vascular development through CLEC-2-SLP-76 signaling.
Bertozzi CC, Schmaier AA, Mericko P, Hess PR, Zou Z, Chen M, Chen CY, Xu B, Lu MM, Zhou D, Sebzda E, Santore MT, Merianos DJ, Stadtfeld M, Flake AW, Graf T, Skoda R, Maltzman JS, Koretzky GA, Kahn ML.
Blood. 2010 Jul 29;116(4):661-70. doi: 10.1182/blood-2010-02-270876. Epub 2010 Apr 2.
PMID 20363774
Platelet ITAM signaling is critical for vascular integrity in inflammation.
Boulaftali Y, Hess PR, Getz TM, Cholka A, Stolla M, Mackman N, Owens AP 3rd, Ware J, Kahn ML, Bergmeier W.
J Clin Invest. 2013 Feb 1;123(2):908-16. doi: 10.1172/JCI65154. Epub 2013 Jan 25.
PMID 23348738
Incorporation of podoplanin into HIV released from HEK-293T cells, but not PBMC, is required for efficient binding to the attachment factor CLEC-2.
Chaipan C, Steffen I, Tsegaye TS, Bertram S, Glowacka I, Kato Y, Schmokel J, Munch J, Simmons G, Gerardy-Schahn R, Pohlmann S.
Retrovirology. 2010 May 19;7:47. doi: 10.1186/1742-4690-7-47.
PMID 20482880
A novel mechanism of cytokine release in phagocytes induced by aggretin, a snake venom C-type lectin protein, through CLEC-2 ligation.
Chang CH, Chung CH, Hsu CC, Huang TY, Huang TF.
Thromb Haemost. 2010 Nov;8(11):2563-70. doi: 10.1111/j.1538-7836.2010.04045.x.
PMID 20738764
Renal cells activate the platelet receptor CLEC-2 through podoplanin.
Christou CM, Pearce AC, Watson AA, Mistry AR, Pollitt AY, Fenton-May AE, Johnson LA, Jackson DG, Watson SP, O'Callaghan CA.
Biochem J. 2008 Apr 1;411(1):133-40. doi: 10.1042/BJ20071216.
PMID 18215137
Molecular characterization of two novel C-type lectin-like receptors, one of which is selectively expressed in human dendritic cells.
Colonna M, Samaridis J, Angman L.
Eur J Immunol. 2000 Feb;30(2):697-704.
PMID 10671229
CLEC-2 and Syk in the megakaryocytic/platelet lineage are essential for development.
Finney BA, Schweighoffer E, Navarro-Nunez L, Benezech C, Barone F, Hughes CE, Langan SA, Lowe KL, Pollitt AY, Mourao-Sa D, Sheardown S, Nash GB, Smithers N, Reis e Sousa C, Tybulewicz VL, Watson SP.
Blood. 2012 Feb 16;119(7):1747-56. doi: 10.1182/blood-2011-09-380709. Epub 2011 Dec 20.
PMID 22186994
Podoplanin maintains high endothelial venule integrity by interacting with platelet CLEC-2.
Herzog BH, Fu J, Wilson SJ, Hess PR, Sen A, McDaniel JM, Pan Y, Sheng M, Yago T, Silasi-Mansat R, McGee S, May F, Nieswandt B, Morris AJ, Lupu F, Coughlin SR, McEver RP, Chen H, Kahn ML, Xia L.
Nature. 2013 Oct 3;502(7469):105-9. doi: 10.1038/nature12501. Epub 2013 Sep 1.
PMID 23995678
Molecular analysis of the pathophysiological binding of the platelet aggregation-inducing factor podoplanin to the C-type lectin-like receptor CLEC-2.
Kato Y, Kaneko MK, Kunita A, Ito H, Kameyama A, Ogasawara S, Matsuura N, Hasegawa Y, Suzuki-Inoue K, Inoue O, Ozaki Y, Narimatsu H.
Cancer Sci. 2008 Jan;99(1):54-61. Epub 2007 Oct 18.
PMID 17944973
CLEC-2 is a phagocytic activation receptor expressed on murine peripheral blood neutrophils.
Kerrigan AM1, Dennehy KM, Mourao-Sa D, Faro-Trindade I, Willment JA, Taylor PR, Eble JA, Reis e Sousa C, Brown GD.
J Immunol. 2009 Apr 1;182(7):4150-7. doi: 10.4049/jimmunol.0802808.
PMID 19299712
CLEC-2 is an essential platelet-activating receptor in hemostasis and thrombosis.
May F, Hagedorn I, Pleines I, Bender M, Vogtle T, Eble J, Elvers M, Nieswandt B.
Blood. 2009 Oct 15;114(16):3464-72. doi: 10.1182/blood-2009-05-222273. Epub 2009 Jul 29.
PMID 19641185
CLEC-2 signaling via Syk in myeloid cells can regulate inflammatory responses.
Mourao-Sa D, Robinson MJ, Zelenay S, Sancho D, Chakravarty P, Larsen R, Plantinga M, Van Rooijen N, Soares MP, Lambrecht B, Reis e Sousa C.
Eur J Immunol. 2011 Oct;41(10):3040-53. doi: 10.1002/eji.201141641. Epub 2011 Aug 17.
PMID 21728173
Lysis of tumor cells by natural killer cells in mice is impeded by platelets.
Nieswandt B, Hafner M, Echtenacher B, Mannel DN.
Cancer Res. 1999 Mar 15;59(6):1295-300.
PMID 10096562
Platelet activation receptor CLEC-2 regulates blood/lymphatic vessel separation by inhibiting proliferation, migration, and tube formation of lymphatic endothelial cells.
Osada M, Inoue O, Ding G, Shirai T, Ichise H, Hirayama K, Takano K, Yatomi Y, Hirashima M, Fujii H, Suzuki-Inoue K, Ozaki Y.
J Biol Chem. 2012 Jun 22;287(26):22241-52. doi: 10.1074/jbc.M111.329987. Epub 2012 May 3.
PMID 22556408
A novel cluster of lectin-like receptor genes expressed in monocytic, dendritic and endothelial cells maps close to the NK receptor genes in the human NK gene complex.
Sobanov Y, Bernreiter A, Derdak S, Mechtcheriakova D, Schweighofer B, Duchler M, Kalthoff F, Hofer E.
Eur J Immunol. 2001 Dec;31(12):3493-503.
PMID 11745369
Novel platelet activation receptor CLEC-2: from discovery to prospects.
Suzuki-Inoue K, Inoue O, Ozaki Y.
J Thromb Haemost. 2011 Jul;9 Suppl 1:44-55. doi: 10.1111/j.1538-7836.2011.04335.x. (REVIEW)
PMID 21781241
Lymphangiogenesis: Molecular mechanisms and future promise.
Tammela T, Alitalo K.
Cell. 2010 Feb 19;140(4):460-76. doi: 10.1016/j.cell.2010.01.045. (REVIEW)
PMID 20178740
A mouse knockout library for secreted and transmembrane proteins.
Tang T, Li L, Tang J, Li Y, Lin WY, Martin F, Grant D, Solloway M, Parker L, Ye W, Forrest W, Ghilardi N, Oravecz T, Platt KA, Rice DS, Hansen GM, Abuin A, Eberhart DE, Godowski P, Holt KH, Peterson A, Zambrowicz BP, de Sauvage FJ.
Nat Biotechnol. 2010 Jul;28(7):749-55. doi: 10.1038/nbt.1644. Epub 2010 Jun 20.
PMID 20562862
Structural and functional conservation of CLEC-2 with the species-specific regulation of transcript expression in evolution.
Wang L, Ren S, Zhu H, Zhang D, Hao Y, Ruan Y, Zhou L, Lee C, Qiu L, Yun X, Xie J.
Glycoconj J. 2012 Aug;29(5-6):335-45. doi: 10.1007/s10719-012-9415-0. Epub 2012 Jun 28.
PMID 22740230
The crystal structure and mutational binding analysis of the extracellular domain of the platelet-activating receptor CLEC-2.
Watson AA, Brown J, Harlos K, Eble JA, Walter TS, O'Callaghan CA.
J Biol Chem. 2007 Feb 2;282(5):3165-72. Epub 2006 Nov 28.
PMID 17132623


This paper should be referenced as such :
Suzuki-Inoue, K
CLEC1B (C-Type Lectin Domain Family 1, Member B)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(7):457-460.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)CLEC1B   24356
Entrez_Gene (NCBI)CLEC1B    C-type lectin domain family 1 member B
Aliases1810061I13Rik; CLEC2; CLEC2B; PRO1384; 
GeneCards (Weizmann)CLEC1B
Ensembl hg19 (Hinxton)ENSG00000165682 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000165682 [Gene_View]  ENSG00000165682 [Sequence]  chr12:9993061-9999300 [Contig_View]  CLEC1B [Vega]
ICGC DataPortalENSG00000165682
Genatlas (Paris)CLEC1B
SOURCE (Princeton)CLEC1B
Genetics Home Reference (NIH)CLEC1B
Genomic and cartography
GoldenPath hg38 (UCSC)CLEC1B  -     chr12:9993061-9999300 -  12p13.31-p13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)CLEC1B  -     12p13.31-p13.2   [Description]    (hg19-Feb_2009)
GoldenPathCLEC1B - 12p13.31-p13.2 [CytoView hg19]  CLEC1B - 12p13.31-p13.2 [CytoView hg38]
genome Data Viewer NCBICLEC1B [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF124841 AY358599 BC029554 BX647321
RefSeq transcript (Entrez)NM_001099431 NM_016509
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)CLEC1B
Alternative Splicing GalleryENSG00000165682
Gene ExpressionCLEC1B [ NCBI-GEO ]   CLEC1B [ EBI - ARRAY_EXPRESS ]   CLEC1B [ SEEK ]   CLEC1B [ MEM ]
Gene Expression Viewer (FireBrowse)CLEC1B [ Firebrowse - Broad ]
GenevisibleExpression of CLEC1B in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)51266
GTEX Portal (Tissue expression)CLEC1B
Human Protein AtlasENSG00000165682-CLEC1B [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9P126   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9P126  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9P126
Splice isoforms : SwissVarQ9P126
Domaine pattern : Prosite (Expaxy)C_TYPE_LECTIN_2 (PS50041)   
Domains : Interpro (EBI)C-type_lectin-like    C-type_lectin-like/link_sf    CTDL_fold    NKR-like_CTLD   
Domain families : Pfam (Sanger)Lectin_C (PF00059)   
Domain families : Pfam (NCBI)pfam00059   
Domain families : Smart (EMBL)CLECT (SM00034)  
Conserved Domain (NCBI)CLEC1B
Blocks (Seattle)CLEC1B
PDB (RSDB)2C6U    3WSR    3WWK   
PDB Europe2C6U    3WSR    3WWK   
PDB (PDBSum)2C6U    3WSR    3WWK   
PDB (IMB)2C6U    3WSR    3WWK   
Structural Biology KnowledgeBase2C6U    3WSR    3WWK   
SCOP (Structural Classification of Proteins)2C6U    3WSR    3WWK   
CATH (Classification of proteins structures)2C6U    3WSR    3WWK   
Human Protein Atlas [tissue]ENSG00000165682-CLEC1B [tissue]
Peptide AtlasQ9P126
IPIIPI00009457   IPI00169302   IPI00871400   IPI00873831   
Protein Interaction databases
IntAct (EBI)Q9P126
Ontologies - Pathways
Ontology : AmiGOtransmembrane signaling receptor activity  protein binding  plasma membrane  integral component of plasma membrane  defense response  cell surface receptor signaling pathway  viral process  signal transduction by protein phosphorylation  platelet activation  platelet formation  carbohydrate binding  
Ontology : EGO-EBItransmembrane signaling receptor activity  protein binding  plasma membrane  integral component of plasma membrane  defense response  cell surface receptor signaling pathway  viral process  signal transduction by protein phosphorylation  platelet activation  platelet formation  carbohydrate binding  
REACTOMEQ9P126 [protein]
REACTOME PathwaysR-HSA-114604 [pathway]   
NDEx NetworkCLEC1B
Atlas of Cancer Signalling NetworkCLEC1B
Wikipedia pathwaysCLEC1B
Orthology - Evolution
GeneTree (enSembl)ENSG00000165682
Phylogenetic Trees/Animal Genes : TreeFamCLEC1B
Homologs : HomoloGeneCLEC1B
Homology/Alignments : Family Browser (UCSC)CLEC1B
Gene fusions - Rearrangements
Fusion : QuiverCLEC1B
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerCLEC1B [hg38]
Exome Variant ServerCLEC1B
GNOMAD BrowserENSG00000165682
Varsome BrowserCLEC1B
Genomic Variants (DGV)CLEC1B [DGVbeta]
DECIPHERCLEC1B [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisCLEC1B 
ICGC Data PortalCLEC1B 
TCGA Data PortalCLEC1B 
Broad Tumor PortalCLEC1B
OASIS PortalCLEC1B [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICCLEC1B  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DCLEC1B
Mutations and Diseases : HGMDCLEC1B
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch CLEC1B
DgiDB (Drug Gene Interaction Database)CLEC1B
DoCM (Curated mutations)CLEC1B (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)CLEC1B (select a term)
NCG6 (London) select CLEC1B
Cancer3DCLEC1B(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry CLEC1B
NextProtQ9P126 [Medical]
Target ValidationCLEC1B
Huge Navigator CLEC1B [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTD
Pharm GKB GenePA142672098
Clinical trialCLEC1B
canSAR (ICR)CLEC1B (select the gene name)
DataMed IndexCLEC1B
PubMed46 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Feb 19 17:48:09 CET 2021

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