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DEFB1 (defensin, beta 1)

Written2010-05Ernesto Prado Montes de Oca
Medical, Pharmaceutical Biotechnology Unit, Research Center in Technology, Design Assistance of Jalisco State (CIATEJ, A.C.), National Council of Science, Technology (CONACYT), Av. Normalistas 800, Col. Colinas de la Normal, C.P. 44270, Guadalajara, Jalisco, Mexico

(Note : for Links provided by Atlas : click)


Alias_symbol (synonym)HBD-1
Other alias
LocusID (NCBI) 1672
Atlas_Id 44352
Location 8p23.1  [Link to chromosome band 8p23]
Location_base_pair Starts at 6728097 and ends at 6735529 bp from pter ( according to hg19-Feb_2009)  [Mapping DEFB1.png]
Local_order AGPAT5-XKR5-DEFB1-DEFA6-DEFA4 (reverse strand, according to
Note DEFB1 is a peptide expressed mainly in epithelia with an antimicrobial function against viruses, Gram-positive, Gram-negative bacteria and Mycobacterium tuberculosis. It also functions as immunomodulator and as a tumor supressor gene. Single Nucleotide Polymorphisms (SNPs) in this gene have been associated with cancer, allergic and infectious diseases as well as with DEFB1 downregulation (Prado-Montes de Oca, 2010).


  Figure 1. DEFB1 gene. The diagram shows pre-propeptide coding sequence (black rectangles) and unstranslated regions (blue rectangles). Signal peptide coding sequence is comprised of 60 bases. Mature peptide coding sequence spans 144 bases ( The pro-peptide segment is in exon 1 and not in exon 2 as in the rest of beta-defensins known to date (Pazgier et al., 2006).
Description DEFB1 is a gene composed of 2 exons and a ~7 kb intron. DEFB1 spans 7488 bp, two exons and one intron of 6962 bp (Liu et al., 1997).
Transcription The transcript is of 207 nt ( No variants are produced by alternative splicing, the entire mature peptide coding sequence is in exon 1, however several hBD-1 amino-terminal processed forms are found in urine (Valore et al., 1998), probably cleaved by chymotrypsin (Zucht et al., 1998) or matrix metalloproteinase 7 (matrylisin) (Wilson et al., 2009) each showing different microbicidal potencies (Valore et al., 1998). The functions and tissue of origin of these processed forms are unknown (Prado-Montes de Oca, 2010).
Pseudogene None reported. DEFB1 is considered as a unique copy gene, although rare duplicons in some individuals have been reported (Linzmeier et al., 2005).


Note Human beta-defensins are produced mainly by various epithelia and secreted in mature forms by the producing cells. The hBD-1 shows three disulfide bridges (with the pro-peptide nomenclature) are formed at cysteines 37-66 (1-5), 44-59 (2-4) and 49-67 (3-6). The disulfide bridge pattern on cysteines 1-5, 2-4 and 3-6 is a hallmark of beta-defensins (Prado-Montes de Oca, 2010).
  Figure 2. (A) Model of hBD-1 peptide (according to PDB:1IJU, (B) Sequence of hBD-1 pro-peptide. Signal peptide sequence (blue), mature peptide (black) with cysteine residues (bold) and disulfide bridges (brackets) are shown.
Description The prepropeptide has 68 aa and the mature peptide is of 48 amino acids. As quaternary structure hBD-1 shows in vitro dimerization by weak intermolecular salt bridges, but if dimers are formed in vivo or if they perform any different function is unknown (Prado Montes de Oca, 2010).
Expression The highest concentrations of hBD-1 are found in the kidney (epithelial layes of the loops of Henle, distal tubules, collecting tubes) and female reproductive tract (layers of vagina, ectocervix, endocervix, uterus, fallopian tubes), especially in pregnant women. It is also expressed in astrocytes, mammary gland, cornea, small intestine, gingival tissue, epithelial cells of testis, mature dendritic cells (for a more complete information of DEFB1-expressing cells see and
Localisation The hBD-1 peptide resides in the cytoplasm of normal cells and in the nucleus of several cancer cells (Bick et al., 2007; Wenghoefer et al., 2008). In normal skin, hBD-1 is localized to the perinuclear region of keratinocytes and in burned skin in dermal glandular structures and hair shafts (Poindexter et al., 2006).
Function hBD-1 functions as an antimicrobial peptide against viruses as HIV, Av1CF2, Gram-positive and Gram-negative bacteria, Mycobacterium tuberculosis. It functions as a chemoattractant to immature dendritic cells and T cells acts as a tumor suppressor inducing caspase-mediated apoptosis. In addition it could be involved as transcription factor in epithelia reorganization (Prado Montes de Oca, 2010).
Homology Homolog genes to human beta-defensin 1 are found in Mus musculus (mouse) (Morrison et al., 1998), Pan troglodytes (chimpanzee) (Prado-Montes de Oca et al., 2009), Macaca mulatta (Rhesus monkey), Canis familiaris (dog), Rattus norvegicus (rat), Sus scrofa (pig, named beta defensin 2), Bos taurus (cow, named protein similar to beta defensin) among other species (;


Note There are 214 annotated polymorphisms in DEFB1, most of them are SNPs (bdSNP build 130, Insertions and deletions are less frequently found (López Campos and Prado Montes de Oca, in process). There are reports of 10 SNPs in DEFB1 with disease association. The most relevant SNPs are those located on 5' unstranslated region namely -52A (higher HIV load and higher risk of perinatal HIV infection, gastritis, asthma), -44C (atopic dermatitis, chronic obstructive pulmonar disease, Crohn's disease, cancer, lepromatous leprosy) and -20 A/G (infections in cystic fibrosis) (gene RIF at; Prado-Montes de Oca, 2010). The variant -44C correlates with lower constitutive expression and -44G correlates with lower IFN-gamma-dependent induction. This could explain the extremely rare heterozygote advantage in this region (Figuera et al., 2005; Prado Montes de Oca, 2010).
  Figure 3. The 214 polymorphisms annotated in both strands of DEFB1 gene according to UCSC Genome Browser (, hg19, Feb 2009). Most polymorphisms are located in intron (black), fewer are located in UTRs (blue) and exons. Those polymorphisms located in exons could be either synonymous (green) or non-synonymous (red).

Implicated in

Entity The 8p23.1 duplication syndrome
Note Associate with variable phenotype that may include one or more of the following: developmental delay, mild dysmorphism and heart defects (Barber et al., 2010).
Cytogenetics The 8p23.1 duplication syndrome and copy number variation of the 8p23.1 defensin gene cluster are cytogenetically indistinguishable but distinct at the molecular level (Barber et al., 2010).
Entity Copy number variation of the 8p23.1 defensin gene cluster
Note From 1 to 12 copies of 8p23.1 defensin gene cluster are normally found per diploid genome (Hollox et al., 2003). The null allele is very rare (allele frequency 0.2%) (Hollox et al., 2008). Predisposition to Crohn's disease and sporadic prostate cancer is higher at low copy number (Huse et al., 2008) and to psoriasis at high copy number (Hollox, 2008).
Entity Oral squamous cell carcinoma (OSCC)
Note DEFB1 basal expression is 50-fold lower in OSCC, and inducibility is significantly reduced (Wenghoefer et al., 2008). Genotypes in DEFB1 gene tend to loss of heterozygosity in OSCC (Joly et al., 2009).
Entity Malignant melanoma
Note It was found weak evidence that genotype -44 GG in DEFB1 increases risk for malignant melanoma in a Spanish population (OR= 2.78, CI 95%= 0.88-8.82, p=0.08) (Fernandez et al., 2009).
Entity Prostate and renal cancers
Note DEFB1 has been proposed as a tumor suppressor because it promotes cancer cells apoptosis and is absent in most tumor samples (Sun et al., 2006; Bullard et al., 2008). There is a marked down-regulation of DEFB1 in 82% of prostate cancers and 90% of renal cell carcinomas (Donald et al., 2003) and this DEFB1 downregulation is associated with malignancy (Wenghoefer et al., 2008; Pantelis et al., 2009). Furthermore, oncogene PAX2 binds to DEFB1 promoter and suppresses its expression independent of p53 (Bose et al., 2009). Parvalbumin and DEFB1 expression could be useful to differentiate papillary renal cell carcinoma (RCC) from conventional RCC (Young et al., 2003).
Entity Leukoplakia
Note DEFB1 is downregulated 2.5 fold in leukoplakia but their role in the disease, if any, is unknown (Wenghoefer et al., 2008).
Entity Several allergic and infectious diseases
Note For allergic and infectious diseases where DEFB1 is implicated see Prado Montes de Oca, 2010.

To be noted

Gene regulation of DEFB1 is not well known. More experimental data is needed to differentiate the constitutive from the inducible pathways (Kalus et al., 2009; Prado Montes de Oca et al., 2009) in order to propose alternative therapies to diseases where DEFB1 is implicated (Prado Montes de Oca, 2010).
This work was supported by the Fondos Sectoriales de Ciencia Basica SEP-CONACYT (CB-2008-01-105813) and CIATEJ A.C. The author receives a research stimulus from the Sistema Nacional de Investigadores (SNI 41290, CONACYT, Mexico) and wishes to thank the Editor for the kind invitation.


8p23.1 duplication syndrome differentiated from copy number variation of the defensin cluster at prenatal diagnosis in four new families.
Barber JC, Bunyan D, Curtis M, Robinson D, Morlot S, Dermitzel A, Liehr T, Alves C, Trindade J, Paramos AI, Cooper C, Ocraft K, Taylor EJ, Maloney VK.
Mol Cytogenet. 2010 Feb 18;3:3.
PMID 20167067
Nuclear localization of HBD-1 in human keratinocytes.
Bick RJ, Poindexter BJ, Buja LM, Lawyer CH, Milner SM, Bhat S.
J Burns Wounds. 2007 Aug 24;7:e3.
PMID 18091980
PAX2 oncogene negatively regulates the expression of the host defense peptide human beta defensin-1 in prostate cancer.
Bose SK, Gibson W, Bullard RS, Donald CD.
Mol Immunol. 2009 Mar;46(6):1140-8. Epub 2008 Dec 31.
PMID 19118900
Functional analysis of the host defense peptide Human Beta Defensin-1: new insight into its potential role in cancer.
Bullard RS, Gibson W, Bose SK, Belgrave JK, Eaddy AC, Wright CJ, Hazen-Martin DJ, Lage JM, Keane TE, Ganz TA, Donald CD.
Mol Immunol. 2008 Feb;45(3):839-48. Epub 2007 Sep 14.
PMID 17868871
Cancer-specific loss of beta-defensin 1 in renal and prostatic carcinomas.
Donald CD, Sun CQ, Lim SD, Macoska J, Cohen C, Amin MB, Young AN, Ganz TA, Marshall FF, Petros JA.
Lab Invest. 2003 Apr;83(4):501-5.
PMID 12695553
Human beta-defensins (HBD1 and HBD3) and malignant melanoma susceptibility.
Fernandez LP, Milne RL, Pita G, Floristan U, Sendagorta E, Feito M, Aviles JA, Martin-Gonzalez M, Lazaro P, Benitez J, Ribas G.
Melanoma Res. 2009 Oct;19(5):340-1.
PMID 19741426
Natural selection and/or gametic drift probably favours genotype of the beta defensin 1 in a Mexican population.
Figuera L, Prado Montes de Oca E, Gallegos-Arreola MP, Sandoval L.
X Human Genome Meeting 2005, Kyoto, Japan.
Extensive normal copy number variation of a beta-defensin antimicrobial-gene cluster.
Hollox EJ, Armour JA, Barber JC.
Am J Hum Genet. 2003 Sep;73(3):591-600. Epub 2003 Aug 12.
PMID 12916016
Defensins and the dynamic genome: what we can learn from structural variation at human chromosome band 8p23.1.
Hollox EJ, Barber JC, Brookes AJ, Armour JA.
Genome Res. 2008 Nov;18(11):1686-97. (REVIEW)
PMID 18974263
Copy number variation of beta-defensins and relevance to disease.
Hollox EJ.
Cytogenet Genome Res. 2008;123(1-4):148-55. Epub 2009 Mar 11. (REVIEW)
PMID 19287149
Genetic variants of the copy number polymorphic beta-defensin locus are associated with sporadic prostate cancer.
Huse K, Taudien S, Groth M, Rosenstiel P, Szafranski K, Hiller M, Hampe J, Junker K, Schubert J, Schreiber S, Birkenmeier G, Krawczak M, Platzer M.
Tumour Biol. 2008;29(2):83-92. Epub 2008 Jun 2.
PMID 18515986
Loss of human beta-defensin 1, 2, and 3 expression in oral squamous cell carcinoma.
Joly S, Compton LM, Pujol C, Kurago ZB, Guthmiller JM.
Oral Microbiol Immunol. 2009 Oct;24(5):353-60.
PMID 19702947
Association of a genetic polymorphism (-44 C/G SNP) in the human DEFB1 gene with expression and inducibility of multiple beta-defensins in gingival keratinocytes.
Kalus AA, Fredericks LP, Hacker BM, Dommisch H, Presland RB, Kimball JR, Dale BA.
BMC Oral Health. 2009 Aug 27;9:21.
PMID 19712472
Human defensin gene copy number polymorphisms: comprehensive analysis of independent variation in alpha- and beta-defensin regions at 8p22-p23.
Linzmeier RM, Ganz T.
Genomics. 2005 Oct;86(4):423-30.
PMID 16039093
The human beta-defensin-1 and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry.
Liu L, Zhao C, Heng HH, Ganz T.
Genomics. 1997 Aug 1;43(3):316-20.
PMID 9268634
Mouse beta defensin-1 is a functional homolog of human beta defensin-1.
Morrison GM, Davidson DJ, Kilanowski FM, Borthwick DW, Crook K, Maxwell AI, Govan JR, Dorin JR.
Mamm Genome. 1998 Jun;9(6):453-7.
PMID 9585433
Down regulation and nuclear localization of human beta-defensin-1 in pleomorphic adenomas of salivary glands.
Pantelis A, Wenghoefer M, Haas S, Merkelbach-Bruse S, Pantelis D, Jepsen S, Bootz F, Winter J.
Oral Oncol. 2009 Jun;45(6):526-30. Epub 2008 Sep 20.
PMID 18805729
Studies of the biological properties of human beta-defensin 1.
Pazgier M, Prahl A, Hoover DM, Lubkowski J.
J Biol Chem. 2007 Jan 19;282(3):1819-29. Epub 2006 Oct 27.
PMID 17071614
Localization of antimicrobial peptides in normal and burned skin.
Poindexter BJ, Bhat S, Buja LM, Bick RJ, Milner SM.
Burns. 2006 Jun;32(4):402-7. Epub 2006 Apr 18.
PMID 16621313
Human beta-defensin 1: a restless warrior against allergies, infections and cancer.
Prado-Montes de Oca E.
Int J Biochem Cell Biol. 2010 Jun;42(6):800-4. Epub 2010 Jan 25.
PMID 20100591
Human beta-defensin-1, a potential chromosome 8p tumor suppressor: control of transcription and induction of apoptosis in renal cell carcinoma.
Sun CQ, Arnold R, Fernandez-Golarz C, Parrish AB, Almekinder T, He J, Ho SM, Svoboda P, Pohl J, Marshall FF, Petros JA.
Cancer Res. 2006 Sep 1;66(17):8542-9.
PMID 16951166
Human beta-defensin-1: an antimicrobial peptide of urogenital tissues.
Valore EV, Park CH, Quayle AJ, Wiles KR, McCray PB Jr, Ganz T.
J Clin Invest. 1998 Apr 15;101(8):1633-42.
PMID 9541493
Decreased gene expression of human beta-defensin-1 in the development of squamous cell carcinoma of the oral cavity.
Wenghoefer M, Pantelis A, Dommisch H, Reich R, Martini M, Allam JP, Novak N, Berge S, Jepsen S, Winter J.
Int J Oral Maxillofac Surg. 2008 Jul;37(7):660-3. Epub 2008 Mar 17.
PMID 18346877
Differential Processing of {alpha}- and {beta}-Defensin Precursors by Matrix Metalloproteinase-7 (MMP-7).
Wilson CL, Schmidt AP, Pirila E, Valore EV, Ferri N, Sorsa T, Ganz T, Parks WC.
J Biol Chem. 2009 Mar 27;284(13):8301-11. Epub 2009 Jan 30.
PMID 19181662
Beta defensin-1, parvalbumin, and vimentin: a panel of diagnostic immunohistochemical markers for renal tumors derived from gene expression profiling studies using cDNA microarrays.
Young AN, de Oliveira Salles PG, Lim SD, Cohen C, Petros JA, Marshall FF, Neish AS, Amin MB.
Am J Surg Pathol. 2003 Feb;27(2):199-205.
PMID 12548166
Human beta-defensin-1: A urinary peptide present in variant molecular forms and its putative functional implication.
Zucht HD, Grabowsky J, Schrader M, Liepke C, Jurgens M, Schulz-Knappe P, Forssmann WG.
Eur J Med Res. 1998 Jul 20;3(7):315-23.
PMID 9682027


This paper should be referenced as such :
Prado, Montes de Oca E
DEFB1 (defensin, beta 1)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(2):136-140.
Free journal version : [ pdf ]   [ DOI ]
On line version :

External links

HGNC (Hugo)DEFB1   2766
Entrez_Gene (NCBI)DEFB1  1672  defensin beta 1
AliasesBD1; DEFB-1; DEFB101; HBD1
GeneCards (Weizmann)DEFB1
Ensembl hg19 (Hinxton)ENSG00000164825 [Gene_View]  chr8:6728097-6735529 [Contig_View]  DEFB1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000164825 [Gene_View]  chr8:6728097-6735529 [Contig_View]  DEFB1 [Vega]
ICGC DataPortalENSG00000164825
TCGA cBioPortalDEFB1
Genatlas (Paris)DEFB1
SOURCE (Princeton)DEFB1
Genetics Home Reference (NIH)DEFB1
Genomic and cartography
GoldenPath hg19 (UCSC)DEFB1  -     chr8:6728097-6735529 -  8p23.1   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)DEFB1  -     8p23.1   [Description]    (hg38-Dec_2013)
EnsemblDEFB1 - 8p23.1 [CytoView hg19]  DEFB1 - 8p23.1 [CytoView hg38]
Mapping of homologs : NCBIDEFB1 [Mapview hg19]  DEFB1 [Mapview hg38]
Gene and transcription
Genbank (Entrez)BC033298 BC047677 BM673094 HQ448540 U73945
RefSeq transcript (Entrez)NM_005218
RefSeq genomic (Entrez)NC_000008 NC_018919 NT_023736 NW_004929335
Consensus coding sequences : CCDS (NCBI)DEFB1
Cluster EST : UnigeneHs.32949 [ NCBI ]
CGAP (NCI)Hs.32949
Alternative Splicing GalleryENSG00000164825
Gene ExpressionDEFB1 [ NCBI-GEO ]   DEFB1 [ EBI - ARRAY_EXPRESS ]   DEFB1 [ SEEK ]   DEFB1 [ MEM ]
Gene Expression Viewer (FireBrowse)DEFB1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1672
GTEX Portal (Tissue expression)DEFB1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP60022   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP60022  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP60022
Splice isoforms : SwissVarP60022
Domains : Interpro (EBI)Defensin_beta-typ   
Domain families : Pfam (Sanger)Defensin_beta (PF00711)   
Domain families : Pfam (NCBI)pfam00711   
Conserved Domain (NCBI)DEFB1
DMDM Disease mutations1672
Blocks (Seattle)DEFB1
PDB (SRS)1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
PDB (PDBSum)1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
PDB (IMB)1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
PDB (RSDB)1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
Structural Biology KnowledgeBase1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
SCOP (Structural Classification of Proteins)1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
CATH (Classification of proteins structures)1E4S    1IJU    1IJV    1KJ5    2NLB    2NLC    2NLD    2NLE    2NLF    2NLG    2NLH    2NLP    2NLQ    2NLS    2PLZ   
Human Protein AtlasENSG00000164825
Peptide AtlasP60022
Protein Interaction databases
IntAct (EBI)P60022
Ontologies - Pathways
Ontology : AmiGOinnate immune response in mucosa  acute inflammatory response  extracellular region  extracellular space  Golgi lumen  chemotaxis  immune response  G-protein coupled receptor signaling pathway  response to bacterium  response to bacterium  antibacterial humoral response  response to testosterone  defense response to bacterium  innate immune response  innate immune response  innate immune response  defense response to Gram-positive bacterium  extracellular exosome  
Ontology : EGO-EBIinnate immune response in mucosa  acute inflammatory response  extracellular region  extracellular space  Golgi lumen  chemotaxis  immune response  G-protein coupled receptor signaling pathway  response to bacterium  response to bacterium  antibacterial humoral response  response to testosterone  defense response to bacterium  innate immune response  innate immune response  innate immune response  defense response to Gram-positive bacterium  extracellular exosome  
REACTOMEP60022 [protein]
REACTOME Pathways1461957 [pathway]   1461973 [pathway]   
NDEx NetworkDEFB1
Atlas of Cancer Signalling NetworkDEFB1
Wikipedia pathwaysDEFB1
Orthology - Evolution
GeneTree (enSembl)ENSG00000164825
Phylogenetic Trees/Animal Genes : TreeFamDEFB1
Homologs : HomoloGeneDEFB1
Homology/Alignments : Family Browser (UCSC)DEFB1
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDEFB1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DEFB1
Exome Variant ServerDEFB1
ExAC (Exome Aggregation Consortium)DEFB1 (select the gene name)
Genetic variants : HAPMAP1672
Genomic Variants (DGV)DEFB1 [DGVbeta]
DECIPHER (Syndromes)8:6728097-6735529  ENSG00000164825
CONAN: Copy Number AnalysisDEFB1 
ICGC Data PortalDEFB1 
TCGA Data PortalDEFB1 
Broad Tumor PortalDEFB1
OASIS PortalDEFB1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDEFB1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDDEFB1
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 DEFB1
DgiDB (Drug Gene Interaction Database)DEFB1
DoCM (Curated mutations)DEFB1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)DEFB1 (select a term)
NCG5 (London)DEFB1
Cancer3DDEFB1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry DEFB1
NextProtP60022 [Medical]
Huge Navigator DEFB1 [HugePedia]
snp3D : Map Gene to Disease1672
BioCentury BCIQDEFB1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1672
Chemical/Pharm GKB GenePA27243
Clinical trialDEFB1
canSAR (ICR)DEFB1 (select the gene name)
Other databaseDefensins Knowledgebase
PubMed174 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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