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VIP (vasoactive intestinal peptide)

Written2013-08Terry Moody
National Cancer Institute, Center for Cancer Research, Office of the Director, 31 Center Drive, Bldg 31, Rm 4A48, Bethesda, Maryland 20892, USA

(Note : for Links provided by Atlas : click)


Other aliasPHM27
LocusID (NCBI) 7432
Atlas_Id 44215
Location 6q25.2  [Link to chromosome band 6q25]
Location_base_pair Starts at 152750797 and ends at 152759766 bp from pter ( according to hg19-Feb_2009)  [Mapping VIP.png]
Local_order The VIP gene has 7 exons.
  Structure of human preproVIP. VIP is derived from the 170 amino acid precursor protein preproVIP. Initially the signal peptide (1-20) is cleaved by signal proteases to generate proVIP. ProVIP (22-170) is metabolized to (22-79), PHM (81-107), (111-122), VIP (125-152) and (156-170) by prohormone convertases. Carboxypeptidase B-like enzymes cleave basic R and K. The C-terminal of PHM and VIP is amidated when G is metabolized by peptidylglycine alpha-amidating monooxygenase (PAM) enzymes.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
Note VIP is a secreted protein which binds to membrane G-protein coupled receptors (GPCR) increasing intracellular cAMP signaling.


Note The human VIP gene encodes 7 exons and is localized to chromosome 6q25.2 (Fahrenkrug, 2010).
Description The VIP gene spans 8837 bp.
Transcription The gene transcript has 1601 bp.


Description Said and Mutt (1970) sequenced an acid extractable peptide from the porcine duodenum which decreased systemic arterial pressure and increased heart rate, stroke volume, mesenteric and femoral blood flow in the dog. The 27 amino acid peptide was named vasoactive intestinal peptide (VIP). VIP is metabolized (Bodner et al., 1985) from a 170 amino acid precursor protein (preproVIP). Each exon encodes a distinct domain of the preproVIP 5' untranslated regions of the mRNA (exon I); signal peptide of preproVIP (exon II); N-terminal peptide (exon III); peptide histidine methionine (PHM) (exon IV); VIP (exon V); C-terminal of preproVIP (exon VI); untranslated region of the mRNA (exon VII). VIP and PHM, which have 48% amino acid homology, are in adjacent exons and the introns surrounding these exons are highly conserved. The substrate prepro-VIP is initially metabolized by a signal protease to form the product 149 amino acid pro-VIP. Pro-VIP is metabolized by prohormone convertases to VIP-GKR (preproVIP(125-155)) and PHM-GKR (preproVIP(81-110)). The basic amino acids are cleaved by carboxypeptidase B and the G is metabolized to an amide by PAM enzymes. Thus the N-terminal of VIP and PHM is free whereas the C-terminal is amidated. VIP is structurally related to pituitary adenylate cyclase activating polypeptide (PACAP) (Arimura, 1992). VIP has a β-turn at residues 2-5 and 7-10 followed by an α-helix at residues 11-26 (Vaudry et al., 2009).
VIP binds with high affinity to 2 GPCR (VPAC1 and VPAC2) which are members of the class II or class B secretin-like receptors but not PAC1 which binds PACAP with high affinity (Harmar et al., 2012). The activated VPAC1 or VPAC2 interacts with a stimulatory guanine nucleotide binding protein (Gs) causing increased adenylylcyclase activity resulting in elevated cAMP. The increased cAMP activates protein kinase (PK) A causing phosphorylation of various proteins such as CREB leading to altered gene expression.
Expression VIP is produced in neurons within the adrenals, brain, gastrointestinal (GI) tract, heart, pituitary and pancreas (Sundler et al., 1988). VIP addition to the adrenals causes catecholamine release (Card et al., 1988). VIP expression in the suprachiasmatic nucleus of the brain is altered by light-dark cycles (Gozes et al., 1989) suggesting that it may play a role in circadian cycles. VIP reduction in knockout mice is associated with human motility disorders (Moody et al., 2011). In the heart, VIP-containing nerve fibers are abundant in arteries but not veins and venules (Sundler et al., 1988). VIP secretion from pancreatic neurons alters enzyme and electrolyte secretion (Konturek et al., 1976). In the pituitary, VIP gene expression is regulated by estrogen leading to altered prolactin secretion (Montagne et al., 1995). VIP is present in and secreted from immune cells especially Th2 cells altering cytokine and chemokine production (Gonzalez-Rey et al., 2007). The VIP gene is in NSCLC cells and its expression is regulated in a PKC and cAMP dependent manner (Davidson et al., 1996). VIP is present in neuroblastoma and pheochromocytoma (Beinfeld et al., 1988). The results indicate that VIP is present in normal neurons and cancer cells.
Localisation PreproVIP is stored in dense core neurosecretory granules in cells. PHM, proVIP and VIP are secreted when cAMP is elevated. While VIP has potent biological activity, PHM and proVIP are also active (Fahrenkrug, 1991). In NSCLC cells, the ratio of PHM/ proVIP/VIP is 1/3/1 respectively (Moody et al., 2003). VIP is metabolized by neutral endopeptidase and has a half life of 2 min (Henning and Sawmiller, 2001).
Function VIP is a cotransmitter with nitric oxide and carbon monoxide of nonadrenergic, noncholinergic vascular and nonvascular smooth muscle (Said and Rattan, 2004). It is a cotransmitter with acetylcholine in exocrine glands (Fahrenkrug, 1993). VIP promotes neuronal survival (Brenneman and Eiden, 1986). VIP causes prolactin secretion from the pituitary (Reichlin, 1988) and catecholamine release from the adrenal medulla (Malhotra et al., 1988). In the immune system VIP regulates T cell traffic and proliferation (Ottaway, 1987).
Homology VIP has 67% sequence homology with PACAP-27. The sequence for VIP is identical in the human, bovine, porcine and rat.


Note The VIP gene is altered in patients with idiopathic pulmonary arterial hypertension (IPAH) (Haberl et al., 2007). The 3' untranslated region in exon 7 is mutated (g.8129T>C) leading to reduced VIP serum levels and higher pulmonary artery pressure (Zhang et al., 2009).

Implicated in

Entity Pancreatic cancer
Note VIPomas were described by Verner and Morrison (1958). Most of the VIPomas occur in the pancreas leading to diarrheal fluid similar to that seen in patient with cholera, hence the term pancreatic cholera of watery diarrhea, hypokalemic and achlorhydric (WDHA) has been used. The plasma VIP levels are significantly elevated in patients with VIPomas (Long et al., 1981).
Entity Lung cancer
Note The VIP gene is expressed in numerous lung cancer cell lines (Davidson et al., 1996). Pro-VIP and VIP are present in lung cancer cell lines (Moody et al., 2003). VIP (10 nM) increases lung cancer colony formation which is inhibited by the VPAC1 antagonist VIPhybrid (Moody et al., 1993). High densities of VPAC1 are present in lung cancer cells (Moody and Gozes, 2007).
Entity Breast cancer
Note VIP addition to breast cancer cells causes transactivation of the EGF receptor and HER2 (Valdehita et al., 2009). Addition of VIP-camptothecin conjugates causes apoptosis of breast cancer cells (Moody et al., 2007).
Entity Renal cell carcinoma
Note Addition of 100 nM VIP to renal cancer cells decreases proliferation (Vacas et al., 2012). High concentrations of VIP may cause differentiation of cancer cells (Hoosein et al., 1989).
Entity Prostate cancer
Note High densities of VPAC1 were detected in prostate cancer cell lines (Reubi et al., 2000).
Entity Colon cancer
Note 123I-VIP can be used to visualize colon cancer tumors in patients (Raderer et al., 1998).
Entity Diabetes
Note Overexpression of the VIP gene in mouse pancreatic beta cells resulted in reduced blood glucose and insensitivity to glucose intolerance (Passemard et al., 2011).
Entity Bronchial asthma
Note VIP nerves are absent in severely asthmatic subjects. Mice with targeted deletion of the VIP gene exhibit histopathologic features of airway inflammation (Said et al., 2010).
Entity Cardiomyopathy
Note Hearts were dilated in VIP knockout mice with thinning of the left ventricular wall and increases in right ventricular and left ventricular chamber size resulting from overexpression of cardiomyophathy genes (Szema et al., 2013). VIP is a potent vasodilator and increases the heart rate (Henning and Sawmiller, 2001).


Pituitary adenylate cyclase activating polypeptide (PACAP): discovery and current status of research.
Arimura A.
Regul Pept. 1992 Feb 18;37(3):287-303. (REVIEW)
PMID 1313597
The regulation of vasoactive intestinal peptide synthesis in neuroblastoma and chromaffin cells.
Beinfeld MC, Brick PL, Howlett AC, Holt IL, Pruss RM, Moskal JR, Eiden LE.
Ann N Y Acad Sci. 1988;527:68-76. (REVIEW)
PMID 2839090
Coding sequences for vasoactive intestinal peptide and PHM-27 peptide are located on two adjacent exons in the human genome.
Bodner M, Fridkin M, Gozes I.
Proc Natl Acad Sci U S A. 1985 Jun;82(11):3548-51.
PMID 2987932
Vasoactive intestinal peptide and electrical activity influence neuronal survival.
Brenneman DE, Eiden LE.
Proc Natl Acad Sci U S A. 1986 Feb;83(4):1159-62.
PMID 3456568
Localization of vasopressin-, vasoactive intestinal polypeptide-, peptide histidine isoleucine- and somatostatin-mRNA in rat suprachiasmatic nucleus.
Card JP, Fitzpatrick-McElligott S, Gozes I, Baldino F Jr.
Cell Tissue Res. 1988 May;252(2):307-15.
PMID 2898292
Regulation of VIP gene expression in general. Human lung cancer cells in particular.
Davidson A, Moody TW, Gozes I.
J Mol Neurosci. 1996 Summer;7(2):99-110. (REVIEW)
PMID 8873894
Fahrenkrug J.
Results Probl Cell Differ. 2010;50:221-34. doi: 10.1007/400_2009_24. (REVIEW)
PMID 19859678
Therapeutical approaches of vasoactive intestinal peptide as a pleiotropic immunomodulator.
Gonzalez-Rey E, Varela N, Chorny A, Delgado M.
Curr Pharm Des. 2007;13(11):1113-39. (REVIEW)
PMID 17430175
Lactation elevates vasoactive intestinal peptide messenger ribonucleic acid in rat suprachiasmatic nucleus.
Gozes I, Avidor R, Biegon A, Baldino F Jr.
Endocrinology. 1989 Jan;124(1):181-6.
PMID 2909364
Vasoactive intestinal peptide gene alterations in patients with idiopathic pulmonary arterial hypertension.
Haberl I, Frei K, Ramsebner R, Doberer D, Petkov V, Albinni S, Lang I, Lucas T, Mosgoeller W.
Eur J Hum Genet. 2007 Jan;15(1):18-22. Epub 2006 Sep 27.
PMID 17003842
Pharmacology and functions of receptors for vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide: IUPHAR review 1.
Harmar AJ, Fahrenkrug J, Gozes I, Laburthe M, May V, Pisegna JR, Vaudry D, Vaudry H, Waschek JA, Said SI.
Br J Pharmacol. 2012 May;166(1):4-17. doi: 10.1111/j.1476-5381.2012.01871.x. (REVIEW)
PMID 22289055
Vasoactive intestinal peptide: cardiovascular effects.
Henning RJ, Sawmiller DR.
Cardiovasc Res. 2001 Jan;49(1):27-37. (REVIEW)
PMID 11121793
Promotion of differentiation in human colon carcinoma cells by vasoactive intestinal polypeptide.
Hoosein NM, Black BE, Brattain DE, Brattain MG.
Regul Pept. 1989 Jan;24(1):15-26.
PMID 2544928
Comparison of vasoactive intestinal peptide and secretin in stimulation of pancreatic secretion.
Konturek SJ, Pucher A, Radecki T.
J Physiol. 1976 Feb;255(2):497-509.
PMID 1255530
Clinicopathological study of pancreatic and ganglioneuroblastoma tumours secreting vasoactive intestinal polypeptide (vipomas).
Long RG, Bryant MG, Mitchell SJ, Adrian TE, Polak JM, Bloom SR.
Br Med J (Clin Res Ed). 1981 May 30;282(6278):1767-71.
PMID 6786616
Vasoactive intestinal polypeptide and muscarine mobilize intracellular Ca2+ through breakdown of phosphoinositides to induce catecholamine secretion. Role of IP3 in exocytosis.
Malhotra RK, Wakade TD, Wakade AR.
J Biol Chem. 1988 Feb 15;263(5):2123-6.
PMID 3123488
Estradiol induces vasoactive intestinal peptide and prolactin gene expression in the rat anterior pituitary independently of plasma prolactin levels.
Montagne MN, Dussaillant M, Chew LJ, Berod A, Lamberts SJ, Carter DA, Rostene W.
J Neuroendocrinol. 1995 Mar;7(3):225-31.
PMID 7606249
Neuropeptides as autocrine growth factors in cancer cells.
Moody TW, Chan D, Fahrenkrug J, Jensen RT.
Curr Pharm Des. 2003;9(6):495-509. (REVIEW)
PMID 12570813
Vasoactive intestinal peptide receptors: a molecular target in breast and lung cancer.
Moody TW, Gozes I.
Curr Pharm Des. 2007;13(11):1099-104. (REVIEW)
PMID 17430173
VIP and PACAP: recent insights into their functions/roles in physiology and disease from molecular and genetic studies.
Moody TW, Ito T, Osefo N, Jensen RT.
Curr Opin Endocrinol Diabetes Obes. 2011 Feb;18(1):61-7. doi: 10.1097/MED.0b013e328342568a. (REVIEW)
PMID 21157320
Vasoactive intestinal peptide-camptothecin conjugates inhibit the proliferation of breast cancer cells.
Moody TW, Mantey SA, Fuselier JA, Coy DH, Jensen RT.
Peptides. 2007 Sep;28(9):1883-90. Epub 2007 May 6.
PMID 17580098
A vasoactive intestinal peptide antagonist inhibits non-small cell lung cancer growth.
Moody TW, Zia F, Draoui M, Brenneman DE, Fridkin M, Davidson A, Gozes I.
Proc Natl Acad Sci U S A. 1993 May 15;90(10):4345-9.
PMID 8389448
Selective effects of vasoactive intestinal peptide on the mitogenic response of murine T cells.
Ottaway CA.
Immunology. 1987 Oct;62(2):291-7.
PMID 2960611
VIP-induced neuroprotection of the developing brain.
Passemard S, Sokolowska P, Schwendimann L, Gressens P.
Curr Pharm Des. 2011;17(10):1036-9. (REVIEW)
PMID 21524251
123I-labelled vasoactive intestinal peptide receptor scintigraphy in patients with colorectal cancer.
Raderer M, Kurtaran A, Hejna M, Vorbeck F, Angelberger P, Scheithauer W, Virgolini I.
Br J Cancer. 1998 Jul;78(1):1-5.
PMID 9662242
Neuroendocrine significance of vasoactive intestinal polypeptide.
Reichlin S.
Ann N Y Acad Sci. 1988;527:431-49. (REVIEW)
PMID 2898911
Vasoactive intestinal peptide/pituitary adenylate cyclase-activating peptide receptor subtypes in human tumors and their tissues of origin.
Reubi JC, Laderach U, Waser B, Gebbers JO, Robberecht P, Laissue JA.
Cancer Res. 2000 Jun 1;60(11):3105-12.
PMID 10850463
Asthma and pulmonary arterial hypertension: do they share a key mechanism of pathogenesis?
Said SI, Hamidi SA, Gonzalez Bosc L.
Eur Respir J. 2010 Apr;35(4):730-4. doi: 10.1183/09031936.00097109.
PMID 20356986
Polypeptide with broad biological activity: isolation from small intestine.
Said SI, Mutt V.
Science. 1970 Sep 18;169(3951):1217-8.
PMID 5450698
The multiple mediators of neurogenic smooth muscle relaxation.
Said SI, Rattan S.
Trends Endocrinol Metab. 2004 Jul;15(5):189-91. (REVIEW)
PMID 15223046
Vasoactive intestinal peptide in the peripheral nervous system.
Sundler F, Ekblad E, Grunditz T, Hakanson R, Uddman R.
Ann N Y Acad Sci. 1988;527:143-67. (REVIEW)
PMID 3291690
VIP gene deletion in mice causes cardiomyopathy associated with upregulation of heart failure genes.
Szema AM, Hamidi SA, Smith SD, Benveniste H.
PLoS One. 2013 May 20;8(5):e61449. doi: 10.1371/journal.pone.0061449. Print 2013.
PMID 23700405
Islet cell tumor and a syndrome of refractory watery diarrhea and hypokalemia.
Am J Med. 1958 Sep;25(3):374-80.
PMID 13571250
Vasoactive intestinal peptide (VIP) inhibits human renal cell carcinoma proliferation.
Vacas E, Fernandez-Martinez AB, Bajo AM, Sanchez-Chapado M, Schally AV, Prieto JC, Carmena MJ.
Biochim Biophys Acta. 2012 Oct;1823(10):1676-85. doi: 10.1016/j.bbamcr.2012.06.018. Epub 2012 Jun 21.
PMID 22728770
Vasoactive intestinal peptide (VIP) induces transactivation of EGFR and HER2 in human breast cancer cells.
Valdehita A, Bajo AM, Schally AV, Varga JL, Carmena MJ, Prieto JC.
Mol Cell Endocrinol. 2009 Apr 10;302(1):41-8. doi: 10.1016/j.mce.2008.11.024. Epub 2008 Dec 3.
PMID 19101605
Pituitary adenylate cyclase-activating polypeptide and its receptors: 20 years after the discovery.
Vaudry D, Falluel-Morel A, Bourgault S, Basille M, Burel D, Wurtz O, Fournier A, Chow BK, Hashimoto H, Galas L, Vaudry H.
Pharmacol Rev. 2009 Sep;61(3):283-357. doi: 10.1124/pr.109.001370. (REVIEW)
PMID 19805477
VIP gene variants related to idiopathic pulmonary arterial hypertension in Chinese population.
Zhang Y, Zhang JQ, Liu ZH, Xiong CM, Ni XH, Hui RT, He JG, Pu JL.
Clin Genet. 2009 Jun;75(6):544-9. doi: 10.1111/j.1399-0004.2009.01196.x.
PMID 19508420


This paper should be referenced as such :
Moody, T
VIP (vasoactive intestinal peptide)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(4):239-242.
Free journal version : [ pdf ]   [ DOI ]
On line version :

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  Neuro-Endocrine/Endocrine system: Carcinoid tumors

External links

HGNC (Hugo)VIP   12693
Entrez_Gene (NCBI)VIP  7432  vasoactive intestinal peptide
GeneCards (Weizmann)VIP
Ensembl hg19 (Hinxton)ENSG00000146469 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000146469 [Gene_View]  ENSG00000146469 [Sequence]  chr6:152750797-152759766 [Contig_View]  VIP [Vega]
ICGC DataPortalENSG00000146469
TCGA cBioPortalVIP
Genatlas (Paris)VIP
SOURCE (Princeton)VIP
Genetics Home Reference (NIH)VIP
Genomic and cartography
GoldenPath hg38 (UCSC)VIP  -     chr6:152750797-152759766 +  6q25.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)VIP  -     6q25.2   [Description]    (hg19-Feb_2009)
EnsemblVIP - 6q25.2 [CytoView hg19]  VIP - 6q25.2 [CytoView hg38]
Mapping of homologs : NCBIVIP [Mapview hg19]  VIP [Mapview hg38]
Gene and transcription
Genbank (Entrez)AK291959 AK313950 BC009794 BM971673 DA914915
RefSeq transcript (Entrez)NM_003381 NM_194435
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)VIP
Cluster EST : UnigeneHs.53973 [ NCBI ]
CGAP (NCI)Hs.53973
Alternative Splicing GalleryENSG00000146469
Gene ExpressionVIP [ NCBI-GEO ]   VIP [ EBI - ARRAY_EXPRESS ]   VIP [ SEEK ]   VIP [ MEM ]
Gene Expression Viewer (FireBrowse)VIP [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)7432
GTEX Portal (Tissue expression)VIP
Human Protein AtlasENSG00000146469-VIP [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP01282   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP01282  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP01282
Splice isoforms : SwissVarP01282
Domaine pattern : Prosite (Expaxy)GLUCAGON (PS00260)   
Domains : Interpro (EBI)Glucagon_GIP_secretin_VIP    VIP   
Domain families : Pfam (Sanger)Hormone_2 (PF00123)   
Domain families : Pfam (NCBI)pfam00123   
Domain families : Smart (EMBL)GLUCA (SM00070)  
Conserved Domain (NCBI)VIP
DMDM Disease mutations7432
Blocks (Seattle)VIP
PDB (SRS)2RRH    2RRI   
PDB (PDBSum)2RRH    2RRI   
PDB (IMB)2RRH    2RRI   
Structural Biology KnowledgeBase2RRH    2RRI   
SCOP (Structural Classification of Proteins)2RRH    2RRI   
CATH (Classification of proteins structures)2RRH    2RRI   
Human Protein Atlas [tissue]ENSG00000146469-VIP [tissue]
Peptide AtlasP01282
IPIIPI00000959   IPI00375701   IPI00647127   
Protein Interaction databases
IntAct (EBI)P01282
Ontologies - Pathways
Ontology : AmiGOhormone activity  neuropeptide hormone activity  protein binding  extracellular region  intracellular  G-protein coupled receptor signaling pathway  adenylate cyclase-activating G-protein coupled receptor signaling pathway  body fluid secretion  positive regulation of cell proliferation  regulation of receptor activity  regulation of protein localization  positive regulation of protein catabolic process  mRNA stabilization  prolactin secretion  
Ontology : EGO-EBIhormone activity  neuropeptide hormone activity  protein binding  extracellular region  intracellular  G-protein coupled receptor signaling pathway  adenylate cyclase-activating G-protein coupled receptor signaling pathway  body fluid secretion  positive regulation of cell proliferation  regulation of receptor activity  regulation of protein localization  positive regulation of protein catabolic process  mRNA stabilization  prolactin secretion  
Pathways : BIOCARTANeuropeptides VIP and PACAP inhibit the apoptosis of activated T cells [Genes]   
Pathways : KEGGNeuroactive ligand-receptor interaction   
REACTOMEP01282 [protein]
REACTOME PathwaysR-HSA-418555 [pathway]   
NDEx NetworkVIP
Atlas of Cancer Signalling NetworkVIP
Wikipedia pathwaysVIP
Orthology - Evolution
GeneTree (enSembl)ENSG00000146469
Phylogenetic Trees/Animal Genes : TreeFamVIP
Homologs : HomoloGeneVIP
Homology/Alignments : Family Browser (UCSC)VIP
Gene fusions - Rearrangements
Fusion : QuiverVIP
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerVIP [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)VIP
Exome Variant ServerVIP
ExAC (Exome Aggregation Consortium)ENSG00000146469
GNOMAD BrowserENSG00000146469
Genetic variants : HAPMAP7432
Genomic Variants (DGV)VIP [DGVbeta]
DECIPHERVIP [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisVIP 
ICGC Data PortalVIP 
TCGA Data PortalVIP 
Broad Tumor PortalVIP
OASIS PortalVIP [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICVIP  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDVIP
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch VIP
DgiDB (Drug Gene Interaction Database)VIP
DoCM (Curated mutations)VIP (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)VIP (select a term)
NCG5 (London)VIP
Cancer3DVIP(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry VIP
NextProtP01282 [Medical]
Target ValidationVIP
Huge Navigator VIP [HugePedia]
snp3D : Map Gene to Disease7432
BioCentury BCIQVIP
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD7432
Chemical/Pharm GKB GenePA37312
Clinical trialVIP
canSAR (ICR)VIP (select the gene name)
PubMed139 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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