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PEBP1 (phosphatidylethanolamine binding protein 1)

Written2007-11Sandy Beach, Kam C Yeung
Department of Cancer Biology, Biochemistry, College of Medicine, University of Toledo, Health Science Campus-(formerly Medical University of Ohio), 3035 Arlington Ave., Toledo, OH 43614, USA

(Note : for Links provided by Atlas : click)


Other namesHCNP
LocusID (NCBI) 5037
Atlas_Id 44021
Location 12q24.23  [Link to chromosome band 12q24]
Location_base_pair Starts at 118573689 and ends at 118583393 bp from pter ( according to hg19-Feb_2009)  [Mapping PEBP1.png]
Fusion genes
(updated 2016)
GLS (2q32.2) / PEBP1 (12q24.23)HECTD4 (12q24.13) / PEBP1 (12q24.23)PEBP1 (12q24.23) / AMIGO1 (1p13.3)
PEBP1 (12q24.23) / HS6ST1 (2q14.3)PEBP1 (12q24.23) / PEBP1 (12q24.23)PEBP1 (12q24.23) / STOM (9q33.2)
PTEN (10q23.31) / PEBP1 (12q24.23)


  Diagram of the RKIP gene. Exons are depicted as filled boxes and untranslated regions are unfilled boxes. Introns are represented as lines between exons. Intron, exon, and untranslated region sizes are described in base pairs.
Description The gene is composed of 4 exons spanning a region of 9,520 base pairs.
Transcription The mRNA contains 1507 nucleotides. Alternative splicing has not been described. In prostate cancer cell lines RKIP transcription is repressed by Snail through an E-box in its promoter. Promoter methylation does not seem to cause loss of RKIP expression.
Pseudogene RKIP has two putative pseudogenes located on chromosomes 2 and 14. These are intronless sequences with no verified expression to date.


Note RKIP belongs to a highly conserved family of phospholipid-binding proteins, which have been recognized and studied for several years as PEBP. These proteins are represented in eukaryotes, bacteria, and archae. One of the interesting properties of some PEBP family members is that they are cleaved at the N-terminus to release an undecapeptide which has been named hippocampal cholinergic neurostimulating peptide (HCNP).
  Stereo view of the human RKIP structure prepared with Pymol (Delano, 2002). Pocket residues H86 (left), H118 (right), D70 (top) and Y120 (bottom) are indicated.
Description RKIP is an 187 amino acid protein with a molecular mass of 21-23 kDa. The crystal structures of human, bovine and plant PEBPs are solved revealing no homologies to domains of known functions. The structure of RKIP features a b-fold formed by two anti-parallel b-sheets, a small C-terminal aba element, and a cavity at the surface, which could accommodate a small anion such as a phosphoryl group (see diagram above). Amino acids forming this cavity are conserved among all PEBP family members and constitute the PEB motif.
Expression RKIP and its mammalian homologs are widely expressed in tissues; it has been detected in lung, oviduct and ovary, mammary glands, uterus, prostate epithelium, thyroid, mesenteric lymph node, megakaryocytes of the heart; spleen, liver, and epididymis, testis, spermatids, Leydig cells, steroidogenic cells of the adrenal gland zona fasiculata, small intestine, plasma cells, and neural cells such as brain oliodendricytes, Schwann cells, and Pukinje cells.
Localisation RKIP is localized in the cytoplasm and at the plasma membrane.
Function RKIP inhibits the Raf/MEK/ERK cascade. Identified as a Raf-1 interacting protein in a yeast two-hybrid screen, RKIP was found to inhibit phosphorylation and activation of MEK by Raf-1. RKIP inhibits the phosphorylation of the N-region of Raf-1 by (21-activated kinase) Pak and Src family kinases thereby inhibiting activation of Raf-1. PKC phosphorylation of RKIP following GPCR stimulation causes its release from Raf-1. Classical and atypical PKCs can phosphorylate RKIP at serine 153 causing dissociation of the Raf-1 kinase domain and RKIP, indicating that PKC can mediate ERK activation through RKIP. Once free from Raf-1, RKIP was shown to bind GRK-2 and block its activity, promoting and enhancing G protein signaling and MEK/ERK signaling.
RKIP appears to support macrophage differentiation via inhibition of the NFKB pathway. RKIP inhibits the NF-kappaB pathway through interaction with NIK, TAK1, and IKK. RKIP was a novel effector of apoptosis signaling; this may occur by modulation of the NF-kappaB pathway and/or the regulation of the spindle checkpoint via Aurora B kinase and the spindle checkpoint by RKIP. RKIP regulation of Aurora kinase B and the spindle checkpoint through Raf-1/MEK/ERK signaling influences cell cycle fidelity.
RKIP has serine protease activity. Purified RKIP was found to inhibit the serine proteases thrombin, chymotrypsin, and neuropsin.
HCNP, the N-terminal fragment of RKIP, may play a role in phospholipid organization of the myelin sheath and septal cholinergic development of the hippocampus. HCNP can act on frog cardiac mechanical performance, exerting a negative inotropism. Results of these experiments suggest that RKIP/HCNP may be a new endocrine factor that regulates cardiac physiology. RKIP downregulation may be associated with the congenital heart disease manifested in Down syndrome. RKIP downregulation was found in the rat right ventricle and in the interventricular septum upon cardiac remodeling.
RKIP has been found in the male reproductive tract with implications in the organization of sperm membranes during spermiogenesis. It has been identified as a decapacitation factor in mouse spermatozoa. RKIP and other proteins inhibited progesterone-induced acrosome reaction and zona pellucida binding of sperm.
Homology No significant sequence homology to other proteins. Humans have two known family members, RKIP and PEBP4. RKIP has high sequence identity to mouse, rat, bovine, and monkey phosphatidylethanolamine binding proteins.

Implicated in

Entity Breast cancer
Oncogenesis Immunohistochemical examination of breast cancer lymph node metastases showed significant loss of RKIP protein expression compared to normal breast duct epithelia and primary tumors. There was a weak negative correlation between RKIP expression and apoptosis in breast tumors that did not have associated lymph node metastases.
Low levels of RKIP may allow cancer cells to evade apoptosis. Breast cancer cell lines expressing low levels of RKIP undergo apoptosis following ectopic RKIP addition or Taxol treatment, which induced RKIP expression.
Entity Prostate cancer
Prognosis Decreased protein expression of RKIP may be a prognostic marker in prostate cancer, with low RKIP levels indicating early PSA failure.
Oncogenesis Low levels of RKIP may protect cancer cells against apoptosis. Tumorgenic prostate cancer cell lines expressing low levels of RKIP increase their RKIP expression following treatment with a chemotherapeutic drug, sensitizing the cells to apoptosis. Cell lines with higher RKIP expression can be made resistant to apoptosis when RKIP is knocked down.
RKIP is downregulated in prostate cancer progression and metastasis. Modulation of RKIP expression in prostate cancer cell lines changes invasive ability in vitro as well as development of metastases in vivo, with loss of RKIP corresponding to increased invasiveness and metastatic spread. MEK/ERK activation was associated with low or decreased RKIP expression in vitro, and vice-versa.
RKIP mRNA can activate interferon-inducible 2',5'-oligoadenylate synthetases (OAS), leading to RNase L activation. RNase L deficiency in prostate cancer cell lines (PC3, Du145, LNCap) is associated with resistance to apoptosis through OAS activation.
Entity Melanoma
Note RKIP mRNA and protein expression is reduced in melanoma cell lines versus normal melanocytes. AP-1 activation and ERK1/ERK2 phosphorylation decreased in Mel Im cells stably transfected with RKIP compared to control transfected cells. Immunohistochemical analyses showed reduced RKIP in primary melanoma versus normal normal skin, and further reduction in melanoma metastases. RKIP may act by inhibiting B-Raf kinase activity, as demonstrated in melanoma cell lines in vitro.
Entity Hepatocellular carcinoma
Note Hepatocellular carcinoma cell lines and HCC liver tissue showed decreased RKIP expression as compared to primary human hepatocytes or adjacent peritumoral tissues. Low RKIP expression was correlated with increased ERK activation and modulation of RKIP expression antagonized MAPK signaling in vitro.
Entity Colorectal cancer
Note Loss of RKIP, as studied in tissue microarrays of MMR-proficient and deficient colorectal cancer samples, was a marker of tumor progression and metastasis. Diminished RKIP expression was significantly positively associated with worse survival.
Entity Insulinoma / Islet neoplasia
Note Insulinomas showed decreased or absent RKIP expression as compared to normal nearby islets. ß-cell line HIT-TI5 proliferation, but not apoptotis, was inhibited by RKIP.


Snail is a repressor of RKIP transcription in metastatic prostate cancer cells.
Beach S, Tang H, Park S, Dhillon AS, Keller ET, Kolch W, Yeung KC
Oncogene. 2008 ; 27 (15) : 2243-2248.
PMID 17952120
RKIP sensitizes prostate and breast cancer cells to drug-induced apoptosis.
Chatterjee D, Bai Y, Wang Z, Beach S, Mott S, Roy R, Braastad C, Sun Y, Mukhopadhyay A, Aggarwal BB, Darnowski J, Pantazis P, Wyche J, Fu Z, Kitagwa Y, Keller ET, Sedivy JM, Yeung KC
The Journal of biological chemistry. 2004 ; 279 (17) : 17515-17523.
PMID 14766752
Identification and characterization of PEBP as a calpain substrate.
Chen Q, Wang S, Thompson SN, Hall ED, Guttmann RP
Journal of neurochemistry. 2006 ; 99 (4) : 1133-1141.
PMID 17018026
Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein.
Corbit KC, Trakul N, Eves EM, Diaz B, Marshall M, Rosner MR
The Journal of biological chemistry. 2003 ; 278 (15) : 13061-13068.
PMID 12551925
Raf kinase inhibitory protein regulates aurora B kinase and the spindle checkpoint.
Eves EM, Shapiro P, Naik K, Klein UR, Trakul N, Rosner MR
Molecular cell. 2006 ; 23 (4) : 561-574.
PMID 16916643
Metastasis suppressor gene Raf kinase inhibitor protein (RKIP) is a novel prognostic marker in prostate cancer.
Fu Z, Kitagawa Y, Shen R, Shah R, Mehra R, Rhodes D, Keller PJ, Mizokami A, Dunn R, Chinnaiyan AM, Yao Z, Keller ET
The Prostate. 2006 ; 66 (3) : 248-256.
PMID 16175585
Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis.
Fu Z, Smith PC, Zhang L, Rubin MA, Dunn RL, Yao Z, Keller ET
Journal of the National Cancer Institute. 2003 ; 95 (12) : 878-889.
PMID 12813171
Reduction of Raf-1 kinase inhibitor protein expression correlates with breast cancer metastasis.
Hagan S, Al-Mulla F, Mallon E, Oien K, Ferrier R, Gusterson B, García JJ, Kolch W
Clinical cancer research : an official journal of the American Association for Cancer Research. 2005 ; 11 (20) : 7392-7397.
PMID 16243812
The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors.
Hengst U, Albrecht H, Hess D, Monard D
The Journal of biological chemistry. 2001 ; 276 (1) : 535-540.
PMID 11034991
Cross-regulation of VPAC(2) receptor desensitization by M(3) receptors via PKC-mediated phosphorylation of RKIP and inhibition of GRK2.
Huang J, Mahavadi S, Sriwai W, Grider JR, Murthy KS
American journal of physiology. Gastrointestinal and liver physiology. 2007 ; 292 (3) : G867-G874.
PMID 17170028
Inhibition of the Raf-MEK1/2-ERK1/2 signaling pathway, Bcl-xL down-regulation, and chemosensitization of non-Hodgkin's lymphoma B cells by Rituximab.
Jazirehi AR, Vega MI, Chatterjee D, Goodglick L, Bonavida B
Cancer research. 2004 ; 64 (19) : 7117-7126.
PMID 15466208
The biology of a prostate cancer metastasis suppressor protein: Raf kinase inhibitor protein.
Keller ET, Fu Z, Brennan M
Journal of cellular biochemistry. 2005 ; 94 (2) : 273-278.
PMID 15565643
Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions.
Kolch W
The Biochemical journal. 2000 ; 351 Pt 2 : 289-305.
PMID 11023813
Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling.
Kroslak T, Koch T, Kahl E, Höllt V
The Journal of biological chemistry. 2001 ; 276 (43) : 39772-39778.
PMID 11514577
Loss of Raf kinase inhibitor protein promotes cell proliferation and migration of human hepatoma cells.
Lee HC, Tian B, Sedivy JM, Wands JR, Kim M
Gastroenterology. 2006 ; 131 (4) : 1208-1217.
PMID 17030190
Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2.
Lorenz K, Lohse MJ, Quitterer U
Nature. 2003 ; 426 (6966) : 574-579.
PMID 14654844
Loss of raf-1 kinase inhibitor protein expression is associated with tumor progression and metastasis in colorectal cancer.
Minoo P, Zlobec I, Baker K, Tornillo L, Terracciano L, Jass JR, Lugli A
American journal of clinical pathology. 2007 ; 127 (5) : 820-827.
PMID 17439843
Selection and cloning of poly(rC)-binding protein 2 and Raf kinase inhibitor protein RNA activators of 2',5'-oligoadenylate synthetase from prostate cancer cells.
Molinaro RJ, Jha BK, Malathi K, Varambally S, Chinnaiyan AM, Silverman RH
Nucleic acids research. 2006 ; 34 (22) : 6684-6695.
PMID 17145707
Sequence analysis and immunolocalisation of phosphatidylethanolamine binding protein (PBP) in human brain tissue.
Moore C, Perry AC, Love S, Hall L
Brain research. Molecular brain research. 1996 ; 37 (1-2) : 74-78.
PMID 8738137
Raf-1 kinase inhibitor protein: structure, function, regulation of cell signaling, and pivotal role in apoptosis.
Odabaei G, Chatterjee D, Jazirehi AR, Goodglick L, Yeung K, Bonavida B
Advances in cancer research. 2004 ; 91 : 169-200.
PMID 15327891
Regulation of RKIP binding to the N-region of the Raf-1 kinase.
Park S, Rath O, Beach S, Xiang X, Kelly SM, Luo Z, Kolch W, Yeung KC
FEBS letters. 2006 ; 580 (27) : 6405-6412.
PMID 17097642
RKIP downregulates B-Raf kinase activity in melanoma cancer cells.
Park S, Yeung ML, Beach S, Shields JM, Yeung KC
Oncogene. 2005 ; 24 (21) : 3535-3540.
PMID 15782137
MAP kinase meets mitosis: a role for Raf Kinase Inhibitory Protein in spindle checkpoint regulation.
Rosner MR
Cell division. 2007 ; 2 : page 1.
PMID 17214889
Reduction in Raf kinase inhibitor protein expression is associated with increased Ras-extracellular signal-regulated kinase signaling in melanoma cell lines.
Schuierer MM, Bataille F, Hagan S, Kolch W, Bosserhoff AK
Cancer research. 2004 ; 64 (15) : 5186-5192.
PMID 15289323
Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues.
Seddiqi N, Bollengier F, Alliel PM, Périn JP, Bonnet F, Bucquoy S, Jollès P, Schoentgen F
Journal of molecular evolution. 1994 ; 39 (6) : 655-660.
PMID 7807553
The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family.
Simister PC, Banfield MJ, Brady RL
Acta crystallographica. Section D, Biological crystallography. 2002 ; 58 (Pt 6 Pt 2) : 1077-1080.
PMID 12037323
Raf kinase inhibitory protein knockout mice: expression in the brain and olfaction deficit.
Theroux S, Pereira M, Casten KS, Burwell RD, Yeung KC, Sedivy JM, Klysik J
Brain research bulletin. 2007 ; 71 (6) : 559-567.
PMID 17292798
Raf kinase inhibitory protein regulates Raf-1 but not B-Raf kinase activation.
Trakul N, Menard RE, Schade GR, Qian Z, Rosner MR
The Journal of biological chemistry. 2005 ; 280 (26) : 24931-24940.
PMID 15886202
Differentiation induction of human keratinocytes by phosphatidylethanolamine-binding protein.
Yamazaki T, Nakano H, Hayakari M, Tanaka M, Mayama J, Tsuchida S
The Journal of biological chemistry. 2004 ; 279 (31) : 32191-32195.
PMID 15155742
Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein.
Yeung K, Janosch P, McFerran B, Rose DW, Mischak H, Sedivy JM, Kolch W
Molecular and cellular biology. 2000 ; 20 (9) : 3079-3085.
PMID 10757792
Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP.
Yeung K, Seitz T, Li S, Janosch P, McFerran B, Kaiser C, Fee F, Katsanakis KD, Rose DW, Mischak H, Sedivy JM, Kolch W
Nature. 1999 ; 401 (6749) : 173-177.
PMID 10490027
Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation.
Yeung KC, Rose DW, Dhillon AS, Yaros D, Gustafsson M, Chatterjee D, McFerran B, Wyche J, Kolch W, Sedivy JM
Molecular and cellular biology. 2001 ; 21 (21) : 7207-7217.
PMID 11585904
Raf kinase inhibitory protein inhibits beta-cell proliferation.
Zhang L, Fu Z, Binkley C, Giordano T, Burant CF, Logsdon CD, Simeone DM
Surgery. 2004 ; 136 (3) : 708-715.
PMID 15349122


This paper should be referenced as such :
Beach, S ; Yeung, KC
PEBP1 (phosphatidylethanolamine binding protein 1)
Atlas Genet Cytogenet Oncol Haematol. 2008;12(4):282-285.
Free journal version : [ pdf ]   [ DOI ]
On line version :

External links

HGNC (Hugo)PEBP1   8630
Entrez_Gene (NCBI)PEBP1  5037  phosphatidylethanolamine binding protein 1
AliasesHCNP; HCNPpp; HEL-210; HEL-S-34; 
GeneCards (Weizmann)PEBP1
Ensembl hg19 (Hinxton)ENSG00000089220 [Gene_View]  chr12:118573689-118583393 [Contig_View]  PEBP1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000089220 [Gene_View]  chr12:118573689-118583393 [Contig_View]  PEBP1 [Vega]
ICGC DataPortalENSG00000089220
TCGA cBioPortalPEBP1
Genatlas (Paris)PEBP1
SOURCE (Princeton)PEBP1
Genetics Home Reference (NIH)PEBP1
Genomic and cartography
GoldenPath hg19 (UCSC)PEBP1  -     chr12:118573689-118583393 +  12q24   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)PEBP1  -     12q24   [Description]    (hg38-Dec_2013)
EnsemblPEBP1 - 12q24 [CytoView hg19]  PEBP1 - 12q24 [CytoView hg38]
Mapping of homologs : NCBIPEBP1 [Mapview hg19]  PEBP1 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AI052513 AK226006 AK299414 AK308056 AK311927
RefSeq transcript (Entrez)NM_002567
RefSeq genomic (Entrez)NC_000012 NC_018923 NT_029419 NW_004929385
Consensus coding sequences : CCDS (NCBI)PEBP1
Cluster EST : UnigeneHs.433863 [ NCBI ]
CGAP (NCI)Hs.433863
Alternative Splicing GalleryENSG00000089220
Gene ExpressionPEBP1 [ NCBI-GEO ]   PEBP1 [ EBI - ARRAY_EXPRESS ]   PEBP1 [ SEEK ]   PEBP1 [ MEM ]
Gene Expression Viewer (FireBrowse)PEBP1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5037
GTEX Portal (Tissue expression)PEBP1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP30086 (Uniprot)
NextProtP30086  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP30086
Splice isoforms : SwissVarP30086 (Swissvar)
Domaine pattern : Prosite (Expaxy)PBP (PS01220)   
Domains : Interpro (EBI)Phosphotidylethanolamine-bd_CS    PtdEtn-bd_prot_PEBP   
Domain families : Pfam (Sanger)PBP (PF01161)   
Domain families : Pfam (NCBI)pfam01161   
DMDM Disease mutations5037
Blocks (Seattle)PEBP1
PDB (SRS)1BD9    1BEH    2L7W    2QYQ   
PDB (PDBSum)1BD9    1BEH    2L7W    2QYQ   
PDB (IMB)1BD9    1BEH    2L7W    2QYQ   
PDB (RSDB)1BD9    1BEH    2L7W    2QYQ   
Structural Biology KnowledgeBase1BD9    1BEH    2L7W    2QYQ   
SCOP (Structural Classification of Proteins)1BD9    1BEH    2L7W    2QYQ   
CATH (Classification of proteins structures)1BD9    1BEH    2L7W    2QYQ   
Human Protein AtlasENSG00000089220
Peptide AtlasP30086
IPIIPI00219446   IPI00908746   IPI00023179   
Protein Interaction databases
IntAct (EBI)P30086
Ontologies - Pathways
Ontology : AmiGOMAPK cascade  serine-type endopeptidase inhibitor activity  protein binding  ATP binding  nucleus  cytosol  phosphatidylethanolamine binding  negative regulation of endopeptidase activity  enzyme binding  protein kinase binding  poly(A) RNA binding  extracellular exosome  
Ontology : EGO-EBIMAPK cascade  serine-type endopeptidase inhibitor activity  protein binding  ATP binding  nucleus  cytosol  phosphatidylethanolamine binding  negative regulation of endopeptidase activity  enzyme binding  protein kinase binding  poly(A) RNA binding  extracellular exosome  
REACTOMEP30086 [protein]
REACTOME PathwaysR-HSA-5674135 MAP2K and MAPK activation [pathway]
REACTOME PathwaysR-HSA-5675221 Negative regulation of MAPK pathway [pathway]
NDEx NetworkPEBP1
Atlas of Cancer Signalling NetworkPEBP1
Wikipedia pathwaysPEBP1
Orthology - Evolution
GeneTree (enSembl)ENSG00000089220
Phylogenetic Trees/Animal Genes : TreeFamPEBP1
Homologs : HomoloGenePEBP1
Homology/Alignments : Family Browser (UCSC)PEBP1
Gene fusions - Rearrangements
Fusion : MitelmanHECTD4/PEBP1 [12q24.13/12q24.23]  [t(12;12)(q24;q24)]  
Fusion: TCGAC12orf51 PEBP1 12q24.23 LUSC
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPEBP1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PEBP1
Exome Variant ServerPEBP1
ExAC (Exome Aggregation Consortium)PEBP1 (select the gene name)
Genetic variants : HAPMAP5037
Genomic Variants (DGV)PEBP1 [DGVbeta]
DECIPHER (Syndromes)12:118573689-118583393  ENSG00000089220
CONAN: Copy Number AnalysisPEBP1 
ICGC Data PortalPEBP1 
TCGA Data PortalPEBP1 
Broad Tumor PortalPEBP1
OASIS PortalPEBP1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPEBP1 
Mutations and Diseases : HGMDPEBP1
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 PEBP1
DgiDB (Drug Gene Interaction Database)PEBP1
DoCM (Curated mutations)PEBP1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PEBP1 (select a term)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PEBP1
NextProtP30086 [Medical]
Huge Navigator PEBP1 [HugePedia]
snp3D : Map Gene to Disease5037
BioCentury BCIQPEBP1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5037
Chemical/Pharm GKB GenePA32968
Clinical trialPEBP1
canSAR (ICR)PEBP1 (select the gene name)
PubMed189 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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