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PRND (Prion Protein 2 (Dublet))

Written2013-12Gabriele Giachin, Giuseppe Legname
Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), via Bonomea 265, Trieste, Italy

(Note : for Links provided by Atlas : click)


Alias_namesprion protein 2 (dublet)
Alias_symbol (synonym)DPL
Other alias
LocusID (NCBI) 23627
Atlas_Id 44172
Location 20p13  [Link to chromosome band 20p13]
Location_base_pair Starts at 4721854 and ends at 4728462 bp from pter ( according to hg19-Feb_2009)  [Mapping PRND.png]
Local_order PRND lies 27 kb downstream the human prion protein gene (PRNP). PRNP starts at 4702556 and ends at 4709106 bps.
  Schematic structural representation of the human PRN locus on chromosome 20p13 containing PRNP, PRND and the putative testis-specific prion protein (PRNT) genes.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
LINC00914 (-) / PRND (20p13)
Note PRND and PRNP genes form the prion gene complex and are regulated by their own promoter. Doppel is an acronym derived from downstream prion protein-like gene (Moore et al., 2001). PRNP and PRND are believed to arise through duplication of a single ancestral gene (Mastrangelo and Westaway, 2001).


Note The Prnd gene was originally identified in mice during DNA sequencing of the cosmid clone isolated from the I/LnJ inbred mice strain (Lee et al., 1998). This gene was discovered in transgenic (Tg) mice where the Prnp gene was ablated (Prnp0/0 mice strains) resulting in a diseased phenotype characterized by loss of Purkinje cells in the cerebellum. Interestingly, Prnp deletion in these mouse lines resulted in the formation of a chimeric Prnd transcript under the control of the strong Prnp promoter. Thus, these studies have shown that only the ectopic expression of Dpl, rather than the absence of the Prnp gene, caused neurodegeneration (Li et al., 2000).
  Schematic representation of the PRND gene. Exon 1 starts at 4705556 bp and ends at 4702615 bp. Exon 2 containing the Doppel open reading frame (ORF) starts at 4705187 bp and ends at 4709106 bp. The sequence surrounding the splice acceptor site is shown with intronic nucleotides in lower case, exonic nucleotides in capital letters and Met start codon ATG underlined.
Description The PRND gene includes two exons separated by one intron. Exon 2 encodes for the Doppel protein.
Transcription Prnd RNA transcription has been reported in different tissues of adult wild-type (WT) mice including testis, heart, spleen and skeletal muscle (Li et al., 2000). In neonatal mice up to 3 weeks, Prnd RNA has been detected in brain blood vessel endothelial cells (Li et al., 2000).
Pseudogene Prnd pseudogenes have been identified in non-mammalian organisms as Anolis (lizard) and Xenopus (frog) (Harrison et al., 2010).


Note Doppel tertiary structure has a fold similar to that of the cellular prion protein, PrPC (encoded by PRNP or Prnp genes) although it shares approximately 25% of aminoacidic sequence identity with PrPC.
  A) Primary sequence alignment between human PrPC (GenBank: BAG32277.1) and human Doppel (NCBI Reference Sequence: NP_036541.2). B) Secondary structure motives of human PrPC and Doppel. Highlighted: signal peptides, N-linked glycosylation sites (CHO), disulfide bridges (S-S) and Glycosylphosphatidylinisotol (GPI) anchor. C) Tertiary NMR structures of Doppel (pdb id 1LG4) and PrPC (2LSB).
Description The immature form of human Doppel includes 176 residues with two N- and C-terminal signal peptides cleaved during protein maturation. The mature sequence includes 126 amino acids spanning from residues 27 to 152, with a molecular weight of approximately 14.5 kDa. Tryptic digestion and mass spectroscopy studies have identified two distinct disulfide bridges (Cys109-Cys143 and Cys95-Cys148) which strongly stabilize the Doppel folding (Baillod et al., 2013; Silverman et al., 2000; Whyte et al., 2003). PNGase F digestion and immunoblots have reported two N-linked glycosylation sites at codons 99 and 111. The GPI anchor targets the protein at the extracellular membrane. NMR structures of recombinant human and mouse Dopple have been solved (Luhrs et al., 2003; Mo et al., 2001). The NMR structures of the N-terminal murine and ovine signal peptides (residues 1-30) have also been determined (Papadopoulos et al., 2006). The human Doppel NMR structure features a short flexible N-terminal segment comprising residues 24-51 and a globular domain including four α-helices (α1: residues 72-80; α2a: residues 101-115; α2b: residues 117-121; α3: residues 127-141) and a short two-stranded anti-parallel β-sheet (β1: residues 58-60; β2: residues 88-90) (Luhrs et al., 2003).
Expression Under physiological conditions Doppel is mostly expressed in testis and, in particular, in spermatozoa and Sertoli cells (Behrens et al., 2002; Peoc'h et al., 2002). Additionally, Doppel is expressed with PrPC in spleen cells, notably B lymphocytes, granulocytes and dendritic cells (Cordier-Dirikoc et al., 2008).
Localisation Doppel is attached to the cell membrane through its GPI anchor (Silverman et al., 2000). A study has shown Doppel localization in detergent-resistant membranes or lipid rafts (Caputo et al., 2010).
Function The Doppel expression in spermatozoa and Sertoli cells infers a role in spermatogenesis. Male Tg mice knock-out for Prnd were sterile, clearly indicating that Doppel plays a role in male reproduction as critical regulator of spermatogenesis and sperm-egg interaction (Behrens et al., 2002). Doppel may enhance in vitro ovine spermatozoa fertilizing ability (Pimenta et al., 2012). Doppel has been implicated in early testis differentiation (Kocer et al., 2007). The detection of Prnd mRNA in brain blood vessel endothelial cells might indicate a possible role in the development of brain blood vessels (Li et al., 2000). The observation that Doppel is expressed with PrPC in B lymphocytes, granulocytes and dendritic cells argues for a role in cell-cell interaction in the immunosystem (Cordier-Dirikoc et al., 2008). Several evidence showed that Doppel is able to coordinate in vitro the binding of copper ions with high affinity (Cereghetti et al., 2004; La Mendola et al., 2010; Qin et al., 2003).


Note Different polymorphic variants have been identified in PRND. The effect of polymorphisms in Doppel function and their implication in the diseases have not been fully clarified.
Germinal S6I, S22P, T26P, H31R, P56L, F70L, L149S, T174M (Clark et al., 2003; Moore et al., 1999; Peoc'h et al., 2000; Schroder et al., 2001).

Implicated in

Entity Ectopic Doppel expression associated with Purkinje cell neurodegeneration in transgenic mouse models.
Note Beside its role in male reproductive system, Doppel has attracted interest for its neurotoxic properties when ectopically expressed in the brain of Tg mice knock-out for the prion protein gene (Prnp0/0 mice). In these mice, denoted as Ngsk PrP-/-, the Doppel-encoding exon was expressed as chimeric mRNA due to the intergenic splicing taking place between Prnp and Prnd. As a result, Prnd became abnormally regulated under the control of Prnp promoter and ectopically expressed in the brain and, in particular, in neurons and glial cells (Li et al., 2000). Similar non-physiological Doppel expression was reported in other Tg mouse lines knock-out for Prnp such as Rcm0 and Zrch mice (Moore et al., 2001; Rossi et al., 2001). Doppel expression in the brain is neurotoxic and causes Purkinje cell degeneration in these mouse models. Doppel neurotoxicity is antagonized by the PrPC N-terminal domain (Atarashi et al., 2003; Yamaguchi et al., 2004). The neuroprotective PrPC role against ectopic Doppel expression has been reported also in human neuronal SH-SY5Y cells (Li et al., 2009) confirming the dominant-negative effects of the PrPC N-terminal region (Yoshikawa et al., 2008). The molecular mechanisms leading to Doppel-induced neurodegeneration in Purkinje and granular cells are still controversial. An earlier study has reported that the chimeric form of Doppel fused to a Fc domain binds specifically granule cells and causes neurodegeneration, raising the possibility that these specific cells expressed a still unidentified protein that mediates the Doppel-induced neurotoxicity (Legname et al., 2002). Oxidative stress may play a role in Doppel-induced neuronal death since NOS activity is induced by Doppel in vitro and in vivo (Cui et al., 2003; Wong et al., 2001). Two independent groups have reported that BAX contributes to Doppel-induced apoptosis (Didonna et al., 2012; Heitz et al., 2007) and that BCL-2 antagonizes Doppel neurotoxicity (Heitz et al., 2008). Another work has observed that ectopic Doppel expression in the brain elicits neurodegeneration through the binding of two metalloproteinase namely the alpha-1-inhibitor-3 (α1I3) and the alpha-2-macroglobin (α2M) (Benvegnu et al., 2009).
Entity Abnormal Doppel expression levels in human astrocytomas and other non-glial brain tumor specimens
Note Doppel is aberrantly expressed in astrocytic tumors where it displays cytoplasmic, nuclear and lysosomal localization and molecular properties (i.e. altered glycosilation pattern) different from Doppel as normally expressed in testis (Azzalin et al., 2006; Azzalin et al., 2008; Comincini et al., 2006; Comincini et al., 2004; Comincini et al., 2007; Rognoni et al., 2010; Sbalchiero et al., 2008).


Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration.
Atarashi R1, Nishida N, Shigematsu K, Goto S, Kondo T, Sakaguchi S, Katamine S.
J Biol Chem. 2003 Aug 1;278(31):28944-9. Epub 2003 May 19.
PMID 12759361
The prion-like protein Doppel (Dpl) interacts with the human receptor for activated C-kinase 1 (RACK1) protein.
Azzalin A, Del Vecchio I, Ferretti L, Comincini S.
Anticancer Res. 2006 Nov-Dec;26(6B):4539-47.
PMID 17201176
The doppel (Dpl) protein influences in vitro migration capability in astrocytoma-derived cells.
Azzalin A, Sbalchiero E, Barbieri G, Palumbo S, Muzzini C, Comincini S.
Cell Oncol. 2008;30(6):491-501.
PMID 18936526
Prion versus doppel protein misfolding: new insights from replica-exchange molecular dynamics simulations.
Baillod P, Garrec J, Tavernelli I, Rothlisberger U.
Biochemistry. 2013 Nov 26;52(47):8518-26. doi: 10.1021/bi400884e. Epub 2013 Nov 13.
PMID 24143866
Absence of the prion protein homologue Doppel causes male sterility.
Behrens A, Genoud N, Naumann H, Rulicke T, Janett F, Heppner FL, Ledermann B, Aguzzi A.
EMBO J. 2002 Jul 15;21(14):3652-8.
PMID 12110578
Prion protein paralog doppel protein interacts with alpha-2-macroglobulin: a plausible mechanism for doppel-mediated neurodegeneration.
Benvegnu S, Franciotta D, Sussman J, Bachi A, Zardini E, Torreri P, Govaerts C, Pizzo S, Legname G.
PLoS One. 2009 Jun 18;4(6):e5968. doi: 10.1371/journal.pone.0005968.
PMID 19536284
Doppel and PrPC co-immunoprecipitate in detergent-resistant membrane domains of epithelial FRT cells.
Caputo A, Sarnataro D, Campana V, Costanzo M, Negro A, Sorgato MC, Zurzolo C.
Biochem J. 2009 Dec 23;425(2):341-51. doi: 10.1042/BJ20091050.
PMID 19888917
Copper(II) binding to the human Doppel protein may mark its functional diversity from the prion protein.
Cereghetti GM, Negro A, Vinck E, Massimino ML, Sorgato MC, Van Doorslaer S.
J Biol Chem. 2004 Aug 27;279(35):36497-503. Epub 2004 Jun 24.
PMID 15218028
The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.
Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A.
Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15.
PMID 12975309
Diagnostic value of PRND gene expression profiles in astrocytomas: relationship to tumor grades of malignancy.
Comincini S, Ferrara V, Arias A, Malovini A, Azzalin A, Ferretti L, Benericetti E, Cardarelli M, Gerosa M, Passarin MG, Turazzi S, Bellazzi R.
Oncol Rep. 2007 May;17(5):989-96.
PMID 17390034
Expression profiles of prion and doppel proteins and of their receptors in mouse splenocytes.
Cordier-Dirikoc S, Zsurger N, Cazareth J, Menard B, Chabry J.
Eur J Immunol. 2008 Aug;38(8):2131-41. doi: 10.1002/eji.200738099.
PMID 18604867
Analysis of doppel protein toxicity.
Cui T, Holme A, Sassoon J, Brown DR.
Mol Cell Neurosci. 2003 May;23(1):144-55.
PMID 12799144
The role of Bax and caspase-3 in doppel-induced apoptosis of cerebellar granule cells.
Didonna A, Sussman J, Benetti F, Legname G.
Prion. 2012 Jul 1;6(3):309-16. doi: 10.4161/pri.20026. Epub 2012 Jul 1.
PMID 22561161
Genomic assessment of the evolution of the prion protein gene family in vertebrates.
Harrison PM, Khachane A, Kumar M.
Genomics. 2010 May;95(5):268-77. doi: 10.1016/j.ygeno.2010.02.008. Epub 2010 Mar 3.
PMID 20206252
BCL-2 counteracts Doppel-induced apoptosis of prion-protein-deficient Purkinje cells in the Ngsk Prnp(0/0) mouse.
Heitz S, Gautheron V, Lutz Y, Rodeau JL, Zanjani HS, Sugihara I, Bombarde G, Richard F, Fuchs JP, Vogel MW, Mariani J, Bailly Y.
Dev Neurobiol. 2008 Feb 15;68(3):332-48.
PMID 18085563
BAX contributes to Doppel-induced apoptosis of prion-protein-deficient Purkinje cells.
Heitz S, Lutz Y, Rodeau JL, Zanjani H, Gautheron V, Bombarde G, Richard F, Fuchs JP, Vogel MW, Mariani J, Bailly Y.
Dev Neurobiol. 2007 Apr;67(5):670-86.
PMID 17443816
Goat PRND expression pattern suggests its involvement in early sex differentiation.
Kocer A, Gallozzi M, Renault L, Tilly G, Pinheiro I, Le Provost F, Pailhoux E, Vilotte JL.
Dev Dyn. 2007 Mar;236(3):836-42.
PMID 17226816
A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein.
La Mendola D1, Magri A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E.
Chemistry. 2010 Jun 1;16(21):6212-23. doi: 10.1002/chem.200902405.
PMID 20411530
Complete genomic sequence and analysis of the prion protein gene region from three mammalian species.
Lee IY, Westaway D, Smit AF, Wang K, Seto J, Chen L, Acharya C, Ankener M, Baskin D, Cooper C, Yao H, Prusiner SB, Hood LE.
Genome Res. 1998 Oct;8(10):1022-37.
PMID 9799790
Prion and doppel proteins bind to granule cells of the cerebellum.
Legname G, Nelken P, Guan Z, Kanyo ZF, DeArmond SJ, Prusiner SB.
Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16285-90. Epub 2002 Nov 21.
PMID 12446843
Identification of a novel gene encoding a PrP-like protein expressed as chimeric transcripts fused to PrP exon 1/2 in ataxic mouse line with a disrupted PrP gene.
Li A, Sakaguchi S, Atarashi R, Roy BC, Nakaoke R, Arima K, Okimura N, Kopacek J, Shigematsu K.
Cell Mol Neurobiol. 2000 Oct;20(5):553-67.
PMID 10930132
Doppel-induced cytotoxicity in human neuronal SH-SY5Y cells is antagonized by the prion protein.
Li P, Dong C, Lei Y, Shan B, Xiao X, Jiang H, Wang X, Gao C, Shi Q, Xu K, Tian C, Han J, Dong X.
Acta Biochim Biophys Sin (Shanghai). 2009 Jan;41(1):42-53.
PMID 19129949
NMR structure of the human doppel protein.
Luhrs T1, Riek R, Guntert P, Wuthrich K.
J Mol Biol. 2003 Mar 7;326(5):1549-57.
PMID 12595265
The prion gene complex encoding PrP(C) and Doppel: insights from mutational analysis.
Mastrangelo P, Westaway D.
Gene. 2001 Sep 5;275(1):1-18. (REVIEW)
PMID 11574147
Two different neurodegenerative diseases caused by proteins with similar structures.
Mo H, Moore RC, Cohen FE, Westaway D, Prusiner SB, Wright PE, Dyson HJ.
Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2352-7.
PMID 11226243
Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel.
Moore RC, Lee IY, Silverman GL, Harrison PM, Strome R, Heinrich C, Karunaratne A, Pasternak SH, Chishti MA, Liang Y, Mastrangelo P, Wang K, Smit AF, Katamine S, Carlson GA, Cohen FE, Prusiner SB, Melton DW, Tremblay P, Hood LE, Westaway D.
J Mol Biol. 1999 Oct 1;292(4):797-817.
PMID 10525406
Doppel-induced cerebellar degeneration in transgenic mice.
Moore RC, Mastrangelo P, Bouzamondo E, Heinrich C, Legname G, Prusiner SB, Hood L, Westaway D, DeArmond SJ, Tremblay P.
Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15288-93. Epub 2001 Dec 4.
PMID 11734625
NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles.
Papadopoulos E, Oglecka K, Maler L, Jarvet J, Wright PE, Dyson HJ, Graslund A.
Biochemistry. 2006 Jan 10;45(1):159-66.
PMID 16388591
First report of polymorphisms in the prion-like protein gene (PRND): implications for human prion diseases.
Peoc'h K, Guerin C, Brandel JP, Launay JM, Laplanche JL.
Neurosci Lett. 2000 Jun 2;286(2):144-8.
PMID 10825657
The human "prion-like" protein Doppel is expressed in both Sertoli cells and spermatozoa.
Peoc'h K, Serres C, Frobert Y, Martin C, Lehmann S, Chasseigneaux S, Sazdovitch V, Grassi J, Jouannet P, Launay JM, Laplanche JL.
J Biol Chem. 2002 Nov 8;277(45):43071-8. Epub 2002 Aug 27.
PMID 12200435
The prion-like protein Doppel enhances ovine spermatozoa fertilizing ability.
Pimenta J1, Dias FM, Marques CC, Baptista MC, Vasques MI, Horta AE, Barbas JP, Soares R, Mesquita P, Cabrita E, Fontes CM, Prates JA, Pereira RM.
Reprod Domest Anim. 2012 Apr;47(2):196-202. doi: 10.1111/j.1439-0531.2011.01827.x. Epub 2011 Aug 2.
PMID 21806689
The PrP-like protein Doppel binds copper.
Qin K, Coomaraswamy J, Mastrangelo P, Yang Y, Lugowski S, Petromilli C, Prusiner SB, Fraser PE, Goldberg JM, Chakrabartty A, Westaway D.
J Biol Chem. 2003 Mar 14;278(11):8888-96. Epub 2002 Dec 13.
PMID 12482851
Biochemical signatures of doppel protein in human astrocytomas to support prediction in tumor malignancy.
Rognoni P, Chiarelli LR, Comincini S, Azzalin A, Miracco C, Valentini G.
J Biomed Biotechnol. 2010;2010:301067. doi: 10.1155/2010/301067. Epub 2010 Oct 14.
PMID 20981146
Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain.
Rossi D, Cozzio A, Flechsig E, Klein MA, Rulicke T, Aguzzi A, Weissmann C.
EMBO J. 2001 Feb 15;20(4):694-702.
PMID 11179214
Altered cellular distribution and sub-cellular sorting of doppel (Dpl) protein in human astrocytoma cell lines.
Sbalchiero E, Azzalin A, Palumbo S, Barbieri G, Arias A, Simonelli L, Ferretti L, Comincini S.
Cell Oncol. 2008;30(4):337-47.
PMID 18607068
Polymorphisms within the prion-like protein gene (Prnd) and their implications in human prion diseases, Alzheimer's disease and other neurological disorders.
Schroder B, Franz B, Hempfling P, Selbert M, Jurgens T, Kretzschmar HA, Bodemer M, Poser S, Zerr I.
Hum Genet. 2001 Sep;109(3):319-25.
PMID 11702213
Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss.
Silverman GL, Qin K, Moore RC, Yang Y, Mastrangelo P, Tremblay P, Prusiner SB, Cohen FE, Westaway D.
J Biol Chem. 2000 Sep 1;275(35):26834-41.
PMID 10842180
Stability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant.
Whyte SM, Sylvester ID, Martin SR, Gill AC, Wopfner F, Schatzl HM, Dodson GG, Bayley PM.
Biochem J. 2003 Jul 15;373(Pt 2):485-94.
PMID 12665426
Induction of HO-1 and NOS in doppel-expressing mice devoid of PrP: implications for doppel function.
Wong BS, Liu T, Paisley D, Li R, Pan T, Chen SG, Perry G, Petersen RB, Smith MA, Melton DW, Gambetti P, Brown DR, Sy MS.
Mol Cell Neurosci. 2001 Apr;17(4):768-75.
PMID 11312611
Doppel-induced Purkinje cell death is stoichiometrically abrogated by prion protein.
Yamaguchi N, Sakaguchi S, Shigematsu K, Okimura N, Katamine S.
Biochem Biophys Res Commun. 2004 Jul 9;319(4):1247-52.
PMID 15194501
Dominant-negative effects of the N-terminal half of prion protein on neurotoxicity of prion protein-like protein/doppel in mice.
Yoshikawa D, Yamaguchi N, Ishibashi D, Yamanaka H, Okimura N, Yamaguchi Y, Mori T, Miyata H, Shigematsu K, Katamine S, Sakaguchi S.
J Biol Chem. 2008 Aug 29;283(35):24202-11. doi: 10.1074/jbc.M804212200. Epub 2008 Jun 18.
PMID 18562311


This paper should be referenced as such :
Giachin, G ; Legname, G
PRND (Prion Protein 2 (Dublet))
Atlas Genet Cytogenet Oncol Haematol. 2014;18(8):576-580.
Free journal version : [ pdf ]   [ DOI ]
On line version :

External links

HGNC (Hugo)PRND   15748
Entrez_Gene (NCBI)PRND  23627  prion like protein doppel
AliasesDOPPEL; DPL; PrPLP; dJ1068H6.4
GeneCards (Weizmann)PRND
Ensembl hg19 (Hinxton)ENSG00000171864 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000171864 [Gene_View]  ENSG00000171864 [Sequence]  chr20:4721854-4728462 [Contig_View]  PRND [Vega]
ICGC DataPortalENSG00000171864
Genatlas (Paris)PRND
SOURCE (Princeton)PRND
Genetics Home Reference (NIH)PRND
Genomic and cartography
GoldenPath hg38 (UCSC)PRND  -     chr20:4721854-4728462 +  20p13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PRND  -     20p13   [Description]    (hg19-Feb_2009)
GoldenPathPRND - 20p13 [CytoView hg19]  PRND - 20p13 [CytoView hg38]
Mapping of homologs : NCBIPRND [Mapview hg19]  PRND [Mapview hg38]
Gene and transcription
Genbank (Entrez)AF086354 AF187843 AF187844 AK313404 AY358985
RefSeq transcript (Entrez)NM_012409
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)PRND
Cluster EST : UnigeneHs.406696 [ NCBI ]
CGAP (NCI)Hs.406696
Alternative Splicing GalleryENSG00000171864
Gene ExpressionPRND [ NCBI-GEO ]   PRND [ EBI - ARRAY_EXPRESS ]   PRND [ SEEK ]   PRND [ MEM ]
Gene Expression Viewer (FireBrowse)PRND [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)23627
GTEX Portal (Tissue expression)PRND
Human Protein AtlasENSG00000171864-PRND [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UKY0   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UKY0  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UKY0
Splice isoforms : SwissVarQ9UKY0
Domains : Interpro (EBI)Doppel    Prion/Doppel_b-ribbon_dom_sf    Prion/Doppel_prot_b-ribbon_dom   
Domain families : Pfam (Sanger)Doppel (PF11466)    Prion (PF00377)   
Domain families : Pfam (NCBI)pfam11466    pfam00377   
Conserved Domain (NCBI)PRND
DMDM Disease mutations23627
Blocks (Seattle)PRND
PDB Europe1LG4   
PDB (PDBSum)1LG4   
PDB (IMB)1LG4   
Structural Biology KnowledgeBase1LG4   
SCOP (Structural Classification of Proteins)1LG4   
CATH (Classification of proteins structures)1LG4   
Human Protein Atlas [tissue]ENSG00000171864-PRND [tissue]
Peptide AtlasQ9UKY0
Protein Interaction databases
IntAct (EBI)Q9UKY0
Ontologies - Pathways
Ontology : AmiGOcopper ion binding  copper ion binding  extracellular region  plasma membrane  cellular copper ion homeostasis  acrosome reaction  anchored component of external side of plasma membrane  anchored component of external side of plasma membrane  protein homooligomerization  
Ontology : EGO-EBIcopper ion binding  copper ion binding  extracellular region  plasma membrane  cellular copper ion homeostasis  acrosome reaction  anchored component of external side of plasma membrane  anchored component of external side of plasma membrane  protein homooligomerization  
REACTOMEQ9UKY0 [protein]
REACTOME PathwaysR-HSA-163125 [pathway]   
NDEx NetworkPRND
Atlas of Cancer Signalling NetworkPRND
Wikipedia pathwaysPRND
Orthology - Evolution
GeneTree (enSembl)ENSG00000171864
Phylogenetic Trees/Animal Genes : TreeFamPRND
Homologs : HomoloGenePRND
Homology/Alignments : Family Browser (UCSC)PRND
Gene fusions - Rearrangements
Fusion PortalRAGE PRND 20p13 HNSC
Fusion : Fusion_HubRAGE--PRND   
Fusion : QuiverPRND
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPRND [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PRND
Exome Variant ServerPRND
ExAC (Exome Aggregation Consortium)ENSG00000171864
GNOMAD BrowserENSG00000171864
Varsome BrowserPRND
Genetic variants : HAPMAP23627
Genomic Variants (DGV)PRND [DGVbeta]
DECIPHERPRND [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPRND 
ICGC Data PortalPRND 
TCGA Data PortalPRND 
Broad Tumor PortalPRND
OASIS PortalPRND [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPRND  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DPRND
Mutations and Diseases : HGMDPRND
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 PRND
DgiDB (Drug Gene Interaction Database)PRND
DoCM (Curated mutations)PRND (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PRND (select a term)
NCG5 (London)PRND
Cancer3DPRND(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PRND
NextProtQ9UKY0 [Medical]
Target ValidationPRND
Huge Navigator PRND [HugePedia]
snp3D : Map Gene to Disease23627
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD23627
Chemical/Pharm GKB GenePA33795
Clinical trialPRND
canSAR (ICR)PRND (select the gene name)
DataMed IndexPRND
PubMed39 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 : Wed Nov 13 21:51:35 CET 2019

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