Atlas of Genetics and Cytogenetics in Oncology and Haematology


Home   Genes   Leukemias   Solid Tumors   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA

PAEP (progestagen-associated endometrial protein)

Written2010-11Hannu Koistinen, Markku Seppälä
Department of Clinical Chemistry, Helsinki University Central Hospital, University of Helsinki, Helsinki, Finland

(Note : for Links provided by Atlas : click)

Identity

Alias_namesprogestagen-associated endometrial protein
Alias_symbol (synonym)PEP
PP14
GdA
GdS
GdF
PAEG
GD
MGC138509
MGC142288
Other alias
HGNC (Hugo) PAEP
LocusID (NCBI) 5047
Atlas_Id 46067
Location 9q34.3  [Link to chromosome band 9q34]
Location_base_pair Starts at 135561756 and ends at 135566776 bp from pter ( according to hg19-Feb_2009)  [Mapping PAEP.png]
Local_order Several other lipocalin genes have been mapped on the same chromosomal region. From centromere to telomere (GeneLoc database): lipocalin 1 (tear prealbumin, LCN1) - ENSG00000221613 - odorant binding protein 2A (OBP2A) - progestagen-associated endometrial protein (PAEP) - ENSG00000237339 - LOC138159 - ENSG00000236543 - glycosyltransferase 6 domain containing 1 (GLT6D1) - lipocalin 9 (LCN9).
 
  Chromosomal location and gene structure of PAEP. Promoter region shows some of the potential regulatory elements. After translation- initiating codon (ATG) exons of the major transcript are shown in black. Some splicing variants contain also parts outside of these exons. PRE: glucocorticoid/progesterone response element; CRE: cAMP responsive element; Sp1: Sp1 transcription factor binding site; AP-1: activator protein-1 element.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
PAEP (9q34.3) / FAR1 (11p15.2)PAEP (9q34.3) / FAR1 (11p15.3)

DNA/RNA

Note Many other lipocalin genes have similar exon/intron organization.
Description Maps to chromosome 9: 138453602-138458801 on forward (plus) strand (5200 bases). Gene consists of 7 exons. Promoter region contains, by sequence similarity, 2 forward and two reverse Sp1-like binding sites, four putative glucocorticoid/progesterone response elements (PREs), cAMP responsive element (CRE) and activator protein-1 (AP-1) element.
Transcription PAEP mRNA (NM_001018049) has 857 bp. Several alternatively spliced mRNA forms have been described, but for most of these evidence for the corresponding protein lacks. Alternative Splicing and Transcript Diversity database (ASTD) reports 16 different transcripts.
Pseudogene Not known.

Protein

Note Some of the localization studies have employed antibodies, the specificity of which is questionable. Some of the biological studies have utilized short peptides derived from PAEP sequence. It is unclear whether such peptides are present in vivo. Glycosylation plays an important part in modulating/dictating the activity of PAEP. In the literature, PAEP is widely referred to as PP14 and glycodelin.
 
  Swiss model-deduced tertiary structure of the PAEP monomer. The S-S bridge is shown as cylinder and side chain nitrogen atoms of asparagines of potential glycosylation sites are shown as balls. Below are representative examples of the major complex-type glycans present at the N-glycosylation sites Asn 28 and Asn 63 of amniotic fluid glycodelin-isoform (glycodelin-A) and seminal plasma glycodelin-isoform (glycodelin-S). Some of the characteristic epitopes are marked by broken line.
Description PAEP (180 amino acids, of which 18 corresponds to signal sequence) is a 28 kDa secreted glycoprotein, belonging to the kernel lipocalin family. Most family members share three conserved sequence motifs. Although sequence similarity between the family members is low, their three dimensional structures are similar. Lipocalins are small extracellular proteins, many of which bind small hydrophobic molecules, such as retinol and steroids. There is no evidence that PAEP exhibits similar binding properties. PAEP is a glycoprotein with three potential glycosylation sites. Two of them are glycosylated. Many differentially glycosylated forms have been characterized in these sites. Glycosylation modulates/dictates the biological activity of PAEP. Some of the alternatively spliced mRNAs lack the sequences encoding glycosylation sites and/or the lipocalin signature sequence.
Expression The expression of PAEP is highly regulated in a spatiotemporal fashion. In the female, PAEP is mainly expressed in secretory/decidualized endometrial glands after progesterone exposure. In secretory endometrium, expression becomes detectable four days after ovulation and reaches maximum at the end of the menstrual cycle unless pregnancy ensues. PAEP is one of the major proteins in endometrial secretions. In the male, the highest expression has been reported in seminal vesicles. PAEP is also expressed in other epithelial cells of reproductive tissues, such as fallopian tubes, ovary and the breast. In addition, other secretory epithelia, such as eccrine sweat glands and the bronchus epithelium express PAEP. It is also expressed in differentiated areas of breast cancer, ovarian tumors, endometrial adenocarcinoma, and synovial sarcoma. In addition to epithelial tissues, PAEP has been found in megakaryocytes and erythroid precursor cells. Experimental evidence suggests that PAEP expression is regulated by progesterone/progestins, relaxin, and histone deacetylase inhibitors.
Localisation PAEP is mostly found in exocrine epithelial cells, from which it is secreted into the gland lumen. In breast cancer, PAEP has been found also in paranuclear vacuoles of lobular carcinoma cells.
Function PAEP/PP14/glycodelin regulates the functions of spermatozoa during fertilization in a glycosylation dependent manner. The various glycoforms of PAEP have different, sometimes even opposite, biological actions at different phases of the fertilization process. Seminal fluid glycodelin-S binds to the sperm head and inhibits premature capacitation. In the female reproductive tract, spermatozoa come into contact with various PAEP glycoforms, that modulate sperm function, e.g., by preventing premature, progesterone-induced acrosome reaction (glycodelin-F). Glycodelin-A inhibits binding of spermatozoa to the zona pellucida, whereas another glycoform (glycodelin-C) stimulates the same. All these actions are glycosylation-dependent.
PAEP also regulates immune cell functions, which too are, at least in part, regulated by glycosylation. Different PAEP glycoforms contain diverse bi-, tri-, and tetra-antennary complex-type glycans with varying levels of fucose and sialic acid substitution. Glycodelin-A and -F are the most heavily sialylated and inhibit cell proliferation, induce cell death, and suppress interleukin-2 secretion of Jurkat cells and peripheral blood mononuclear cells. No such immunosuppressive effect has been observed for glycodelin-C and -S carrying less or no sialic acids, or for desialylated glycodelin-A and -F. By its immunosuppressive properties one of the PAEP glycoforms (glycodelin-A) may contribute to immunotolerance at the fetomaternal interface and prevent rejection of the fetal semi-allograft.
In early pregnancy, glycodelin-A restrains inappropriate invasion of extravillous cytotrophoblasts by suppressing activity of some key metalloproteinases. In breast and endometrial cancer cell lines, PAEP has been found to revert the malignant phenotype in vitro by inducing morphological differentiation and specific gene expression changes. In a preclinical mouse model, transgenic PAEP expression in breast cancer cells has reduced tumor growth.
Homology Most lipocalins do not share high sequence similarity, but they are likely to be homologous.
Functional PAEP gene has been found in higher primates. Beta-lactoglobulins represent orthologs of PAEP, but they are likely to be functionally different from human PAEP, not least because of their differences in glycosylation. No convincing evidence of a PAEP ortholog in mouse or rat has been reported.

Mutations

Note NCBI SNP database reports 128 PAEP SNPs (Homo sapiens, 13 September 2010). Also HinfI restriction enzyme polymorphism has been reported in Finnish population with 5% frequency for allele A1 and 95% frequency for allele A2. No disease associations for mutations have been described.

Implicated in

Note
  
Entity Ovarian carcinoma
Note PAEP is expressed in both normal and malignant ovarian tissue. PAEP has been localized to the cytoplasm of tumor cells and its staining is more frequent in well-differentiated than in poorly differentiated carcinomas. Nuclear progesterone receptors (PRA and PRB) are often coexpressed with cytoplasmic PAEP.
Disease In 2002, ovarian cancer was the 6th most common cancer in women, and 7th most common cause of cancer death. Most malignant neoplasms of the ovary originate from the coelomic epithelium.
Prognosis In ovarian serous carcinoma, PAEP expression is associated with a more favorable prognosis, even in patients with the same tumor grade and clinical stage.
  
  
Entity Breast cancer
Note In breast cancer tissue, PAEP staining has been found in both estrogen and progesterone receptor negative and positive cancers. PAEP is also present in normal breast tissue. Transfection of PAEP in MCF-7 breast cancer cells reverted the malignant phenotype of the cells by inducing morphological differentiation and specific gene expression changes. Furthermore, these cells showed reduced tumor growth in a preclinical xenograft tumor mouse model.
Disease Breast cancer is the most common cancer among women worldwide. Although the prognosis has improved following improved diagnosis and therapies, breast cancer remains an important cause of death among women. Most of the neoplasms of the breast originate from the ductal epithelium, while a minority originates from the lobular epithelium. Family history of breast cancer is associated with a 2-3-fold higher risk of the disease.
Prognosis In sporadic breast cancer, PAEP is associated with low proliferation rate and well-differentiated tumors, whereas in familial "non BRCA1/BRCA2" patients, PAEP expression is associated with a less favorable phenotype and increased risk of metastases.
  
  
Entity Reproductive failure
Note During the period of endometrial receptivity for implantation, reduced PAEP secretion/serum levels have been observed in reproductive failure, e.g. in unexplained infertility or recurrent early pregnancy loss.
Disease Unexplained infertility or recurrent miscarriage may result from inadequate implantation and/or placentation.
  
  
Entity Polycystic ovary syndrome (PCOS)
Note Pregnant women with PCOS who subsequently miscarry show subnormal rise of PAEP serum concentration during the first trimester.
Disease PCOS is a common endocrine disorder in fertile-aged women. It is associated with ovulatory disturbance, insulin resistance and androgen excess, and is a frequent cause of menstrual disorders and infertility in women.
  

Bibliography

Lipocalins: unity in diversity.
Akerstrom B, Flower DR, Salier JP.
Biochim Biophys Acta. 2000 Oct 18;1482(1-2):1-8. (REVIEW)
PMID 11058742
 
The role of glycodelin as an immune-modulating agent at the feto-maternal interface.
Alok A, Karande AA.
J Reprod Immunol. 2009 Dec;83(1-2):124-7. Epub 2009 Nov 5.
PMID 19896207
 
Identification of placental protein 14 as an immunosuppressive factor in human reproduction.
Bolton AE, Pockley AG, Clough KJ, Mowles EA, Stoker RJ, Westwood OM, Chapman MG.
Lancet. 1987 Mar 14;1(8533):593-5.
PMID 2881133
 
Cumulus oophorus-associated glycodelin-C displaces sperm-bound glycodelin-A and -F and stimulates spermatozoa-zona pellucida binding.
Chiu PC, Chung MK, Koistinen R, Koistinen H, Seppala M, Ho PC, Ng EH, Lee KF, Yeung WS.
J Biol Chem. 2007 Feb 23;282(8):5378-88. Epub 2006 Dec 27.
PMID 17192260
 
Cumulus-associated alpha2-macroglobulin derivative retai~s prgc/nceptive glycodelin-C in the human cumulus matrix.
Chung MK, Chiu PC, Lee CL, Pang RT, Ng EH, Lee KF, Koistinen R, Koistinen H, Seppala M, Yeung WS.
Hum Reprod. 2009 Nov;24(11):2856-67. Epub 2009 Jul 22.
PMID 19625311
 
A role for glycoconjugates in human development: the human feto-embryonic defence system hypothesis.
Clark GF, Oehninger S, Patankar MS, Koistinen R, Dell A, Morris HR, Koistinen H, Seppala M.
Hum Reprod. 1996 Mar;11(3):467-73. (REVIEW)
PMID 8671249
 
Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
Dell A, Morris HR, Easton RL, Panico M, Patankar M, Oehniger S, Koistinen R, Koistinen H, Seppala M, Clark GF.
J Biol Chem. 1995 Oct 13;270(41):24116-26.
PMID 7592613
 
Modulation of the baboon (Papio anubis) uterine endometrium by chorionic gonadotrophin during the period of uterine receptivity.
Fazleabas AT, Donnelly KM, Srinivasan S, Fortman JD, Miller JB.
Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2543-8.
PMID 10051679
 
The lipocalin protein family: structural and sequence overview.
Flower DR, North AC, Sansom CE.
Biochim Biophys Acta. 2000 Oct 18;1482(1-2):9-24. (REVIEW)
PMID 11058743
 
The lipocalin protein family: structure and function.
Flower DR.
Biochem J. 1996 Aug 15;318 ( Pt 1):1-14. (REVIEW)
PMID 8761444
 
Ligand activated hPR modulates the glycodelin promoter activity through the Sp1 sites in human endometrial adenocarcinoma cells.
Gao J, Mazella J, Seppala M, Tseng L.
Mol Cell Endocrinol. 2001 May 15;176(1-2):97-102.
PMID 11369448
 
Multiple forms of mRNA encoding human pregnancy-associated endometrial alpha 2-globulin, a beta-lactoglobulin homologue.
Garde J, Bell SC, Eperon IC.
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2456-60.
PMID 2006183
 
Evolution of the lipocalin family as inferred from a protein sequence phylogeny.
Gutierrez G, Ganfornina MD, Sanchez D.
Biochim Biophys Acta. 2000 Oct 18;1482(1-2):35-45. (REVIEW)
PMID 11058745
 
Glycodelin: a reproduction-related lipocalin.
Halttunen M, Kamarainen M, Koistinen H.
Biochim Biophys Acta. 2000 Oct 18;1482(1-2):149-56. (REVIEW)
PMID 11058757
 
Glycodelin expression associates with differential tumour phenotype and outcome in sporadic and familial non-BRCA1/2 breast cancer patients.
Hautala LC, Greco D, Koistinen R, Heikkinen T, Heikkila P, Aittomaki K, Blomqvist C, Koistinen H, Nevanlinna H.
Breast Cancer Res Treat. 2010 Jul 30. [Epub ahead of print]
PMID 20676758
 
alpha2,6-Sialylation promotes binding of placental protein 14 via its Ca2+-dependent lectin activity: insights into differential effects on CD45RO and CD45RA T cells.
Ish-Shalom E, Gargir A, Andre S, Borovsky Z, Ochanuna Z, Gabius HJ, Tykocinski ML, Rachmilewitz J.
Glycobiology. 2006 Mar;16(3):173-83. Epub 2005 Nov 3.
PMID 16269626
 
Reduced serum glycodelin and insulin-like growth factor-binding protein-1 in women with polycystic ovary syndrome during first trimester of pregnancy.
Jakubowicz DJ, Essah PA, Seppala M, Jakubowicz S, Baillargeon JP, Koistinen R, Nestler JE.
J Clin Endocrinol Metab. 2004 Feb;89(2):833-9.
PMID 14764802
 
Analysis of the role of oligosaccharides in the apoptotic activity of glycodelin A.
Jayachandran R, Shaila MS, Karande AA.
J Biol Chem. 2004 Mar 5;279(10):8585-91. Epub 2003 Dec 16.
PMID 14679202
 
A progestagen-dependent endometrial protein in human amniotic fluid.
Joshi SG, Smith RA, Stokes DK.
J Reprod Fertil. 1980 Nov;60(2):317-21.
PMID 6776278
 
Complete amino acid sequence of human placental protein 14: a progesterone-regulated uterine protein homologous to beta-lactoglobulins.
Julkunen M, Seppala M, Janne OA.
Proc Natl Acad Sci U S A. 1988 Dec;85(23):8845-9.
PMID 3194393
 
Expression of glycodelin in human breast and breast cancer.
Kamarainen M, Halttunen M, Koistinen R, von Boguslawsky K, von Smitten K, Andersson LC, Seppala M.
Int J Cancer. 1999 Dec 10;83(6):738-42.
PMID 10597188
 
The role of glycodelin in cell differentiation and tumor growth.
Koistinen H, Hautala LC, Seppala M, Stenman UH, Laakkonen P, Koistinen R.
Scand J Clin Lab Invest. 2009;69(4):452-9. (REVIEW)
PMID 19551557
 
Glycodelin-A as a modulator of trophoblast invasion.
Lam KK, Chiu PC, Chung MK, Lee CL, Lee KF, Koistinen R, Koistinen H, Seppala M, Ho PC, Yeung WS.
Hum Reprod. 2009 Sep;24(9):2093-103. Epub 2009 Jun 11.
PMID 19520712
 
Glycodelin-A modulates cytokine production of peripheral blood natural killer cells.
Lee CL, Chiu PC, Lam KK, Chan RW, Chu IK, Koistinen R, Koistinen H, Seppala M, Lee KF, Yeung WS.
Fertil Steril. 2010 Jul;94(2):769-71. Epub 2009 Nov 27.
PMID 19945098
 
Effects of differential glycosylation of glycodelins on lymphocyte survival.
Lee CL, Pang PC, Yeung WS, Tissot B, Panico M, Lao TT, Chu IK, Lee KF, Chung MK, Lam KK, Koistinen R, Koistinen H, Seppala M, Morris HR, Dell A, Chiu PC.
J Biol Chem. 2009 May 29;284(22):15084-96. Epub 2009 Feb 24.
PMID 19240032
 
Glycodelin in ovarian serous carcinoma: association with differentiation and survival.
Mandelin E, Lassus H, Seppala M, Leminen A, Gustafsson JA, Cheng G, Butzow R, Koistinen R.
Cancer Res. 2003 Oct 1;63(19):6258-64.
PMID 14559812
 
Differential regulation of Th1/Th2 cytokine responses by placental protein 14.
Mishan-Eisenberg G, Borovsky Z, Weber MC, Gazit R, Tykocinski ML, Rachmilewitz J.
J Immunol. 2004 Nov 1;173(9):5524-30.
PMID 15494501
 
Gender-specific glycosylation of human glycodelin affects its contraceptive activity.
Morris HR, Dell A, Easton RL, Panico M, Koistinen H, Koistinen R, Oehninger S, Patankar MS, Seppala M, Clark GF.
J Biol Chem. 1996 Dec 13;271(50):32159-67.
PMID 8943270
 
Hematopoietic placental protein 14. An immunosuppressive factor in cells of the megakaryocytic lineage.
Morrow DM, Xiong N, Getty RR, Ratajczak MZ, Morgan D, Seppala M, Riittinen L, Gewirtz AM, Tykocinski ML.
Am J Pathol. 1994 Dec;145(6):1485-95.
PMID 7992851
 
Placental protein 14 induces apoptosis in T cells but not in monocytes.
Mukhopadhyay D, Sundereshan S, Rao C, Karande AA.
J Biol Chem. 2001 Jul 27;276(30):28268-73. Epub 2001 Apr 26.
PMID 11325960
 
Factors affecting fertilization: endometrial placental protein 14 reduces the capacity of human spermatozoa to bind to the human zona pellucida.
Oehninger S, Coddington CC, Hodgen GD, Seppala M.
Fertil Steril. 1995 Feb;63(2):377-83.
PMID 7531163
 
Glycodelin blocks progression to S phase and inhibits cell growth: a possible progesterone-induced regulator for endometrial epithelial cell growth.
Ohta K, Maruyama T, Uchida H, Ono M, Nagashima T, Arase T, Kajitani T, Oda H, Morita M, Yoshimura Y.
Mol Hum Reprod. 2008 Jan;14(1):17-22. Epub 2008 Jan 4.
PMID 18178606
 
Suppression by human placental protein 14 of natural killer cell activity.
Okamoto N, Uchida A, Takakura K, Kariya Y, Kanzaki H, Riittinen L, Koistinen R, Seppala M, Mori T.
Am J Reprod Immunol. 1991 Dec;26(4):137-42.
PMID 1840727
 
Differential sialylation regulates the apoptotic activity of glycodelin A.
Poornima BL, Karande AA.
FEBS Lett. 2007 Sep 4;581(22):4366-70. Epub 2007 Aug 10.
PMID 17716661
 
Negative regulation of T cell activation by placental protein 14 is mediated by the tyrosine phosphatase receptor CD45.
Rachmilewitz J, Borovsky Z, Riely GJ, Miller R, Tykocinski ML.
J Biol Chem. 2003 Apr 18;278(16):14059-65. Epub 2003 Jan 29.
PMID 12556471
 
alpha2-macroglobulin modulates the immunoregulatory function of the lipocalin placental protein 14.
Riely GJ, Rachmilewitz J, Koo PH, Tykocinski ML.
Biochem J. 2000 Oct 15;351 Pt 2:503-8.
PMID 11023837
 
Glycodelin expression in correlation to grading, nodal involvement and steroid receptor expression in human breast cancer patients.
Scholz C, Toth B, Barthell E, Mylonas I, Weissenbacher T, Friese K, Jeschke U.
Anticancer Res. 2010 May;30(5):1599-603.
PMID 20592348
 
Glycodelins.
Seppala M, Bohn H, Tatarinov Y.
Tumour Biol. 1998;19(3):213-20. (REVIEW)
PMID 9591048
 
Glycodelin in reproductive endocrinology and hormone-related cancer.
Seppala M, Koistinen H, Koistinen R, Hautala L, Chiu PC, Yeung WS.
Eur J Endocrinol. 2009 Feb;160(2):121-33. Epub 2008 Nov 27. (REVIEW)
PMID 19039086
 
Glycodelin: a major lipocalin protein of the reproductive axis with diverse actions in cell recognition and differentiation.
Seppala M, Taylor RN, Koistinen H, Koistinen R, Milgrom E.
Endocr Rev. 2002 Aug;23(4):401-30. (REVIEW)
PMID 12202458
 
The role of relaxin in glycodelin secretion.
Stewart DR, Erikson MS, Erikson ME, Nakajima ST, Overstreet JW, Lasley BL, Amento EP, Seppala M.
J Clin Endocrinol Metab. 1997 Mar;82(3):839-46.
PMID 9062493
 
Promegestone (R5020) and mifepristone (RU486) both function as progestational agonists of human glycodelin gene expression in isolated human epithelial cells.
Taylor RN, Savouret JF, Vaisse C, Vigne JL, Ryan I, Hornung D, Seppala M, Milgrom E.
J Clin Endocrinol Metab. 1998 Nov;83(11):4006-12.
PMID 9814484
 
Relaxin stimulates glycodelin mRNA and protein concentrations in human endometrial glandular epithelial cells.
Tseng L, Zhu HH, Mazella J, Koistinen H, Seppala M.
Mol Hum Reprod. 1999 Apr;5(4):372-5.
PMID 10321810
 
Determination of glycodelin-A expression correlated to grading and staging in ovarian carcinoma tissue.
Tsviliana A, Mayr D, Kuhn C, Kunze S, Mylonas I, Jeschke U, Friese K.
Anticancer Res. 2010 May;30(5):1637-40.
PMID 20592354
 
Histone deacetylase inhibitor-induced glycodelin enhances the initial step of implantation.
Uchida H, Maruyama T, Ohta K, Ono M, Arase T, Kagami M, Oda H, Kajitani T, Asada H, Yoshimura Y.
Hum Reprod. 2007 Oct;22(10):2615-22. Epub 2007 Aug 24.
PMID 17720699
 
Human placental protein 14 gene: sequence and characterization of a short duplication.
Vaisse C, Atger M, Potier B, Milgrom E.
DNA Cell Biol. 1990 Jul-Aug;9(6):401-13.
PMID 2206398
 
The human placental protein 14 (PP14) gene is localized on chromosome 9q34.
Van Cong N, Vaisse C, Gross MS, Slim R, Milgrom E, Bernheim A.
Hum Genet. 1991 Mar;86(5):515-8.
PMID 2016092
 

Citation

This paper should be referenced as such :
Koistinen, H ; Seppè_lè_, M
PAEP (progestagen-associated endometrial protein)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(7):576-581.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/PAEPID46067ch9q34.html


External links

Nomenclature
HGNC (Hugo)PAEP   8573
Cards
AtlasPAEPID46067ch9q34
Entrez_Gene (NCBI)PAEP  5047  progestagen associated endometrial protein
AliasesGD; GdA; GdF; GdS; 
PAEG; PEP; PP14
GeneCards (Weizmann)PAEP
Ensembl hg19 (Hinxton)ENSG00000122133 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000122133 [Gene_View]  chr9:135561756-135566776 [Contig_View]  PAEP [Vega]
ICGC DataPortalENSG00000122133
TCGA cBioPortalPAEP
AceView (NCBI)PAEP
Genatlas (Paris)PAEP
WikiGenes5047
SOURCE (Princeton)PAEP
Genetics Home Reference (NIH)PAEP
Genomic and cartography
GoldenPath hg38 (UCSC)PAEP  -     chr9:135561756-135566776 +  9q34.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PAEP  -     9q34.3   [Description]    (hg19-Feb_2009)
EnsemblPAEP - 9q34.3 [CytoView hg19]  PAEP - 9q34.3 [CytoView hg38]
Mapping of homologs : NCBIPAEP [Mapview hg19]  PAEP [Mapview hg38]
OMIM173310   
Gene and transcription
Genbank (Entrez)AK304657 AK309965 AK309983 AK311007 AK311730
RefSeq transcript (Entrez)NM_001018048 NM_001018049 NM_002571
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)PAEP
Cluster EST : UnigeneHs.532325 [ NCBI ]
CGAP (NCI)Hs.532325
Alternative Splicing GalleryENSG00000122133
Gene ExpressionPAEP [ NCBI-GEO ]   PAEP [ EBI - ARRAY_EXPRESS ]   PAEP [ SEEK ]   PAEP [ MEM ]
Gene Expression Viewer (FireBrowse)PAEP [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5047
GTEX Portal (Tissue expression)PAEP
Human Protein AtlasENSG00000122133-PAEP [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP09466   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP09466  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP09466
Splice isoforms : SwissVarP09466
PhosPhoSitePlusP09466
Domaine pattern : Prosite (Expaxy)LIPOCALIN (PS00213)   
Domains : Interpro (EBI)Blactoglobulin    Calycin    Calycin-like    Lipocalin    Lipocalin_CS    Lipocln_cytosolic_FA-bd_dom   
Domain families : Pfam (Sanger)Lipocalin (PF00061)   
Domain families : Pfam (NCBI)pfam00061   
Conserved Domain (NCBI)PAEP
DMDM Disease mutations5047
Blocks (Seattle)PAEP
PDB (SRS)4R0B   
PDB (PDBSum)4R0B   
PDB (IMB)4R0B   
PDB (RSDB)4R0B   
Structural Biology KnowledgeBase4R0B   
SCOP (Structural Classification of Proteins)4R0B   
CATH (Classification of proteins structures)4R0B   
SuperfamilyP09466
Human Protein Atlas [tissue]ENSG00000122133-PAEP [tissue]
Peptide AtlasP09466
HPRD01411
IPIIPI00014544   IPI00218735   IPI00218736   IPI01009026   IPI00643941   IPI00514756   IPI01025980   IPI00981955   IPI00640131   
Protein Interaction databases
DIP (DOE-UCLA)P09466
IntAct (EBI)P09466
FunCoupENSG00000122133
BioGRIDPAEP
STRING (EMBL)PAEP
ZODIACPAEP
Ontologies - Pathways
QuickGOP09466
Ontology : AmiGOprotein binding  extracellular region  transport  apoptotic process  multicellular organism development  positive regulation of granulocyte macrophage colony-stimulating factor production  small molecule binding  positive regulation of interleukin-13 secretion  positive regulation of interleukin-6 secretion  
Ontology : EGO-EBIprotein binding  extracellular region  transport  apoptotic process  multicellular organism development  positive regulation of granulocyte macrophage colony-stimulating factor production  small molecule binding  positive regulation of interleukin-13 secretion  positive regulation of interleukin-6 secretion  
NDEx NetworkPAEP
Atlas of Cancer Signalling NetworkPAEP
Wikipedia pathwaysPAEP
Orthology - Evolution
OrthoDB5047
GeneTree (enSembl)ENSG00000122133
Phylogenetic Trees/Animal Genes : TreeFamPAEP
HOVERGENP09466
HOGENOMP09466
Homologs : HomoloGenePAEP
Homology/Alignments : Family Browser (UCSC)PAEP
Gene fusions - Rearrangements
Fusion : MitelmanPAEP/FAR1 [9q34.3/11p15.2]  
Fusion: TCGA_MDACCPAEP 9q34.3 FAR1 11p15.2 KIRC
Tumor Fusion PortalPAEP
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPAEP [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PAEP
dbVarPAEP
ClinVarPAEP
1000_GenomesPAEP 
Exome Variant ServerPAEP
ExAC (Exome Aggregation Consortium)ENSG00000122133
GNOMAD BrowserENSG00000122133
Genetic variants : HAPMAP5047
Genomic Variants (DGV)PAEP [DGVbeta]
DECIPHERPAEP [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPAEP 
Mutations
ICGC Data PortalPAEP 
TCGA Data PortalPAEP 
Broad Tumor PortalPAEP
OASIS PortalPAEP [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPAEP  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDPAEP
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 PAEP
DgiDB (Drug Gene Interaction Database)PAEP
DoCM (Curated mutations)PAEP (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PAEP (select a term)
intoGenPAEP
NCG5 (London)PAEP
Cancer3DPAEP(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM173310   
Orphanet
DisGeNETPAEP
MedgenPAEP
Genetic Testing Registry PAEP
NextProtP09466 [Medical]
TSGene5047
GENETestsPAEP
Target ValidationPAEP
Huge Navigator PAEP [HugePedia]
snp3D : Map Gene to Disease5047
BioCentury BCIQPAEP
ClinGenPAEP
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5047
Chemical/Pharm GKB GenePA32904
Clinical trialPAEP
Miscellaneous
canSAR (ICR)PAEP (select the gene name)
Probes
Litterature
PubMed121 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMinePAEP
EVEXPAEP
GoPubMedPAEP
iHOPPAEP
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Tue Nov 21 14:58:29 CET 2017

Home   Genes   Leukemias   Solid Tumors   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.