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

HTRA3 (HtrA serine peptidase 3)

Written2012-04Przemyslaw Glaza, Dorota Zurawa-Janicka, Barbara Lipinska
Department of Biochemistry, University of Gdansk, Kladki 24, 80-822 Gdansk, Poland

(Note : for Links provided by Atlas : click)


Alias (NCBI)Prsp
HGNC Alias symbTasp
HGNC Alias namepregnancy-related serine protease
LocusID (NCBI) 94031
Atlas_Id 45757
Location 4p16.1  [Link to chromosome band 4p16]
Location_base_pair Starts at 8269754 and ends at 8307098 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping HTRA3.png]
Local_order Genes flanking HTRA3 in telomere to centromere direction:
- GMPSP1: guanine monophosphate synthetase pseudogene 1
- SH3TC1: SH3 domain and tetratricopeptide repeats 1
- ACOX3: acyl-CoA oxidase 3
- METTL19: methyltransferase-like 19
  Figure 1. Localization and schematic organization of the HTRA3 gene on chromosome 4. The numbers indicate the length in kilo bases. Green boxes represent exons. Exons present in the long variant of HTRA3 mRNA (A) and in the short form HTRA3 mRNA (B) are shown. Black boxes indicate untranslated regions.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
TBC1D14 (4p16.1)::HTRA3 (4p16.1)
Note Deletions and translocations of the 4p16.1 region are associated with the development of Wolf-Hirschhorn Syndrome (Iwanowski et al., 2011). The neocentromere from a giant supernumerary chromosome in the well-differentiated liposarcoma cell line (94T778) is originated from a region at 4p16.1, which shows high frequency of AT sequences and contains a long interspersed nucleotide element (LINE)1 (Italiano et al., 2009).


Description The HTRA3 gene encompasses 37350 bases of DNA. The coding part is composed of ten exons (Figure 1).
Transcription Two alternatively spliced variants of HTRA3 mRNA have been sequenced, a long variant, length of 2543 bases, and a short form mRNA, length of 1953 bases (Figure 1). The long HTRA3 variant has an open frame of 1362 bases and lacks exon 7. It encodes a 49 kDa protein of 453 amino acid residues. The short form HTRA3 mRNA has an open frame of 1074 bases, and lacks three exons: 8, 9 and 10. It encodes a 38 kDa protein of 357 amino acid residues (Nie et al., 2003). The 5' promoter region of HTRA3 is methylated in some cases of cervical carcinomas but not in normal cervix tissues (Ongenaert et al., 2008). Expression of HTRA3 is regulated through methylation in the first exon. This epigenetic modification causes downregulation of HTRA3 expression in human lung cancer cell lines. Moreover, low levels of HTRA3 expression in primary lung tumors strongly correlate with heavy smoking history (Beleford et al., 2010a). It was also shown that expression of HTRA3 is stimulated through an indirect mechanism involving the MEK/ERK pathway in clear cell renal carcinoma (Theoleyre et al., 2010). However, transcription factors for HTRA3 are unknown.
Pseudogene No pseudogenes have been identified.


Note HtrA3 belongs to the HtrA family of ATP-independent serine proteases, homologues of the HtrA serine protease from the bacterium Escherichia coli. HtrA proteins are very well conserved in evolution. Structurally, they are characterized by the presence of a trypsin-like protease domain with the catalytic triad His-Asp-Ser and at least one PDZ domain at the C-terminal end. General function of the HtrA proteins is the defense against cellular stresses (such as heat shock, oxidative stress) causing aberrations in protein structure. At least, four human HtrA proteins have been identified. They are involved in important physiological processes including maintenance of mitochondrial homeostasis, cell death (apoptosis, necrosis, anoikis) and cell signaling. Disturbances in their functions may contribute to the development of several disorders such as cancer, arthritis and neurodegenerative disorders (reviewed by Chien et al., 2009a; Zurawa-Janicka et al., 2010; Clausen et al., 2011).
  Figure 2. Domain organization of human HtrA3 protein. Schematic organization of the long (A) and short (B) isoform of HtrA3 is presented. S: signal peptide, IB: domain with homology to insulin-like growth factor binding proteins, KM: Kazal type serine protease inhibitor motif, PROTEOLYTIC: trypsin-like domain, PDZ: PDZ domain, DWKKRFI/APSLAVH: amino acid residues different in the HtrA3 variants. The insulin-like growth factor binding domain (IB) and Kazal type inhibitor motif (KM) are homologous to Mac25 protein. Amino acid residues of the HtrA3 catalytic triad are marked (numbers indicate the position of the given residue in a polypeptide chain).
Description The open reading frame (ORF) of the long splice variant of HTRA3 mRNA encodes a polypeptide of 453 aa, mass of approximately 49 kDa. The long isoform of HtrA3 (HtrA3-L) contains a signal secretory peptide at the N-terminus (1-17), a domain with homology to the insulin-like growth factor binding proteins (29-94 aa) and a Kazal-type inhibitor motif (89-126) followed by a serine protease domain (176-341 aa) with the catalytic triad His191-Asp219-Ser305 and one PDZ domain (384-440 aa) at the C-terminal end. Domain with homology to the insulin-like growth factor binding proteins and a Kazal-type inhibitor motif shares homology with Mac25 protein. The PDZ domain mediates specific protein-protein interactions (Figure 2).
The ORF of the short splice variant of HTRA3 mRNA encodes a polypeptide of 357 aa, mass of about 38 kDa. Contrary to HtrA3-L, the short isoform of HtrA3 (HtrA3-S) lacks the PDZ domain. Moreover, the last seven C-terminal residues of HtrA3-S (APSLAVH) are completely different from the corresponding residues in HtrA3-L (DWKKRFI) (Figure 2) (Nie et al., 2003).
Under treatment of lung cancer cell lines with chemotherapeutic agents (cisplatin, etoposide) a removal of the N-terminal Mac25 domain has been observed (Beleford et al., 2010b). The proteolytic processing is believed to be an autocatalytic process since the catalytically inactive mutant did not undergo such modification. Substitution of the serine residue belonging to the protease catalytic site with alanine abolished autocatalytic degradation (Singh et al., 2012). Solely the structure of PDZ domain of HtrA3 was determined by the X-ray crystallography (Runyon et al., 2008). The Myosin-9 was identified as a first endogenous binding protein of HtrA3 in the placenta (Singh et al., 2012).
Expression Both variants of HTRA3 transcripts are widely expressed in the human body with variable levels in different organs (Nie et al., 2003). Reciprocal ratio of the long HTRA3 mRNA to short HTRA3 mRNA is dependent on the type of tissue. The highest expression of HTRA3 was observed in heart tissues and reproductive organs (ovary, uterus and placenta) (Nie et al., 2003).
HTRA3 is expressed predominantly in the glandular epithelium, endometrium and decidual cells during preparation of endometrium for embryo implantation in the early pregnancy. The maximal expression of placental HTRA3 is observed during the first trimester and then it decreases dramatically (Nie et al., 2005; Nie et al., 2006a; Li et al., 2011). Placental HtrA3 expression is negatively regulated through oxygen tension in the placenta (Li et al., 2011). It was clearly demonstrated that expression of HTRA3 is up-regulated during folliculogenesis and luteinisation in the rhesus monkey ovary (Bowden et al., 2008). These data indicate an important role of HTRA3 in placenta development and function.
Transcription of HTRA3 gene is stimulated through an indirect mechanism involving the MEK/ERK pathway in clear cell renal carcinoma (Theoleyre et al., 2010). In vitro transcriptional studies revealed that infection of chicken chondrocytes by bacterium Mycoplasma synoviae up-regulates of HTRA3 gene as an apoptosis-like event (Dusanic et al., 2012).
Beleford with co-workers showed that expression of HTRA3 is silenced by cigarette smoke-mediated methylation in lung tumors. This epigenetic modification increased the resistance of lung cancer cell lines to etoposide- and cisplatin-induced cytotoxicity (Beleford et al., 2010a). These results suggest that cigarette smoke-induced down-regulation of HTRA3 could contribute to the development of chemoresistant lung cancer.
Localisation HtrA3 is a nuclear-encoded mitochondrial protease (Chien et al., 2009b). Localisation of HtrA3 in the mitochondrium depends on the presence of Mac25 domain and is regulated by protease function of HtrA3 (Beleford et al., 2010b). Processed forms of HtrA3 have been also found in the cytoplasm (Beleford et al., 2010b). However, HtrA3 is also classified as a secreted protein (Nie et al., 2003).
Function HTRA3 functions as an ATP-independent serine protease.
HtrA3 has been shown to act as an inhibitor of TGF-beta signaling. HtrA3 binds to several members of the TGF-beta proteins family, including BMP4, TGF-beta1, TGF-beta2, GDF5, and suppresses signal transduction mediated by these extracellular cytokines (Tocharus et al., 2004). The proteolytic activity of HtrA3 is indispensable for this inhibitory function (Tocharus et al., 2004).
HtrA3 plays a significant role during embryo implantation and formation of placenta in mammals in the early stage of pregnancy (Nie et al., 2005; Nie et al., 2006a; Nie et al., 2006b; Bowden et al., 2008). Placental HtrA3 is secreted into the maternal circulation and distinctly detectable in serum of pregnant women in the first trimester (Nie et al., 2006a). At this stage of pregnancy cellular and serum level of HtrA3 is the highest and then HtrA3 level is dramatically down-regulated by an increase of placental oxygen tension at 13-14 week of pregnancy (Li et al., 2011). HtrA3, due to its proteolytic activity, negatively regulates trophoblast invasion during placental development (Singh et al., 2010; Singh et al., 2011).
HtrA3 is involved in the programmed cell death, apoptosis. It has been demonstrated that stable small hairpin RNA- and epigenetic-mediated down-regulation of HTRA3 expression attenuates cisplatin- and ethoposide-induced cytotoxicity in lung cancer cell lines while HTRA3 re-expression of proteolytic active HtrA3 promotes etopiside and cisplatine cytotoxicity (Beleford et al., 2010a, Beleford et al., 2010b).
Homology The HtrA3 protein is evolutionarily conserved among mammalian species.
At the amino acid level homology between human HtrA3 and its orthologs from rat and mouse reaches 92,3 and 92,7 %, respectively.
At least three paralogs of human HtrA3 have been identified: HtrA1 (L56, ORF480, PRSS11, ARMD7), HtrA2 (Omi) and HtrA4. HtrA3 shares the 76, 74 and 72 % homology with HtrA1, HtrA2 and HtrA4, respectively. The identity between HtrA3 and its paralogs reaches 59, 52 and 53 %, respectively.


Germinal Not known.
Somatic Not known.

Implicated in

Entity Various cancers
Note Expression of HTRA3 varies according to the tumor type. The variable expression of HTRA3 is manifested in hematologic malignancies and depends on specific molecular alterations. For instance, expression of HTRA3 is up-regulated in pro-B Acute Lymphoblastic Leukemia with hyperploidy but down-regulated in B-cell Acute Lymphoblastic Leukemia and acute myeloid leukemia (reviewed by Chien et al., 2009a). HTRA3 is up-regulated in esophageal adenocarcinoma (Hao et al., 2006), pancreatic adenocarcinoma (Iacobuzio-Donhue et al., 2003) and seminoma (Korkola et al., 2006). In contrast, its diminished expression was observed in ovarian (Narkiewicz et al., 2008), endometrial (Bowden et al., 2006; Narkiewicz et al., 2009) and lung cancers (Beleford et al., 2010a; Beleford et al., 2010b). In endometrial cancer the HTRA3 mRNA and protein levels were reduced with the increasing tumor staging. Moreover, a significant negative correlation between HtrA3 and TGF-beta1 protein levels found in endometrial cancer suggests that HtrA3 is involved in regulation of the TGF-beta1 signaling pathway in this type of cancer (Narkiewicz et al., 2009).
It was demonstrated that HtrA3 is involved in the induction of apoptosis in response to cytotoxic stress induced by chemotherapeutic agents in lung cancer cell lines (Beleford et al., 2010b). Resistance of cancer cells to cisplatin- and etoposide-mediated cytotoxicity is suggested to be a consequence of disturbances in the HtrA3 pro-apoptotic activity (Beleford et al., 2010b).
Oncogenesis Several studies argue the involvement of HtrA3 in oncogenesis. HtrA3 acts as a proapoptotic protein and is suggested to function as a tumor suppressor (Beleford et al., 2010a; Beleford et al., 2010b). However, variable expression of HTRA3 depending on cancer type makes unambiguous definition of the HtrA3 role in carcinogenesis difficult.
HtrA3 involvement in regulation of TGF-beta signaling (Tocharus et al., 2004) forms another link between HtrA3 and carcinogenesis. At early stages of tumorigenesis, TGF-β proteins act as tumor suppressors, inhibiting tumor outgrowth, but in advanced phases they stimulate tumor progression, invasion and metastasis.
Entity Preeclampsia
Note Li et al. (2011) showed that placental HtrA3 level and secretion of the protein into the maternal circulation is regulated by oxygen tension in the placental tissue. Abnormally high level of HtrA3 in the maternal serum at the 13-14 week of gestation is associated with the development of preeclampsia (Li et al., 2011).
Disease Preeclampsia is a severe disorder of human pregnancy. It is a multifactorial disease characterized by hypertension with proteinuria and is responsible for about 18% of maternal deaths and up to 40% of fetal mortality. Every year, 8,5 millions cases of preeclampsia are reported. Defective remodeling of the maternal vessels in the early stage of pregnancy is recognized as important factors in the initiation of the disorder (Anderson et al., 2012; Mary et al., 2012).


Note No breakpoints described so far.


Review: Biochemical markers to predict preeclampsia.
Anderson UD, Olsson MG, Kristensen KH, Akerstrom B, Hansson SR.
Placenta. 2012 Feb;33 Suppl:S42-7. Epub 2011 Dec 23. (REVIEW)
PMID 22197626
High temperature requirement A3 (HtrA3) promotes etoposide- and cisplatin-induced cytotoxicity in lung cancer cell lines.
Beleford D, Rattan R, Chien J, Shridhar V.
J Biol Chem. 2010b Apr 16;285(16):12011-27. Epub 2010 Feb 12.
PMID 20154083
Serine proteases HTRA1 and HTRA3 are down-regulated with increasing grades of human endometrial cancer.
Bowden MA, Di Nezza-Cossens LA, Jobling T, Salamonsen LA, Nie G.
Gynecol Oncol. 2006 Oct;103(1):253-60. Epub 2006 May 2.
PMID 16650464
HTRA3 expression in non-pregnant rhesus monkey ovary and endometrium, and at the maternal-fetal interface during early pregnancy.
Bowden MA, Li Y, Liu YX, Findlay JK, Salamonsen LA, Nie G.
Reprod Biol Endocrinol. 2008 Jun 18;6:22.
PMID 18559118
HtrA serine proteases as potential therapeutic targets in cancer.
Chien J, Campioni M, Shridhar V, Baldi A.
Curr Cancer Drug Targets. 2009a Jun;9(4):451-68.
PMID 19519315
Serine protease HtrA1 associates with microtubules and inhibits cell migration.
Chien J, Ota T, Aletti G, Shridhar R, Boccellino M, Quagliuolo L, Baldi A, Shridhar V.
Mol Cell Biol. 2009b Aug;29(15):4177-87. Epub 2009 May 26.
PMID 19470753
HTRA proteases: regulated proteolysis in protein quality control.
Clausen T, Kaiser M, Huber R, Ehrmann M.
Nat Rev Mol Cell Biol. 2011 Mar;12(3):152-62. Epub 2011 Feb 16. (REVIEW)
PMID 21326199
Mycoplasma synoviae induces upregulation of apoptotic genes, secretion of nitric oxide and appearance of an apoptotic phenotype in infected chicken chondrocytes.
Dusanic D, Bencina D, Oven I, Cizelj I, Bencina M, Narat M.
Vet Res. 2012 Jan 26;43(1):7.
PMID 22280251
Gene expression profiling reveals stromal genes expressed in common between Barrett's esophagus and adenocarcinoma.
Hao Y, Triadafilopoulos G, Sahbaie P, Young HS, Omary MB, Lowe AW.
Gastroenterology. 2006 Sep;131(3):925-33.
PMID 16952561
Exploration of global gene expression patterns in pancreatic adenocarcinoma using cDNA microarrays.
Iacobuzio-Donahue CA, Maitra A, Olsen M, Lowe AW, van Heek NT, Rosty C, Walter K, Sato N, Parker A, Ashfaq R, Jaffee E, Ryu B, Jones J, Eshleman JR, Yeo CJ, Cameron JL, Kern SE, Hruban RH, Brown PO, Goggins M.
Am J Pathol. 2003 Apr;162(4):1151-62.
PMID 12651607
Variability of origin for the neocentromeric sequences in analphoid supernumerary marker chromosomes of well-differentiated liposarcomas.
Italiano A, Maire G, Sirvent N, Nuin PA, Keslair F, Foa C, Louis C, Aurias A, Pedeutour F.
Cancer Lett. 2009 Jan 18;273(2):323-30. Epub 2008 Sep 26.
PMID 18823700
Wolf-Hirschhorn syndrome due to pure and translocation forms of monosomy 4p16.1 → pter.
Iwanowski PS, Panasiuk B, Van Buggenhout G, Murdolo M, Mys'liwiec M, Maas NM, Lattante S, Korniszewski L, Posmyk R, Pilch J, Zajaczek S, Fryns JP, Zollino M, Midro AT.
Am J Med Genet A. 2011 Aug;155A(8):1833-47. doi: 10.1002/ajmg.a.34005. Epub 2011 Jul 8.
PMID 21744486
Down-regulation of stem cell genes, including those in a 200-kb gene cluster at 12p13.31, is associated with in vivo differentiation of human male germ cell tumors.
Korkola JE, Houldsworth J, Chadalavada RS, Olshen AB, Dobrzynski D, Reuter VE, Bosl GJ, Chaganti RS.
Cancer Res. 2006 Jan 15;66(2):820-7.
PMID 16424014
Placental HtrA3 is regulated by oxygen tension and serum levels are altered during early pregnancy in women destined to develop preeclampsia.
Li Y, Puryer M, Lin E, Hale K, Salamonsen LA, Manuelpillai U, Tong S, Chan W, Wallace EM, Nie G.
J Clin Endocrinol Metab. 2011 Feb;96(2):403-11. Epub 2010 Nov 3.
PMID 21047919
Dynamic proteome in enigmatic preeclampsia: an account of molecular mechanisms and biomarker discovery.
Mary S, Patil GV, Kulkarni AV, Kulkarni MJ, Joshi SR, Mehendale SS, Giri AP.
Proteomics Clin Appl. 2012 Jan;6(1-2):79-90. doi: 10.1002/prca.201100089. (REVIEW)
PMID 22447695
Expression of human HtrA1, HtrA2, HtrA3 and TGF-beta1 genes in primary endometrial cancer.
Narkiewicz J, Lapinska-Szumczyk S, Zurawa-Janicka D, Skorko-Glonek J, Emerich J, Lipinska B.
Oncol Rep. 2009 Jun;21(6):1529-37.
PMID 19424634
Identification of novel endometrial targets for contraception.
Nie G, Findlay JK, Salamonsen LA.
Contraception. 2005 Apr;71(4):272-81. (REVIEW)
PMID 15792646
HtrA3, a serine protease possessing an IGF-binding domain, is selectively expressed at the maternal-fetal interface during placentation in the mouse.
Nie G, Li Y, He H, Findlay JK, Salamonsen LA.
Placenta. 2006b Apr-May;27(4-5):491-501. Epub 2005 Jun 13.
PMID 15951015
Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2.
Nie GY, Hampton A, Li Y, Findlay JK, Salamonsen LA.
Biochem J. 2003 Apr 1;371(Pt 1):39-48.
PMID 12513693
Discovery of DNA methylation markers in cervical cancer using relaxation ranking.
Ongenaert M, Wisman GB, Volders HH, Koning AJ, Zee AG, van Criekinge W, Schuuring E.
BMC Med Genomics. 2008 Nov 24;1:57.
PMID 19025626
Structural and functional analysis of the PDZ domains of human HtrA1 and HtrA3.
Runyon ST, Zhang Y, Appleton BA, Sazinsky SL, Wu P, Pan B, Wiesmann C, Skelton NJ, Sidhu SS.
Protein Sci. 2007 Nov;16(11):2454-71.
PMID 17962403
Decidual HtrA3 negatively regulates trophoblast invasion during human placentation.
Singh H, Endo Y, Nie G.
Hum Reprod. 2011 Apr;26(4):748-57. Epub 2011 Feb 14.
PMID 21321049
Application of the wheat-germ cell-free translation system to produce high temperature requirement A3 (HtrA3) proteases.
Singh H, Makino S, Endo Y, Li Y, Stephens AN, Nie G.
Biotechniques. 2012 Jan;52(1):23-8.
PMID 22229724
HtrA3 is regulated by 15-deoxy-Delta12,14-prostaglandin J2 independently of PPARgamma in clear cell renal cell carcinomas.
Theoleyre S, Mottier S, Masson D, Denis MG.
Biochem Biophys Res Commun. 2010 Apr 9;394(3):453-8. Epub 2009 Nov 29.
PMID 19951697
Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signaling.
Tocharus J, Tsuchiya A, Kajikawa M, Ueta Y, Oka C, Kawaichi M.
Dev Growth Differ. 2004 Jun;46(3):257-74.
PMID 15206957
HtrA proteins as targets in therapy of cancer and other diseases.
Zurawa-Janicka D, Skorko-Glonek J, Lipinska B.
Expert Opin Ther Targets. 2010 Jul;14(7):665-79. (REVIEW)
PMID 20469960


This paper should be referenced as such :
Glaza, P ; Zurawa-Janicka, D ; Lipinska, B
HTRA3 (HtrA serine peptidase 3)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(9):644-648.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)HTRA3   30406
Entrez_Gene (NCBI)HTRA3    HtrA serine peptidase 3
AliasesPrsp; Tasp
GeneCards (Weizmann)HTRA3
Ensembl hg19 (Hinxton)ENSG00000170801 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000170801 [Gene_View]  ENSG00000170801 [Sequence]  chr4:8269754-8307098 [Contig_View]  HTRA3 [Vega]
ICGC DataPortalENSG00000170801
TCGA cBioPortalHTRA3
Genatlas (Paris)HTRA3
SOURCE (Princeton)HTRA3
Genetics Home Reference (NIH)HTRA3
Genomic and cartography
GoldenPath hg38 (UCSC)HTRA3  -     chr4:8269754-8307098 +  4p16.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)HTRA3  -     4p16.1   [Description]    (hg19-Feb_2009)
GoldenPathHTRA3 - 4p16.1 [CytoView hg19]  HTRA3 - 4p16.1 [CytoView hg38]
Genome Data Viewer NCBIHTRA3 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AL547377 AW072765 AY040094 AY280665 AY280666
RefSeq transcript (Entrez)NM_001297559 NM_053044
Consensus coding sequences : CCDS (NCBI)HTRA3
Gene ExpressionHTRA3 [ NCBI-GEO ]   HTRA3 [ EBI - ARRAY_EXPRESS ]   HTRA3 [ SEEK ]   HTRA3 [ MEM ]
Gene Expression Viewer (FireBrowse)HTRA3 [ Firebrowse - Broad ]
GenevisibleExpression of HTRA3 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)94031
GTEX Portal (Tissue expression)HTRA3
Human Protein AtlasENSG00000170801-HTRA3 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP83110   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP83110  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP83110
Catalytic activity : Enzyme3.4.21.- [ Enzyme-Expasy ]   3.4.21.-3.4.21.- [ IntEnz-EBI ]   3.4.21.- [ BRENDA ]   3.4.21.- [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)IGFBP_N_2 (PS51323)    KAZAL_2 (PS51465)    PDZ (PS50106)   
Domains : Interpro (EBI)Growth_fac_rcpt_cys_sf    IGFBP-like    Kazal_dom    Kazal_dom_sf    PDZ    PDZ_6    PDZ_sf    Peptidase_S1_PA    Peptidase_S1C   
Domain families : Pfam (Sanger)IGFBP (PF00219)    Kazal_2 (PF07648)    PDZ_6 (PF17820)   
Domain families : Pfam (NCBI)pfam00219    pfam07648    pfam17820   
Domain families : Smart (EMBL)IB (SM00121)  KAZAL (SM00280)  PDZ (SM00228)  
Conserved Domain (NCBI)HTRA3
PDB (RSDB)2P3W    4RI0   
PDB Europe2P3W    4RI0   
PDB (PDBSum)2P3W    4RI0   
PDB (IMB)2P3W    4RI0   
Structural Biology KnowledgeBase2P3W    4RI0   
SCOP (Structural Classification of Proteins)2P3W    4RI0   
CATH (Classification of proteins structures)2P3W    4RI0   
AlphaFold pdb e-kbP83110   
Human Protein Atlas [tissue]ENSG00000170801-HTRA3 [tissue]
Protein Interaction databases
IntAct (EBI)P83110
Ontologies - Pathways
Ontology : AmiGOendopeptidase activity  serine-type endopeptidase activity  protein binding  insulin-like growth factor binding  extracellular region  proteolysis  serine-type peptidase activity  negative regulation of transforming growth factor beta receptor signaling pathway  negative regulation of BMP signaling pathway  identical protein binding  
Ontology : EGO-EBIendopeptidase activity  serine-type endopeptidase activity  protein binding  insulin-like growth factor binding  extracellular region  proteolysis  serine-type peptidase activity  negative regulation of transforming growth factor beta receptor signaling pathway  negative regulation of BMP signaling pathway  identical protein binding  
NDEx NetworkHTRA3
Atlas of Cancer Signalling NetworkHTRA3
Wikipedia pathwaysHTRA3
Orthology - Evolution
GeneTree (enSembl)ENSG00000170801
Phylogenetic Trees/Animal Genes : TreeFamHTRA3
Homologs : HomoloGeneHTRA3
Homology/Alignments : Family Browser (UCSC)HTRA3
Gene fusions - Rearrangements
Fusion : MitelmanTBC1D14::HTRA3 [4p16.1/4p16.1]  
Fusion : QuiverHTRA3
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerHTRA3 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)HTRA3
Exome Variant ServerHTRA3
GNOMAD BrowserENSG00000170801
Varsome BrowserHTRA3
ACMGHTRA3 variants
Genomic Variants (DGV)HTRA3 [DGVbeta]
DECIPHERHTRA3 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisHTRA3 
ICGC Data PortalHTRA3 
TCGA Data PortalHTRA3 
Broad Tumor PortalHTRA3
OASIS PortalHTRA3 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICHTRA3  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DHTRA3
Mutations and Diseases : HGMDHTRA3
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)HTRA3
DoCM (Curated mutations)HTRA3
CIViC (Clinical Interpretations of Variants in Cancer)HTRA3
NCG (London)HTRA3
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry HTRA3
NextProtP83110 [Medical]
Target ValidationHTRA3
Huge Navigator HTRA3 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDHTRA3
Pharm GKB GenePA134908281
Clinical trialHTRA3
DataMed IndexHTRA3
PubMed49 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
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 : Fri Oct 8 21:19:54 CEST 2021

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

For comments and suggestions or contributions, please contact us