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TRAP1 (TNF receptor-associated protein 1)

Written2010-07Dina Bellizzi, Giuseppe Passarino
Department of Cell Biology, University of Calabria, Rende, 87036, Italy

(Note : for Links provided by Atlas : click)


Alias (NCBI)HSP75
HGNC Alias symbHSP75
HGNC Previous nameTNF receptor-associated protein 1
LocusID (NCBI) 10131
Atlas_Id 42692
Location 16p13.3  [Link to chromosome band 16p13]
Location_base_pair Starts at 3658037 and ends at 3717524 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping TRAP1.png]
Local_order Genes flanking TRAP1 (from telomere to centromere):
- NLRC3: 16p13.3, NLR family, CARD domain containing 3;
- : 16p13.3, BTB (POZ) domain containing 12;
- DNASEI: 16p13.3, Deoxyribonuclease I;
- TRAP-1;
- CREBBP: 16p13.3, CREB binding protein;
- ADCY9: 16p13.3, adenylate cyclase 9;
- SRL: 16p13.3, sarcalumenin.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
HNRNPH1 (5q35.3)::TRAP1 (16p13.3)KIF13B (8p12)::TRAP1 (16p13.3)TRAP1 (16p13.3)::PODXL (7q32.3)
Note TRAP-1 gene encodes for an intra-mitochondrial protein highly homolog to members of the Hsp90 family which play a fundamental role in protein folding, protein degradation and signal transduction. TRAP1 is highly conserved through evolution, binds ATP and exhibits an ATPase activity that is inhibited by both geldanamycin and radicicol.


  Map of the chromosome 16p13.3 region showing the in scale position of the TRAP1 gene and its organization in exons (purple boxes) and introns (blue lines).
Description According to the NCBI map viewer, TRAP1 gene maps to NC_000016.9 and encompasses about 60 Kb. The gene contains 18 exons.
Transcription The mRNA is 2263 bp long.
Pseudogene No TRAP1 pseudogenes were reported in human.


  Schematic representation of the domain organization of TRAP1 protein (Data from SwissProt, InterPro, Ensembl).
Description TRAP1 has a molecular weight of 80110 Da and consists of 704 amino acid residues. It contains a N-terminal domain (transit peptide) required for its transport from cytoplasm to mitochondria, a middle domain involved in ATPase activity, a charged domain, and a C-terminal domain. Of note, it lacks the charged domain found immediately after the N-terminal domain in other HSP90 proteins. It contains four ATP binding sites in 119, 158, 171 and 205 position. TRAP1 undergoes to following post translational modifications:
- N6-acetyllysine in 87, 332, 382, 424, 466 position;
- phosphotyrosine in 366 position;
- phosphoserine in 401 position;
- phosphothreonine in 494 position.
Expression Northern blot analysis has revealed that the protein is expressed, although at different levels, in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.
Localisation TRAP1 is located in mitochondria, although immunoelectron microscopy has been provided evidence that it can also be found at specific extramitochondrial sites (pancreatic zymogen granules, insulin secretory granules, cardiac sarcomeres, nuclei of pancreatic and heart cells and cell surface of blood vessel endothelial cells).
Function TRAP1 binds the intracellular N-terminal half of the tumor necrosis factor receptor (TNFR1) and, thus, it is involved in signal transduction pathways TNFR-1-mediated. Through these pathways TRAP1 up-regulates the expression of different genes, such as those involved in cell cycle, cell motility and metastatic spread. In particular, in the brain the interaction TRAP1-TNFR1 is involved in modulating the expression of the N-cadherin, that is downregulated in TRAP1 knockdown cells, and in regulating the inter-cellular adhesion and synaptic morphology of neuronal cells. TRAP1 interacts, by means of a LxCxE motif, also with the T antigen-binding domain of the retinoblastoma protein (Rb), during the mitosis and after heat shock promoting in vitro the refolding of RB, and with the tumor suppressor EXT1 and EXT2, and the mitochondrial ribosomal protein S12 3'-UTR. In contrast with Hsp90 protein, TRAP1 does not associate with the classic Hsp90 co-chaperones p23 and Hop (p60). Recently, it has been demonstrated that TRAP1 is an in vitro substrate of PARPs (Poly(ADP-ribose) polymerases). PARPs catalyze the transfer of adenine phosphate ribose units from NAD to proteins and are involved in DNA repair, transcription, mitosis and telomere length maintenance.

TRAP1 plays an important role in protecting cells against oxidative stress and apoptosis. To this purpose it has been observed that TRAP1 suppression in mitochondria induces the apoptosis process by means of ROS production. What is more TRAP1 overexpression decreases ROS production and preserves mitochondrial membrane potential during the ischemia-like condition of glucose deprivation and preserves ATP levels and cell viability during oxygen-glucose deprivation. TRAP1 protects cells from granzyme M-mediated apoptosis by preventing the accumulation of ROS. The cleavage of TRAP1 by the granzyme abolishes its antagonistic function to ROS, and leads to ROS accumulation. It has been proposed that mitochondrial homeostasis is differentially regulated in tumor versus normal cells, in part due to elevated expression of TRAP1 in mitochondria. The overexpression of TRAP1 might buffer mitochondrial proteins from direct damage caused by exposure to prolonged oxidative stress. To this regard, it was reported that TRAP1 is a member of a prosurvival mitochondrial pathway highly activated in tumor cells that antagonizes the proapototic activity of cyclophilin D (CypD), a protein involved in the regulation of the mitochondrial permeability transition pore.
TRAP1-overexpression induces a decrease in levels of ROS, Caveolin-1, glutathione peroxidase (GPX), and manganese superoxide dismutase (MnSOD) as well as of the senescence-associated beta-galactosidase in cells treated with deferoxamine (DFO), an iron chelator responsible of mitochondrial dysfunction and senescence-like cellular morphology. It has been shown that TRAP1 is a MYC target, thus it may be considered involved in increased apoptosis in MYC-overexpressing cells and accountable for the elevated susceptibility of such cells to tumor necrosis factor alpha-mediated apoptosis.

Hypoxia conditions induce an up-regulation of protein levels of TRAP1 in osteoarthritic chondrocyte and in cartilage tissue, and in cardiomyocytes, in which TRAP1 plays a protective role by regulating the opening of the mitochondrial permeability transition pore.

TRAP1 is phosphorylated by PINK1, a serine/threonine protein kinase that localizes to mitochondria, and this phosphorylation mediates the PINK1 protective effects against oxidative stress-induced cell death by preventing the release of cytochrome c from mitochondria. PINK1 mutations that cause the Parkinson disease induce a reduced phosporylation of TRAP1 and thus a sensitization of the cells to the lethal effects of reactive oxygen species.

The expression of TRAP1 in heat stress conditions is modulated by the common variability of the mitochondrial DNA. In fact TRAP1 is over-expressed at both mRNA and intra-mitochondrial protein levels in cybrid line harbouring mtDNA of haplogroup H than in the other cybrid lines (lines J, U, X, T).

Homology - Canis familiaris: TRAP1 (TNF receptor-associated protein 1)
- Pan troglodytes: TRAP1 (TNF receptor-associated protein 1)
- Bos taurus: TRAP1 (TNF receptor-associated protein 1)
- Rattus norvegicus: Trap1 (TNF receptor-associated protein 1)
- Mus musculus: Trap1 (TNF receptor-associated protein 1)


Note Six SNPs in the TRAP1 gene are found associated with neurological diseases. In particular :
- schizophrenia: SNP rs2108430, T/C, intron 3;
- bipolar disorders: SNP rs6500552, T/C, intron 1;
- major depression: SNP rs1639150, T/C, intron 1; SNP rs2108430, T/C, intron 3; SNP rs13926, C/G, exon 9 (R307G); SNP rs1136948, C/G, exon 11 (D395E).

Implicated in

Entity Prostate cancer
Note It has been shown that TRAP1 is overexpressed at both mRNA and protein level in human primary and metastatic prostate cancer tissues but not expressed in normal prostate or benign prostatic hyperplasia. This up-regulation is also shown in different cell lines such as PC-3, LNCaP, 293, K562 and HeLa. Silencing of TRAP1 gene by siRNAs in prostate cancer cells induces apoptotic cell death thus giving evidence upon an antiapoptotic function of TRAP1. In presence of gamitrinibs, a Hsp90 inhibithor acting as ATPase antagonists that accumulates in the mitochondria of human tumor cell lines causing rapid tumor cell death, it is observed a complete death of prostate cancer cells but not of nontransformed BPH-1 cells. On the other hand, the introduction in these cells of TRAP1 induces the gamitrinibs-mediated cell death. By protein microarray analysis of serum from patients affected by prostate cancer, obtained before and after treatment with GM-CSF secreting whole cell immunotherapy (GVAX® immunotherapy), it was demonstrated an antibody response to TRAP1 in post-treatment samples. In particular, analysis of antibody induction in metastatic, castration-resistant prostate cancer (mCRPC) patients, individuated only from 2 of 3 phase 1/2 studies of prostate cancer immunotherapy (G-9803 and G-0010), revealed an induction of TRAP1 antibody and its association with survival time.
Entity Ovarian cancer
Note Several studies have identified TRAP1 as a potential target in ovarian cancer. In fact TRAP1 is upregulated in human cisplatin (CCDP)-resistant ovarian tumor cells, in endometrial cancer following progesterone stimulation and in estrogen receptor-positive ovarian cell lines. Moreover the TRAP1 estrogen-induced up-regulation is reversed by the anti-estrogen tamoxifen. For ovarian cancer patients treated with the aromatase inhibitor letrozole, differences in expression levels of TRAP1, such as in aromatase expression, were observed between tumors from responsive/stable patients and tumors from patients whose disease was progressing, using serum levels of CA125 marker as an indicator of response.
Entity Colorectal carcinoma
Note TRAP1 expression is up-regulated in colorectal carcinoma. In fact TRAP1 levels were increased in HT-29 colorectal carcinoma cells in which, as in other neoplastic cells, the above overexpression is involved in 5-fluorouracil-, oxaliplatin- and irinotecan-resistant phenotypes. Conversely, the inhibition of TRAP1 activity by shepherdin, a TRAP1 ATPase antagonist, has been shown to rescue the resistance to apoptosis induced by oxaliplatin and irinotecan in colorectal carcinoma cells resistant to the single agents. These results suggest that TRAP1 could be a component of a pro-survival pathway responsible for multi-drug resistance.
Entity Nasopharyngeal carcinoma
Note Microarray analysis carried out by using total RNA from 32 pathologically-confirmed cases of poorly-differentiated nasopharyngeal carcinoma (NPC) and RNA from 24 normal non-cancerous nasopharyngeal tissues (NP) have demonstrated that TRAP1 is up-regulated in NPC compared to NP, thus indentifying this protein as potential candidate biomarker in nasopharyngeal carcinoma.
Entity Lymphoma
Note In ALK-positive anaplastic large-cell lymphoma, a type of non-Hodgkin lymphoma, the knockdown of TRAP1 determine cell death induced by TRAIL or doxorubicin. Expression levels of TRAP1 has been shown increased in EBV infected B cells and, since this infection resulted in the induction of ROS in Burkitt's lymphoma, it was suggested that over-expression of TRAP1 play a role in the protection of the EBV infected cells against ROS and apoptosis.


Mitochondrial dysregulation of osteoarthritic human articular chondrocytes analyzed by proteomics: a decrease in mitochondrial superoxide dismutase points to a redox imbalance.
Ruiz-Romero C, Calamia V, Mateos J, Carreira V, Martinez-Gomariz M, Fernandez M, Blanco FJ.
Mol Cell Proteomics. 2009 Jan;8(1):172-89. Epub 2008 Sep 9.
PMID 18784066
Mitochondrial DNA variability modulates mRNA and intra-mitochondrial protein levels of HSP60 and HSP75: experimental evidence from cybrid lines.
Bellizzi D, Taverna D, D'Aquila P, De Blasi S, De Benedictis G.
Cell Stress Chaperones. 2009 May;14(3):265-71. Epub 2008 Sep 25.
PMID 18815895
Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites.
Cechetto JD, Gupta RS.
Exp Cell Res. 2000 Oct 10;260(1):30-9.
PMID 11010808
The HSP90 family of genes in the human genome: insights into their divergence and evolution.
Chen B, Piel WH, Gui L, Bruford E, Monteiro A.
Genomics. 2005 Dec;86(6):627-37. Epub 2005 Nov 2.
PMID 16269234
A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock.
Chen CF, Chen Y, Dai K, Chen PL, Riley DJ, Lee WH.
Mol Cell Biol. 1996 Sep;16(9):4691-9.
PMID 8756626
Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion.
Coller HA, Grandori C, Tamayo P, Colbert T, Lander ES, Eisenman RN, Golub TR.
Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3260-5.
PMID 10737792
Transcriptional patterns, biomarkers and pathways characterizing nasopharyngeal carcinoma of Southern China.
Fang W, Li X, Jiang Q, Liu Z, Yang H, Wang S, Xie S, Liu Q, Liu T, Huang J, Xie W, Li Z, Zhao Y, Wang E, Marincola FM, Yao K.
J Transl Med. 2008 Jun 20;6:32.
PMID 18570662
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties.
Felts SJ, Owen BA, Nguyen P, Trepel J, Donner DB, Toft DO.
J Biol Chem. 2000 Feb 4;275(5):3305-12.
PMID 10652318
Heat shock protein 75 (TRAP1) antagonizes reactive oxygen species generation and protects cells from granzyme M-mediated apoptosis.
Hua G, Zhang Q, Fan Z.
J Biol Chem. 2007 Jul 13;282(28):20553-60. Epub 2007 May 18.
PMID 17513296
Iron chelation study in a normal human hepatocyte cell line suggests that tumor necrosis factor receptor-associated protein 1 (TRAP1) regulates production of reactive oxygen species.
Im CN, Lee JS, Zheng Y, Seo JS.
J Cell Biochem. 2007 Feb 1;100(2):474-86.
PMID 16927372
Identification of tumor necrosis factor signaling-related proteins during Epstein-Barr virus-induced B cell transformation.
Jeon JP, Kim JW, Park B, Nam HY, Shim SM, Lee MH, Han BG.
Acta Virol. 2008;52(3):151-9.
PMID 18999889
Clickable NAD analogues for labeling substrate proteins of poly(ADP-ribose) polymerases.
Jiang H, Kim JH, Frizzell KM, Kraus WL, Lin H.
J Am Chem Soc. 2010 Jul 14;132(27):9363-72.
PMID 20560583
Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network.
Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ, Altieri DC.
Cell. 2007 Oct 19;131(2):257-70.
PMID 17956728
Tumor necrosis factor receptor-associated protein 1 regulates cell adhesion and synaptic morphology via modulation of N-cadherin expression.
Kubota K, Inoue K, Hashimoto R, Kumamoto N, Kosuga A, Tatsumi M, Kamijima K, Kunugi H, Iwata N, Ozaki N, Takeda M, Tohyama M.
J Neurochem. 2009 Jul;110(2):496-508. Epub 2009 Apr 20.
PMID 19490362
Heat shock proteins, cell survival and drug resistance: the mitochondrial chaperone TRAP1, a potential novel target for ovarian cancer therapy.
Landriscina M, Amoroso MR, Piscazzi A, Esposito F.
Gynecol Oncol. 2010 May;117(2):177-82. Epub 2009 Nov 25. (REVIEW)
PMID 19942270
Cytoprotective mitochondrial chaperone TRAP-1 as a novel molecular target in localized and metastatic prostate cancer.
Leav I, Plescia J, Goel HL, Li J, Jiang Z, Cohen RJ, Languino LR, Altieri DC.
Am J Pathol. 2010 Jan;176(1):393-401. Epub 2009 Nov 30.
PMID 19948822
Tumor necrosis factor receptor-associated protein 1(TRAP1) regulates genes involved in cell cycle and metastases.
Liu D, Hu J, Agorreta J, Cesario A, Zhang Y, Harris AL, Gatter K, Pezzella F.
Cancer Lett. 2010 Oct 28;296(2):194-205. Epub 2010 May 14.
PMID 20471161
Altered ErbB receptor signaling and gene expression in cisplatin-resistant ovarian cancer.
Macleod K, Mullen P, Sewell J, Rabiasz G, Lawrie S, Miller E, Smyth JF, Langdon SP.
Cancer Res. 2005 Aug 1;65(15):6789-800.
PMID 16061661
Involvement of tumor necrosis factor receptor-associated protein 1 (TRAP1) in apoptosis induced by beta-hydroxyisovalerylshikonin.
Masuda Y, Shima G, Aiuchi T, Horie M, Hori K, Nakajo S, Kajimoto S, Shibayama-Imazu T, Nakaya K.
J Biol Chem. 2004 Oct 8;279(41):42503-15. Epub 2004 Jul 28.
PMID 15292218
Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis.
Montesano Gesualdi N, Chirico G, Pirozzi G, Costantino E, Landriscina M, Esposito F.
Stress. 2007 Nov;10(4):342-50.
PMID 17853063
PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1.
Pridgeon JW, Olzmann JA, Chin LS, Li L.
PLoS Biol. 2007 Jul;5(7):e172. Epub 2007 Jun 19.
PMID 17579517
Hypoxia conditions differentially modulate human normal and osteoarthritic chondrocyte proteomes.
Ruiz-Romero C, Calamia V, Rocha B, Mateos J, Fernandez-Puente P, Blanco FJ.
J Proteome Res. 2010 Jun 4;9(6):3035-45.
PMID 20387907
cis-acting sequences and trans-acting factors in the localization of mRNA for mitochondrial ribosomal proteins.
Russo A, Cirulli C, Amoresano A, Pucci P, Pietropaolo C, Russo G.
Biochim Biophys Acta. 2008 Dec;1779(12):820-9. Epub 2008 Aug 23.
PMID 18790094
Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor.
Song HY, Dunbar JD, Zhang YX, Guo D, Donner DB.
J Biol Chem. 1995 Feb 24;270(8):3574-81.
PMID 7876093
Overexpression of mitochondrial Hsp70/Hsp75 protects astrocytes against ischemic injury in vitro.
Voloboueva LA, Duan M, Ouyang Y, Emery JF, Stoy C, Giffard RG.
J Cereb Blood Flow Metab. 2008 May;28(5):1009-16. Epub 2007 Dec 19.
PMID 18091755
Estrogen-regulated gene expression predicts response to endocrine therapy in patients with ovarian cancer.
Walker G, MacLeod K, Williams AR, Cameron DA, Smyth JF, Langdon SP.
Gynecol Oncol. 2007 Sep;106(3):461-8. Epub 2007 Jul 10.
PMID 17624412
Studies of phosphoproteomic changes induced by nucleophosmin-anaplastic lymphoma kinase (ALK) highlight deregulation of tumor necrosis factor (TNF)/Fas/TNF-related apoptosis-induced ligand signaling pathway in ALK-positive anaplastic large cell lymphoma.
Wu F, Wang P, Zhang J, Young LC, Lai R, Li L.
Mol Cell Proteomics. 2010 Jul;9(7):1616-32. Epub 2010 Apr 14.
PMID 20393185
Mitochondrial chaperone tumour necrosis factor receptor-associated protein 1 protects cardiomyocytes from hypoxic injury by regulating mitochondrial permeability transition pore opening.
Xiang F, Huang YS, Shi XH, Zhang Q.
FEBS J. 2010 Apr;277(8):1929-38. Epub 2010 Mar 3.
PMID 20236315


This paper should be referenced as such :
Bellizzi, D ; Passarino, G
TRAP1 (TNF receptor-associated protein 1)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(4):347-351.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)TRAP1   16264
Entrez_Gene (NCBI)TRAP1    TNF receptor associated protein 1
AliasesHSP; HSP75; HSP90L; TRAP-1
GeneCards (Weizmann)TRAP1
Ensembl hg19 (Hinxton)ENSG00000126602 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000126602 [Gene_View]  ENSG00000126602 [Sequence]  chr16:3658037-3717524 [Contig_View]  TRAP1 [Vega]
ICGC DataPortalENSG00000126602
TCGA cBioPortalTRAP1
Genatlas (Paris)TRAP1
SOURCE (Princeton)TRAP1
Genetics Home Reference (NIH)TRAP1
Genomic and cartography
GoldenPath hg38 (UCSC)TRAP1  -     chr16:3658037-3717524 -  16p13.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TRAP1  -     16p13.3   [Description]    (hg19-Feb_2009)
GoldenPathTRAP1 - 16p13.3 [CytoView hg19]  TRAP1 - 16p13.3 [CytoView hg38]
Genome Data Viewer NCBITRAP1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB209805 AF043254 AF154108 AJ890085 AK057620
RefSeq transcript (Entrez)NM_001272049 NM_016292
Consensus coding sequences : CCDS (NCBI)TRAP1
Gene ExpressionTRAP1 [ NCBI-GEO ]   TRAP1 [ EBI - ARRAY_EXPRESS ]   TRAP1 [ SEEK ]   TRAP1 [ MEM ]
Gene Expression Viewer (FireBrowse)TRAP1 [ Firebrowse - Broad ]
GenevisibleExpression of TRAP1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10131
GTEX Portal (Tissue expression)TRAP1
Human Protein AtlasENSG00000126602-TRAP1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ12931   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ12931  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ12931
Domains : Interpro (EBI)HATPase_C    HATPase_C_sf    HSP90_C    Hsp90_fam    Hsp90_N    Ribosomal_S5_D2-typ_fold   
Domain families : Pfam (Sanger)HSP90 (PF00183)   
Domain families : Pfam (NCBI)pfam00183   
Domain families : Smart (EMBL)HATPase_c (SM00387)  
Conserved Domain (NCBI)TRAP1
PDB (RSDB)4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
PDB Europe4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
PDB (PDBSum)4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
PDB (IMB)4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
Structural Biology KnowledgeBase4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
SCOP (Structural Classification of Proteins)4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
CATH (Classification of proteins structures)4Z1F    4Z1G    4Z1H    4Z1I    5F3K    5F5R    5HPH    5Y3N    5Y3O    6XG6    7C04    7C05   
AlphaFold pdb e-kbQ12931   
Human Protein Atlas [tissue]ENSG00000126602-TRAP1 [tissue]
Protein Interaction databases
IntAct (EBI)Q12931
Ontologies - Pathways
Ontology : AmiGORNA binding  tumor necrosis factor receptor binding  protein binding  ATP binding  nucleoplasm  mitochondrion  mitochondrial inner membrane  mitochondrial inner membrane  mitochondrial intermembrane space  mitochondrial matrix  protein folding  translational attenuation  membrane  protein kinase binding  protein kinase binding  unfolded protein binding  chaperone-mediated protein folding  negative regulation of cellular respiration  negative regulation of reactive oxygen species biosynthetic process  negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide  
Ontology : EGO-EBIRNA binding  tumor necrosis factor receptor binding  protein binding  ATP binding  nucleoplasm  mitochondrion  mitochondrial inner membrane  mitochondrial inner membrane  mitochondrial intermembrane space  mitochondrial matrix  protein folding  translational attenuation  membrane  protein kinase binding  protein kinase binding  unfolded protein binding  chaperone-mediated protein folding  negative regulation of cellular respiration  negative regulation of reactive oxygen species biosynthetic process  negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide  
REACTOMEQ12931 [protein]
REACTOME PathwaysR-HSA-611105 [pathway]   
NDEx NetworkTRAP1
Atlas of Cancer Signalling NetworkTRAP1
Wikipedia pathwaysTRAP1
Orthology - Evolution
GeneTree (enSembl)ENSG00000126602
Phylogenetic Trees/Animal Genes : TreeFamTRAP1
Homologs : HomoloGeneTRAP1
Homology/Alignments : Family Browser (UCSC)TRAP1
Gene fusions - Rearrangements
Fusion : QuiverTRAP1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTRAP1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TRAP1
Exome Variant ServerTRAP1
GNOMAD BrowserENSG00000126602
Varsome BrowserTRAP1
ACMGTRAP1 variants
Genomic Variants (DGV)TRAP1 [DGVbeta]
DECIPHERTRAP1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTRAP1 
ICGC Data PortalTRAP1 
TCGA Data PortalTRAP1 
Broad Tumor PortalTRAP1
OASIS PortalTRAP1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTRAP1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DTRAP1
Mutations and Diseases : HGMDTRAP1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)TRAP1
DoCM (Curated mutations)TRAP1
CIViC (Clinical Interpretations of Variants in Cancer)TRAP1
NCG (London)TRAP1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry TRAP1
NextProtQ12931 [Medical]
Target ValidationTRAP1
Huge Navigator TRAP1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDTRAP1
Pharm GKB GenePA36781
Clinical trialTRAP1
DataMed IndexTRAP1
PubMed171 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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