| Tchem | Transmembrane protease serine 2 |
Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.
This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2008]
This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2008]
Comments
| Disease | Target Count |
|---|---|
| Down syndrome | 548 |
| Muscle Weakness | 92 |
| Prostatic Neoplasms | 471 |
| Disease | Target Count | P-value |
|---|---|---|
| lung carcinoma | 2844 | 7.95645919593272E-49 |
| psoriasis | 6685 | 4.05832561412406E-22 |
| non-small cell lung cancer | 2798 | 3.67712623963654E-12 |
| ovarian cancer | 8492 | 2.16764708847169E-9 |
| osteosarcoma | 7933 | 8.52486648275131E-8 |
| Breast cancer | 3099 | 4.51192215678621E-7 |
| lung adenocarcinoma | 2714 | 8.23492730765393E-7 |
| nasopharyngeal carcinoma | 1056 | 5.40438460362716E-6 |
| interstitial cystitis | 2299 | 1.90862589135466E-5 |
| lung cancer | 4473 | 3.15206386279433E-5 |
| medulloblastoma, large-cell | 6234 | 1.68924178059642E-4 |
| adult high grade glioma | 2148 | 0.00158746279059501 |
| intraductal papillary-mucinous neoplasm (IPMN) | 3289 | 0.00278001018350946 |
| gastric carcinoma | 832 | 0.0399415993706637 |
| Disease | log2 FC | p |
|---|---|---|
| osteosarcoma | 1.670 | 0.000 |
| medulloblastoma, large-cell | 1.100 | 0.000 |
| non-small cell lung cancer | -1.884 | 0.000 |
| intraductal papillary-mucinous neoplasm ... | 1.400 | 0.003 |
| lung cancer | -3.700 | 0.000 |
| interstitial cystitis | -3.300 | 0.000 |
| lung adenocarcinoma | -1.500 | 0.000 |
| adult high grade glioma | 1.100 | 0.002 |
| nasopharyngeal carcinoma | -1.300 | 0.000 |
| Breast cancer | -1.400 | 0.000 |
| lung carcinoma | -4.400 | 0.000 |
| gastric carcinoma | -1.900 | 0.040 |
| ovarian cancer | 1.700 | 0.000 |
| psoriasis | -1.400 | 0.000 |
| Species | Source |
|---|---|
| Chimp | OMA EggNOG |
| Macaque | OMA EggNOG |
| Mouse | OMA EggNOG Inparanoid |
| Rat | OMA EggNOG Inparanoid |
| Dog | OMA EggNOG |
| Horse | OMA EggNOG Inparanoid |
| Cow | OMA EggNOG Inparanoid |
| Opossum | OMA EggNOG Inparanoid |
| Platypus | EggNOG Inparanoid |
| Chicken | OMA Inparanoid |
| Anole lizard | OMA Inparanoid |
| PMID | Text |
|---|---|
| 27028521 | the type II transmembrane serine protease TMPRSS2 was able to activate hemagglutinin for cell entry indicating that bat influenza A virus can utilize human proteases for hemagglutinin activation. |
| 26978019 | The relatively low rate of ERG-positive prostatic intraepithelial neoplasia counts in favor of the limited role of chimeric transcript TMPRSS2/ERG in the differential diagnosis of prostatic intraepithelial neoplasia |
| 26615022 | The potential for TMPRSS2:ERG gene fusion, detected by IHC, to modify the role of PTEN loss in lethal progression of prostate cancer. |
| 26503111 | Aspirin was associated with a significant reduction in the relative risk of TMPRSS2:ERG (T2E )fusion positive, but not T2E negative |
| 26424596 | Results indicate that PTEN loss occurs in cooperation with TMPRSS2-ERG fusion in prostate cancer and the majority of the samples harbor TMPRSS2-ERG fusion as well as PTEN gene deletion. |
| 26379044 | TMPRSS2 isoform 1 is expressed in viral target cells. |
| 26251449 | Membrane bound meprin Beta is activated by transmembrane serine protease matriptase-2 at the cell surface. |
| 26026052 | The TMPRSS2-ERG Gene Fusion Blocks XRCC4-Mediated Nonhomologous End-Joining Repair and Radiosensitizes Prostate Cancer Cells to PARP Inhibition |
| 26018085 | TMPRSS2 promotes the growth, invasion, and metastasis of prostate cancer cells via matriptase activation and extracellular matrix disruption. |
| 25977336 | Analysis of prostate cancer tissues showed that the presence of a TMPRSS2-ERG rearrangement was highly correlated with lower levels of NKX3.1 expression consistent with the role of NKX3.1 as a suppressor of the pathogenic gene rearrangement. |
| More... |
MALNSGSPPAIGPYYENHGYQPENPYPAQPTVVPTVYEVHPAQYYPSPVPQYAPRVLTQASNPVVCTQPK 1 - 70 SPSGTVCTSKTKKALCITLTLGTFLVGAALAAGLLWKFMGSKCSNSGIECDSSGTCINPSNWCDGVSHCP 71 - 140 GGEDENRCVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSGSTSFM 141 - 210 KLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSSRQSRIVGGESALPGAWPWQVSLHVQNVHV 211 - 280 CGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGILRQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMK 281 - 350 LQKPLTFNDLVKPVCLPNPGMMLQPEQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLI 351 - 420 TPAMICAGFLQGNVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRA 421 - 490 DG 491 - 492 //
| PMID | Year | Title |
|---|---|---|
| 27028521 | 2016 | The Hemagglutinin of Bat-Associated Influenza Viruses Is Activated by TMPRSS2 for pH-Dependent Entry into Bat but Not Human Cells. |
| 26978019 | [Diagnostic value of estimation of ERG expression in prostate adenocarcinoma and high-grade prostatic intraepithelial neoplasia]. | |
| 26615022 | 2016 | A Prospective Investigation of PTEN Loss and ERG Expression in Lethal Prostate Cancer. |
| 26503111 | 2016 | Aspirin and NSAID use in association with molecular subtypes of prostate cancer defined by TMPRSS2:ERG fusion status. |
| 26424596 | 2016 | Frequency of PTEN alterations, TMPRSS2-ERG fusion and their association in prostate cancer. |
| 26379044 | 2015 | TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells. |
| 26251449 | 2015 | Metalloprotease meprin ? is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding. |
| 26026052 | 2015 | The TMPRSS2-ERG Gene Fusion Blocks XRCC4-Mediated Nonhomologous End-Joining Repair and Radiosensitizes Prostate Cancer Cells to PARP Inhibition. |
| 26018085 | 2015 | Androgen-Induced TMPRSS2 Activates Matriptase and Promotes Extracellular Matrix Degradation, Prostate Cancer Cell Invasion, Tumor Growth, and Metastasis. |
| 25977336 | 2015 | NKX3.1 Suppresses TMPRSS2-ERG Gene Rearrangement and Mediates Repair of Androgen Receptor-Induced DNA Damage. |
| More... |
