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O15393

- TMPS2_HUMAN

UniProt

O15393 - TMPS2_HUMAN

Protein

Transmembrane protease serine 2

Gene

TMPRSS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei255 – 2562CleavageSequence Analysis
    Active sitei296 – 2961Charge relay systemBy similarity
    Active sitei345 – 3451Charge relay systemBy similarity
    Active sitei441 – 4411Charge relay system

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. scavenger receptor activity Source: InterPro
    3. serine-type endopeptidase activity Source: InterPro
    4. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. positive regulation of viral entry into host cell Source: UniProtKB
    2. protein autoprocessing Source: UniProtKB
    3. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.247.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transmembrane protease serine 2 (EC:3.4.21.-)
    Alternative name(s):
    Serine protease 10
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TMPRSS2
    Synonyms:PRSS10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:11876. TMPRSS2.

    Subcellular locationi

    Cell membrane 2 Publications; Single-pass type II membrane protein 2 Publications
    Transmembrane protease serine 2 catalytic chain : Secreted
    Note: Activated by cleavage and secreted.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi255 – 2551R → Q: Loss of cleavage. 1 Publication
    Mutagenesisi441 – 4411S → A: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA36577.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 255255Transmembrane protease serine 2 non-catalytic chainPRO_0000027855Add
    BLAST
    Chaini256 – 492237Transmembrane protease serine 2 catalytic chainPRO_0000027856Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi113 ↔ 126By similarity
    Disulfide bondi120 ↔ 139By similarity
    Disulfide bondi133 ↔ 148By similarity
    Disulfide bondi172 ↔ 231By similarity
    Disulfide bondi185 ↔ 241By similarity
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi244 ↔ 365Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi281 ↔ 297By similarity
    Disulfide bondi410 ↔ 426By similarity
    Disulfide bondi437 ↔ 465By similarity

    Post-translational modificationi

    Proteolytically processed; by an autocatalytic mechanism.

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiO15393.
    PaxDbiO15393.
    PRIDEiO15393.

    PTM databases

    PhosphoSiteiO15393.

    Expressioni

    Tissue specificityi

    Highly expressed in prostate epithelial cells and in prostate cancers. Expressed in type II pneumocytes in the lung (at protein level). Expressed strongly in small intestine. Also expressed in colon, stomach and salivary gland.3 Publications

    Gene expression databases

    ArrayExpressiO15393.
    BgeeiO15393.
    CleanExiHS_TMPRSS2.
    GenevestigatoriO15393.

    Organism-specific databases

    HPAiHPA013182.

    Interactioni

    Subunit structurei

    The catalytically active form interacts with ACE2.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000330330.

    Structurei

    3D structure databases

    ProteinModelPortaliO15393.
    SMRiO15393. Positions 158-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8484CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini106 – 492387ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei85 – 10521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 14938LDL-receptor class APROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 24293SRCRPROSITE-ProRule annotationAdd
    BLAST
    Domaini256 – 489234Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 LDL-receptor class A domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 1 SRCR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG013304.
    KOiK09633.
    OMAiKSWHPVC.
    OrthoDBiEOG75B84T.
    PhylomeDBiO15393.
    TreeFamiTF351678.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    4.10.400.10. 1 hit.
    InterProiIPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00192. LDLa. 1 hit.
    SM00202. SR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    SSF57424. SSF57424. 1 hit.
    PROSITEiPS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS50287. SRCR_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15393-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALNSGSPPA IGPYYENHGY QPENPYPAQP TVVPTVYEVH PAQYYPSPVP    50
    QYAPRVLTQA SNPVVCTQPK SPSGTVCTSK TKKALCITLT LGTFLVGAAL 100
    AAGLLWKFMG SKCSNSGIEC DSSGTCINPS NWCDGVSHCP GGEDENRCVR 150
    LYGPNFILQV YSSQRKSWHP VCQDDWNENY GRAACRDMGY KNNFYSSQGI 200
    VDDSGSTSFM KLNTSAGNVD IYKKLYHSDA CSSKAVVSLR CIACGVNLNS 250
    SRQSRIVGGE SALPGAWPWQ VSLHVQNVHV CGGSIITPEW IVTAAHCVEK 300
    PLNNPWHWTA FAGILRQSFM FYGAGYQVEK VISHPNYDSK TKNNDIALMK 350
    LQKPLTFNDL VKPVCLPNPG MMLQPEQLCW ISGWGATEEK GKTSEVLNAA 400
    KVLLIETQRC NSRYVYDNLI TPAMICAGFL QGNVDSCQGD SGGPLVTSKN 450
    NIWWLIGDTS WGSGCAKAYR PGVYGNVMVF TDWIYRQMRA DG 492
    Length:492
    Mass (Da):53,859
    Last modified:October 3, 2006 - v3
    Checksum:iC05B5531C8A311C7
    GO
    Isoform 2 (identifier: O15393-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPPAPPGGESGCEERGAAGHIEHSRYLSLLDAVDNSKM

    Note: No experimental confirmation available.

    Show »
    Length:529
    Mass (Da):57,690
    Checksum:i444EBB1FFF3ACDFA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261Y → H in BAF84502. (PubMed:14702039)Curated
    Sequence conflicti62 – 621N → S in BAH12445. (PubMed:14702039)Curated
    Sequence conflicti163 – 1631S → P in BAF84502. (PubMed:14702039)Curated
    Sequence conflicti242 – 2421I → L in AAC51784. (PubMed:9325052)Curated
    Sequence conflicti489 – 4913RAD → KAN in AAC51784. (PubMed:9325052)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti160 – 1601V → M.3 Publications
    Corresponds to variant rs12329760 [ dbSNP | Ensembl ].
    VAR_027674
    Natural varianti254 – 2541S → C.1 Publication
    VAR_038002
    Natural varianti329 – 3291E → Q.2 Publications
    VAR_038003
    Natural varianti449 – 4491K → N.
    Corresponds to variant rs1056602 [ dbSNP | Ensembl ].
    VAR_011692
    Natural varianti491 – 4911D → N.1 Publication
    VAR_038004

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPPAPPGGESGCEERGAAGH IEHSRYLSLLDAVDNSKM in isoform 2. 1 PublicationVSP_045083

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75329 mRNA. Translation: AAC51784.1.
    AF123453 mRNA. Translation: AAD37117.1.
    AF270487 mRNA. Translation: AAK29280.1.
    AK291813 mRNA. Translation: BAF84502.1.
    AK296860 mRNA. Translation: BAH12445.1.
    AK313338 mRNA. Translation: BAG36142.1.
    AK222784 mRNA. Translation: BAD96504.1.
    AP001610 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09597.1.
    CH471079 Genomic DNA. Translation: EAX09598.1.
    BC051839 mRNA. Translation: AAH51839.1.
    CCDSiCCDS33564.1. [O15393-1]
    CCDS54486.1. [O15393-2]
    RefSeqiNP_001128571.1. NM_001135099.1. [O15393-2]
    NP_005647.3. NM_005656.3. [O15393-1]
    UniGeneiHs.439309.

    Genome annotation databases

    EnsembliENST00000332149; ENSP00000330330; ENSG00000184012. [O15393-1]
    ENST00000398585; ENSP00000381588; ENSG00000184012. [O15393-2]
    ENST00000458356; ENSP00000391216; ENSG00000184012. [O15393-1]
    GeneIDi7113.
    KEGGihsa:7113.
    UCSCiuc002yzj.3. human. [O15393-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75329 mRNA. Translation: AAC51784.1 .
    AF123453 mRNA. Translation: AAD37117.1 .
    AF270487 mRNA. Translation: AAK29280.1 .
    AK291813 mRNA. Translation: BAF84502.1 .
    AK296860 mRNA. Translation: BAH12445.1 .
    AK313338 mRNA. Translation: BAG36142.1 .
    AK222784 mRNA. Translation: BAD96504.1 .
    AP001610 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09597.1 .
    CH471079 Genomic DNA. Translation: EAX09598.1 .
    BC051839 mRNA. Translation: AAH51839.1 .
    CCDSi CCDS33564.1. [O15393-1 ]
    CCDS54486.1. [O15393-2 ]
    RefSeqi NP_001128571.1. NM_001135099.1. [O15393-2 ]
    NP_005647.3. NM_005656.3. [O15393-1 ]
    UniGenei Hs.439309.

    3D structure databases

    ProteinModelPortali O15393.
    SMRi O15393. Positions 158-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000330330.

    Chemistry

    BindingDBi O15393.
    ChEMBLi CHEMBL1795140.

    Protein family/group databases

    MEROPSi S01.247.

    PTM databases

    PhosphoSitei O15393.

    Proteomic databases

    MaxQBi O15393.
    PaxDbi O15393.
    PRIDEi O15393.

    Protocols and materials databases

    DNASUi 7113.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332149 ; ENSP00000330330 ; ENSG00000184012 . [O15393-1 ]
    ENST00000398585 ; ENSP00000381588 ; ENSG00000184012 . [O15393-2 ]
    ENST00000458356 ; ENSP00000391216 ; ENSG00000184012 . [O15393-1 ]
    GeneIDi 7113.
    KEGGi hsa:7113.
    UCSCi uc002yzj.3. human. [O15393-1 ]

    Organism-specific databases

    CTDi 7113.
    GeneCardsi GC21M042836.
    HGNCi HGNC:11876. TMPRSS2.
    HPAi HPA013182.
    MIMi 602060. gene.
    neXtProti NX_O15393.
    PharmGKBi PA36577.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG013304.
    KOi K09633.
    OMAi KSWHPVC.
    OrthoDBi EOG75B84T.
    PhylomeDBi O15393.
    TreeFami TF351678.

    Miscellaneous databases

    ChiTaRSi TMPRSS2. human.
    GeneWikii TMPRSS2.
    GenomeRNAii 7113.
    NextBioi 27847.
    PROi O15393.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15393.
    Bgeei O15393.
    CleanExi HS_TMPRSS2.
    Genevestigatori O15393.

    Family and domain databases

    Gene3Di 3.10.250.10. 1 hit.
    4.10.400.10. 1 hit.
    InterProi IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00192. LDLa. 1 hit.
    SM00202. SR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    SSF57424. SSF57424. 1 hit.
    PROSITEi PS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS50287. SRCR_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3."
      Paoloni-Giacobino A., Chen H., Peitsch M.C., Rossier C., Antonarakis S.E.
      Genomics 44:309-320(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-160 AND GLN-329.
    2. "Mutation analyses of 268 candidate genes in human tumor cell lines."
      Teng D.-H., Chen Y., Lian L., Ha P.C., Tavtigian S.V., Wong A.K.C.
      Genomics 74:352-364(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-160.
    3. "Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia."
      Afar D.E.H., Vivanco I., Hubert R.S., Kuo J., Chen E., Saffran D.C., Raitano A.B., Jakobovits A.
      Cancer Res. 61:1686-1692(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Prostate, Testis and Tongue.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    6. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: PNS.
    9. "Expression of transmembrane serine protease TMPRSS2 in mouse and human tissues."
      Vaarala M.H., Porvari K.S., Kellokumpu S., Kyllonen A.P., Vihko P.T.
      J. Pathol. 193:134-140(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "TMPRSS2, a serine protease expressed in the prostate on the apical surface of luminal epithelial cells and released into semen in prostasomes, is misregulated in prostate cancer cells."
      Chen Y.W., Lee M.S., Lucht A., Chou F.P., Huang W., Havighurst T.C., Kim K., Wang J.K., Antalis T.M., Johnson M.D., Lin C.Y.
      Am. J. Pathol. 176:2986-2996(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    11. "A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry."
      Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., Gallagher T.
      J. Virol. 85:873-882(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOCATALYTIC CLEAVAGE, INTERACTION WITH ACE2.
    12. "Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response."
      Glowacka I., Bertram S., Muller M.A., Allen P., Soilleux E., Pfefferle S., Steffen I., Tsegaye T.S., He Y., Gnirss K., Niemeyer D., Schneider H., Drosten C., Pohlmann S.
      J. Virol. 85:4122-4134(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. "TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium."
      Bertram S., Dijkman R., Habjan M., Heurich A., Gierer S., Glowacka I., Welsch K., Winkler M., Schneider H., Hofmann-Winkler H., Thiel V., Pohlmann S.
      J. Virol. 87:6150-6160(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: FUNCTION.
    15. "Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2."
      Shirato K., Kawase M., Matsuyama S.
      J. Virol. 87:12552-12561(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
      Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
      J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss."
      Guipponi M., Toh M.-Y., Tan J., Park D., Hanson K., Ballana E., Kwong D., Cannon P.Z.F., Wu Q., Gout A., Delorenzi M., Speed T.P., Smith R.J.H., Dahl H.-H.M., Petersen M., Teasdale R.D., Estivill X., Park W.J., Scott H.S.
      Hum. Mutat. 29:130-141(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MET-160; CYS-254; GLN-329 AND ASN-491.

    Entry informationi

    Entry nameiTMPS2_HUMAN
    AccessioniPrimary (citable) accession number: O15393
    Secondary accession number(s): A8K6Z8
    , B2R8E5, B7Z459, D3DSJ2, F8WES1, Q6GTK7, Q9BXX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3