Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15393

- TMPS2_HUMAN

UniProt

O15393 - TMPS2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Transmembrane protease serine 2

Gene

TMPRSS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. scavenger receptor activity Source: InterPro
  2. serine-type endopeptidase activity Source: InterPro
  3. 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8484CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei85 – 10521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini106 – 492387ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiO15393.
CleanExiHS_TMPRSS2.
ExpressionAtlasiO15393. baseline and differential.
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...

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.
GeneTreeiENSGT00760000118962.
HOVERGENiHBG013304.
InParanoidiO15393.
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

        10         20         30         40         50
MALNSGSPPA IGPYYENHGY QPENPYPAQP TVVPTVYEVH PAQYYPSPVP
60 70 80 90 100
QYAPRVLTQA SNPVVCTQPK SPSGTVCTSK TKKALCITLT LGTFLVGAAL
110 120 130 140 150
AAGLLWKFMG SKCSNSGIEC DSSGTCINPS NWCDGVSHCP GGEDENRCVR
160 170 180 190 200
LYGPNFILQV YSSQRKSWHP VCQDDWNENY GRAACRDMGY KNNFYSSQGI
210 220 230 240 250
VDDSGSTSFM KLNTSAGNVD IYKKLYHSDA CSSKAVVSLR CIACGVNLNS
260 270 280 290 300
SRQSRIVGGE SALPGAWPWQ VSLHVQNVHV CGGSIITPEW IVTAAHCVEK
310 320 330 340 350
PLNNPWHWTA FAGILRQSFM FYGAGYQVEK VISHPNYDSK TKNNDIALMK
360 370 380 390 400
LQKPLTFNDL VKPVCLPNPG MMLQPEQLCW ISGWGATEEK GKTSEVLNAA
410 420 430 440 450
KVLLIETQRC NSRYVYDNLI TPAMICAGFL QGNVDSCQGD SGGPLVTSKN
460 470 480 490
NIWWLIGDTS WGSGCAKAYR PGVYGNVMVF TDWIYRQMRA DG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00760000118962.
HOVERGENi HBG013304.
InParanoidi O15393.
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

Bgeei O15393.
CleanExi HS_TMPRSS2.
ExpressionAtlasi O15393. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 146 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