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Q9UL52

- TM11E_HUMAN

UniProt

Q9UL52 - TM11E_HUMAN

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Protein

Transmembrane protease serine 11E

Gene

TMPRSS11E

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

Functioni

Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (By similarity).By similarity

Enzyme regulationi

Inhibited by SERPINA5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321Charge relay system1 Publication
Active sitei277 – 2771Charge relay system1 Publication
Active sitei373 – 3731Charge relay system1 Publication

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. cognition Source: UniProt
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane protease serine 11E (EC:3.4.21.-)
Alternative name(s):
Serine protease DESC1
Transmembrane protease serine 11E2
Cleaved into the following 2 chains:
Gene namesi
Name:TMPRSS11E
Synonyms:DESC1, TMPRSS11E2
ORF Names:UNQ742/PRO1461
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:24465. TMPRSS11E.

Subcellular locationi

Transmembrane protease serine 11E catalytic chain : Secreted By similarity
Note: Activated by cleavage and secreted.By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670729.
PA162406637.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Transmembrane protease serine 11E non-catalytic chainSequence AnalysisPRO_0000027891Add
BLAST
Chaini192 – 423232Transmembrane protease serine 11E catalytic chainSequence AnalysisPRO_0000027892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi177 ↔ 297Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
Disulfide bondi217 ↔ 2331 PublicationPROSITE-ProRule annotation
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi342 ↔ 3581 PublicationPROSITE-ProRule annotation
Disulfide bondi369 ↔ 3981 PublicationPROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9UL52.
PRIDEiQ9UL52.

PTM databases

PhosphoSiteiQ9UL52.

Expressioni

Tissue specificityi

Expression can only be detected in tissues derived from the head and neck, and in skin, prostate and testis.1 Publication

Gene expression databases

BgeeiQ9UL52.
CleanExiHS_TMPRSS11E.
ExpressionAtlasiQ9UL52. baseline and differential.
GenevestigatoriQ9UL52.

Organism-specific databases

HPAiHPA051062.

Interactioni

Subunit structurei

Forms a heterodimer with SERPINA5 and SERPINE1.

Protein-protein interaction databases

STRINGi9606.ENSP00000307519.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi206 – 2116Combined sources
Beta strandi214 – 22310Combined sources
Beta strandi226 – 2294Combined sources
Helixi231 – 2344Combined sources
Helixi240 – 2423Combined sources
Beta strandi243 – 2519Combined sources
Beta strandi255 – 26511Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi310 – 3167Combined sources
Beta strandi330 – 3378Combined sources
Helixi339 – 3424Combined sources
Turni345 – 3506Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi376 – 3805Combined sources
Beta strandi386 – 3949Combined sources
Beta strandi396 – 4005Combined sources
Beta strandi405 – 4095Combined sources
Helixi411 – 4133Combined sources
Helixi414 – 4218Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OQ5X-ray1.61A192-423[»]
ProteinModelPortaliQ9UL52.
SMRiQ9UL52. Positions 48-124, 164-423.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UL52.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini41 – 423383ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 167119SEAPROSITE-ProRule annotationAdd
BLAST
Domaini192 – 422231Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ9UL52.
KOiK09642.
OMAiYEGISKC.
OrthoDBiEOG75B84T.
PhylomeDBiQ9UL52.
TreeFamiTF351684.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEiPS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UL52 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMYRPDVVRA RKRVCWEPWV IGLVIFISLI VLAVCIGLTV HYVRYNQKKT
60 70 80 90 100
YNYYSTLSFT TDKLYAEFGR EASNNFTEMS QRLESMVKNA FYKSPLREEF
110 120 130 140 150
VKSQVIKFSQ QKHGVLAHML LICRFHSTED PETVDKIVQL VLHEKLQDAV
160 170 180 190 200
GPPKVDPHSV KIKKINKTET DSYLNHCCGT RRSKTLGQSL RIVGGTEVEE
210 220 230 240 250
GEWPWQASLQ WDGSHRCGAT LINATWLVSA AHCFTTYKNP ARWTASFGVT
260 270 280 290 300
IKPSKMKRGL RRIIVHEKYK HPSHDYDISL AELSSPVPYT NAVHRVCLPD
310 320 330 340 350
ASYEFQPGDV MFVTGFGALK NDGYSQNHLR QAQVTLIDAT TCNEPQAYND
360 370 380 390 400
AITPRMLCAG SLEGKTDACQ GDSGGPLVSS DARDIWYLAG IVSWGDECAK
410 420
PNKPGVYTRV TALRDWITSK TGI
Length:423
Mass (Da):47,696
Last modified:January 4, 2005 - v2
Checksum:iEB1476807C0B613D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581H → Q in AC019173. (PubMed:15815621)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031Y → C.
Corresponds to variant rs976002 [ dbSNP | Ensembl ].
VAR_051847

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064819 mRNA. Translation: AAF04328.1.
AY359017 mRNA. Translation: AAQ89376.1.
AC140484 Genomic DNA. No translation available.
AC019173 Genomic DNA. No translation available.
BC113412 mRNA. Translation: AAI13413.1.
BC113414 mRNA. Translation: AAI13415.1.
CCDSiCCDS33993.1.
RefSeqiNP_054777.2. NM_014058.3.
UniGeneiHs.201877.

Genome annotation databases

EnsembliENST00000305363; ENSP00000307519; ENSG00000087128.
GeneIDi28983.
KEGGihsa:28983.
UCSCiuc003hdz.4. human.

Polymorphism databases

DMDMi57015324.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064819 mRNA. Translation: AAF04328.1 .
AY359017 mRNA. Translation: AAQ89376.1 .
AC140484 Genomic DNA. No translation available.
AC019173 Genomic DNA. No translation available.
BC113412 mRNA. Translation: AAI13413.1 .
BC113414 mRNA. Translation: AAI13415.1 .
CCDSi CCDS33993.1.
RefSeqi NP_054777.2. NM_014058.3.
UniGenei Hs.201877.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OQ5 X-ray 1.61 A 192-423 [» ]
ProteinModelPortali Q9UL52.
SMRi Q9UL52. Positions 48-124, 164-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000307519.

Protein family/group databases

MEROPSi S01.021.

PTM databases

PhosphoSitei Q9UL52.

Polymorphism databases

DMDMi 57015324.

Proteomic databases

PaxDbi Q9UL52.
PRIDEi Q9UL52.

Protocols and materials databases

DNASUi 28983.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305363 ; ENSP00000307519 ; ENSG00000087128 .
GeneIDi 28983.
KEGGi hsa:28983.
UCSCi uc003hdz.4. human.

Organism-specific databases

CTDi 28983.
GeneCardsi GC04P069313.
HGNCi HGNC:24465. TMPRSS11E.
HPAi HPA051062.
MIMi 610399. gene.
neXtProti NX_Q9UL52.
PharmGKBi PA142670729.
PA162406637.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118962.
HOGENOMi HOG000251823.
HOVERGENi HBG013304.
InParanoidi Q9UL52.
KOi K09642.
OMAi YEGISKC.
OrthoDBi EOG75B84T.
PhylomeDBi Q9UL52.
TreeFami TF351684.

Miscellaneous databases

EvolutionaryTracei Q9UL52.
GenomeRNAii 28983.
NextBioi 51877.
PROi Q9UL52.
SOURCEi Search...

Gene expression databases

Bgeei Q9UL52.
CleanExi HS_TMPRSS11E.
ExpressionAtlasi Q9UL52. baseline and differential.
Genevestigatori Q9UL52.

Family and domain databases

Gene3Di 3.30.70.960. 1 hit.
InterProi IPR017329. Pept_S1A_HAT/DESC1.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEi PS50024. SEA. 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. "Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck."
    Lang J.C., Schuller D.E.
    Br. J. Cancer 84:237-243(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. "Regulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinoma."
    Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K., Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.
    Int. J. Cancer 108:516-523(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
  6. "Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family."
    Kyrieleis O.J., Huber R., Ong E., Oehler R., Hunter M., Madison E.L., Jacob U.
    FEBS J. 274:2148-2160(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 192-423, ACTIVE SITE, DISULFIDE BONDS.

Entry informationi

Entry nameiTM11E_HUMAN
AccessioniPrimary (citable) accession number: Q9UL52
Secondary accession number(s): A6NL71, Q14DC8, Q6UW31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 4, 2005
Last modified: October 29, 2014
This is version 124 of the entry and version 2 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

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3