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P20231

- TRYB2_HUMAN

UniProt

P20231 - TRYB2_HUMAN

Protein

Tryptase beta-2

Gene

TPSB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Has an immunoprotective role during bacterial infection. Required to efficiently combat K.pneumoniae infection By similarity.By similarity

    Catalytic activityi

    Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei74 – 741Charge relay system
    Active sitei121 – 1211Charge relay system
    Active sitei224 – 2241Charge relay system

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptase beta-2 (EC:3.4.21.59)
    Short name:
    Tryptase-2
    Alternative name(s):
    Tryptase II
    Gene namesi
    Name:TPSB2
    Synonyms:TPS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:14120. TPSB2.

    Subcellular locationi

    Secreted
    Note: Released from the secretory granules upon mast cell activation.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36698.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 3012Activation peptidePRO_0000027481Add
    BLAST
    Chaini31 – 275245Tryptase beta-2PRO_0000027482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi59 ↔ 75
    Modified residuei97 – 971PhosphotyrosineBy similarity
    Disulfide bondi155 ↔ 230
    Disulfide bondi188 ↔ 211
    Disulfide bondi220 ↔ 248
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

    Proteomic databases

    PaxDbiP20231.
    PRIDEiP20231.

    PTM databases

    PhosphoSiteiP20231.

    Expressioni

    Gene expression databases

    ArrayExpressiP20231.
    BgeeiP20231.
    CleanExiHS_TPSB2.
    GenevestigatoriP20231.

    Organism-specific databases

    HPAiCAB016369.
    CAB022175.
    HPA049153.
    HPA049554.

    Interactioni

    Subunit structurei

    Homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6.1 Publication

    Protein-protein interaction databases

    BioGridi113029. 1 interaction.
    122201. 1 interaction.
    IntActiP20231. 2 interactions.
    STRINGi9606.ENSP00000420825.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 365
    Beta strandi39 – 413
    Beta strandi45 – 506
    Beta strandi52 – 543
    Beta strandi56 – 6510
    Beta strandi68 – 714
    Helixi73 – 764
    Helixi83 – 853
    Beta strandi86 – 894
    Turni95 – 984
    Beta strandi102 – 1098
    Turni116 – 1183
    Beta strandi123 – 1297
    Beta strandi135 – 1373
    Beta strandi154 – 1618
    Beta strandi176 – 1838
    Helixi185 – 1939
    Beta strandi209 – 2124
    Beta strandi215 – 2184
    Turni221 – 2255
    Beta strandi227 – 2326
    Beta strandi235 – 24410
    Beta strandi246 – 2505
    Beta strandi255 – 2595
    Helixi260 – 2634
    Helixi264 – 2674
    Turni268 – 2703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A0LX-ray3.00A/B/C/D31-274[»]
    1AAOmodel-A31-275[»]
    2BM2X-ray2.20A/B/C/D31-275[»]
    2FPZX-ray2.00A/B/C/D31-275[»]
    2FS8X-ray2.50A/B/C/D31-275[»]
    2FS9X-ray2.30A/B/C/D31-275[»]
    2FWWX-ray2.25A/B/C/D31-275[»]
    2FXRX-ray2.50A/B/C/D31-275[»]
    2GDDX-ray2.35A/B/C/D31-275[»]
    2ZA5X-ray2.30A/B/C/D31-275[»]
    3V7TX-ray2.09A/B/C/D31-275[»]
    ProteinModelPortaliP20231.
    SMRiP20231. Positions 31-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20231.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 272242Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG013304.
    InParanoidiP20231.
    KOiK01340.
    PhylomeDBiP20231.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. 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.

    P20231-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV    50
    HGPYWMHFCG GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ 100
    LLPVSRIIVH PQFYTAQIGA DIALLELEEP VNVSSHVHTV TLPPASETFP 150
    PGMPCWVTGW GDVDNDERLP PPFPLKQVKV PIMENHICDA KYHLGAYTGD 200
    DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG VVSWGEGCAQ 250
    PNRPGIYTRV TYYLDWIHHY VPKKP 275
    Length:275
    Mass (Da):30,515
    Last modified:October 17, 2006 - v2
    Checksum:iADC48FDC51F37112
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321N → K in AAA51843. (PubMed:2203827)Curated
    Sequence conflicti132 – 1321N → K in AAD13876. (PubMed:8434231)Curated
    Sequence conflicti132 – 1321N → K in AAD17858. (PubMed:9920877)Curated
    Sequence conflicti132 – 1321N → K in ACZ98911. (PubMed:19748655)Curated
    Sequence conflicti132 – 1321N → K in AAH29356. (PubMed:15489334)Curated
    Sequence conflicti132 – 1321N → K in AAA36779. (PubMed:2187193)Curated
    Sequence conflicti132 – 1321N → K in AAA36780. (PubMed:2187193)Curated
    Sequence conflicti141 – 1411T → A in ACZ98913. (PubMed:19748655)Curated
    Sequence conflicti240 – 2401G → D in ACZ98913. (PubMed:19748655)Curated

    Polymorphismi

    There are two alleles; beta-II and beta-III. Beta-II is the most commun allele. There are two forms of the beta-III allele, a short and a long form. The short form (also named frameshifted form) is carried by 23% and 19% of individuals of European and African ancestry but 0% of Asian subjects. In the human genome reference version GRCh37/hg19, the allele beta-III short form is represented.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 533HGP → RDR in beta-III.
    VAR_012104

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37488 mRNA. Translation: AAA51843.1.
    S55551 mRNA. Translation: AAD13876.1.
    AF099143 Genomic DNA. Translation: AAD17859.2.
    AF099145 Genomic DNA. Translation: AAD17857.1.
    AF099146 Genomic DNA. Translation: AAD17858.1.
    FJ931117 Genomic DNA. Translation: ACZ98911.1.
    FJ931120 mRNA. Translation: ACZ98913.1.
    AC120498 Genomic DNA. No translation available.
    BC029356 mRNA. Translation: AAH29356.1.
    M33492 mRNA. Translation: AAA36779.1.
    M33493 mRNA. Translation: AAA36780.1.
    PIRiB35863.
    C35863.
    RefSeqiNP_003285.2. NM_003294.3.
    NP_077078.5. NM_024164.5.
    UniGeneiHs.405479.
    Hs.592982.

    Genome annotation databases

    GeneIDi64499.
    7177.
    KEGGihsa:64499.
    hsa:7177.

    Polymorphism databases

    DMDMi116242830.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37488 mRNA. Translation: AAA51843.1 .
    S55551 mRNA. Translation: AAD13876.1 .
    AF099143 Genomic DNA. Translation: AAD17859.2 .
    AF099145 Genomic DNA. Translation: AAD17857.1 .
    AF099146 Genomic DNA. Translation: AAD17858.1 .
    FJ931117 Genomic DNA. Translation: ACZ98911.1 .
    FJ931120 mRNA. Translation: ACZ98913.1 .
    AC120498 Genomic DNA. No translation available.
    BC029356 mRNA. Translation: AAH29356.1 .
    M33492 mRNA. Translation: AAA36779.1 .
    M33493 mRNA. Translation: AAA36780.1 .
    PIRi B35863.
    C35863.
    RefSeqi NP_003285.2. NM_003294.3.
    NP_077078.5. NM_024164.5.
    UniGenei Hs.405479.
    Hs.592982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A0L X-ray 3.00 A/B/C/D 31-274 [» ]
    1AAO model - A 31-275 [» ]
    2BM2 X-ray 2.20 A/B/C/D 31-275 [» ]
    2FPZ X-ray 2.00 A/B/C/D 31-275 [» ]
    2FS8 X-ray 2.50 A/B/C/D 31-275 [» ]
    2FS9 X-ray 2.30 A/B/C/D 31-275 [» ]
    2FWW X-ray 2.25 A/B/C/D 31-275 [» ]
    2FXR X-ray 2.50 A/B/C/D 31-275 [» ]
    2GDD X-ray 2.35 A/B/C/D 31-275 [» ]
    2ZA5 X-ray 2.30 A/B/C/D 31-275 [» ]
    3V7T X-ray 2.09 A/B/C/D 31-275 [» ]
    ProteinModelPortali P20231.
    SMRi P20231. Positions 31-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113029. 1 interaction.
    122201. 1 interaction.
    IntActi P20231. 2 interactions.
    STRINGi 9606.ENSP00000420825.

    Chemistry

    BindingDBi P20231.

    Protein family/group databases

    MEROPSi S01.015.

    PTM databases

    PhosphoSitei P20231.

    Polymorphism databases

    DMDMi 116242830.

    Proteomic databases

    PaxDbi P20231.
    PRIDEi P20231.

    Protocols and materials databases

    DNASUi 64499.
    7177.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64499.
    7177.
    KEGGi hsa:64499.
    hsa:7177.

    Organism-specific databases

    CTDi 64499.
    7177.
    GeneCardsi GC16M001281.
    HGNCi HGNC:14120. TPSB2.
    HPAi CAB016369.
    CAB022175.
    HPA049153.
    HPA049554.
    MIMi 191081. gene.
    neXtProti NX_P20231.
    PharmGKBi PA36698.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG013304.
    InParanoidi P20231.
    KOi K01340.
    PhylomeDBi P20231.

    Miscellaneous databases

    EvolutionaryTracei P20231.
    GeneWikii TPSAB1.
    TPSB2.
    NextBioi 28132.
    PROi P20231.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20231.
    Bgeei P20231.
    CleanExi HS_TPSB2.
    Genevestigatori P20231.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a second complementary DNA for human tryptase."
      Miller J.S., Moxley G., Schwartz L.B.
      J. Clin. Invest. 86:864-870(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT BETA-2).
      Tissue: Lung.
    2. "Characterization of a tryptase mRNA expressed in the human basophil cell line KU812."
      Blom T., Hellman L.
      Scand. J. Immunol. 37:203-208(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT BETA-2).
    3. "Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3."
      Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H.
      J. Biol. Chem. 274:3355-3362(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS BETA-2 AND BETA-3).
    4. Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. "Human subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutations."
      Trivedi N.N., Tamraz B., Chu C., Kwok P.Y., Caughey G.H.
      J. Allergy Clin. Immunol. 124:1099-1105(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT BETA-2), NUCLEOTIDE SEQUENCE [MRNA] OF 50-275 (VARIANT BETA-3).
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (VARIANT BETA-2).
      Tissue: Lung.
    8. "Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family."
      Vanderslice P., Ballinger S.M., Tam E.K., Goldstein S.M., Craik C.S., Caughey G.H.
      Proc. Natl. Acad. Sci. U.S.A. 87:3811-3815(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-275 (VARIANT BETA-2), NUCLEOTIDE SEQUENCE [MRNA] OF 9-275 (VARIANT BETA-3).
    9. "Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast cells and forms complexes with beta-tryptase monomers."
      Strik M.C., Wolbink A., Wouters D., Bladergroen B.A., Verlaan A.R., van Houdt I.S., Hijlkema S., Hack C.E., Kummer J.A.
      Blood 103:2710-2717(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FORMATION OF A COMPLEX WITH SERPINB6.
    10. "Active monomers of human beta-tryptase have expanded substrate specificities."
      Fukuoka Y., Schwartz L.B.
      Int. Immunopharmacol. 7:1900-1908(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Human beta-tryptase is a ring-like tetramer with active sites facing a central pore."
      Pereira P.J.B., Bergner A., Macedo-Ribeiro S., Huber R., Matschiner G., Fritz H., Sommerhoff C.P., Bode W.
      Nature 392:306-311(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    12. Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).

    Entry informationi

    Entry nameiTRYB2_HUMAN
    AccessioniPrimary (citable) accession number: P20231
    Secondary accession number(s): D2E6S0
    , D2E6S2, O95827, Q15664, Q9UQI6, Q9UQI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 141 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3