Skip Header

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

Tryptase beta-2

Gene

TPSB2

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

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.59. 2681.

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:14120. TPSB2.

Subcellular locationi

  1. Secreted

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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36698.

Polymorphism and mutation databases

BioMutaiTPSB2.
DMDMi116242830.

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

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 – 365Combined sources
Beta strandi39 – 413Combined sources
Beta strandi45 – 506Combined sources
Beta strandi52 – 543Combined sources
Beta strandi56 – 6510Combined sources
Beta strandi68 – 714Combined sources
Helixi73 – 764Combined sources
Helixi83 – 853Combined sources
Beta strandi86 – 894Combined sources
Turni95 – 984Combined sources
Beta strandi102 – 1098Combined sources
Turni116 – 1183Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi154 – 1618Combined sources
Beta strandi176 – 1838Combined sources
Helixi185 – 1939Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2184Combined sources
Turni221 – 2255Combined sources
Beta strandi227 – 2326Combined sources
Beta strandi235 – 24410Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi255 – 2595Combined sources
Helixi260 – 2634Combined sources
Helixi264 – 2674Combined sources
Turni268 – 2703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV
60 70 80 90 100
HGPYWMHFCG GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ
110 120 130 140 150
LLPVSRIIVH PQFYTAQIGA DIALLELEEP VNVSSHVHTV TLPPASETFP
160 170 180 190 200
PGMPCWVTGW GDVDNDERLP PPFPLKQVKV PIMENHICDA KYHLGAYTGD
210 220 230 240 250
DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG VVSWGEGCAQ
260 270
PNRPGIYTRV TYYLDWIHHY VPKKP
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000606293; ENSP00000482743; ENSG00000197253.
GeneIDi64499.
7177.
KEGGihsa:64499.
hsa:7177.

Polymorphism and mutation databases

BioMutaiTPSB2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP20231.

Protein family/group databases

MEROPSiS01.015.

PTM databases

PhosphoSiteiP20231.

Polymorphism and mutation databases

BioMutaiTPSB2.
DMDMi116242830.

Proteomic databases

PaxDbiP20231.
PRIDEiP20231.

Protocols and materials databases

DNASUi64499.
7177.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000606293; ENSP00000482743; ENSG00000197253.
GeneIDi64499.
7177.
KEGGihsa:64499.
hsa:7177.

Organism-specific databases

CTDi64499.
7177.
GeneCardsiGC16M001281.
HGNCiHGNC:14120. TPSB2.
HPAiCAB016369.
CAB022175.
HPA049153.
HPA049554.
MIMi191081. gene.
neXtProtiNX_P20231.
PharmGKBiPA36698.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
HOVERGENiHBG013304.
InParanoidiP20231.
KOiK01340.
PhylomeDBiP20231.

Enzyme and pathway databases

BRENDAi3.4.21.59. 2681.

Miscellaneous databases

EvolutionaryTraceiP20231.
GeneWikiiTPSAB1.
TPSB2.
NextBioi28132.
PROiP20231.
SOURCEiSearch...

Gene expression databases

BgeeiP20231.
CleanExiHS_TPSB2.
GenevestigatoriP20231.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.