Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P20231 (TRYB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptase beta-2

Short name=Tryptase-2
EC=3.4.21.59
Alternative name(s):
Tryptase II
Gene names
Name:TPSB2
Synonyms:TPS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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. Ref.10

Subcellular location

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

Polymorphism

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.

Sequence similarities

Belongs to the peptidase S1 family. Tryptase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Non-traceable author statement Ref.3. Source: UniProtKB

serine-type peptidase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 3012Activation peptide
PRO_0000027481
Chain31 – 275245Tryptase beta-2
PRO_0000027482

Regions

Domain31 – 272242Peptidase S1

Sites

Active site741Charge relay system
Active site1211Charge relay system
Active site2241Charge relay system

Amino acid modifications

Modified residue971Phosphotyrosine By similarity
Glycosylation2331N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 75
Disulfide bond155 ↔ 230
Disulfide bond188 ↔ 211
Disulfide bond220 ↔ 248

Natural variations

Natural variant51 – 533HGP → RDR in beta-III.
VAR_012104

Experimental info

Sequence conflict1321N → K in AAA51843. Ref.1
Sequence conflict1321N → K in AAD13876. Ref.2
Sequence conflict1321N → K in AAD17858. Ref.3
Sequence conflict1321N → K in ACZ98911. Ref.5
Sequence conflict1321N → K in AAH29356. Ref.7
Sequence conflict1321N → K in AAA36779. Ref.8
Sequence conflict1321N → K in AAA36780. Ref.8
Sequence conflict1411T → A in ACZ98913. Ref.5
Sequence conflict2401G → D in ACZ98913. Ref.5

Secondary structure

................................................... 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20231 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: ADC48FDC51F37112

FASTA27530,515
        10         20         30         40         50         60 
MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV HGPYWMHFCG 

        70         80         90        100        110        120 
GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ LLPVSRIIVH PQFYTAQIGA 

       130        140        150        160        170        180 
DIALLELEEP VNVSSHVHTV TLPPASETFP PGMPCWVTGW GDVDNDERLP PPFPLKQVKV 

       190        200        210        220        230        240 
PIMENHICDA KYHLGAYTGD DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG 

       250        260        270 
VVSWGEGCAQ PNRPGIYTRV TYYLDWIHHY VPKKP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The structure of the human betaII-tryptase tetramer: fo(u)r better or worse."
Sommerhoff C.P., Bode W., Pereira P.J.B., Stubbs M.T., Stuerzebecher J., Piechottka G.P., Matschiner G., Bergner A.
Proc. Natl. Acad. Sci. U.S.A. 96:10984-10991(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB35863.
C35863.
RefSeqNP_003285.2. NM_003294.3.
NP_077078.5. NM_024164.5.
UniGeneHs.405479.
Hs.592982.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP20231.
SMRP20231. Positions 31-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113029. 1 interaction.
122201. 1 interaction.
IntActP20231. 2 interactions.
STRING9606.ENSP00000420825.

Chemistry

BindingDBP20231.

Protein family/group databases

MEROPSS01.015.

PTM databases

PhosphoSiteP20231.

Polymorphism databases

DMDM116242830.

Proteomic databases

PaxDbP20231.
PRIDEP20231.

Protocols and materials databases

DNASU64499.
7177.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64499.
7177.
KEGGhsa:64499.
hsa:7177.

Organism-specific databases

CTD64499.
7177.
GeneCardsGC16M001281.
HGNCHGNC:14120. TPSB2.
HPACAB016369.
CAB022175.
HPA049153.
HPA049554.
MIM191081. gene.
neXtProtNX_P20231.
PharmGKBPA36698.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG013304.
InParanoidP20231.
KOK01340.
PhylomeDBP20231.

Gene expression databases

ArrayExpressP20231.
BgeeP20231.
CleanExHS_TPSB2.
GenevestigatorP20231.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20231.
GeneWikiTPSAB1.
TPSB2.
NextBio28132.
PROP20231.
SOURCESearch...

Entry information

Entry nameTRYB2_HUMAN
AccessionPrimary (citable) accession number: P20231
Secondary accession number(s): D2E6S0 expand/collapse secondary AC list , D2E6S2, O95827, Q15664, Q9UQI6, Q9UQI7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM