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Reviewed, UniProtKB/Swiss-Prot P20231 (TRYB2_HUMAN)

Last modified January 19, 2010. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.

Subcellular location

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

Polymorphism

There are two alleles; beta-II and beta-III which differ by 3 residues.

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
Gene Ontology (GO)
   Biological processproteolysis

Non-traceable author statement. Source: UniProtKB

   Cellular componentextracellular region

Non-traceable author statement. Source: UniProtKB

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

serine-type endopeptidase activity Ref.4

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163331EBI-1761383,EBI-389883
PIK3R1P279861EBI-1761383,EBI-79464

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 AAA36779. Ref.3
Sequence conflict1321N → K in AAA36780. Ref.3
Sequence conflict1321N → K in AAD17858. Ref.4
Sequence conflict1321N → K in AAH29356. Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P20231-1 [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: 2203827] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT BETA-2).
Tissue: Lung.
[2]"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: 2187193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANTS BETA-2 AND BETA-3).
[3]"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: 8434231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT BETA-2).
[4]"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: 9920877] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS BETA-2 AND BETA-3).
[5]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.
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"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: 9521329] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[8]"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: 10500112] [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.
M33492 mRNA. Translation: AAA36779.1.
M33493 mRNA. Translation: AAA36780.1.
S55551 mRNA. Translation: AAD13876.1.
AF099143 Genomic DNA. Translation: AAD17859.2.
AF099145 Genomic DNA. Translation: AAD17857.1.
AF099146 Genomic DNA. Translation: AAD17858.1.
BC029356 mRNA. Translation: AAH29356.1.
IPIIPI00419942.
PIRB35863.
C35863.
RefSeqNP_003285.2.
NP_077078.5.
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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP20231. 2 interactions.
STRINGP20231.

Protein family/group databases

MEROPSS01.015.

PTM databases

PhosphoSiteP20231.

Proteomic databases

PRIDEP20231.

Genome annotation databases

EnsemblENST00000338844; ENSP00000343577; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000382804; ENSP00000372254; ENSG00000172236; Homo sapiens. [Genome view]
ENST00000461509; ENSP00000418247; ENSG00000172236; Homo sapiens. [Genome view]
GeneID64499.
7177.
KEGGhsa:64499.
hsa:7177.

Organism-specific databases

CTD64499.
7177.
GeneCardsGC16M001219.
H-InvDBHIX0012676.
HGNCHGNC:14120. TPSB2.
MIM191081. gene.
PharmGKBPA37846.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05667.
HOVERGENP20231.
InParanoidP20231.
PhylomeDBP20231.

Enzyme and pathway databases

BRENDA3.4.21.59. 247.

Gene expression databases

ArrayExpressP20231.
BgeeP20231.
CleanExHS_TPSB2.
GenevestigatorP20231.
GermOnlineENSG00000172236. Homo sapiens.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio28132.
SOURCESearch...

Entry information

Entry nameTRYB2_HUMAN
AccessionPrimary (citable) accession number: P20231
Secondary accession number(s): O95827 expand/collapse secondary AC list , Q15664, Q9UQI6, Q9UQI7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 17, 2006
Last modified: January 19, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 16

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents