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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. May play a role in innate immunity.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei74Charge relay system1
Active sitei121Charge relay system1
Active sitei224Charge relay system1

GO - Molecular functioni

  • serine-type endopeptidase activity Source: UniProtKB
  • serine-type peptidase activity Source: ProtInc

Keywordsi

Molecular functionHydrolase, 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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000197253.13.
HGNCiHGNC:14120. TPSB2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi64499.
7177.
OpenTargetsiENSG00000172236.
PharmGKBiPA36698.

Chemistry databases

DrugBankiDB04654. 4-PIPERIDIN-4-YLBUTANAL.
DB04764. [4-(3-AMINOMETHYL-PHENYL)-PIPERIDIN-1-YL]-(5-PHENETHYL- PYRIDIN-3-YL)-METHANONE.
DB02018. Amido Phenyl Pyruvic Acid.

Polymorphism and mutation databases

BioMutaiTPSB2.
DMDMi116242830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002748119 – 30Activation peptideAdd BLAST12
ChainiPRO_000002748231 – 275Tryptase beta-2Add BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi59 ↔ 75
Modified residuei97PhosphotyrosineBy similarity1
Disulfide bondi155 ↔ 230
Disulfide bondi188 ↔ 211
Disulfide bondi220 ↔ 248
Glycosylationi233N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP20231.
PeptideAtlasiP20231.
PRIDEiP20231.

PTM databases

iPTMnetiP20231.
PhosphoSitePlusiP20231.

Expressioni

Gene expression databases

BgeeiENSG00000197253.
CleanExiHS_TPSB2.
ExpressionAtlasiP20231. baseline and differential.
GenevisibleiP20231. HS.

Organism-specific databases

HPAiHPA049153.
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. 2 interactors.
122201. 16 interactors.
IntActiP20231. 2 interactors.

Chemistry databases

BindingDBiP20231.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 36Combined sources5
Beta strandi39 – 41Combined sources3
Beta strandi45 – 50Combined sources6
Beta strandi52 – 54Combined sources3
Beta strandi56 – 65Combined sources10
Beta strandi68 – 71Combined sources4
Helixi73 – 76Combined sources4
Helixi83 – 85Combined sources3
Beta strandi86 – 89Combined sources4
Turni95 – 98Combined sources4
Beta strandi102 – 109Combined sources8
Turni116 – 118Combined sources3
Beta strandi123 – 129Combined sources7
Beta strandi135 – 137Combined sources3
Beta strandi154 – 161Combined sources8
Beta strandi176 – 183Combined sources8
Helixi185 – 193Combined sources9
Beta strandi209 – 212Combined sources4
Beta strandi215 – 218Combined sources4
Turni221 – 225Combined sources5
Beta strandi227 – 232Combined sources6
Beta strandi235 – 244Combined sources10
Beta strandi246 – 250Combined sources5
Beta strandi255 – 259Combined sources5
Helixi260 – 263Combined sources4
Helixi264 – 267Combined sources4
Turni268 – 270Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20231.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 272Peptidase S1PROSITE-ProRule annotationAdd BLAST242

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG013304.
InParanoidiP20231.
KOiK01340.
PhylomeDBiP20231.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiView protein in InterPro
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
PfamiView protein in Pfam
PF00089. Trypsin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiView protein in SMART
SM00020. Tryp_SPc. 1 hit.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiView protein in PROSITE
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti132N → K in AAA51843 (PubMed:2203827).Curated1
Sequence conflicti132N → K in AAD13876 (PubMed:8434231).Curated1
Sequence conflicti132N → K in AAD17858 (PubMed:9920877).Curated1
Sequence conflicti132N → K in ACZ98911 (PubMed:19748655).Curated1
Sequence conflicti132N → K in AAH29356 (PubMed:15489334).Curated1
Sequence conflicti132N → K in AAA36779 (PubMed:2187193).Curated1
Sequence conflicti132N → K in AAA36780 (PubMed:2187193).Curated1
Sequence conflicti141T → A in ACZ98913 (PubMed:19748655).Curated1
Sequence conflicti240G → D in ACZ98913 (PubMed:19748655).Curated1

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.5 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01210451 – 53HGP → RDR in beta-III. 3

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.
UCSCiuc032dnv.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTRYB2_HUMAN
AccessioniPrimary (citable) accession number: P20231
Secondary accession number(s): D2E6S0
, D2E6S2, O95827, Q15664, Q9UQI6, Q9UQI7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 17, 2006
Last modified: September 27, 2017
This is version 167 of the entry and version 2 of the sequence. See 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