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TPSAB1 protein (human) - STRING interaction network
"TPSAB1" - Tryptase alpha/beta-1 in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
TPSAB1Tryptase alpha/beta-1; 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. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates; Belongs to the peptidase S1 family. Tryptase subfamily (275 aa)    
Predicted Functional Partners:
MMP1
Interstitial collagenase; Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat’s mediated neurotoxicity; Endogenous ligands (469 aa)
         
  0.901
CPA3
M14 carboxypeptidases (417 aa)
     
 
  0.888
TREH
Trehalase; Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose; Belongs to the glycosyl hydrolase 37 family (583 aa)
           
  0.679
CPA4
Carboxypeptidase A4; Metalloprotease that could be involved in the histone hyperacetylation pathway. Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val; Belongs to the peptidase M14 family (421 aa)
       
 
  0.643
TPSB2
Tryptase beta 2; Belongs to the peptidase S1 family (275 aa)
   
 
0.608
CD1A
T-cell surface glycoprotein CD1a; Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells; C1-set domain containing (327 aa)
           
  0.558
CTSC
Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII (463 aa)
           
  0.540
UGP2
UTP--glucose-1-phosphate uridylyltransferase; Plays a central role as a glucosyl donor in cellular metabolic pathways; Belongs to the UDPGP type 1 family (508 aa)
           
  0.536
NTHL1
Endonuclease III-like protein 1; Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N- glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3’ to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA gly [...] (312 aa)
           
  0.491
TRMT13
tRNA-m(4)X modification enzyme TRM13 homolog; tRNA methylase which 2’-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His) (481 aa)
           
  0.464
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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