• Version:
  • 11.0 [archived version]
STRINGSTRING
ERAP1 ERAP1 ERAP2 ERAP2 LNPEP LNPEP PPP1R42 PPP1R42 TPP2 TPP2 POLB POLB DPP3 DPP3 NPEPPS NPEPPS MSH2 MSH2 CSE1L CSE1L TIPRL TIPRL
"TPP2" - Tripeptidyl-peptidase 2 in Homo sapiens
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
TPP2Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity) (1249 aa)    
Predicted Functional Partners:
TIPRL
TIP41-like protein; May be a allosteric regulator of serine/threonine- protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C)-TIPRL complex does not show phosphatase activity. Acts as negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiting the formation of the active PPP4C-PPP4R2 complex; the function is proposed to implicate it in DNA damage response by promoting H2AFX phosphorylated on Ser-140 (gamma-H2AFX). May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replica [...] (272 aa)
       
      0.871
ERAP2
Endoplasmic reticulum aminopeptidase 2; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys; Aminopeptidases (960 aa)
   
   
  0.769
CSE1L
Exportin-2; Export receptor for importin-alpha. Mediates importin- alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause relea [...] (971 aa)
     
      0.744
MSH2
DNA mismatch repair protein Msh2; Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers- MutS alpha (MSH2- MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a [...] (934 aa)
     
 
  0.742
DPP3
Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro); Belongs to the peptidase M49 family (737 aa)
     
   
  0.702
PPP1R42
Protein phosphatase 1 regulatory subunit 42; Regulates phosphatase activity of protein phosphatase 1 (PP1) complexes in the testis (228 aa)
     
   
  0.694
ERAP1
Endoplasmic reticulum aminopeptidase 1; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play [...] (948 aa)
   
   
  0.683
POLB
DNA polymerase beta; Repair polymerase that plays a key role in base-excision repair. Has 5’-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5’ sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3’ end of the arising single-nucleotide gap. Conducts ’gap-filling’ DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases (335 aa)
     
      0.674
NPEPPS
Puromycin-sensitive aminopeptidase; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain; Aminopeptidases (919 aa)
   
   
  0.662
LNPEP
Leucyl-cystinyl aminopeptidase; Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain; Aminopeptidases (1025 aa)
   
   
  0.652
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
Server load: low (0%) [HD]