PPIG PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. Ubiquitous. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Cyclophilin; EC 5.2.1.8; Isomerase
Chromosomal Location of Human Ortholog: 2|2 C2
Cellular Component:  cytosol; nuclear matrix; nuclear speck; nucleus
Molecular Function:  cyclosporin A binding; isomerase activity; peptidyl-prolyl cis-trans isomerase activity; unfolded protein binding
Biological Process:  protein folding; protein peptidyl-prolyl isomerization; protein refolding
Reference #:  A2AR02 (UniProtKB)
Alt. Names/Synonyms: AU019516; AU022200; B230312B02Rik; Cyclophilin G; CYP; OTTMUSP00000014021; OTTMUSP00000014022; Peptidyl-prolyl cis-trans isomerase G; Peptidyl-prolyl isomerase G; peptidyl-prolyl isomerase G (cyclophilin G); peptidylprolyl isomerase G; PPIase G; Ppig; Rotamase G; SRCyp
Gene Symbols: Ppig
Molecular weight: 88,325 Da
Basal Isoelectric point: 10.27  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PPIG

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene