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| PPIF | Peptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in act [...] (207 aa) | |||
| NKTR | NK-tumor recognition protein; Component of a putative tumor-recognition complex. Involved in the function of NK cells; Cyclophilin peptidylprolyl isomerases (1462 aa) | |||
| PPIL4 | Peptidyl-prolyl cis-trans isomerase-like 4; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily (492 aa) | |||
| TACO1 | Translational activator of cytochrome c oxidase 1; Acts as a translational activator of mitochondrially- encoded cytochrome c oxidase 1; Belongs to the TACO1 family (297 aa) | |||
| PPIG | Peptidyl-prolyl cis-trans isomerase G; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing; Cyclophilin peptidylprolyl isomerases (754 aa) | |||
| RANBP2 | E3 SUMO-protein ligase RanBP2; E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single- stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at ’Lys-490’ which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore comple [...] (3224 aa) | |||
| PPIL3 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (165 aa) | |||
| PPIB | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (216 aa) | |||
| PPIC | Peptidyl-prolyl cis-trans isomerase C; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (212 aa) | |||
| PPID | Peptidyl-prolyl cis-trans isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexe [...] (370 aa) | |||
| PPIH | Peptidyl-prolyl cis-trans isomerase H; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone; Cyclophilin peptidylprolyl isomerases (177 aa) | |||
| NADSYN1 | Glutamine-dependent NAD(+) synthetase; NAD synthetase 1; In the C-terminal section; belongs to the NAD synthetase family (706 aa) | |||
| PPIL2 | Peptidyl-prolyl cis-trans isomerase-like 2; May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins (By similarity). May also function as a chaperone, playing a role in transport to the cell membrane of BSG for instance. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating ’Lys-48’-linked polyubiquitination of proteins could target them for proteasomal degradation; Cyclo [...] (520 aa) | |||
| CUTC | Copper homeostasis protein cutC homolog; May play a role in copper homeostasis. Can bind one Cu(1+) per subunit (273 aa) | |||
| PPIE | Peptidyl-prolyl cis-trans isomerase E; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing; Cyclophilin peptidylprolyl isomerases (314 aa) | |||
| PPIL1 | Peptidyl-prolyl cis-trans isomerase-like 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing; Cyclophilin peptidylprolyl isomerases (166 aa) | |||
| CSGALNACT2 | Chondroitin sulfate N-acetylgalactosaminyltransferase 2; Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP- GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains (542 aa) | |||
| FKBPL | FK506-binding protein-like; May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21; FKBP prolyl isomerases (349 aa) | |||
| CWC27 | Peptidyl-prolyl cis-trans isomerase CWC27 homolog; PPIases accelerate the folding of proteins; Belongs to the cyclophilin-type PPIase family (472 aa) | |||
| PPIL6 | Peptidyl-prolyl cis-trans isomerase-like 6; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (337 aa) | |||
| PPIAL4G | Peptidyl-prolyl cis-trans isomerase A-like 4G; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily (164 aa) | |||
| PPIA | Peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily (165 aa) | |||
| PPIAL4D | Peptidyl-prolyl cis-trans isomerase A-like 4D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily (164 aa) | |||
| ENSG00000263464 | Peptidyl-prolyl cis-trans isomerase A-like 4C; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily (164 aa) | |||
| PPIAL4F | Peptidylprolyl isomerase A like 4F (164 aa) | |||
| UPF1 | Regulator of nonsense transcripts 1; RNA-dependent helicase and ATPase required for nonsense- mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1- eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more [...] (1129 aa) | |||
