1XYH
Crystal Structure of Recombinant Human Cyclophilin J
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000398 | biological_process | mRNA splicing, via spliceosome |
| A | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005681 | cellular_component | spliceosomal complex |
| A | 0006397 | biological_process | mRNA processing |
| A | 0006457 | biological_process | protein folding |
| A | 0008380 | biological_process | RNA splicing |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0071013 | cellular_component | catalytic step 2 spliceosome |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YngCiFHRNIkgFMvQTG |
| Chain | Residue | Details |
| A | TYR37-GLY54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 152 |
| Details | Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q9D6L8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
