PPIE
entrez
10450
canonical
uniprot
Q9UNP9
canonical
ensembl
ENSG00000084072
resolver
ensp
ENSP00000312769
resolver
ensp
ENSP00000348904
resolver
ensp
ENSP00000361918
resolver
ensp
ENSP00000431714
resolver
ensp
ENSP00000433475
resolver
ensp
ENSP00000541363
resolver
ensp
ENSP00000661268
resolver
ensp
ENSP00000770222
resolver
ensp
ENSP00000770224
resolver
ensp
ENSP00000789135
resolver
enst
ENST00000470213
resolver
genesymbol
PPIE
resolver
genesymbol_syn
CYP33
resolver
hgnc
HGNC:9258
resolver
uniprot
B2R971
resolver
uniprot
E9PK21
resolver
uniprot
O43634
resolver
uniprot
O43635
resolver
uniprot
Q32Q72
resolver
uniprot
Q3S611
resolver
uniprot
Q5TGA0
resolver
uniprot
Q5TGA2
resolver
uniprot
Q5TGA3
resolver
uniprot
Q9UIZ5
resolver
uniprot_entry
E9PK21_HUMAN
resolver
uniprot_entry
PPIE_HUMAN
resolver
uniprot_sec
B2R971
resolver
uniprot_sec
O43634
resolver
uniprot_sec
O43635
resolver
uniprot_sec
Q32Q72
resolver
uniprot_sec
Q3S611
resolver
uniprot_sec
Q5TGA0
resolver
uniprot_sec
Q5TGA2
resolver
uniprot_sec
Q5TGA3
resolver
uniprot_sec
Q9UIZ5
resolver
activity_regulation
ACTIVITY REGULATION: Enzyme activity is inhibited by cyclosporin A. {ECO:0000269|PubMed:18258190, ECO:0000269|PubMed:8977107}.
uniprot
proteins
amino_acid_sequence
MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKAETQEGEPIAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIEAQGSKDGKPKQKVIIADCGEYV
uniprot
proteins
ec_number
5.2.1.8
uniprot
proteins
function
FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346). Combines RNA-binding and PPIase activities (PubMed:18258190, PubMed:20460131, PubMed:20677832, PubMed:8977107). Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules (PubMed:18258190, PubMed:20460131, PubMed:8977107). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins (PubMed:18258190, PubMed:20541251, PubMed:20677832, PubMed:8977107). Inhibits KMT2A activity; this requires proline isomerase activity (PubMed:20460131, PubMed:20541251, PubMed:20677832). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:18258190, ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20541251, ECO:0000269|PubMed:20677832, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:8977107}.
uniprot
proteins
mass_dalton
33431
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="Y->A: Decreased affinity for RNA."; /evidence="ECO:0000269|PubMed:20460131"; MUTAGEN 39; /note="L->A: Decreased affinity for KMT2A."; /evidence="ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20677832"; MUTAGEN 40..45; /note="Missing: Abolishes interaction with KMT2A."; /evidence="ECO:0000269|PubMed:20460131"; MUTAGEN 42; /note="E->A: Slightly decreased affinity for KMT2A."; /evidence="ECO:0000269|PubMed:20460131"; MUTAGEN 45; /note="K->A: No effect on interaction with KMT2A."; /evidence="ECO:0000269|PubMed:20677832"; MUTAGEN 47; /note="R->A: No effect on interaction with KMT2A."; /evidence="ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20677832"; MUTAGEN 49; /note="F->A: Strongly decreased affinity for KMT2A. Decreased affinity for RNA."; /evidence="ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20677832"; MUTAGEN 51; /note="F->A: Impairs protein folding."; /evidence="ECO:0000269|PubMed:20460131, ECO:0000269|PubMed:20677832"; MUTAGEN 51; /note="F->D: Abolishes interaction with KMT2A. Abolishes inhibition of KMT2A activity."; /evidence="ECO:0000269|PubMed:20541251"; MUTAGEN 191; /note="R->A: Expected to disrupt proline isomerase activity. Abolishes inhibition of KMT2A activity; when associated with A-196."; /evidence="ECO:0000269|PubMed:20677832"; MUTAGEN 196..197; /note="FM->EE: Expected to disrupt peptidylproline binding. Decreases interaction with KMT2A. Abolishes inhibition of KMT2A activity."; /evidence="ECO:0000269|PubMed:20541251"; MUTAGEN 196; /note="F->A: Expected to disrupt proline isomerase activity. Abolishes inhibition of KMT2A activity; when associated with A-191."; /evidence="ECO:0000269|PubMed:20677832
uniprot
proteins
protein_family
Cyclophilin-type PPIase family
uniprot
proteins
protein_family
PPIase E subfamily
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15963461
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17981804
uniprot
proteins
pubmed
18258190
uniprot
proteins
pubmed
20460131
uniprot
proteins
pubmed
20541251
uniprot
proteins
pubmed
20677832
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25599396
uniprot
proteins
pubmed
28076346
uniprot
proteins
pubmed
8977107
uniprot
proteins
pubmed
9747881
uniprot
proteins
sequence_length
301
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:8977107}.
uniprot
proteins