PPID
entrez
5481
canonical
uniprot
Q08752
canonical
ensembl
ENSG00000171497
resolver
ensp
ENSP00000303754
resolver
ensp
ENSP00000759985
resolver
enst
ENST00000307720
resolver
genesymbol
PPID
resolver
genesymbol_syn
CYP40
resolver
genesymbol_syn
CYPD
resolver
hgnc
HGNC:9257
resolver
uniprot
B2R9V2
resolver
uniprot
E5KN55
resolver
uniprot_entry
E5KN55_HUMAN
resolver
uniprot_entry
PPID_HUMAN
resolver
uniprot_sec
B2R9V2
resolver
activity_regulation
ACTIVITY REGULATION: Less sensitive to inhibition by cyclosporin A than is CYP-18. {ECO:0000269|PubMed:20676357}.
uniprot
proteins
amino_acid_sequence
MSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGELKEGDDGGIFPKDGSGDSHPDFPEDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYAKMFA
uniprot
proteins
ec_number
5.2.1.8
uniprot
proteins
function
FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:11350175, PubMed:20676357). 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 complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. {ECO:0000269|PubMed:11350175, ECO:0000269|PubMed:18708059, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22681779, ECO:0000269|PubMed:23220213, ECO:0000269|PubMed:9659917}.; FUNCTION: (Microbial infection) May be involved in hepatitis C virus (HCV) replication and release. {ECO:0000269|PubMed:19932913, ECO:0000269|PubMed:21711559}.
uniprot
proteins
mass_dalton
40764
uniprot
proteins
mutagenesis
MUTAGEN 227; /note="K->A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 231; /note="N->A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 234; /note="F->A: Impairs interaction with HSP90AB1 and HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 274; /note="S->L: Impairs interaction with HSP90AB1 and HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 278; /note="N->A: Abolishes interaction with HSP90AB1."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 284; /note="L->A: Impairs interaction with HSP90AB1 and HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 285; /note="K->A: Impairs interaction with HSP90AB1 and HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 308; /note="K->A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 312; /note="R->A: Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8."; /evidence="ECO:0000269|PubMed:12145316, ECO:0000269|PubMed:15497503"; MUTAGEN 329; /note="D->A: Impairs interaction with HSP90AB1."; /evidence="ECO:0000269|PubMed:12145316
uniprot
proteins
protein_family
Cyclophilin-type PPIase family
uniprot
proteins
protein_family
PPIase D subfamily
uniprot
proteins
pubmed
11350175
uniprot
proteins
pubmed
11525244
uniprot
proteins
pubmed
12145316
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
14580201
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15497503
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18708059
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19932913
uniprot
proteins
pubmed
20676357
uniprot
proteins
pubmed
21146485
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21711559
uniprot
proteins
pubmed
22681779
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23220213
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
8509368
uniprot
proteins
pubmed
8812478
uniprot
proteins
pubmed
9659917
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}. Nucleus, nucleolus {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11525244, ECO:0000269|PubMed:18708059}.
uniprot
proteins