Overview
| Uniprot ID | Q08752 |
|---|
| Protein Name | Peptidyl-prolyl cis-trans isomerase D |
|---|
| Gene Name | PPID |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 245 |
NWEMAIKKYAEVLRY |
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
Protein Sequence
10
MSHPSPQAKP
20
SNPSNPRVFF
30
DVDIGGERVG
40
RIVLELFADI
50
VPKTAENFRA
60
LCTGEKGIGH
70
TTGKPLHFKG
80
CPFHRIIKKF
90
MIQGGDFSNQ
100
NGTGGESIYG
110
EKFEDENFHY
120
KHDREGLLSM
130
ANAGRNTNGS
140
QFFITTVPTP
150
HLDGKHVVFG
160
QVIKGIGVAR
170
ILENVEVKGE
180
KPAKLCVIAE
190
CGELKEGDDG
200
GIFPKDGSGD
210
SHPDFPEDAD
220
IDLKDVDKIL
230
LITEDLKNIG
240
NTFFKSQNWE
250
MAIKKYAEVL
260
RYVDSSKAVI
270
ETADRAKLQP
280
IALSCVLNIG
290
ACKLKMSNWQ
300
GAIDSCLEAL
310
ELDPSNTKAL
320
YRRAQGWQGL
330
KEYDQALADL
340
KKAQGIAPED
350
KAIQAELLKV
360
KQKIKAQKDK
370
EKAVYAKMFA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0016018 |
cyclosporin A binding |
| Molecular Function |
GO:0031072 |
heat shock protein binding |
| Molecular Function |
GO:0030544 |
Hsp70 protein binding |
| Molecular Function |
GO:0051879 |
Hsp90 protein binding |
| Molecular Function |
GO:0030331 |
nuclear estrogen receptor binding |
| Molecular Function |
GO:0003755 |
peptidyl-prolyl cis-trans isomerase activity |
| Molecular Function |
GO:0008134 |
transcription factor binding |
| Biological Process |
GO:0006915 |
apoptotic process |
| Biological Process |
GO:0071492 |
cellular response to UV-A |
| Biological Process |
GO:0034389 |
lipid droplet organization |
| Biological Process |
GO:0000122 |
negative regulation of transcription by RNA polymerase II |
| Biological Process |
GO:0043065 |
positive regulation of apoptotic process |
| Biological Process |
GO:0050714 |
positive regulation of protein secretion |
| Biological Process |
GO:0045070 |
positive regulation of viral genome replication |
| Biological Process |
GO:0006457 |
protein folding |
| Biological Process |
GO:0015031 |
protein transport |
| Biological Process |
GO:0065003 |
protein-containing complex assembly |
| Biological Process |
GO:0019076 |
viral release from host cell |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.