Search Results
Overview
| Uniprot ID | A0A287B3M2 |
|---|---|
| Protein Name | DnaJ homolog subfamily C member 7 |
| Gene Name | DNAJC7 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 289 | NNIKTNAKLYCNRGT |
| 303 | TVNSKLRKLDDAIED |
Function
Acts as a co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm
Protein Sequence
10
MAAAAECDVV
20
MAATGPELLD
30
DEEAKREAES
40
FKEQGNAYYA
50
KKDYNEAYNY
60
YTKAIDMCPK
70
NASYYGNRAA
80
TLMMLGRFRE
90
ALGDAQQSVR
100
LDDSFVRGHL
110
REGKCHLSLG
120
NAMAACRKLD
130
HKNAQAQQEF
140
KNANAVIEYE
150
KIAETDFEKR
160
DFRKVVFCMD
170
RALEFAPACH
180
RFKILKAECL
190
AMLGRYPEAQ
200
SVASDILRMD
210
STNADALYVR
220
GLCLYYEDCI
230
EKAVQFFVQA
240
LRMAPDHEKA
250
CIACRNAKAL
260
KAKKEDGNKA
270
FKEGNYKLAY
280
ELYTEALGID
290
PNNIKTNAKL
300
YCNRGTVNSK
310
LRKLDDAIED
320
CTHAVKLDDT
330
YIKAYLRRAQ
340
CYMDTEQYEE
350
AVRDYEKVYQ
360
TEKTKEHKQL
370
LKNAQLELKK
380
SKRKDYYKIL
390
GVDKNASEDE
400
IKKAYRKRAL
410
MHHPDRHSGA
420
SAEVQKEEEK
430
KFKEVGEAFT
440
ILSDPKKKTR
450
YDSGQDLDEE
460
GMNMGGESGA
470
AWGSPGSSSP
480
AASGPGNFFF
QFG
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0031072 | heat shock protein binding |
| Biological Process | GO:0006457 | protein folding |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.