Overview
| Uniprot ID | A0A8D1EYW1 |
|---|
| Protein Name | DnaJ homolog subfamily C member 2 |
|---|
| Gene Name | DNAJC2 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 452 |
KAFDKFKKEHGVVPQ |
Function
Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation
Protein Sequence
10
MLLLPSAADG
20
QSTAITHALT
30
SASTFCQVEP
40
VGRWFEAFVK
50
RRNRNASASF
60
QELEDKKELS
70
EESEDEELQL
80
EEFPMLKTLD
90
PKDWKNQDHY
100
AVLGLGHVRY
110
KATQRQIKAA
120
HKAMVLKHHP
130
DKRKAAGEPI
140
KEGDNDYFTC
150
ITKAYEMLSD
160
PVKRRAFNSV
170
DPTFDNSVPS
180
KSEAKDNFFE
190
VFSPVFERNS
200
RWSNKKNVPK
210
LGDMNSSFED
220
VDAFYSFCRD
230
ERRWIEKQNR
240
ATRAQRKKEE
250
MNRIRTLVDN
260
AYSCDPRIKK
270
FKEEEKAKKE
280
AEKKAKAEAK
290
RKEQEAKEKQ
300
RQAELEAARL
310
AKEKEEEEVR
320
QQALLAKKEK
330
DIQKKAIKKE
340
RQKLRNSCKI
350
EEINEQIRKE
360
KEEAEARMRQ
370
ASKNAEKSTG
380
GGGNGSKHWS
390
EDDLQLLIKA
400
VNLFPAGTNS
410
RWEVIANYMN
420
IHSSSGVKRT
430
AKDVIGKAKS
440
LQKLDPHQKD
450
DINKKAFDKF
460
KKEHGVVPQA
470
DNATPSERFE
480
GPCTDFTPWT
490
TEEQKLLEQA
500
LKTYPVNTPE
510
RWEKIAEAVP
520
GRTKKDCMKR
530
YKELVEMVKA
540
KKAAQEQVLN
ASRAKK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0030544 |
Hsp70 protein binding |
| Molecular Function |
GO:0043022 |
ribosome binding |
| Biological Process |
GO:0051083 |
'de novo' cotranslational protein folding |
| Biological Process |
GO:0006325 |
chromatin organization |
| Biological Process |
GO:0006450 |
regulation of translational fidelity |
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.