Overview
| Uniprot ID | Q99543 |
|---|
| Protein Name | DnaJ homolog subfamily C member 2 |
|---|
| Gene Name | DNAJC2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 527 |
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
RGTAITHALT
30
SASTLCQVEP
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
VFTPVFERNS
200
RWSNKKNVPK
210
LGDMNSSFED
220
VDIFYSFWYN
230
FDSWREFSYL
240
DEEEKEKAEC
250
RDERRWIEKQ
260
NRATRAQRKK
270
EEMNRIRTLV
280
DNAYSCDPRI
290
KKFKEEEKAK
300
KEAEKKAKAE
310
AKRKEQEAKE
320
KQRQAELEAA
330
RLAKEKEEEE
340
VRQQALLAKK
350
EKDIQKKAIK
360
KERQKLRNSC
370
KTWNHFSDNE
380
AERVKMMEEV
390
EKLCDRLELA
400
SLQCLNETLT
410
SCTKEVGKAA
420
LEKQIEEINE
430
QIRKEKEEAE
440
ARMRQASKNT
450
EKSTGGGGNG
460
SKNWSEDDLQ
470
LLIKAVNLFP
480
AGTNSRWEVI
490
ANYMNIHSSS
500
GVKRTAKDVI
510
GKAKSLQKLD
520
PHQKDDINKK
530
AFDKFKKEHG
540
VVPQADNATP
550
SERFEGPYTD
560
FTPWTTEEQK
570
LLEQALKTYP
580
VNTPERWEKI
590
AEAVPGRTKK
600
DCMKRYKELV
610
EMVKAKKAAQ
620
EQVLNASRAK
K
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:0001671 |
ATPase activator activity |
| Molecular Function |
GO:0003682 |
chromatin binding |
| Molecular Function |
GO:0042393 |
histone binding |
| Molecular Function |
GO:0030544 |
Hsp70 protein binding |
| Molecular Function |
GO:0043022 |
ribosome binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0061649 |
ubiquitin-modified histone reader activity |
| Biological Process |
GO:0051083 |
'de novo' cotranslational protein folding |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0045893 |
positive regulation of DNA-templated transcription |
| Biological Process |
GO:0006457 |
protein folding |
| Biological Process |
GO:1900034 |
regulation of cellular response to heat |
| Biological Process |
GO:0006450 |
regulation of translational fidelity |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.