DNAJC9
entrez
23234
canonical
uniprot
Q8WXX5
canonical
ensembl
ENSG00000213551
resolver
ensp
ENSP00000362041
resolver
enst
ENST00000372950
resolver
genesymbol
DNAJC9
resolver
hgnc
HGNC:19123
resolver
uniprot
B2RMW6
resolver
uniprot_entry
DNJC9_HUMAN
resolver
uniprot_sec
B2RMW6
resolver
amino_acid_sequence
MGLLDLCEEVFGTADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAYLDFKGDMDQIMESVLCVQYTEEPRIRNIIQQAIDAGEVPSYNAFVKESKQKMNARKRRAQEEAKEAEMSRKELGLDEGVDSLKAAIQSRQKDRQKEMDNFLAQMEAKYCKSSKGGGKKSALKKEKK
uniprot
proteins
function
FUNCTION: Acts as a dual histone chaperone and heat shock co-chaperone (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes (PubMed:33857403). May also act as a histone co-chaperone together with TONSL (PubMed:33857403). May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity (PubMed:33857403). Exhibits activity to assemble histones onto DNA in vitro (PubMed:33857403). {ECO:0000269|PubMed:17182002, ECO:0000269|PubMed:33857403}.
uniprot
proteins
mass_dalton
29910
uniprot
proteins
mutagenesis
MUTAGEN 43..45; /note="HPD->QPN: Increased binding to histones H3 and H4. Less integration of histones H3 and H4 in chromatin. Increased recruitment of histone deposition factors to chromatin. Trapped on chromatin throughout the cell cycle in a manner depending on histone-binding. Released from chromatin trap; when associated with Ala-224; Ala-227; Ala-238 and Ala-242."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 195..200; /note="EEAKEA->AAAKAE: Reduces the co-chaperone complex formation with MCM2; histone H3.3 and H4."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 216..220; /note="LKAAI->AKAAA: Disrupts the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 224..242; /note="QKDRQKEMDNFLAQMEAKY->AKDAQKEMDNFLAQAEAKA: Abolishes the interaction with MCM2, TONSL and histones H3.3 and H4. Disrupts the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 224..227; /note="QKDR->AKDA: Partial loss of histone dimer H3-H4 interaction. Reduces the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 234..235; /note="FL->AA: Reduces the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 238..242; /note="MEAKY->AEAKA: Partial loss of histone dimer H3-H4 interaction. Reduces the co-chaperone complex formation with MCM2; histone H3.3 and H4."; /evidence="ECO:0000269|PubMed:33857403"; MUTAGEN 243; /note="C->S: Does not affect interaction with histones."; /evidence="ECO:0000269|PubMed:33857403
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17182002
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
33857403
uniprot
proteins
sequence_length
260
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17182002}. Cytoplasm {ECO:0000269|PubMed:17182002}. Cell membrane {ECO:0000269|PubMed:17182002}. Note=Predominantly nuclear. Translocates to the cytoplasm and membrane after heat shock. {ECO:0000269|PubMed:17182002}.
uniprot
proteins