DNAJC7
entrez
7266
canonical
uniprot
Q99615
canonical
ensembl
ENSG00000168259
resolver
ensp
ENSP00000313311
resolver
ensp
ENSP00000394327
resolver
ensp
ENSP00000406463
resolver
ensp
ENSP00000501364
resolver
ensp
ENSP00000501366
resolver
genesymbol
DNAJC7
resolver
genesymbol_syn
TPR2
resolver
genesymbol_syn
TTC2
resolver
hgnc
HGNC:12392
resolver
uniprot
Q7Z784
resolver
uniprot_entry
DNJC7_HUMAN
resolver
uniprot_sec
Q7Z784
resolver
amino_acid_sequence
MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG
uniprot
proteins
function
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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:18620420}.
uniprot
proteins
mass_dalton
56441
uniprot
proteins
mutagenesis
MUTAGEN 101; /note="R->A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-333 and A-409."; /evidence="ECO:0000269|PubMed:12853476"; MUTAGEN 333; /note="R->A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-409."; /evidence="ECO:0000269|PubMed:12853476"; MUTAGEN 409; /note="H->A: Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333."; /evidence="ECO:0000269|PubMed:11573955, ECO:0000269|PubMed:12853476
uniprot
proteins
pubmed
10567422
uniprot
proteins
pubmed
11573955
uniprot
proteins
pubmed
12853476
uniprot
proteins
pubmed
14573755
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18620420
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8836031
uniprot
proteins
sequence_length
494
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11573955, ECO:0000269|PubMed:12853476}. Nucleus {ECO:0000269|PubMed:11573955}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QYI3}. Note=Colocalizes with NR1I3 to microtubules. {ECO:0000250|UniProtKB:Q9QYI3}.
uniprot
proteins