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dnajc7

Gene
dnajc7
Protein
DnaJ homolog subfamily C member 7 homolog
Organism
Dictyostelium discoideum
Length
539 amino acids
Mass
59.624 kDa
Sequence
MDHEECKTQGNNYFKQSQYMDAIRCYTQAIELSNGTIAAYYGNRAAAYLAICTKSSLQDSIKDSLKAIELERSFIKGYTRASKAYIHLAQYDQAASIIVRGLVFDPRNNELLQEKNQIDSIQRTISSLTKEKALSNPSSSLNQIENVLSQSKYNTQLQVLKARVLIELKQYPQASNLMTTLLQEDSRNPEYLYVRGLSLYYQNNFPLALQHFQNSLTYDPDYSESRVALKRLRSIESKKKEGNEYFQSKNYQAAYDSFTEALSIDPKLETMNSQLYSNRAAALVHLNRISEAINDCTSAVTIDPNYGKAYIRRAQCQMKQENYEDAVRDYEKAQSLDPENGELQRNIKEAKIAHKKSLRKDYYKILGVSKEAGETEIKKAYRKLALQYHPDKNNQLPEEEKAQAEKMFKDIGEAYSVLSDEKKKRQYDMGQDENGMPFDADMGGVDINSVFSQFFNQGGMGGGMGGGGFGGMGGGGFGGMGGGGFSGMGGGGGFGGMPFGFDMGGGGGYGGMGGGFGGHSGHSHGGSRSRSSRGGNEYR

Gene
DNAJC7
Protein
DnaJ homolog subfamily C member 7
Organism
Homo sapiens
Length
494 amino acids
Function
Acts as 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).
Mass
56.441 kDa
Sequence
MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG

Gene
Dnajc7
Protein
DnaJ homolog subfamily C member 7
Organism
Mus musculus
Length
494 amino acids
Function
Acts as 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 (By similarity). Recruits NR1I3 to the cytoplasm.
Mass
56.476 kDa
Sequence
MAATAECDVVMAATEPELLEDEDAKREAESFKEQGNAYYAKKDYNEAYNYYTKAIDMCPNNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAEVDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQFVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACVACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRQLEDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQFEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDANNIFKAFFGGPGGFSFEASGPGNFYFQFG

Gene
DNAJC7
Protein
DnaJ homolog subfamily C member 7
Organism
Pongo abelii
Length
494 amino acids
Function
Acts as 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).
Mass
56.431 kDa
Sequence
MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGRLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKSAQLELKKSKRRDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGTNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG