Dnajc5
entrez
13002
canonical
uniprot
P60904
canonical
ensembl
ENSMUSG00000000826
resolver
ensp
ENSMUSP00000072175
resolver
ensp
ENSMUSP00000104424
resolver
ensp
ENSMUSP00000104425
resolver
ensp
ENSMUSP00000264119
resolver
ensp
ENSMUSP00000264146
resolver
enst
ENSMUST00000072334
resolver
enst
ENSMUST00000108796
resolver
enst
ENSMUST00000108797
resolver
genesymbol
Dnajc5
resolver
genesymbol_syn
Cspalpha
resolver
uniprot
P54101
resolver
uniprot_entry
DNJC5_MOUSE
resolver
uniprot_sec
P54101
resolver
amino_acid_sequence
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVVCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
uniprot
proteins
function
FUNCTION: Acts as a co-chaperone for the SNARE protein SNAP-25 (PubMed:22187053). Involved in the calcium-mediated control of a late stage of exocytosis (PubMed:20847230). Acts as a general chaperone in regulated exocytosis (By similarity). May have an important role in presynaptic function (By similarity). May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:20847230, ECO:0000269|PubMed:22187053}.
uniprot
proteins
mass_dalton
22101
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="S->D: Reduced interaction with SYT9, but no effect on the interaction with HSC70."; /evidence="ECO:0000269|PubMed:20847230"; MUTAGEN 93; /note="E->V: Reduced interaction with SYT9."; /evidence="ECO:0000269|PubMed:20847230"; MUTAGEN 113; /note="C->V: No effect on palmitoylation. No change in subcellular location; when associated with G-118 and F-121."; /evidence="ECO:0000269|PubMed:17034881"; MUTAGEN 118; /note="C->G: No effect on palmitoylation. No change in subcellular location; when associated with V-113 and F-121."; /evidence="ECO:0000269|PubMed:17034881"; MUTAGEN 121; /note="C->F: No effect on palmitoylation. No change in subcellular location; when associated with V-113 and G-118."; /evidence="ECO:0000269|PubMed:17034881"; MUTAGEN 129; /note="F->C: No effect on palmitoylation. No change in subcellular location; when associated with H-135."; /evidence="ECO:0000269|PubMed:17034881"; MUTAGEN 135; /note="K->H: No effect on palmitoylation. No change in subcellular location; when associated with C-129."; /evidence="ECO:0000269|PubMed:17034881
uniprot
proteins
post_translational_modification
PTM: Formation of the chaperone complex DNAJC5/HSC70 is not regulated by phosphorylation (PubMed:20847230). Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58 (By similarity). This conformational switch modulates DNAJC5's cellular functions by reducing binding to syntaxin and synaptogamin without altering HSC70 interactions (By similarity). {ECO:0000250|UniProtKB:Q9H3Z4, ECO:0000269|PubMed:20847230}.; PTM: Palmitoylated (PubMed:17034881). Could be palmitoylated by DHHC3, DHHC7, DHHC15 and DHHC17 (By similarity). Palmitoylation occurs probably in the cysteine-rich domain and regulates DNAJC5 membrane attachment (PubMed:17034881). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:17034881}.
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17034881
uniprot
proteins
pubmed
17208939
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20847230
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22187053
uniprot
proteins
pubmed
25253725
uniprot
proteins
pubmed
25800794
uniprot
proteins
pubmed
26198635
uniprot
proteins
sequence_length
198
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29455}. Membrane {ECO:0000269|PubMed:17034881}; Lipid-anchor {ECO:0000269|PubMed:17034881}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:Q29455}. Melanosome {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane {ECO:0000250|UniProtKB:Q9H3Z4}. Note=The association with membranes is regulated by palmitoylation (By similarity). Colocalizes with insulin granules, when overexpressed in an islet cell line (PubMed:17034881). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:17034881}.
uniprot
proteins