Dnajc5
entrez
79130
canonical
uniprot
P60905
canonical
ensembl
ENSRNOG00000015202
resolver
ensembl
ENSRNOG00055001200
resolver
ensembl
ENSRNOG00060001351
resolver
ensembl
ENSRNOG00065013976
resolver
ensp
ENSRNOP00000078729
resolver
ensp
ENSRNOP00055001572
resolver
ensp
ENSRNOP00060001172
resolver
ensp
ENSRNOP00065017966
resolver
enst
ENSRNOT00000102827
resolver
enst
ENSRNOT00055001997
resolver
enst
ENSRNOT00060001968
resolver
enst
ENSRNOT00065023078
resolver
genesymbol
Dnajc5
resolver
uniprot
P54101
resolver
uniprot_entry
DNJC5_RAT
resolver
uniprot_sec
P54101
resolver
amino_acid_sequence
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVVCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
uniprot
proteins
function
FUNCTION: Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P60904, ECO:0000250|UniProtKB:Q29455}.
uniprot
proteins
mass_dalton
22101
uniprot
proteins
post_translational_modification
PTM: Phosphorylated (PubMed:11931641). Phosphorylation results in a profound decrease in the affinity for syntaxin but has no effect on the affinity for HSC70 (PubMed:11604405, PubMed:11931641). 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:11604405, ECO:0000269|PubMed:11931641}.; PTM: Palmitoylated. Could be palmitoylated by DHHC3, DHHC7, DHHC15 and DHHC17. Palmitoylation occurs probably in the cysteine-rich domain and regulates DNAJC5 membrane attachment. {ECO:0000250|UniProtKB:Q29455}.
uniprot
proteins
pubmed
11257428
uniprot
proteins
pubmed
11604405
uniprot
proteins
pubmed
11931641
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
25253725
uniprot
proteins
pubmed
25800794
uniprot
proteins
pubmed
7535880
uniprot
proteins
pubmed
8606785
uniprot
proteins
sequence_length
198
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29455}. Membrane {ECO:0000250|UniProtKB:Q29455}; Lipid-anchor {ECO:0000250|UniProtKB:Q29455}. 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. {ECO:0000250|UniProtKB:Q29455}.
uniprot
proteins