DNAJC5
entrez
80331
canonical
uniprot
Q9H3Z4
canonical
ensembl
ENSG00000101152
resolver
ensp
ENSP00000354111
resolver
ensp
ENSP00000568635
resolver
ensp
ENSP00000631756
resolver
ensp
ENSP00000631757
resolver
ensp
ENSP00000631758
resolver
genesymbol
DNAJC5
resolver
genesymbol_syn
CLN4
resolver
hgnc
HGNC:16235
resolver
uniprot
A8K0M0
resolver
uniprot
B3KY68
resolver
uniprot
E1P5G8
resolver
uniprot
Q9H3Z5
resolver
uniprot
Q9H7H2
resolver
uniprot_entry
DNJC5_HUMAN
resolver
uniprot_sec
A8K0M0
resolver
uniprot_sec
B3KY68
resolver
uniprot_sec
E1P5G8
resolver
uniprot_sec
Q9H3Z5
resolver
uniprot_sec
Q9H7H2
resolver
amino_acid_sequence
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVFCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
uniprot
proteins
disease_involvement
DISEASE: Ceroid lipofuscinosis, neuronal, 4B (Kufs type), autosomal dominant (CLN4B) [MIM:162350]: An adult-onset neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. CLN4B has no visual involvement and is characterized by seizures and other neurologic symptoms. {ECO:0000269|PubMed:21820099, ECO:0000269|PubMed:22073189, ECO:0000269|PubMed:22235333, ECO:0000269|PubMed:22902780, ECO:0000269|PubMed:22978711}. Note=The disease is caused by variants affecting the gene represented in this entry.
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|UniProtKB:P60904, ECO:0000250|UniProtKB:Q29455}.
uniprot
proteins
mass_dalton
22149
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="S->A,E: Increased syntaxin binding."; /evidence="ECO:0000269|PubMed:11604405"; MUTAGEN 113..136; /note="CGLLTCCYCCCCLCCCFNCCCGKC->SGLLTSSYSSSSLSSSFNSSSGKS: No effect on oligomerization."; /evidence="ECO:0000269|PubMed:27452402
uniprot
proteins
post_translational_modification
PTM: Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58 (PubMed:27452402). This conformational switch modulates DNAJC5's cellular functions by reducing binding to syntaxin and synaptogamin without altering HSC70 interactions (PubMed:27452402). {ECO:0000269|PubMed:27452402}.; 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
11214971
uniprot
proteins
pubmed
11604405
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14997482
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21820099
uniprot
proteins
pubmed
22073189
uniprot
proteins
pubmed
22235333
uniprot
proteins
pubmed
22902780
uniprot
proteins
pubmed
22978711
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25800794
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27452402
uniprot
proteins
pubmed
28882895
uniprot
proteins
pubmed
8764987
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:0000269|PubMed:17081065}. Cell membrane {ECO:0000269|PubMed:21820099}. Note=The association with membranes is regulated by palmitoylation (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:17081065}.
uniprot
proteins