DNAJC6
entrez
9829
canonical
uniprot
O75061
canonical
ensembl
ENSG00000116675
resolver
ensp
ENSP00000263441
resolver
ensp
ENSP00000360108
resolver
ensp
ENSP00000378735
resolver
genesymbol
DNAJC6
resolver
genesymbol_syn
KIAA0473
resolver
hgnc
HGNC:15469
resolver
uniprot
B7Z3V8
resolver
uniprot
D3DQ65
resolver
uniprot
D3DQ66
resolver
uniprot
Q32M66
resolver
uniprot
Q4G0K1
resolver
uniprot
Q5T614
resolver
uniprot
Q5T615
resolver
uniprot_entry
AUXI_HUMAN
resolver
uniprot_sec
B7Z3V8
resolver
uniprot_sec
D3DQ65
resolver
uniprot_sec
D3DQ66
resolver
uniprot_sec
Q32M66
resolver
uniprot_sec
Q4G0K1
resolver
uniprot_sec
Q5T614
resolver
uniprot_sec
Q5T615
resolver
amino_acid_sequence
MKDSENKGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVTSYTKGDLDFTYVTSRIIVMSFPLDNVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAIRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKSITVSPIPFFNKQRNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVVVSMYHLRSTIGSRLQAKVTNTQIFQLQFHTGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDVELQPHDKVIDLTPPWEHYCTKDVNPSILFSSHQEHQDTLALGGQAPIDIPPDNPRHYGQSGFFASLCWQDQKSEKSFCEEDHAALVNQESEQSDDELLTLSSPHGNANGDKPHGVKKPSKKQQEPAAPPPPEDVDLLGLEGSAMSNSFSPPAAPPTNSELLSDLFGGGGAAGPTQAGQSGVEDVFHPSGPASTQSTPRRSATSTSASPTLRVGEGATFDPFGAPSKPSGQDLLGSFLNTSSASSDPFLQPTRSPSPTVHASSTPAVNIQPDVSGGWDWHAKPGGFGMGSKSAATSPTGSSHGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQGGAYNWQQPQPKPQPSMPHSSPQNRPNYNVSFSAMPGGQNERGKGSSNLEGKQKAADFEDLLSGQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY
uniprot
proteins
disease_involvement
DISEASE: Parkinson disease 19A, juvenile-onset (PARK19A) [MIM:615528]: A juvenile form of Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK19A is characterized by onset of parkinsonian symptoms in the first or second decade of life. Some patients may have additional neurologic features, including intellectual disability and seizures. {ECO:0000269|PubMed:22563501, ECO:0000269|PubMed:23211418, ECO:0000269|PubMed:26703368}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Parkinson disease 19B, early-onset (PARK19B) [MIM:615528]: An early-onset form of Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK19B is characterized by symptoms onset in the third-to-fifth decade, slow disease progression, and prominent. response to dopaminergic therapies. Inheritance is autosomal recessive. {ECO:0000269|PubMed:26528954}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
function
FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase. Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin from CCVs and participates in clathrin-mediated endocytosis of synaptic vesicles and their recycling and also in intracellular trafficking (PubMed:18489706). Firstly, binds tightly to the clathrin cages, at a ratio of one DNAJC6 per clathrin triskelion. The HSPA8:ATP complex then binds to the clathrin-auxilin cage, initially at a ratio of one HSPA8 per triskelion leading to ATP hydrolysis stimulation and causing a conformational change in the HSPA8. This cycle is repeated three times to drive to a complex containing the clathrin-auxilin cage associated to three HSPA8:ADP complex. The ATP hydrolysis of the third HSPA8:ATP complex leads to a concerted dismantling of the cage into component triskelia. Then, dissociates from the released triskelia and be recycled to initiate another cycle of HSPA8's recruitment. Also acts during the early steps of clathrin-coated vesicle (CCV) formation through its interaction with the GTP bound form of DNM1 (By similarity). {ECO:0000250|UniProtKB:Q27974, ECO:0000269|PubMed:18489706}.
uniprot
proteins
mass_dalton
99997
uniprot
proteins
mutagenesis
MUTAGEN 570; /note="S->A: Increase interaction with CLTC. Does not affect interaction with HSPA8."; /evidence="ECO:0000269|PubMed:29735704"; MUTAGEN 570; /note="S->D: Does not affect interaction with CLTC. Does not affect interaction with HSPA8."; /evidence="ECO:0000269|PubMed:29735704
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-570 modulates its ability to bind CLTC and therefore the synaptic vesicle endocytosis (SVE). {ECO:0000269|PubMed:29735704}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q27974}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18489706
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
22563501
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23211418
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26528954
uniprot
proteins
pubmed
26703368
uniprot
proteins
pubmed
29735704
uniprot
proteins
pubmed
9455484
uniprot
proteins
sequence_length
913
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q27974}. Note=Appears on coated vesicles in successive transient bursts, immediately after the vesicle release from the plasma membrane. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles. {ECO:0000250|UniProtKB:Q27974}.
uniprot
proteins