Dnajc6
entrez
72685
canonical
uniprot
Q80TZ3
canonical
ensembl
ENSMUSG00000028528
resolver
ensp
ENSMUSP00000044251
resolver
ensp
ENSMUSP00000102542
resolver
ensp
ENSMUSP00000102543
resolver
ensp
ENSMUSP00000102546
resolver
genesymbol
Dnajc6
resolver
genesymbol_syn
Kiaa0473
resolver
uniprot
B1B0B9
resolver
uniprot
Q6P2K9
resolver
uniprot
Q8C7L9
resolver
uniprot_entry
AUXI_MOUSE
resolver
uniprot_sec
B1B0B9
resolver
uniprot_sec
Q6P2K9
resolver
uniprot_sec
Q8C7L9
resolver
amino_acid_sequence
MTNPKSGVAESAGLACSRAAAGENRMKDSENKGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVSSYTKGDLDFTYVTSRIIVMSFPVDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKAITVSPVPFFNKQRNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVIVSMYHLRSTIGSRLQAKVTNTQIFQLQFHSGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDIEVQPQDKVIDLTPPWEHYCTKDVNPSILFSSQQEHQDTLALGGQAPADLPPDHPRNLGQGGFFASLCWQDQKSEKSRCEEDHAALVNQESEQSDDELLTLSSPHGNAEGDKPHGAKKPGKKQQEPAAPPPPEEVDLLGLEGSDVSTNFSSLAAPPSNSELLSDLFGGVGATGPAQAGQAGVEDVFHPSGPVSAQSTPRRTATSASASPTLRVGEGATFDPFGAPAKPPGQDLLGSFLNTSSASSDPFLQPTRSPSPTVHASSTPAVNIQPDIAGGWDWHTKPGGFGMGSKSAATSPTGSSHGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQPAGYNWQQTQSKPQSSMPHSSPQNRPNYNVSFSAMPAGQSERGKGSTNLEGKQKAADFEDLLSSQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRRAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY
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:20160091). 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:20160091}.
uniprot
proteins
mass_dalton
102299
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q27974}.; PTM: Phosphorylation at Ser-595 modulates its ability to bind CLTC and therefore the synaptic vesicle endocytosis (SVE). {ECO:0000250|UniProtKB:O75061}.
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20160091
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
938
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