Overview
| Uniprot ID | O75061 |
|---|
| Protein Name | Auxilin |
|---|
| Gene Name | DNAJC6 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 38 |
GRLFSNLKDNLKDTL |
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)
Protein Sequence
10
MKDSENKGAS
20
SPDMEPSYGG
30
GLFDMVKGGA
40
GRLFSNLKDN
50
LKDTLKDTSS
60
RVIQSVTSYT
70
KGDLDFTYVT
80
SRIIVMSFPL
90
DNVDIGFRNQ
100
VDDIRSFLDS
110
RHLDHYTVYN
120
LSPKSYRTAK
130
FHSRVSECSW
140
PIRQAPSLHN
150
LFAVCRNMYN
160
WLLQNPKNVC
170
VVHCLDGRAA
180
SSILVGAMFI
190
FCNLYSTPGP
200
AIRLLYAKRP
210
GIGLSPSHRR
220
YLGYMCDLLA
230
DKPYRPHFKP
240
LTIKSITVSP
250
IPFFNKQRNG
260
CRPYCDVLIG
270
ETKIYSTCTD
280
FERMKEYRVQ
290
DGKIFIPLNI
300
TVQGDVVVSM
310
YHLRSTIGSR
320
LQAKVTNTQI
330
FQLQFHTGFI
340
PLDTTVLKFT
350
KPELDACDVP
360
EKYPQLFQVT
370
LDVELQPHDK
380
VIDLTPPWEH
390
YCTKDVNPSI
400
LFSSHQEHQD
410
TLALGGQAPI
420
DIPPDNPRHY
430
GQSGFFASLC
440
WQDQKSEKSF
450
CEEDHAALVN
460
QESEQSDDEL
470
LTLSSPHGNA
480
NGDKPHGVKK
490
PSKKQQEPAA
500
PPPPEDVDLL
510
GLEGSAMSNS
520
FSPPAAPPTN
530
SELLSDLFGG
540
GGAAGPTQAG
550
QSGVEDVFHP
560
SGPASTQSTP
570
RRSATSTSAS
580
PTLRVGEGAT
590
FDPFGAPSKP
600
SGQDLLGSFL
610
NTSSASSDPF
620
LQPTRSPSPT
630
VHASSTPAVN
640
IQPDVSGGWD
650
WHAKPGGFGM
660
GSKSAATSPT
670
GSSHGTPTHQ
680
SKPQTLDPFA
690
DLGTLGSSSF
700
ASKPTTPTGL
710
GGGFPPLSSP
720
QKASPQPMGG
730
GWQQGGAYNW
740
QQPQPKPQPS
750
MPHSSPQNRP
760
NYNVSFSAMP
770
GGQNERGKGS
780
SNLEGKQKAA
790
DFEDLLSGQG
800
FNAHKDKKGP
810
RTIAEMRKEE
820
MAKEMDPEKL
830
KILEWIEGKE
840
RNIRALLSTM
850
HTVLWAGETK
860
WKPVGMADLV
870
TPEQVKKVYR
880
KAVLVVHPDK
890
ATGQPYEQYA
900
KMIFMELNDA
910
WSEFENQGQK
PLY
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0030136 |
clathrin-coated vesicle |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0098894 |
extrinsic component of presynaptic endocytic zone membrane |
| Cellular Component |
GO:0014069 |
postsynaptic density |
| Cellular Component |
GO:0031982 |
vesicle |
| Molecular Function |
GO:0030276 |
clathrin binding |
| Molecular Function |
GO:0032050 |
clathrin heavy chain binding |
| Molecular Function |
GO:0031072 |
heat shock protein binding |
| Molecular Function |
GO:0004721 |
phosphoprotein phosphatase activity |
| Molecular Function |
GO:0017124 |
SH3 domain binding |
| Biological Process |
GO:0072318 |
clathrin coat disassembly |
| Biological Process |
GO:0072583 |
clathrin-dependent endocytosis |
| Biological Process |
GO:0046907 |
intracellular transport |
| Biological Process |
GO:1905443 |
regulation of clathrin coat assembly |
| Biological Process |
GO:0036465 |
synaptic vesicle recycling |
| Biological Process |
GO:0016191 |
synaptic vesicle uncoating |
Reference
[1] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.