DNAJB2
entrez
3300
canonical
uniprot
P25686
canonical
ensembl
ENSG00000135924
resolver
ensp
ENSP00000338019
resolver
ensp
ENSP00000375936
resolver
genesymbol
DNAJB2
resolver
genesymbol_syn
HSJ1
resolver
genesymbol_syn
HSPF3
resolver
hgnc
HGNC:5228
resolver
uniprot
A8K9P6
resolver
uniprot
Q53QD7
resolver
uniprot
Q8IUK1
resolver
uniprot
Q8IUK2
resolver
uniprot
Q96F52
resolver
uniprot_entry
DNJB2_HUMAN
resolver
uniprot_sec
A8K9P6
resolver
uniprot_sec
Q53QD7
resolver
uniprot_sec
Q8IUK1
resolver
uniprot_sec
Q8IUK2
resolver
uniprot_sec
Q96F52
resolver
amino_acid_sequence
MASYYEILDVPRSASADDIKKAYRRKALQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTGTGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELFDDLGPFSELQNRGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSVSTSTTFVQGRRITTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTSRSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPAGGREAQHRRQGRPKAQHQDPGLGGTQEGARGEATKRSPSPEEKASRCLIL
uniprot
proteins
disease_involvement
DISEASE: Neuronopathy, distal hereditary motor, autosomal recessive 5 (HMNR5) [MIM:614881]: A form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. HMNR5 is characterized by young adult onset of slowly progressive distal muscle weakness and atrophy resulting in gait impairment and loss of reflexes. {ECO:0000269|PubMed:22522442, ECO:0000269|PubMed:24627108, ECO:0000269|PubMed:25274842}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family (PubMed:22219199, PubMed:7957263). In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins (PubMed:15936278, PubMed:21625540). Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and be crucial for many biological processes (PubMed:12754272, PubMed:20889486, PubMed:21719532, PubMed:22396390, PubMed:24023695). Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER-associated protein degradation of misfolded proteins (PubMed:15936278). {ECO:0000269|PubMed:12754272, ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:20889486, ECO:0000269|PubMed:21625540, ECO:0000269|PubMed:21719532, ECO:0000269|PubMed:22219199, ECO:0000269|PubMed:22396390, ECO:0000269|PubMed:24023695, ECO:0000269|PubMed:7957263}.
uniprot
proteins
mass_dalton
35580
uniprot
proteins
mutagenesis
MUTAGEN 31..33; /note="HPD->QPN: Loss of interaction with HSP70 and loss of the ability to promote ATXN3 proteasomal degradation."; /evidence="ECO:0000269|PubMed:21625540"; MUTAGEN 31; /note="H->Q: Probable loss of interaction with HSP70 and loss of the ability to reduce PRKN aggregation."; /evidence="ECO:0000269|PubMed:12754272, ECO:0000269|PubMed:20889486"; MUTAGEN 219; /note="S->A: Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-222; A-262 and A-265."; /evidence="ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:21625540"; MUTAGEN 222; /note="E->A: Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-219; A-262 and A-265."; /evidence="ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:21625540"; MUTAGEN 262; /note="S->A: Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-219; A-222 and A-265."; /evidence="ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:21625540"; MUTAGEN 265; /note="E->A: Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-219; A-222 and A-262."; /evidence="ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:21625540"; MUTAGEN 321; /note="C->S: Loss of localization to the endoplasmic reticulum and relocalization to cytoplasm and nucleus."; /evidence="ECO:0000269|PubMed:12754272"; MUTAGEN 324; /note="L->M: No effect on localization to the endoplasmic reticulum membrane."; /evidence="ECO:0000269|PubMed:12754272
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by STUB1; does not lead to proteasomal degradation. {ECO:0000269|PubMed:15936278}.
uniprot
proteins
pubmed
12754272
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15936278
uniprot
proteins
pubmed
1599432
uniprot
proteins
pubmed
20889486
uniprot
proteins
pubmed
21625540
uniprot
proteins
pubmed
21719532
uniprot
proteins
pubmed
22219199
uniprot
proteins
pubmed
22396390
uniprot
proteins
pubmed
22522442
uniprot
proteins
pubmed
24023695
uniprot
proteins
pubmed
24627108
uniprot
proteins
pubmed
25274842
uniprot
proteins
pubmed
7957263
uniprot
proteins
sequence_length
324
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:12754272, ECO:0000269|PubMed:21625540}. Nucleus {ECO:0000269|PubMed:12754272}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12754272}; Lipid-anchor {ECO:0000269|PubMed:12754272}; Cytoplasmic side {ECO:0000269|PubMed:12754272}.
uniprot
proteins