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DnaJ homolog subfamily B member 2 (Heat shock 40 kDa protein 3) (Heat shock protein J1) (HSJ-1)

 DNJB2_HUMAN             Reviewed;         324 AA.
P25686; A8K9P6; Q53QD7; Q8IUK1; Q8IUK2; Q96F52;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 3.
27-SEP-2017, entry version 168.
RecName: Full=DnaJ homolog subfamily B member 2 {ECO:0000305};
AltName: Full=Heat shock 40 kDa protein 3 {ECO:0000312|MIM:604139};
AltName: Full=Heat shock protein J1 {ECO:0000303|PubMed:1599432};
Short=HSJ-1 {ECO:0000303|PubMed:1599432};
Flags: Precursor;
Name=DNAJB2 {ECO:0000312|HGNC:HGNC:5228};
Synonyms=HSJ1 {ECO:0000303|PubMed:1599432},
HSPF3 {ECO:0000312|MIM:604139};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1599432; DOI=10.1042/bj2840469;
Cheetham M.E., Brion J.-P., Anderton B.H.;
"Human homologues of the bacterial heat-shock protein DnaJ are
preferentially expressed in neurons.";
Biochem. J. 284:469-476(1992).
[2]
SEQUENCE REVISION TO 214.
Cheetham M.E.;
Submitted (JUL-1998) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION.
PubMed=7957263; DOI=10.1111/j.1432-1033.1994.tb20030.x;
Cheetham M.E., Jackson A.P., Anderton B.H.;
"Regulation of 70-kDa heat-shock-protein ATPase activity and substrate
binding by human DnaJ-like proteins, HSJ1a and HSJ1b.";
Eur. J. Biochem. 226:99-107(1994).
[9]
FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TOPOLOGY (ISOFORM
1), TISSUE SPECIFICITY (ISOFORMS 1 AND 2), MUTAGENESIS OF HIS-31;
CYS-321 AND LEU-324, ISOPRENYLATION AT CYS-321, METHYLATION AT
CYS-321, AND MOTIF.
PubMed=12754272; DOI=10.1074/jbc.M212349200;
Chapple J.P., Cheetham M.E.;
"The chaperone environment at the cytoplasmic face of the endoplasmic
reticulum can modulate rhodopsin processing and inclusion formation.";
J. Biol. Chem. 278:19087-19094(2003).
[10]
FUNCTION, INTERACTION WITH HSPA8 AND PSMA3, UBIQUITINATION BY STUB1,
DOMAIN, AND MUTAGENESIS OF 31-HIS--ASP-33; SER-219; GLU-222; SER-262
AND GLU-265.
PubMed=15936278; DOI=10.1016/j.cub.2005.04.058;
Westhoff B., Chapple J.P., van der Spuy J., Hoehfeld J.,
Cheetham M.E.;
"HSJ1 is a neuronal shuttling factor for the sorting of chaperone
clients to the proteasome.";
Curr. Biol. 15:1058-1064(2005).
[11]
FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-31.
PubMed=20889486; DOI=10.1093/hmg/ddq428;
Rose J.M., Novoselov S.S., Robinson P.A., Cheetham M.E.;
"Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1
domain mutant.";
Hum. Mol. Genet. 20:16-27(2011).
[12]
FUNCTION.
PubMed=21719532; DOI=10.1210/me.2011-1020;
Meimaridou E., Gooljar S.B., Ramnarace N., Anthonypillai L.,
Clark A.J., Chapple J.P.;
"The cytosolic chaperone Hsc70 promotes traffic to the cell surface of
intracellular retained melanocortin-4 receptor mutants.";
Mol. Endocrinol. 25:1650-1660(2011).
[13]
FUNCTION, INTERACTION WITH HSP70, SUBCELLULAR LOCATION, DOMAIN, AND
MUTAGENESIS OF 31-HIS--ASP-33; SER-219; GLU-222; SER-262 AND GLU-265.
PubMed=21625540; DOI=10.1371/journal.pone.0019763;
Gao X.C., Zhou C.J., Zhou Z.R., Zhang Y.H., Zheng X.M., Song A.X.,
Hu H.Y.;
"Co-chaperone HSJ1a dually regulates the proteasomal degradation of
ataxin-3.";
PLoS ONE 6:E19763-E19763(2011).
[14]
INVOLVEMENT IN DSMA5.
PubMed=22522442; DOI=10.1002/ana.22684;
Blumen S.C., Astord S., Robin V., Vignaud L., Toumi N., Cieslik A.,
Achiron A., Carasso R.L., Gurevich M., Braverman I., Blumen N.,
Munich A., Barkats M., Viollet L.;
"A rare recessive distal hereditary motor neuropathy with HSJ1
chaperone mutation.";
Ann. Neurol. 71:509-519(2012).
[15]
FUNCTION.
PubMed=22396390; DOI=10.1093/brain/aws022;
Labbadia J., Novoselov S.S., Bett J.S., Weiss A., Paganetti P.,
Bates G.P., Cheetham M.E.;
"Suppression of protein aggregation by chaperone modification of high
molecular weight complexes.";
Brain 135:1180-1196(2012).
[16]
FUNCTION.
PubMed=24023695; DOI=10.1371/journal.pone.0073944;
Novoselov S.S., Mustill W.J., Gray A.L., Dick J.R., Kanuga N.,
Kalmar B., Greensmith L., Cheetham M.E.;
"Molecular chaperone mediated late-stage neuroprotection in the
SOD1(G93A) mouse model of amyotrophic lateral sclerosis.";
PLoS ONE 8:E73944-E73944(2013).
[17]
INVOLVEMENT IN DSMA5, AND VARIANT DSMA5 CYS-5.
PubMed=24627108; DOI=10.1007/s00415-014-7289-8;
Schabhuettl M., Wieland T., Senderek J., Baets J., Timmerman V.,
De Jonghe P., Reilly M.M., Stieglbauer K., Laich E., Windhager R.,
Erwa W., Trajanoski S., Strom T.M., Auer-Grumbach M.;
"Whole-exome sequencing in patients with inherited neuropathies:
outcome and challenges.";
J. Neurol. 261:970-982(2014).
[18]
INVOLVEMENT IN DSMA5, AND VARIANT DSMA5 CYS-5.
PubMed=25274842; DOI=10.1212/WNL.0000000000000966;
Gess B., Auer-Grumbach M., Schirmacher A., Strom T., Zitzelsberger M.,
Rudnik-Schoneborn S., Rohr D., Halfter H., Young P., Senderek J.;
"HSJ1-related hereditary neuropathies: novel mutations and extended
clinical spectrum.";
Neurology 83:1726-1732(2014).
[19]
STRUCTURE BY NMR OF 1-71, FUNCTION, INTERACTION WITH HSP70, AND
DOMAIN.
PubMed=22219199; DOI=10.1074/jbc.M111.294728;
Gao X.C., Zhou C.J., Zhou Z.R., Wu M., Cao C.Y., Hu H.Y.;
"The C-terminal helices of heat shock protein 70 are essential for J-
domain binding and ATPase activation.";
J. Biol. Chem. 287:6044-6052(2012).
-!- 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:7957263,
PubMed:22219199). 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}.
-!- SUBUNIT: Interacts with HSP70 (HSPA1A or HSPA1B) (PubMed:21625540,
PubMed:22219199). Interacts with HSPA8/Hsc70 (PubMed:15936278).
Interacts with PSMA3 and most probably with the whole proteasomal
complex (PubMed:15936278). {ECO:0000269|PubMed:15936278,
ECO:0000269|PubMed:21625540, ECO:0000269|PubMed:22219199}.
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=HSJ1b {ECO:0000303|PubMed:1599432};
IsoId=P25686-3; Sequence=Displayed;
Name=2; Synonyms=HSJ1a {ECO:0000303|PubMed:1599432}, DNAJB2a
{ECO:0000303|PubMed:20889486};
IsoId=P25686-2; Sequence=VSP_001286, VSP_001287;
-!- TISSUE SPECIFICITY: More abundantly expressed in neocortex,
cerebellum, spinal cord and retina where it is expressed by
neuronal cells (at protein level) (PubMed:1599432,
PubMed:12754272). Detected at much lower level in non-neuronal
tissues including kidney, lung, heart, skeletal muscle, spleen and
testis (at protein level) (PubMed:12754272, PubMed:1599432).
Isoform 1 is more abundant in neocortex and cerebellum compared to
isoform 2 (at protein level) (PubMed:12754272).
{ECO:0000269|PubMed:12754272, ECO:0000269|PubMed:1599432}.
-!- DOMAIN: The J domain is sufficient to interact with HSP70 (HSPA1A
or HSPA1B) and activate its ATPase activity (PubMed:22219199). The
J domain is also required for the HSP70-mediated and ubiquitin-
dependent proteasomal degradation of proteins like ATXN3
(PubMed:21625540). The J domain is required to reduce PRKN
cytoplasmic aggregation (PubMed:20889486).
{ECO:0000269|PubMed:20889486, ECO:0000269|PubMed:21625540,
ECO:0000269|PubMed:22219199}.
-!- DOMAIN: The UIM domains mediate interaction with ubiquitinated
chaperone clients and with the proteasome (PubMed:15936278). The
UIM domains may have an opposite activity to the J domain, binding
ubiquitinated proteins and protecting them from HSP70-mediated
proteasomal degradation (PubMed:21625540). The UIM domains are not
required to reduce PRKN cytoplasmic aggregation (PubMed:20889486).
{ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:20889486,
ECO:0000269|PubMed:21625540}.
-!- PTM: Ubiquitinated by STUB1; does not lead to proteasomal
degradation. {ECO:0000269|PubMed:15936278}.
-!- DISEASE: Distal spinal muscular atrophy, autosomal recessive, 5
(DSMA5) [MIM:614881]: An autosomal recessive neurologic disorder
characterized by young adult onset of slowly progressive distal
muscle weakness and atrophy resulting in gait impairment and loss
of reflexes due to impaired function of motor nerves. Sensation
and cognition are not impaired. {ECO:0000269|PubMed:22522442,
ECO:0000269|PubMed:24627108, ECO:0000269|PubMed:25274842}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA09035.1; Type=Frameshift; Positions=288; Evidence={ECO:0000305};
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EMBL; S37375; AAA09034.1; -; mRNA.
EMBL; S37374; AAA09035.1; ALT_FRAME; mRNA.
EMBL; X63368; CAA44968.2; -; Genomic_DNA.
EMBL; X63368; CAA44969.2; -; Genomic_DNA.
EMBL; BT007088; AAP35751.1; -; mRNA.
EMBL; AK292761; BAF85450.1; -; mRNA.
EMBL; AK312723; BAG35597.1; -; mRNA.
EMBL; AC114803; AAY24037.1; -; Genomic_DNA.
EMBL; CH471063; EAW70722.1; -; Genomic_DNA.
EMBL; BC011609; AAH11609.1; -; mRNA.
EMBL; BC047056; AAH47056.1; -; mRNA.
CCDS; CCDS2439.1; -. [P25686-3]
CCDS; CCDS46519.1; -. [P25686-2]
PIR; S23508; S23508.
RefSeq; NP_001034639.1; NM_001039550.1. [P25686-2]
RefSeq; NP_006727.2; NM_006736.5. [P25686-3]
UniGene; Hs.77768; -.
PDB; 2LGW; NMR; -; A=1-91.
PDBsum; 2LGW; -.
ProteinModelPortal; P25686; -.
SMR; P25686; -.
BioGrid; 109533; 47.
CORUM; P25686; -.
DIP; DIP-29051N; -.
IntAct; P25686; 15.
MINT; MINT-1192251; -.
STRING; 9606.ENSP00000338019; -.
iPTMnet; P25686; -.
PhosphoSitePlus; P25686; -.
BioMuta; DNAJB2; -.
DMDM; 158518384; -.
EPD; P25686; -.
PaxDb; P25686; -.
PeptideAtlas; P25686; -.
PRIDE; P25686; -.
DNASU; 3300; -.
Ensembl; ENST00000336576; ENSP00000338019; ENSG00000135924. [P25686-3]
Ensembl; ENST00000392086; ENSP00000375936; ENSG00000135924. [P25686-2]
GeneID; 3300; -.
KEGG; hsa:3300; -.
UCSC; uc002vkw.2; human. [P25686-3]
CTD; 3300; -.
DisGeNET; 3300; -.
EuPathDB; HostDB:ENSG00000135924.15; -.
GeneCards; DNAJB2; -.
HGNC; HGNC:5228; DNAJB2.
HPA; HPA036268; -.
MalaCards; DNAJB2; -.
MIM; 604139; gene.
MIM; 614881; phenotype.
neXtProt; NX_P25686; -.
OpenTargets; ENSG00000135924; -.
Orphanet; 314485; Young adult-onset distal hereditary motor neuropathy.
PharmGKB; PA27415; -.
eggNOG; KOG0714; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00760000118947; -.
HOGENOM; HOG000111538; -.
HOVERGEN; HBG066998; -.
InParanoid; P25686; -.
KO; K09508; -.
OMA; TFTFRNP; -.
OrthoDB; EOG091G152F; -.
PhylomeDB; P25686; -.
TreeFam; TF105142; -.
ChiTaRS; DNAJB2; human.
GeneWiki; DNAJB2; -.
GenomeRNAi; 3300; -.
PRO; PR:P25686; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000135924; -.
CleanEx; HS_DNAJB2; -.
ExpressionAtlas; P25686; baseline and differential.
Genevisible; P25686; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
GO; GO:0061077; P:chaperone-mediated protein folding; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IGI:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:UniProtKB.
GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0090086; P:negative regulation of protein deubiquitination; IDA:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
GO; GO:1903644; P:regulation of chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; IMP:ParkinsonsUK-UCL.
GO; GO:0031396; P:regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:BHF-UCL.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR003903; UIM_dom.
Pfam; PF00226; DnaJ; 1.
Pfam; PF02809; UIM; 2.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SMART; SM00726; UIM; 2.
SUPFAM; SSF46565; SSF46565; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS50330; UIM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chaperone;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Lipoprotein;
Membrane; Methylation; Neurodegeneration; Nucleus; Phosphoprotein;
Polymorphism; Prenylation; Reference proteome; Repeat;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9QYI5}.
CHAIN 2 321 DnaJ homolog subfamily B member 2.
/FTId=PRO_0000071018.
PROPEP 322 324 Removed in mature form.
{ECO:0000305|PubMed:12754272}.
/FTId=PRO_0000438687.
DOMAIN 2 71 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
DOMAIN 210 226 UIM 1. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 250 269 UIM 2. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
MOTIF 321 324 CAAX motif.
{ECO:0000269|PubMed:12754272}.
COMPBIAS 141 170 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9QYI5}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QYI5}.
MOD_RES 321 321 Cysteine methyl ester.
{ECO:0000305|PubMed:12754272}.
LIPID 321 321 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:12754272}.
VAR_SEQ 275 277 GGR -> DVF (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_001286.
VAR_SEQ 278 324 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_001287.
VARIANT 5 5 Y -> C (in DSMA5; dbSNP:rs730882140).
{ECO:0000269|PubMed:24627108,
ECO:0000269|PubMed:25274842}.
/FTId=VAR_073286.
VARIANT 270 270 G -> R (in dbSNP:rs34127289).
/FTId=VAR_048910.
MUTAGEN 31 33 HPD->QPN: Loss of interaction with HSP70
and loss of the ability to promote ATXN3
proteasomal degradation.
{ECO:0000269|PubMed:21625540}.
MUTAGEN 31 31 H->Q: Probable loss of interaction with
HSP70 and loss of the ability to reduce
PRKN aggregation.
{ECO:0000269|PubMed:12754272,
ECO:0000269|PubMed:20889486}.
MUTAGEN 219 219 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.
{ECO:0000269|PubMed:15936278,
ECO:0000269|PubMed:21625540}.
MUTAGEN 222 222 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.
{ECO:0000269|PubMed:15936278,
ECO:0000269|PubMed:21625540}.
MUTAGEN 262 262 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.
{ECO:0000269|PubMed:15936278,
ECO:0000269|PubMed:21625540}.
MUTAGEN 265 265 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.
{ECO:0000269|PubMed:15936278,
ECO:0000269|PubMed:21625540}.
MUTAGEN 321 321 C->S: Loss of localization to the
endoplasmic reticulum and relocalization
to cytoplasm and nucleus.
{ECO:0000269|PubMed:12754272}.
MUTAGEN 324 324 L->M: No effect on localization to the
endoplasmic reticulum membrane.
{ECO:0000269|PubMed:12754272}.
CONFLICT 214 214 L -> R (in Ref. 1; AAA09034/AAA09035).
{ECO:0000305}.
HELIX 4 7 {ECO:0000244|PDB:2LGW}.
STRAND 8 10 {ECO:0000244|PDB:2LGW}.
HELIX 16 29 {ECO:0000244|PDB:2LGW}.
TURN 32 34 {ECO:0000244|PDB:2LGW}.
HELIX 40 57 {ECO:0000244|PDB:2LGW}.
HELIX 59 70 {ECO:0000244|PDB:2LGW}.
SEQUENCE 324 AA; 35580 MW; 0154ED3E29F34B4A CRC64;
MASYYEILDV PRSASADDIK KAYRRKALQW HPDKNPDNKE FAEKKFKEVA EAYEVLSDKH
KREIYDRYGR EGLTGTGTGP SRAEAGSGGP GFTFTFRSPE EVFREFFGSG DPFAELFDDL
GPFSELQNRG SRHSGPFFTF SSSFPGHSDF SSSSFSFSPG AGAFRSVSTS TTFVQGRRIT
TRRIMENGQE RVEVEEDGQL KSVTINGVPD DLALGLELSR REQQPSVTSR SGGTQVQQTP
ASCPLDSDLS EDEDLQLAMA YSLSEMEAAG KKPAGGREAQ HRRQGRPKAQ HQDPGLGGTQ
EGARGEATKR SPSPEEKASR CLIL


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