DNJB2_MOUSE
ID DNJB2_MOUSE Reviewed; 324 AA.
AC Q9QYI5; Q3TB24; Q8BPF6; Q921S2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DnaJ homolog subfamily B member 2 {ECO:0000305};
DE AltName: Full=DnaJ homolog subfamily B member 10 {ECO:0000303|PubMed:11147971};
DE AltName: Full=mDj8 {ECO:0000312|EMBL:BAA88306.1};
DE Flags: Precursor;
GN Name=Dnajb2 {ECO:0000312|MGI:MGI:1928739};
GN Synonyms=Dnajb10 {ECO:0000303|PubMed:11147971};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
RX PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for
RT their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as a co-chaperone, regulating the substrate binding
CC and activating the ATPase activity of chaperones of the HSP70/heat
CC shock protein 70 family. In parallel, also contributes to the
CC ubiquitin-dependent proteasomal degradation of misfolded proteins.
CC Thereby, may regulate the aggregation and promote the functional
CC recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and
CC be crucial for many biological processes. Isoform 1 which is localized
CC to the endoplasmic reticulum membranes may specifically function in ER-
CC associated protein degradation of misfolded proteins.
CC {ECO:0000250|UniProtKB:P25686}.
CC -!- SUBUNIT: Interacts with HSP70 (HSPA1A or HSPA1B). Interacts with
CC HSPA8/Hsc70. Interacts with PSMA3 and most probably with the whole
CC proteasomal complex. {ECO:0000250|UniProtKB:P25686}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:P25686}. Nucleus {ECO:0000250|UniProtKB:P25686}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P25686}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P25686}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P25686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QYI5-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYI5-1; Sequence=VSP_058709, VSP_058710;
CC Name=3;
CC IsoId=Q9QYI5-2; Sequence=VSP_058708, VSP_058709, VSP_058710;
CC -!- DOMAIN: The J domain is sufficient to interact with HSP70 (HSPA1A or
CC HSPA1B) and activate its ATPase activity. The J domain is also required
CC for the HSP70-mediated and ubiquitin-dependent proteasomal degradation
CC of proteins like ATXN3. The J domain is required to reduce PRKN
CC cytoplasmic aggregation. {ECO:0000250|UniProtKB:P25686}.
CC -!- DOMAIN: The UIM domains mediate interaction with ubiquitinated
CC chaperone clients and with the proteasome. The UIM domains may have an
CC opposite activity to the J domain, binding ubiquitinated proteins and
CC protecting them from HSP70-mediated proteasomal degradation. The UIM
CC domains are not required to reduce PRKN cytoplasmic aggregation.
CC {ECO:0000250|UniProtKB:P25686}.
CC -!- PTM: Ubiquitinated by STUB1; does not lead to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P25686}.
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DR EMBL; AB028858; BAA88306.1; -; mRNA.
DR EMBL; AK076061; BAC36155.1; -; mRNA.
DR EMBL; AK156083; BAE33579.1; -; mRNA.
DR EMBL; AK171494; BAE42490.1; -; mRNA.
DR EMBL; AC166150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011090; AAH11090.1; -; mRNA.
DR CCDS; CCDS15068.1; -. [Q9QYI5-2]
DR CCDS; CCDS35624.1; -. [Q9QYI5-1]
DR CCDS; CCDS78622.1; -. [Q9QYI5-3]
DR RefSeq; NP_001153355.1; NM_001159883.1. [Q9QYI5-3]
DR RefSeq; NP_001153356.1; NM_001159884.1. [Q9QYI5-1]
DR RefSeq; NP_001153357.1; NM_001159885.1. [Q9QYI5-1]
DR RefSeq; NP_064662.2; NM_020266.2. [Q9QYI5-2]
DR RefSeq; NP_835156.1; NM_178055.4. [Q9QYI5-1]
DR AlphaFoldDB; Q9QYI5; -.
DR SMR; Q9QYI5; -.
DR BioGRID; 208186; 3.
DR IntAct; Q9QYI5; 1.
DR STRING; 10090.ENSMUSP00000140566; -.
DR iPTMnet; Q9QYI5; -.
DR PhosphoSitePlus; Q9QYI5; -.
DR EPD; Q9QYI5; -.
DR MaxQB; Q9QYI5; -.
DR PaxDb; Q9QYI5; -.
DR PeptideAtlas; Q9QYI5; -.
DR PRIDE; Q9QYI5; -.
DR ProteomicsDB; 279743; -. [Q9QYI5-3]
DR ProteomicsDB; 279744; -. [Q9QYI5-1]
DR ProteomicsDB; 279745; -. [Q9QYI5-2]
DR Antibodypedia; 34321; 372 antibodies from 32 providers.
DR DNASU; 56812; -.
DR Ensembl; ENSMUST00000055223; ENSMUSP00000052520; ENSMUSG00000026203. [Q9QYI5-2]
DR Ensembl; ENSMUST00000082158; ENSMUSP00000080796; ENSMUSG00000026203. [Q9QYI5-1]
DR Ensembl; ENSMUST00000187058; ENSMUSP00000140637; ENSMUSG00000026203. [Q9QYI5-2]
DR Ensembl; ENSMUST00000188290; ENSMUSP00000140634; ENSMUSG00000026203. [Q9QYI5-1]
DR Ensembl; ENSMUST00000188346; ENSMUSP00000140588; ENSMUSG00000026203. [Q9QYI5-1]
DR Ensembl; ENSMUST00000188931; ENSMUSP00000140566; ENSMUSG00000026203. [Q9QYI5-3]
DR GeneID; 56812; -.
DR KEGG; mmu:56812; -.
DR UCSC; uc007bom.2; mouse. [Q9QYI5-3]
DR UCSC; uc007bon.2; mouse.
DR UCSC; uc007bop.2; mouse. [Q9QYI5-2]
DR CTD; 3300; -.
DR MGI; MGI:1928739; Dnajb2.
DR VEuPathDB; HostDB:ENSMUSG00000026203; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000160220; -.
DR HOGENOM; CLU_017633_12_0_1; -.
DR InParanoid; Q9QYI5; -.
DR OMA; FFDDMLP; -.
DR OrthoDB; 1472647at2759; -.
DR TreeFam; TF105142; -.
DR BioGRID-ORCS; 56812; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Dnajb2; mouse.
DR PRO; PR:Q9QYI5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QYI5; protein.
DR Bgee; ENSMUSG00000026203; Expressed in motor neuron and 260 other tissues.
DR ExpressionAtlas; Q9QYI5; baseline and differential.
DR Genevisible; Q9QYI5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0140036; F:ubiquitin-dependent protein binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0090086; P:negative regulation of protein deubiquitination; ISO:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0042026; P:protein refolding; ISO:MGI.
DR GO; GO:1903644; P:regulation of chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR043183; DNJB2.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR45168; PTHR45168; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50330; UIM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CHAIN 2..321
FT /note="DnaJ homolog subfamily B member 2"
FT /id="PRO_0000438688"
FT PROPEP 322..324
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P25686"
FT /id="PRO_0000438689"
FT DOMAIN 3..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 207..226
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 250..269
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 70..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 321..324
FT /note="CAAX motif"
FT /evidence="ECO:0000250|UniProtKB:P25686"
FT COMPBIAS 286..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P25686"
FT LIPID 321
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P25686"
FT VAR_SEQ 59..77
FT /note="KHKREIYDRYGREGLTGAG -> R (in isoform 3)"
FT /id="VSP_058708"
FT VAR_SEQ 275..277
FT /note="GGR -> DVF (in isoform 3 and isoform 2)"
FT /id="VSP_058709"
FT VAR_SEQ 278..324
FT /note="Missing (in isoform 3 and isoform 2)"
FT /id="VSP_058710"
FT CONFLICT 15
FT /note="S -> F (in Ref. 3; AAH11090)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="V -> F (in Ref. 1; BAA88306)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="D -> N (in Ref. 1; BAA88306)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> K (in Ref. 1; BAA88306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 35593 MW; C00006AAC12574FA CRC64;
MASYYEILDV PRSASPDDIK KAYRKKALQW HPDKNPDNKE FAEKKFKEVA EAYEVLSDKH
KREIYDRYGR EGLTGAGSGP SRSETGGAGP GFTFTFRSPE EVFREFFGSG DPFSELFDDL
GVFSELQNQG PRLTGPFFTF SSSFPANSDF SSSSFSFSPG AGAFRSVSTS TTFVQGRRIT
TRRIMENGQE RVEVEEDGQL KSVSINGVPD DLALGLELSR REQQPSVAPG LGVMQVRPTS
LSRPPDHDLS EDEDLQLAMA YSLSEMEAAG QKPAGGRGAQ QRQHGQPKAQ HRDLDVGGTH
KSVRGEAAKL SPSSEEKASR CHIL
