DNJB6_MOUSE
ID DNJB6_MOUSE Reviewed; 365 AA.
AC O54946; Q3TE94; Q3U6L0; Q3UNJ5; Q3UYT7; Q99LA5; Q9QYI9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DnaJ homolog subfamily B member 6;
DE AltName: Full=Heat shock protein J2;
DE Short=HSJ-2;
DE AltName: Full=MRJ;
DE AltName: Full=mDj4;
GN Name=Dnajb6; Synonyms=Hsj2, Mrj;
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 B).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [MRNA] (ISOFORM B).
RC STRAIN=129; TISSUE=Trophoblast;
RA Hunter P.J., Swanson B.J., Haendel M., Lyons G.E., Cross J.C.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=B-cell, Bone marrow, Embryo, Embryonic stomach, Embryonic testis,
RC and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary gland;
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 [5]
RP INTERACTION WITH ALKBH1.
RX PubMed=18163532; DOI=10.1002/dvdy.21418;
RA Pan Z., Sikandar S., Witherspoon M., Dizon D., Nguyen T., Benirschke K.,
RA Wiley C., Vrana P., Lipkin S.M.;
RT "Impaired placental trophoblast lineage differentiation in Alkbh1(-/-)
RT mice.";
RL Dev. Dyn. 237:316-327(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays an indispensable role in the organization of KRT8/KRT18
CC filaments. Acts as an endogenous molecular chaperone for neuronal
CC proteins including huntingtin. Suppresses aggregation and toxicity of
CC polyglutamine-containing, aggregation-prone proteins (By similarity).
CC Has a stimulatory effect on the ATPase activity of HSP70 in a dose-
CC dependent and time-dependent manner and hence acts as a co-chaperone of
CC HSP70. Also reduces cellular toxicity and caspase-3 activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with BAG3, HSPB8 and
CC STUB1 (By similarity). Interacts with HSP70, KRT18 and PTTG. Isoform B
CC interacts with histone deacetylases HDAC4, HDAC6, and SIRT2, HDAC
CC activity is required for antiaggregation (By similarity). Interacts
CC with ALKBH1. {ECO:0000250, ECO:0000269|PubMed:18163532}.
CC -!- INTERACTION:
CC O54946; Q8BWG8: Arrb1; NbExp=6; IntAct=EBI-642500, EBI-641778;
CC O54946-2; P0CB42: Alkbh1; NbExp=2; IntAct=EBI-13941040, EBI-13941048;
CC O54946-2; P56524: HDAC4; Xeno; NbExp=2; IntAct=EBI-13941040, EBI-308629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}.
CC Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O54946-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O54946-2; Sequence=VSP_026212, VSP_026213;
CC -!- DOMAIN: The antiaggregation activity of resides in the serine-rich
CC region and the C-terminus. {ECO:0000250}.
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DR EMBL; AB028854; BAA88302.1; -; mRNA.
DR EMBL; AF035962; AAC16759.1; -; mRNA.
DR EMBL; AK133805; BAE21853.1; -; mRNA.
DR EMBL; AK134387; BAE22124.1; -; mRNA.
DR EMBL; AK144182; BAE25752.1; -; mRNA.
DR EMBL; AK151219; BAE30213.1; -; mRNA.
DR EMBL; AK151752; BAE30661.1; -; mRNA.
DR EMBL; AK152626; BAE31369.1; -; mRNA.
DR EMBL; AK152632; BAE31375.1; -; mRNA.
DR EMBL; AK153091; BAE31714.1; -; mRNA.
DR EMBL; AK169332; BAE41085.1; -; mRNA.
DR EMBL; AK169767; BAE41354.1; -; mRNA.
DR EMBL; BC003702; AAH03702.1; -; mRNA.
DR EMBL; BC083349; AAH83349.1; -; mRNA.
DR CCDS; CCDS19151.1; -. [O54946-1]
DR CCDS; CCDS39043.1; -. [O54946-2]
DR RefSeq; NP_001033029.1; NM_001037940.4. [O54946-1]
DR RefSeq; NP_001120839.1; NM_001127367.1.
DR RefSeq; NP_035977.2; NM_011847.4. [O54946-2]
DR AlphaFoldDB; O54946; -.
DR SMR; O54946; -.
DR BioGRID; 204812; 15.
DR IntAct; O54946; 7.
DR MINT; O54946; -.
DR STRING; 10090.ENSMUSP00000008733; -.
DR iPTMnet; O54946; -.
DR PhosphoSitePlus; O54946; -.
DR SwissPalm; O54946; -.
DR EPD; O54946; -.
DR MaxQB; O54946; -.
DR PaxDb; O54946; -.
DR PeptideAtlas; O54946; -.
DR PRIDE; O54946; -.
DR ProteomicsDB; 277479; -. [O54946-1]
DR ProteomicsDB; 277480; -. [O54946-2]
DR Antibodypedia; 3316; 330 antibodies from 31 providers.
DR DNASU; 23950; -.
DR Ensembl; ENSMUST00000008733; ENSMUSP00000008733; ENSMUSG00000029131. [O54946-1]
DR Ensembl; ENSMUST00000114839; ENSMUSP00000110488; ENSMUSG00000029131. [O54946-2]
DR GeneID; 23950; -.
DR KEGG; mmu:23950; -.
DR UCSC; uc008wup.2; mouse. [O54946-2]
DR UCSC; uc008wur.2; mouse. [O54946-1]
DR CTD; 10049; -.
DR MGI; MGI:1344381; Dnajb6.
DR VEuPathDB; HostDB:ENSMUSG00000029131; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000154205; -.
DR HOGENOM; CLU_017633_12_0_1; -.
DR InParanoid; O54946; -.
DR OMA; MFFGDST; -.
DR OrthoDB; 1152652at2759; -.
DR PhylomeDB; O54946; -.
DR TreeFam; TF105142; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 23950; 7 hits in 40 CRISPR screens.
DR ChiTaRS; Dnajb6; mouse.
DR PRO; PR:O54946; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O54946; protein.
DR Bgee; ENSMUSG00000029131; Expressed in animal zygote and 166 other tissues.
DR ExpressionAtlas; O54946; baseline and differential.
DR Genevisible; O54946; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR GO; GO:0060717; P:chorion development; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0060715; P:syncytiotrophoblast cell differentiation involved in labyrinthine layer development; IMP: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; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cytoplasm; Methylation; Nucleus;
KW Reference proteome.
FT CHAIN 1..365
FT /note="DnaJ homolog subfamily B member 6"
FT /id="PRO_0000071026"
FT DOMAIN 3..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..147
FT /note="Interaction with HSP70"
FT /evidence="ECO:0000250"
FT REGION 120..235
FT /note="Interaction with KRT18"
FT /evidence="ECO:0000250"
FT REGION 243..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 233..242
FT /note="VADENALAEE -> KEHLLRLDNK (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11147971,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.2"
FT /id="VSP_026212"
FT VAR_SEQ 243..365
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11147971,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.2"
FT /id="VSP_026213"
FT CONFLICT 117
FT /note="Missing (in Ref. 3; BAE41354)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..140
FT /note="GS -> AP (in Ref. 2; AAC16759)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="Missing (in Ref. 3; BAE25752)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="E -> V (in Ref. 4; AAH03702)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="S -> P (in Ref. 2; AAC16759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 39807 MW; 7B0102218E8DAA99 CRC64;
MVDYYEVLGV QRHASPEDIK KAYRKQALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK
KRDIYDKYGK EGLNGGGGGG GIHFDSPFEF GFTFRNPDDV FREFFGGRDP FSFDFFEDPF
DDFFGNRRGP RGNRSRGAGS FFSTFSGFPS FGSGFPAFDT GFTPFGSLGH GGLTSFSSTS
FGGSGMGNFK SISTSTKIVN GKKITTKRIV ENGQERVEVE EDGQLKSLTI NGVADENALA
EECQRRGQPT PALAPGPAPA PVRVPSQARP LAPTPAPTPA PTPAPAPAQT PAPSVSTRPQ
KPPRPAPTAK LGSKSNWEDD EQDRQRVPGN WDAPMTSAGL KEGGKRKKQK QKEDLKKKKS
TKGNH
