DNJB8_MOUSE
ID DNJB8_MOUSE Reviewed; 227 AA.
AC Q9QYI7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=DnaJ homolog subfamily B member 8;
DE AltName: Full=mDj6;
GN Name=Dnajb8;
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].
RC STRAIN=CD-1;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Efficient suppressor of aggregation and toxicity of disease-
CC associated polyglutamine proteins. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with histone deacetylases HDAC4, HDAC6, and SIRT2,
CC HDAC activity is required for antiaggregation. {ECO:0000250}.
CC -!- DOMAIN: The antiaggregation activity resides in the serine-rich region
CC and the C-terminus. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB028856; BAA88304.1; -; mRNA.
DR EMBL; AK006026; BAB24372.1; -; mRNA.
DR EMBL; BC049591; AAH49591.1; -; mRNA.
DR EMBL; BC061112; AAH61112.1; -; mRNA.
DR CCDS; CCDS20334.1; -.
DR RefSeq; NP_064348.1; NM_019964.1.
DR AlphaFoldDB; Q9QYI7; -.
DR SMR; Q9QYI7; -.
DR IntAct; Q9QYI7; 1.
DR STRING; 10090.ENSMUSP00000056592; -.
DR iPTMnet; Q9QYI7; -.
DR PhosphoSitePlus; Q9QYI7; -.
DR PaxDb; Q9QYI7; -.
DR PRIDE; Q9QYI7; -.
DR ProteomicsDB; 279458; -.
DR Antibodypedia; 33195; 114 antibodies from 19 providers.
DR DNASU; 56691; -.
DR Ensembl; ENSMUST00000061866; ENSMUSP00000056592; ENSMUSG00000048206.
DR GeneID; 56691; -.
DR KEGG; mmu:56691; -.
DR UCSC; uc009cve.1; mouse.
DR CTD; 165721; -.
DR MGI; MGI:1922801; Dnajb8.
DR VEuPathDB; HostDB:ENSMUSG00000048206; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000162567; -.
DR HOGENOM; CLU_017633_12_0_1; -.
DR InParanoid; Q9QYI7; -.
DR OMA; DFWDNPF; -.
DR OrthoDB; 1149729at2759; -.
DR PhylomeDB; Q9QYI7; -.
DR TreeFam; TF105142; -.
DR BioGRID-ORCS; 56691; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9QYI7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QYI7; protein.
DR Bgee; ENSMUSG00000048206; Expressed in seminiferous tubule of testis and 9 other tissues.
DR ExpressionAtlas; Q9QYI7; baseline and differential.
DR Genevisible; Q9QYI7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0051087; F:chaperone 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:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; 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; 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 2: Evidence at transcript level;
KW Chaperone; Reference proteome.
FT CHAIN 1..227
FT /note="DnaJ homolog subfamily B member 8"
FT /id="PRO_0000071030"
FT DOMAIN 3..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ SEQUENCE 227 AA; 25230 MW; 7A6E4CB7989FC095 CRC64;
MANYYEVLGV QSSASPEDIK KAYRKLALRW HPDKNPDNKE EAEKKFKQVS EAYEVLSDSK
KRSVYDRAGC DRWRAGGGAN VPHSSPFGAG YPFRNPEDIF REFFGGLDPF SFEFWDTPFS
GRGRPHGLHR VFPSGFGEFP AFMEALSSFN TLGHGGGSRS TFSSASFGGS GSSGFKSVMS
STEMVNGRKV TTKRIIENGQ ERVEVEEDGQ LRSVTVNGKE KLMRVDK