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DNJB8_HUMAN
ID   DNJB8_HUMAN             Reviewed;         232 AA.
AC   Q8NHS0; B3KWV7;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=DnaJ homolog subfamily B member 8;
GN   Name=DNAJB8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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).
RN   [4]
RP   FUNCTION, INTERACTION WITH HDACS, AND MUTAGENESIS OF LYS-216.
RX   PubMed=20159555; DOI=10.1016/j.molcel.2010.01.001;
RA   Hageman J., Rujano M.A., van Waarde M.A., Kakkar V., Dirks R.P.,
RA   Govorukhina N., Oosterveld-Hut H.M., Lubsen N.H., Kampinga H.H.;
RT   "A DNAJB chaperone subfamily with HDAC-dependent activities suppresses
RT   toxic protein aggregation.";
RL   Mol. Cell 37:355-369(2010).
RN   [5]
RP   STRUCTURE BY NMR OF 1-82.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the J domain of DnaJ homolog subfamily B member 8.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: Efficient suppressor of aggregation and toxicity of disease-
CC       associated polyglutamine proteins. {ECO:0000269|PubMed:20159555}.
CC   -!- SUBUNIT: Interacts with histone deacetylases HDAC4, HDAC6, and SIRT2,
CC       HDAC activity is required for antiaggregation.
CC       {ECO:0000269|PubMed:20159555}.
CC   -!- DOMAIN: The antiaggregation activity resides in the serine-rich region
CC       and the C-terminus.
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DR   EMBL; AK125946; BAG54269.1; -; mRNA.
DR   EMBL; AK126068; BAG54285.1; -; mRNA.
DR   EMBL; CH471052; EAW79320.1; -; Genomic_DNA.
DR   EMBL; BC029521; AAH29521.1; -; mRNA.
DR   EMBL; BC050288; AAH50288.1; -; mRNA.
DR   CCDS; CCDS3048.1; -.
DR   RefSeq; NP_699161.1; NM_153330.4.
DR   RefSeq; XP_006713582.1; XM_006713519.3.
DR   PDB; 2DMX; NMR; -; A=1-79.
DR   PDBsum; 2DMX; -.
DR   AlphaFoldDB; Q8NHS0; -.
DR   BMRB; Q8NHS0; -.
DR   SMR; Q8NHS0; -.
DR   BioGRID; 127919; 81.
DR   IntAct; Q8NHS0; 9.
DR   STRING; 9606.ENSP00000417418; -.
DR   iPTMnet; Q8NHS0; -.
DR   PhosphoSitePlus; Q8NHS0; -.
DR   BioMuta; DNAJB8; -.
DR   DMDM; 27805461; -.
DR   jPOST; Q8NHS0; -.
DR   MassIVE; Q8NHS0; -.
DR   MaxQB; Q8NHS0; -.
DR   PaxDb; Q8NHS0; -.
DR   PeptideAtlas; Q8NHS0; -.
DR   PRIDE; Q8NHS0; -.
DR   ProteomicsDB; 73744; -.
DR   Antibodypedia; 33195; 114 antibodies from 19 providers.
DR   DNASU; 165721; -.
DR   Ensembl; ENST00000319153.4; ENSP00000316053.3; ENSG00000179407.4.
DR   Ensembl; ENST00000469083.1; ENSP00000417418.1; ENSG00000179407.4.
DR   GeneID; 165721; -.
DR   KEGG; hsa:165721; -.
DR   MANE-Select; ENST00000319153.4; ENSP00000316053.3; NM_153330.6; NP_699161.1.
DR   UCSC; uc003ekk.3; human.
DR   CTD; 165721; -.
DR   DisGeNET; 165721; -.
DR   GeneCards; DNAJB8; -.
DR   HGNC; HGNC:23699; DNAJB8.
DR   HPA; ENSG00000179407; Tissue enriched (testis).
DR   MIM; 611337; gene.
DR   neXtProt; NX_Q8NHS0; -.
DR   OpenTargets; ENSG00000179407; -.
DR   PharmGKB; PA134881798; -.
DR   VEuPathDB; HostDB:ENSG00000179407; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000162567; -.
DR   HOGENOM; CLU_017633_12_0_1; -.
DR   InParanoid; Q8NHS0; -.
DR   OMA; DFWDNPF; -.
DR   OrthoDB; 1149729at2759; -.
DR   PhylomeDB; Q8NHS0; -.
DR   TreeFam; TF105142; -.
DR   PathwayCommons; Q8NHS0; -.
DR   SignaLink; Q8NHS0; -.
DR   BioGRID-ORCS; 165721; 11 hits in 1070 CRISPR screens.
DR   EvolutionaryTrace; Q8NHS0; -.
DR   GenomeRNAi; 165721; -.
DR   Pharos; Q8NHS0; Tbio.
DR   PRO; PR:Q8NHS0; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8NHS0; protein.
DR   Bgee; ENSG00000179407; Expressed in sperm and 28 other tissues.
DR   ExpressionAtlas; Q8NHS0; baseline and differential.
DR   Genevisible; Q8NHS0; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR   GO; GO:0044183; F:protein folding chaperone; IDA:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IDA:MGI.
DR   GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
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   3D-structure; Chaperone; Reference proteome.
FT   CHAIN           1..232
FT                   /note="DnaJ homolog subfamily B member 8"
FT                   /id="PRO_0000071029"
FT   DOMAIN          3..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   VARIANT         153
FT                   /note="M -> L (in dbSNP:rs35948511)"
FT                   /id="VAR_033881"
FT   MUTAGEN         216
FT                   /note="K->A: Significant loss of activity."
FT                   /evidence="ECO:0000269|PubMed:20159555"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:2DMX"
FT   HELIX           18..29
FT                   /evidence="ECO:0007829|PDB:2DMX"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:2DMX"
FT   HELIX           40..57
FT                   /evidence="ECO:0007829|PDB:2DMX"
FT   HELIX           59..68
FT                   /evidence="ECO:0007829|PDB:2DMX"
SQ   SEQUENCE   232 AA;  25686 MW;  058B180995B772F6 CRC64;
     MANYYEVLGV QASASPEDIK KAYRKLALRW HPDKNPDNKE EAEKKFKLVS EAYEVLSDSK
     KRSLYDRAGC DSWRAGGGAS TPYHSPFDTG YTFRNPEDIF REFFGGLDPF SFEFWDSPFN
     SDRGGRGHGL RGAFSAGFGE FPAFMEAFSS FNMLGCSGGS HTTFSSTSFG GSSSGSSGFK
     SVMSSTEMIN GHKVTTKRIV ENGQERVEVE EDGQLKSVTV NGKEQLKWMD SK
 
 
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