DNJB9_HUMAN
ID DNJB9_HUMAN Reviewed; 223 AA.
AC Q9UBS3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DnaJ homolog subfamily B member 9 {ECO:0000305};
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 4 {ECO:0000303|PubMed:18400946};
DE Short=ER-resident protein ERdj4 {ECO:0000303|PubMed:18400946};
DE Short=ERdj4 {ECO:0000303|PubMed:18400946};
DE AltName: Full=Microvascular endothelial differentiation gene 1 protein {ECO:0000303|Ref.1};
DE Short=Mdg-1 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=DNAJB9; Synonyms=MDG1 {ECO:0000303|Ref.1};
GN ORFNames=UNQ743/PRO1471 {ECO:0000303|PubMed:12975309};
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 [MRNA].
RA Seki N., Hattori A., Muramatsu M., Miyajima N., Saito T.;
RT "Human microvascular endothelial differentiation gene 1.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=11836248; DOI=10.1074/jbc.m112214200;
RA Shen Y., Meunier L., Hendershot L.M.;
RT "Identification and characterization of a novel endoplasmic reticulum (ER)
RT DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is
RT induced by ER stress.";
RL J. Biol. Chem. 277:15947-15956(2002).
RN [7]
RP FUNCTION.
RX PubMed=18400946; DOI=10.1091/mbc.e07-07-0674;
RA Dong M., Bridges J.P., Apsley K., Xu Y., Weaver T.E.;
RT "ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein
RT degradation of misfolded surfactant protein C.";
RL Mol. Biol. Cell 19:2620-2630(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP STRUCTURE BY NMR OF 24-102.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of J-domain from human DnaJ subfamily B member 9.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key
CC repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By
CC similarity). J domain-containing co-chaperones stimulate the ATPase
CC activity of Hsp70 proteins and are required for efficient substrate
CC recognition by Hsp70 proteins (PubMed:18400946). In the unstressed
CC endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1
CC and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization
CC of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1
CC (By similarity). Also involved in endoplasmic reticulum-associated
CC degradation (ERAD) of misfolded proteins. Required for survival of B-
CC cell progenitors and normal antibody production (By similarity).
CC {ECO:0000250|UniProtKB:G3H0N9, ECO:0000250|UniProtKB:Q9QYI6,
CC ECO:0000269|PubMed:18400946}.
CC -!- SUBUNIT: Interacts with HSPA5/BiP; interaction is direct (By
CC similarity). Interacts with ERN1/IRE1 (via the luminal region) (By
CC similarity). Interacts with DERL1 (By similarity).
CC {ECO:0000250|UniProtKB:G3H0N9, ECO:0000250|UniProtKB:Q9QYI6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q9QYI6}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at highest level in the
CC liver, placenta and kidney (PubMed:11836248).
CC {ECO:0000269|PubMed:11836248}.
CC -!- DOMAIN: The J domain stimulates the ATPase activity of HSPA5/BiP, while
CC the divergent targeting domain is required for efficient substrate
CC recognition by HSPA5/BiP. The divergent targeting domain specifically
CC recognizes and binds to aggregation-prone sequences.
CC {ECO:0000250|UniProtKB:Q9QYI6}.
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DR EMBL; AB026908; BAA84703.1; -; mRNA.
DR EMBL; AF083247; AAD39845.1; -; mRNA.
DR EMBL; AL080081; CAB45701.1; -; mRNA.
DR EMBL; AY359045; AAQ89404.1; -; mRNA.
DR EMBL; BC028912; AAH28912.1; -; mRNA.
DR CCDS; CCDS5752.1; -.
DR PIR; T12472; T12472.
DR RefSeq; NP_036460.1; NM_012328.2.
DR PDB; 2CTR; NMR; -; A=26-100.
DR PDBsum; 2CTR; -.
DR AlphaFoldDB; Q9UBS3; -.
DR SMR; Q9UBS3; -.
DR BioGRID; 110354; 219.
DR IntAct; Q9UBS3; 38.
DR MINT; Q9UBS3; -.
DR STRING; 9606.ENSP00000249356; -.
DR iPTMnet; Q9UBS3; -.
DR PhosphoSitePlus; Q9UBS3; -.
DR BioMuta; DNAJB9; -.
DR DMDM; 18203496; -.
DR EPD; Q9UBS3; -.
DR jPOST; Q9UBS3; -.
DR MassIVE; Q9UBS3; -.
DR MaxQB; Q9UBS3; -.
DR PaxDb; Q9UBS3; -.
DR PeptideAtlas; Q9UBS3; -.
DR PRIDE; Q9UBS3; -.
DR ProteomicsDB; 84045; -.
DR Antibodypedia; 31469; 238 antibodies from 32 providers.
DR DNASU; 4189; -.
DR Ensembl; ENST00000249356.4; ENSP00000249356.3; ENSG00000128590.5.
DR GeneID; 4189; -.
DR KEGG; hsa:4189; -.
DR MANE-Select; ENST00000249356.4; ENSP00000249356.3; NM_012328.3; NP_036460.1.
DR UCSC; uc003vfn.4; human.
DR CTD; 4189; -.
DR DisGeNET; 4189; -.
DR GeneCards; DNAJB9; -.
DR HGNC; HGNC:6968; DNAJB9.
DR HPA; ENSG00000128590; Low tissue specificity.
DR MIM; 602634; gene.
DR neXtProt; NX_Q9UBS3; -.
DR OpenTargets; ENSG00000128590; -.
DR PharmGKB; PA27419; -.
DR VEuPathDB; HostDB:ENSG00000128590; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000156246; -.
DR HOGENOM; CLU_077239_0_0_1; -.
DR InParanoid; Q9UBS3; -.
DR OMA; HFDSHFQ; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q9UBS3; -.
DR TreeFam; TF105143; -.
DR PathwayCommons; Q9UBS3; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q9UBS3; -.
DR SIGNOR; Q9UBS3; -.
DR BioGRID-ORCS; 4189; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; DNAJB9; human.
DR EvolutionaryTrace; Q9UBS3; -.
DR GeneWiki; DNAJB9; -.
DR GenomeRNAi; 4189; -.
DR Pharos; Q9UBS3; Tbio.
DR PRO; PR:Q9UBS3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UBS3; protein.
DR Bgee; ENSG00000128590; Expressed in choroid plexus epithelium and 208 other tissues.
DR ExpressionAtlas; Q9UBS3; baseline and differential.
DR Genevisible; Q9UBS3; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0051787; F:misfolded protein binding; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP: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; Endoplasmic reticulum; Phosphoprotein;
KW Reference proteome; Signal; Unfolded protein response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..223
FT /note="DnaJ homolog subfamily B member 9"
FT /id="PRO_0000071031"
FT DOMAIN 26..90
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 91..223
FT /note="Divergent targeting domain"
FT /evidence="ECO:0000250|UniProtKB:Q9QYI6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 136
FT /note="R -> H (in dbSNP:rs17155937)"
FT /id="VAR_048911"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:2CTR"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:2CTR"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2CTR"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:2CTR"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2CTR"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2CTR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2CTR"
SQ SEQUENCE 223 AA; 25518 MW; 59E3E57FF8B378BC CRC64;
MATPQSIFIF AICILMITEL ILASKSYYDI LGVPKSASER QIKKAFHKLA MKYHPDKNKS
PDAEAKFREI AEAYETLSDA NRRKEYDTLG HSAFTSGKGQ RGSGSSFEQS FNFNFDDLFK
DFGFFGQNQN TGSKKRFENH FQTRQDGGSS RQRHHFQEFS FGGGLFDDMF EDMEKMFSFS
GFDSTNQHTV QTENRFHGSS KHCRTVTQRR GNMVTTYTDC SGQ
