Full text data of DNAJB11
DNAJB11
(EDJ, ERJ3, HDJ9)
[Confidence: high (present in two of the MS resources)]
DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2; ABBP-2; DnaJ protein homolog 9; ER-associated DNAJ; ER-associated Hsp40 co-chaperone; Endoplasmic reticulum DNA J domain-containing protein 3; ER-resident protein ERdj3; ERdj3; ERj3p; HEDJ; Human DnaJ protein 9; hDj-9; PWP1-interacting protein 4; Flags: Precursor)
DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2; ABBP-2; DnaJ protein homolog 9; ER-associated DNAJ; ER-associated Hsp40 co-chaperone; Endoplasmic reticulum DNA J domain-containing protein 3; ER-resident protein ERdj3; ERdj3; ERj3p; HEDJ; Human DnaJ protein 9; hDj-9; PWP1-interacting protein 4; Flags: Precursor)
UniProt
Q9UBS4
ID DJB11_HUMAN Reviewed; 358 AA.
AC Q9UBS4; Q542Y5; Q542Y9; Q6IAQ8; Q96JC6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=DnaJ homolog subfamily B member 11;
DE AltName: Full=APOBEC1-binding protein 2;
DE Short=ABBP-2;
DE AltName: Full=DnaJ protein homolog 9;
DE AltName: Full=ER-associated DNAJ;
DE AltName: Full=ER-associated Hsp40 co-chaperone;
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3;
DE Short=ER-resident protein ERdj3;
DE Short=ERdj3;
DE Short=ERj3p;
DE AltName: Full=HEDJ;
DE AltName: Full=Human DnaJ protein 9;
DE Short=hDj-9;
DE AltName: Full=PWP1-interacting protein 4;
DE Flags: Precursor;
GN Name=DNAJB11; Synonyms=EDJ, ERJ3, HDJ9;
GN ORFNames=PSEC0121, UNQ537/PRO1080;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11147971;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal
RT for their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH HSPA5, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Skeletal muscle;
RX PubMed=10827079; DOI=10.1074/jbc.M000739200;
RA Yu M., Haslam R.H.A., Haslam D.B.;
RT "HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of
RT human cells.";
RL J. Biol. Chem. 275:24984-24992(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC TISSUE=Placenta;
RX PubMed=15195998; DOI=10.1515/BC.2004.043;
RA Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M.,
RA Zimmermann R.;
RT "Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like
RT protein Scj1p.";
RL Biol. Chem. 385:389-395(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-264.
RC TISSUE=Tonsil;
RA Honore B.;
RT "hPWP1-interacting protein 4.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-264.
RC TISSUE=Placenta, and Retinoblastoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=11584023; DOI=10.1074/jbc.M109215200;
RA Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J.,
RA Chan L.;
RT "A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein
RT B mRNA editing.";
RL J. Biol. Chem. 276:46445-46452(2001).
RN [12]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein
RT complexes in endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15544163;
RA Nakanishi K., Kamiguchi K., Torigoe T., Nabeta C., Hirohashi Y.,
RA Asanuma H., Tobioka H., Koge N., Harada O., Tamura Y., Nagano H.,
RA Yano S., Chiba S., Matsumoto H., Sato N.;
RT "Localization and function in endoplasmic reticulum stress tolerance
RT of ERdj3, a new member of Hsp40 family protein.";
RL Cell Stress Chaperones 9:253-264(2004).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY,
RP GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, AND MUTAGENESIS
RP OF HIS-53.
RX PubMed=15525676; DOI=10.1091/mbc.E04-05-0434;
RA Shen Y., Hendershot L.M.;
RT "ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue,
RT serves as a cofactor for BiP's interactions with unfolded
RT substrates.";
RL Mol. Biol. Cell 16:40-50(2005).
RN [15]
RP MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, AND INTERACTION
RP WITH DENATURED SUBSTRATES.
RX PubMed=17976514; DOI=10.1016/j.abb.2007.10.001;
RA Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B.;
RT "Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate
RT interactions.";
RL Arch. Biochem. Biophys. 468:147-158(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Serves as a co-chaperone for HSPA5. Binds directly to
CC both unfolded proteins that are substrates for ERAD and nascent
CC unfolded peptide chains, but dissociates from the HSPA5-unfolded
CC protein complex before folding is completed. May help recruiting
CC HSPA5 and other chaperones to the substrate. Stimulates HSPA5
CC ATPase activity.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC UGT1A1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX. Binds to denatured substrates in an ATP-
CC independent manner. Interacts via the J domain with HSPA5 in an
CC ATP-dependent manner.
CC -!- INTERACTION:
CC P11021:HSPA5; NbExp=2; IntAct=EBI-713113, EBI-354921;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Associated
CC with the ER membrane in a C-terminally epitope-tagged construct.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
CC thapsigargin and tunicamycin.
CC -!- PTM: Contains high-mannose Endo H-sensitive carbohydrates.
CC -!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
CC disulfide bonds. The preferential partner for each Cys is not
CC known.
CC -!- PTM: Thr-188 was reported (PubMed:17525332) to be phosphorylated
CC upon DNA damage by ATM or ATR; however as this position has been
CC shown to be in the ER lumen, the in vivo relevance is not proven.
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
CC subcellular location. This result was obtained using an N-
CC terminally GFP-tagged construct which most probably affected
CC signal peptide-driven targeting to the ER. As a consequence, the
CC in vivo revelance of the observed interaction with APOBEC1, a
CC nuclear protein, is dubious. This holds true for the interaction
CC with PWP1.
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DR EMBL; AB028859; BAA88307.1; -; mRNA.
DR EMBL; AF228505; AAF61711.1; -; mRNA.
DR EMBL; AJ250137; CAB65118.1; -; mRNA.
DR EMBL; AF277317; AAK69110.1; -; mRNA.
DR EMBL; AY359043; AAQ89402.1; -; mRNA.
DR EMBL; AK075300; BAC11533.1; -; mRNA.
DR EMBL; AK075430; BAC11617.1; -; mRNA.
DR EMBL; BT007063; AAP35712.1; -; mRNA.
DR EMBL; CR457096; CAG33377.1; -; mRNA.
DR EMBL; CH471052; EAW78190.1; -; Genomic_DNA.
DR EMBL; BC001144; AAH01144.1; -; mRNA.
DR PIR; T52073; T52073.
DR RefSeq; NP_057390.1; NM_016306.4.
DR UniGene; Hs.317192; -.
DR ProteinModelPortal; Q9UBS4; -.
DR SMR; Q9UBS4; 25-90, 130-343.
DR DIP; DIP-29678N; -.
DR IntAct; Q9UBS4; 30.
DR MINT; MINT-1417807; -.
DR STRING; 9606.ENSP00000265028; -.
DR PhosphoSite; Q9UBS4; -.
DR DMDM; 18203497; -.
DR OGP; Q9UBS4; -.
DR REPRODUCTION-2DPAGE; IPI00008454; -.
DR PaxDb; Q9UBS4; -.
DR PeptideAtlas; Q9UBS4; -.
DR PRIDE; Q9UBS4; -.
DR DNASU; 51726; -.
DR Ensembl; ENST00000265028; ENSP00000265028; ENSG00000090520.
DR Ensembl; ENST00000439351; ENSP00000414398; ENSG00000090520.
DR GeneID; 51726; -.
DR KEGG; hsa:51726; -.
DR UCSC; uc003fqi.3; human.
DR CTD; 51726; -.
DR GeneCards; GC03P186285; -.
DR HGNC; HGNC:14889; DNAJB11.
DR HPA; HPA010814; -.
DR HPA; HPA017051; -.
DR MIM; 611341; gene.
DR neXtProt; NX_Q9UBS4; -.
DR PharmGKB; PA27413; -.
DR eggNOG; COG0484; -.
DR HOGENOM; HOG000226718; -.
DR HOVERGEN; HBG066727; -.
DR InParanoid; Q9UBS4; -.
DR KO; K09517; -.
DR OMA; GLKEGHH; -.
DR OrthoDB; EOG7Z3F59; -.
DR PhylomeDB; Q9UBS4; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; DNAJB11; human.
DR GeneWiki; DNAJB11; -.
DR GenomeRNAi; 51726; -.
DR NextBio; 55780; -.
DR PRO; PR:Q9UBS4; -.
DR ArrayExpress; Q9UBS4; -.
DR Bgee; Q9UBS4; -.
DR CleanEx; HS_DNAJB11; -.
DR Genevestigator; Q9UBS4; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR Pfam; PF01556; CTDII; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 3.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Phosphoprotein; Polymorphism; Reference proteome;
KW Signal.
FT SIGNAL 1 22 By similarity.
FT CHAIN 23 358 DnaJ homolog subfamily B member 11.
FT /FTId=PRO_0000007260.
FT DOMAIN 25 90 J.
FT MOD_RES 188 188 Phosphothreonine.
FT CARBOHYD 261 261 N-linked (GlcNAc...).
FT VARIANT 264 264 I -> V (in dbSNP:rs8147).
FT /FTId=VAR_016092.
FT MUTAGEN 53 53 H->Q: Loss of HSPA5-binding, but no
FT effect on interaction with denatured
FT substrates.
FT MUTAGEN 169 169 C->S: Drastic loss of interaction with
FT denatured substrates.
FT MUTAGEN 171 171 C->S: Drastic loss of interaction with
FT denatured substrates.
FT MUTAGEN 193 193 C->S: Drastic loss of interaction with
FT denatured substrates.
FT MUTAGEN 196 196 C->S: Drastic loss of interaction with
FT denatured substrates.
FT CONFLICT 247 247 K -> R (in Ref. 8; CAG33377).
SQ SEQUENCE 358 AA; 40514 MW; 580CC4D66A06B734 CRC64;
MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK VYNGLQGY
//
ID DJB11_HUMAN Reviewed; 358 AA.
AC Q9UBS4; Q542Y5; Q542Y9; Q6IAQ8; Q96JC6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=DnaJ homolog subfamily B member 11;
DE AltName: Full=APOBEC1-binding protein 2;
DE Short=ABBP-2;
DE AltName: Full=DnaJ protein homolog 9;
DE AltName: Full=ER-associated DNAJ;
DE AltName: Full=ER-associated Hsp40 co-chaperone;
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3;
DE Short=ER-resident protein ERdj3;
DE Short=ERdj3;
DE Short=ERj3p;
DE AltName: Full=HEDJ;
DE AltName: Full=Human DnaJ protein 9;
DE Short=hDj-9;
DE AltName: Full=PWP1-interacting protein 4;
DE Flags: Precursor;
GN Name=DNAJB11; Synonyms=EDJ, ERJ3, HDJ9;
GN ORFNames=PSEC0121, UNQ537/PRO1080;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11147971;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal
RT for their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH HSPA5, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Skeletal muscle;
RX PubMed=10827079; DOI=10.1074/jbc.M000739200;
RA Yu M., Haslam R.H.A., Haslam D.B.;
RT "HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of
RT human cells.";
RL J. Biol. Chem. 275:24984-24992(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC TISSUE=Placenta;
RX PubMed=15195998; DOI=10.1515/BC.2004.043;
RA Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M.,
RA Zimmermann R.;
RT "Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like
RT protein Scj1p.";
RL Biol. Chem. 385:389-395(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-264.
RC TISSUE=Tonsil;
RA Honore B.;
RT "hPWP1-interacting protein 4.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-264.
RC TISSUE=Placenta, and Retinoblastoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=11584023; DOI=10.1074/jbc.M109215200;
RA Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J.,
RA Chan L.;
RT "A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein
RT B mRNA editing.";
RL J. Biol. Chem. 276:46445-46452(2001).
RN [12]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein
RT complexes in endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15544163;
RA Nakanishi K., Kamiguchi K., Torigoe T., Nabeta C., Hirohashi Y.,
RA Asanuma H., Tobioka H., Koge N., Harada O., Tamura Y., Nagano H.,
RA Yano S., Chiba S., Matsumoto H., Sato N.;
RT "Localization and function in endoplasmic reticulum stress tolerance
RT of ERdj3, a new member of Hsp40 family protein.";
RL Cell Stress Chaperones 9:253-264(2004).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY,
RP GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, AND MUTAGENESIS
RP OF HIS-53.
RX PubMed=15525676; DOI=10.1091/mbc.E04-05-0434;
RA Shen Y., Hendershot L.M.;
RT "ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue,
RT serves as a cofactor for BiP's interactions with unfolded
RT substrates.";
RL Mol. Biol. Cell 16:40-50(2005).
RN [15]
RP MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, AND INTERACTION
RP WITH DENATURED SUBSTRATES.
RX PubMed=17976514; DOI=10.1016/j.abb.2007.10.001;
RA Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B.;
RT "Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate
RT interactions.";
RL Arch. Biochem. Biophys. 468:147-158(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Serves as a co-chaperone for HSPA5. Binds directly to
CC both unfolded proteins that are substrates for ERAD and nascent
CC unfolded peptide chains, but dissociates from the HSPA5-unfolded
CC protein complex before folding is completed. May help recruiting
CC HSPA5 and other chaperones to the substrate. Stimulates HSPA5
CC ATPase activity.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC UGT1A1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX. Binds to denatured substrates in an ATP-
CC independent manner. Interacts via the J domain with HSPA5 in an
CC ATP-dependent manner.
CC -!- INTERACTION:
CC P11021:HSPA5; NbExp=2; IntAct=EBI-713113, EBI-354921;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Associated
CC with the ER membrane in a C-terminally epitope-tagged construct.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
CC thapsigargin and tunicamycin.
CC -!- PTM: Contains high-mannose Endo H-sensitive carbohydrates.
CC -!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
CC disulfide bonds. The preferential partner for each Cys is not
CC known.
CC -!- PTM: Thr-188 was reported (PubMed:17525332) to be phosphorylated
CC upon DNA damage by ATM or ATR; however as this position has been
CC shown to be in the ER lumen, the in vivo relevance is not proven.
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
CC subcellular location. This result was obtained using an N-
CC terminally GFP-tagged construct which most probably affected
CC signal peptide-driven targeting to the ER. As a consequence, the
CC in vivo revelance of the observed interaction with APOBEC1, a
CC nuclear protein, is dubious. This holds true for the interaction
CC with PWP1.
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DR EMBL; AB028859; BAA88307.1; -; mRNA.
DR EMBL; AF228505; AAF61711.1; -; mRNA.
DR EMBL; AJ250137; CAB65118.1; -; mRNA.
DR EMBL; AF277317; AAK69110.1; -; mRNA.
DR EMBL; AY359043; AAQ89402.1; -; mRNA.
DR EMBL; AK075300; BAC11533.1; -; mRNA.
DR EMBL; AK075430; BAC11617.1; -; mRNA.
DR EMBL; BT007063; AAP35712.1; -; mRNA.
DR EMBL; CR457096; CAG33377.1; -; mRNA.
DR EMBL; CH471052; EAW78190.1; -; Genomic_DNA.
DR EMBL; BC001144; AAH01144.1; -; mRNA.
DR PIR; T52073; T52073.
DR RefSeq; NP_057390.1; NM_016306.4.
DR UniGene; Hs.317192; -.
DR ProteinModelPortal; Q9UBS4; -.
DR SMR; Q9UBS4; 25-90, 130-343.
DR DIP; DIP-29678N; -.
DR IntAct; Q9UBS4; 30.
DR MINT; MINT-1417807; -.
DR STRING; 9606.ENSP00000265028; -.
DR PhosphoSite; Q9UBS4; -.
DR DMDM; 18203497; -.
DR OGP; Q9UBS4; -.
DR REPRODUCTION-2DPAGE; IPI00008454; -.
DR PaxDb; Q9UBS4; -.
DR PeptideAtlas; Q9UBS4; -.
DR PRIDE; Q9UBS4; -.
DR DNASU; 51726; -.
DR Ensembl; ENST00000265028; ENSP00000265028; ENSG00000090520.
DR Ensembl; ENST00000439351; ENSP00000414398; ENSG00000090520.
DR GeneID; 51726; -.
DR KEGG; hsa:51726; -.
DR UCSC; uc003fqi.3; human.
DR CTD; 51726; -.
DR GeneCards; GC03P186285; -.
DR HGNC; HGNC:14889; DNAJB11.
DR HPA; HPA010814; -.
DR HPA; HPA017051; -.
DR MIM; 611341; gene.
DR neXtProt; NX_Q9UBS4; -.
DR PharmGKB; PA27413; -.
DR eggNOG; COG0484; -.
DR HOGENOM; HOG000226718; -.
DR HOVERGEN; HBG066727; -.
DR InParanoid; Q9UBS4; -.
DR KO; K09517; -.
DR OMA; GLKEGHH; -.
DR OrthoDB; EOG7Z3F59; -.
DR PhylomeDB; Q9UBS4; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; DNAJB11; human.
DR GeneWiki; DNAJB11; -.
DR GenomeRNAi; 51726; -.
DR NextBio; 55780; -.
DR PRO; PR:Q9UBS4; -.
DR ArrayExpress; Q9UBS4; -.
DR Bgee; Q9UBS4; -.
DR CleanEx; HS_DNAJB11; -.
DR Genevestigator; Q9UBS4; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR Pfam; PF01556; CTDII; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 3.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Phosphoprotein; Polymorphism; Reference proteome;
KW Signal.
FT SIGNAL 1 22 By similarity.
FT CHAIN 23 358 DnaJ homolog subfamily B member 11.
FT /FTId=PRO_0000007260.
FT DOMAIN 25 90 J.
FT MOD_RES 188 188 Phosphothreonine.
FT CARBOHYD 261 261 N-linked (GlcNAc...).
FT VARIANT 264 264 I -> V (in dbSNP:rs8147).
FT /FTId=VAR_016092.
FT MUTAGEN 53 53 H->Q: Loss of HSPA5-binding, but no
FT effect on interaction with denatured
FT substrates.
FT MUTAGEN 169 169 C->S: Drastic loss of interaction with
FT denatured substrates.
FT MUTAGEN 171 171 C->S: Drastic loss of interaction with
FT denatured substrates.
FT MUTAGEN 193 193 C->S: Drastic loss of interaction with
FT denatured substrates.
FT MUTAGEN 196 196 C->S: Drastic loss of interaction with
FT denatured substrates.
FT CONFLICT 247 247 K -> R (in Ref. 8; CAG33377).
SQ SEQUENCE 358 AA; 40514 MW; 580CC4D66A06B734 CRC64;
MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK VYNGLQGY
//
MIM
611341
*RECORD*
*FIELD* NO
611341
*FIELD* TI
*611341 DNAJ/HSP40 HOMOLOG, SUBFAMILY B, MEMBER 11; DNAJB11
;;HUMAN ENDOPLASMIC RETICULUM-ASSOCIATED DNAJ; HEDJ;;
read moreDJ9;;
APOBEC1-BINDING PROTEIN 2; ABBP2
*FIELD* TX
DESCRIPTION
DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of
proteins, which regulate molecular chaperone activity by stimulating
ATPase activity. DNAJ proteins may have up to 3 distinct domains: a
conserved 70-amino acid J domain, usually at the N terminus; a
glycine/phenylalanine (G/F)-rich region; and a C-terminal cysteine-rich
region (Ohtsuka and Hata, 2000).
CLONING
By searching EST databases for J domain-containing proteins, Ohtsuka and
Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse
Dnajb11. The deduced type II transmembrane protein contains 358 amino
acids with an N-terminal J domain. Dnajb11 is predicted to have an
N-terminal signal peptide.
Using database analysis to identify human homologs of a protein involved
in Shiga toxin trafficking in monkey kidney cells, followed by PCR of a
human skeletal muscle cDNA library, Yu et al. (2000) cloned DNAJB11,
which they called HEDJ. Northern blot analysis detected transcripts of
2.2 and 2.0 kb in all tissues examined, with highest expression in
pancreas and testis, and weakest expression in thymus and small
intestine. Confocal microscopy showed that epitope-tagged DNAJB11
localized to the endoplasmic reticulum (ER). Protease susceptibility,
glycosidase treatment, and detergent solubility assays demonstrated that
DNAJB11 is luminally oriented and membrane-associated.
Using APOBEC1 (600130) as bait in a yeast 2-hybrid analysis of a liver
cDNA library, followed by 5-prime RACE, Lau et al. (2001) cloned
DNAJB11, which they called ABBP2. The deduced 358-amino acid protein has
a calculated molecular mass of 40.5 kD and shares 99% sequence identity
with the mouse protein. DNAJB11 contains a conserved J domain, a weak
G/F region, and a region that contains 4 cysteines but lacks the zinc
finger domain found in some DNAJ proteins. The secondary and tertiary
structures of DNAJB11 closely resemble those of HDJ1 (DNAJB1; 604570).
Northern blot analysis detected transcripts of 1.5 and 2.0 kb in all
tissues examined.
GENE FUNCTION
Using in vitro experiments, Yu et al. (2000) demonstrated that the J
domain of DNAJB11 interacted with the ER-associated heat-shock protein
BIP (HSPA5; 138120) in an ATP-dependent manner and was capable of
stimulating its ATPase activity.
Lau et al. (2001) showed that DNAJB11 bound to APOBEC1 via its J domain
and neighboring G/F domain. Downregulation of DNAJB11 expression in a
human hepatocarcinoma cell line inhibited endogenous APOBEC1-mediated
apolipoprotein B (APOB; 107730) mRNA editing. Like other HSP40 proteins,
DNAJB11 bound to HSP70 (see HSPA1A, 140550) and had ATPase-stimulating
activity. APOBEC1-mediated APOB mRNA editing activity of in vitro tissue
extracts required the presence of HSP70/DNAJB11. Although exogenously
added ATP was not required for editing activity, removal of the
endogenous ATP present in these extracts disrupted DNAJB11-HSP70
interaction and completely inhibited editing.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNAJB11
gene to chromosome 3 (TMAP SHGC-77609).
*FIELD* RF
1. Lau, P. P.; Villanueva, H.; Kobayashi, K.; Nakamuta, M.; Chang,
B. H.-J.; Chan, L.: A DnaJ protein, Apobec-1-binding protein-2, modulates
apolipoprotein B mRNA editing. J. Biol. Chem. 276: 46445-46452,
2001.
2. Ohtsuka, K.; Hata, M.: Mammalian HSP40/DNAJ homologs: cloning
of novel cDNAs and a proposal for their classification and nomenclature. Cell
Stress Chaperones 5: 98-112, 2000.
3. Yu, M.; Haslam, R. H. A.; Haslam, D. B.: HEDJ, an Hsp40 co-chaperone
localized to the endoplasmic reticulum of human cells. J. Biol. Chem. 275:
24984-24992, 2000.
*FIELD* CD
Patricia A. Hartz: 8/16/2007
*FIELD* ED
carol: 08/17/2007
carol: 8/17/2007
*RECORD*
*FIELD* NO
611341
*FIELD* TI
*611341 DNAJ/HSP40 HOMOLOG, SUBFAMILY B, MEMBER 11; DNAJB11
;;HUMAN ENDOPLASMIC RETICULUM-ASSOCIATED DNAJ; HEDJ;;
read moreDJ9;;
APOBEC1-BINDING PROTEIN 2; ABBP2
*FIELD* TX
DESCRIPTION
DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of
proteins, which regulate molecular chaperone activity by stimulating
ATPase activity. DNAJ proteins may have up to 3 distinct domains: a
conserved 70-amino acid J domain, usually at the N terminus; a
glycine/phenylalanine (G/F)-rich region; and a C-terminal cysteine-rich
region (Ohtsuka and Hata, 2000).
CLONING
By searching EST databases for J domain-containing proteins, Ohtsuka and
Hata (2000) identified 10 mouse and human DNAJ homologs, including mouse
Dnajb11. The deduced type II transmembrane protein contains 358 amino
acids with an N-terminal J domain. Dnajb11 is predicted to have an
N-terminal signal peptide.
Using database analysis to identify human homologs of a protein involved
in Shiga toxin trafficking in monkey kidney cells, followed by PCR of a
human skeletal muscle cDNA library, Yu et al. (2000) cloned DNAJB11,
which they called HEDJ. Northern blot analysis detected transcripts of
2.2 and 2.0 kb in all tissues examined, with highest expression in
pancreas and testis, and weakest expression in thymus and small
intestine. Confocal microscopy showed that epitope-tagged DNAJB11
localized to the endoplasmic reticulum (ER). Protease susceptibility,
glycosidase treatment, and detergent solubility assays demonstrated that
DNAJB11 is luminally oriented and membrane-associated.
Using APOBEC1 (600130) as bait in a yeast 2-hybrid analysis of a liver
cDNA library, followed by 5-prime RACE, Lau et al. (2001) cloned
DNAJB11, which they called ABBP2. The deduced 358-amino acid protein has
a calculated molecular mass of 40.5 kD and shares 99% sequence identity
with the mouse protein. DNAJB11 contains a conserved J domain, a weak
G/F region, and a region that contains 4 cysteines but lacks the zinc
finger domain found in some DNAJ proteins. The secondary and tertiary
structures of DNAJB11 closely resemble those of HDJ1 (DNAJB1; 604570).
Northern blot analysis detected transcripts of 1.5 and 2.0 kb in all
tissues examined.
GENE FUNCTION
Using in vitro experiments, Yu et al. (2000) demonstrated that the J
domain of DNAJB11 interacted with the ER-associated heat-shock protein
BIP (HSPA5; 138120) in an ATP-dependent manner and was capable of
stimulating its ATPase activity.
Lau et al. (2001) showed that DNAJB11 bound to APOBEC1 via its J domain
and neighboring G/F domain. Downregulation of DNAJB11 expression in a
human hepatocarcinoma cell line inhibited endogenous APOBEC1-mediated
apolipoprotein B (APOB; 107730) mRNA editing. Like other HSP40 proteins,
DNAJB11 bound to HSP70 (see HSPA1A, 140550) and had ATPase-stimulating
activity. APOBEC1-mediated APOB mRNA editing activity of in vitro tissue
extracts required the presence of HSP70/DNAJB11. Although exogenously
added ATP was not required for editing activity, removal of the
endogenous ATP present in these extracts disrupted DNAJB11-HSP70
interaction and completely inhibited editing.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DNAJB11
gene to chromosome 3 (TMAP SHGC-77609).
*FIELD* RF
1. Lau, P. P.; Villanueva, H.; Kobayashi, K.; Nakamuta, M.; Chang,
B. H.-J.; Chan, L.: A DnaJ protein, Apobec-1-binding protein-2, modulates
apolipoprotein B mRNA editing. J. Biol. Chem. 276: 46445-46452,
2001.
2. Ohtsuka, K.; Hata, M.: Mammalian HSP40/DNAJ homologs: cloning
of novel cDNAs and a proposal for their classification and nomenclature. Cell
Stress Chaperones 5: 98-112, 2000.
3. Yu, M.; Haslam, R. H. A.; Haslam, D. B.: HEDJ, an Hsp40 co-chaperone
localized to the endoplasmic reticulum of human cells. J. Biol. Chem. 275:
24984-24992, 2000.
*FIELD* CD
Patricia A. Hartz: 8/16/2007
*FIELD* ED
carol: 08/17/2007
carol: 8/17/2007