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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)

 DJB11_HUMAN             Reviewed;         358 AA.
Q9UBS4; Q542Y5; Q542Y9; Q6IAQ8; Q96JC6;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-SEP-2019, entry version 181.
RecName: Full=DnaJ homolog subfamily B member 11;
AltName: Full=APOBEC1-binding protein 2;
Short=ABBP-2;
AltName: Full=DnaJ protein homolog 9;
AltName: Full=ER-associated DNAJ;
AltName: Full=ER-associated Hsp40 co-chaperone;
AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 3;
Short=ER-resident protein ERdj3;
Short=ERdj3;
Short=ERj3p;
AltName: Full=HEDJ;
AltName: Full=Human DnaJ protein 9;
Short=hDj-9;
AltName: Full=PWP1-interacting protein 4;
Flags: Precursor;
Name=DNAJB11; Synonyms=EDJ, ERJ3, HDJ9;
ORFNames=PSEC0121, UNQ537/PRO1080;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
INTERACTION WITH HSPA5, TISSUE SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Skeletal muscle;
PubMed=10827079; DOI=10.1074/jbc.m000739200;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
TISSUE=Placenta;
PubMed=15195998; DOI=10.1515/bc.2004.043;
Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M.,
Zimmermann R.;
"Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like
protein Scj1p.";
Biol. Chem. 385:389-395(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-264.
TISSUE=Tonsil;
Honore B.;
"hPWP1-interacting protein 4.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-264.
TISSUE=Placenta, and Retinoblastoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
TISSUE SPECIFICITY.
PubMed=11584023; DOI=10.1074/jbc.m109215200;
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).
[12]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[13]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15544163; DOI=10.1379/csc-52.1;
Nakanishi K., Kamiguchi K., Torigoe T., Nabeta C., Hirohashi Y.,
Asanuma H., Tobioka H., Koge N., Harada O., Tamura Y., Nagano H.,
Yano S., Chiba S., Matsumoto H., Sato N.;
"Localization and function in endoplasmic reticulum stress tolerance
of ERdj3, a new member of Hsp40 family protein.";
Cell Stress Chaperones 9:253-264(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY,
GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, AND MUTAGENESIS
OF HIS-53.
PubMed=15525676; DOI=10.1091/mbc.e04-05-0434;
Shen Y., Hendershot L.M.;
"ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue,
serves as a cofactor for BiP's interactions with unfolded
substrates.";
Mol. Biol. Cell 16:40-50(2005).
[15]
MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, AND INTERACTION
WITH DENATURED SUBSTRATES.
PubMed=17976514; DOI=10.1016/j.abb.2007.10.001;
Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B.;
"Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate
interactions.";
Arch. Biochem. Biophys. 468:147-158(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
FUNCTION, INVOLVEMENT IN PKD6, AND VARIANTS PKD6 ARG-54; PRO-77 AND
206-ARG--TYR-358 DEL.
PubMed=29706351; DOI=10.1016/j.ajhg.2018.03.013;
Genkyst Study Group;
HALT Progression of Polycystic Kidney Disease Group;
Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease;
Cornec-Le Gall E., Olson R.J., Besse W., Heyer C.M., Gainullin V.G.,
Smith J.M., Audrezet M.P., Hopp K., Porath B., Shi B., Baheti S.,
Senum S.R., Arroyo J., Madsen C.D., Ferec C., Joly D., Jouret F.,
Fikri-Benbrahim O., Charasse C., Coulibaly J.M., Yu A.S., Khalili K.,
Pei Y., Somlo S., Le Meur Y., Torres V.E., Harris P.C.;
"Monoallelic mutations to DNAJB11 cause atypical autosomal-dominant
polycystic kidney disease.";
Am. J. Hum. Genet. 102:832-844(2018).
-!- FUNCTION: As a co-chaperone for HSPA5 it is required for proper
folding, trafficking or degradation of proteins (PubMed:10827079,
PubMed:15525676, PubMed:29706351). Binds directly to both unfolded
proteins that are substrates for ERAD and nascent unfolded peptide
chains, but dissociates from the HSPA5-unfolded protein complex
before folding is completed (PubMed:15525676). May help recruiting
HSPA5 and other chaperones to the substrate. Stimulates HSPA5
ATPase activity (PubMed:10827079). It is necessary for maturation
and correct trafficking of PKD1 (PubMed:29706351).
{ECO:0000269|PubMed:10827079,