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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.
10-OCT-2018, entry version 172.
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).
-!- FUNCTION: Serves as a co-chaperone for HSPA5. 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. May help recruiting
HSPA5 and other chaperones to the substrate. Stimulates HSPA5
ATPase activity. {ECO:0000269|PubMed:10827079,
ECO:0000269|PubMed:15525676}.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX. Binds to denatured substrates in an ATP-
independent manner. Interacts via the J domain with HSPA5 in an
ATP-dependent manner. {ECO:0000269|PubMed:10827079,
ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:17976514}.
-!- INTERACTION:
P11021:HSPA5; NbExp=3; IntAct=EBI-713113, EBI-354921;
Q8ZQQ2:slrP (xeno); NbExp=4; IntAct=EBI-713113, EBI-10712653;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15195998,
ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}.
Note=Associated with the ER membrane in a C-terminally epitope-
tagged construct.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:11584023,
ECO:0000269|PubMed:15525676}.
-!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
thapsigargin and tunicamycin. {ECO:0000269|PubMed:15525676,
ECO:0000269|PubMed:15544163}.
-!- PTM: Contains high-mannose Endo H-sensitive carbohydrates.
-!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
disulfide bonds. The preferential partner for each Cys is not
known.
-!- PTM: Thr-188 was reported to be phosphorylated upon DNA damage by
ATM or ATR; however as this position has been shown to be in the
ER lumen, the in vivo relevance is not proven.
-!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
subcellular location. This result was obtained using an N-
terminally GFP-tagged construct which most probably affected
signal peptide-driven targeting to the ER. As a consequence, the
in vivo revelance of the observed interaction with APOBEC1, a
nuclear protein, is dubious. This holds true for the interaction
with PWP1. {ECO:0000305}.
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EMBL; AB028859; BAA88307.1; -; mRNA.
EMBL; AF228505; AAF61711.1; -; mRNA.
EMBL; AJ250137; CAB65118.1; -; mRNA.
EMBL; AF277317; AAK69110.1; -; mRNA.
EMBL; AY359043; AAQ89402.1; -; mRNA.
EMBL; AK075300; BAC11533.1; -; mRNA.
EMBL; AK075430; BAC11617.1; -; mRNA.
EMBL; BT007063; AAP35712.1; -; mRNA.
EMBL; CR457096; CAG33377.1; -; mRNA.
EMBL; CH471052; EAW78190.1; -; Genomic_DNA.
EMBL; BC001144; AAH01144.1; -; mRNA.
CCDS; CCDS3277.1; -.
PIR; T52073; T52073.
RefSeq; NP_057390.1; NM_016306.5.
UniGene; Hs.317192; -.
UniGene; Hs.712822; -.
ProteinModelPortal; Q9UBS4; -.
SMR; Q9UBS4; -.
BioGrid; 119699; 91.
DIP; DIP-29678N; -.
IntAct; Q9UBS4; 50.
MINT; Q9UBS4; -.
STRING; 9606.ENSP00000265028; -.
GlyConnect; 1185; -.
iPTMnet; Q9UBS4; -.
PhosphoSitePlus; Q9UBS4; -.
BioMuta; DNAJB11; -.
DMDM; 18203497; -.
OGP; Q9UBS4; -.
REPRODUCTION-2DPAGE; IPI00008454; -.
EPD; Q9UBS4; -.
MaxQB; Q9UBS4; -.
PaxDb; Q9UBS4; -.
PeptideAtlas; Q9UBS4; -.
PRIDE; Q9UBS4; -.
ProteomicsDB; 84046; -.
TopDownProteomics; Q9UBS4; -.
DNASU; 51726; -.
Ensembl; ENST00000265028; ENSP00000265028; ENSG00000090520.
Ensembl; ENST00000439351; ENSP00000414398; ENSG00000090520.
GeneID; 51726; -.
KEGG; hsa:51726; -.
UCSC; uc003fqi.4; human.
CTD; 51726; -.
DisGeNET; 51726; -.
EuPathDB; HostDB:ENSG00000090520.10; -.
GeneCards; DNAJB11; -.
HGNC; HGNC:14889; DNAJB11.
HPA; HPA010814; -.
HPA; HPA017051; -.
MIM; 611341; gene.
neXtProt; NX_Q9UBS4; -.
OpenTargets; ENSG00000090520; -.
PharmGKB; PA27413; -.
eggNOG; KOG0713; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00860000133716; -.
HOGENOM; HOG000226718; -.
HOVERGEN; HBG066727; -.
InParanoid; Q9UBS4; -.
KO; K09517; -.
OMA; KEGMMDH; -.
OrthoDB; EOG091G0GWF; -.
PhylomeDB; Q9UBS4; -.
TreeFam; TF105144; -.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
ChiTaRS; DNAJB11; human.
GeneWiki; DNAJB11; -.
GenomeRNAi; 51726; -.
PRO; PR:Q9UBS4; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000090520; Expressed in 200 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_DNAJB11; -.
Genevisible; Q9UBS4; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:AgBase.
GO; GO:0006457; P:protein folding; IEA:InterPro.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR036869; J_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 3.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Phosphoprotein; Polymorphism; Reference proteome;
Signal.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 358 DnaJ homolog subfamily B member 11.
/FTId=PRO_0000007260.
DOMAIN 25 90 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
MOD_RES 188 188 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VARIANT 264 264 I -> V (in dbSNP:rs8147).
{ECO:0000269|PubMed:16303743,
ECO:0000269|Ref.4}.
/FTId=VAR_016092.
MUTAGEN 53 53 H->Q: Loss of HSPA5-binding, but no
effect on interaction with denatured
substrates.
{ECO:0000269|PubMed:15525676}.
MUTAGEN 169 169 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
MUTAGEN 171 171 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
MUTAGEN 193 193 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
MUTAGEN 196 196 C->S: Drastic loss of interaction with
denatured substrates.
{ECO:0000269|PubMed:17976514}.
CONFLICT 247 247 K -> R (in Ref. 8; CAG33377).
{ECO:0000305}.
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


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EIAAB11532 DnaJ homolog subfamily A member 1,Dnaja1,DnaJ-like protein 1,Heat shock protein J2,Hsj2,HSJ-2,Rat,Rattus norvegicus,Rdj1
EIAAB11564 DnaJ homolog subfamily C member 1,DnaJ protein homolog MTJ1,DNAJC1,Homo sapiens,HTJ1,Human
EIAAB11542 DnaJ homolog subfamily B member 2,DnaJ protein homolog 1,DNAJB2,Heat shock 40 kDa protein 3,Heat shock protein J1,Homo sapiens,HSJ1,HSJ-1,HSPF3,Human
EIAAB11537 DnaJ homolog subfamily A member 3, mitochondrial,DnaJ protein Tid-1,DNAJA3,HCA57,Hepatocellular carcinoma-associated antigen 57,Homo sapiens,hTid-1,Human,TID1,Tumorous imaginal discs protein Tid56 hom
10-782-55040 DnaJ homolog subfamily B member 1 - Heat shock 40 kDa protein 1; Heat shock protein 40; HSP40; DnaJ protein homolog 1; HDJ-1 N_A 0.05 mg
10-782-55040 DnaJ homolog subfamily B member 1 - Heat shock 40 kDa protein 1; Heat shock protein 40; HSP40; DnaJ protein homolog 1; HDJ-1 N_A 0.2 mg
EIAAB11586 DnaJ homolog subfamily C member 9,DnaJ protein SB73,DNAJC9,Homo sapiens,Human


 

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