DJB11_HUMAN
ID DJB11_HUMAN Reviewed; 358 AA.
AC Q9UBS4; Q542Y5; Q542Y9; Q6IAQ8; Q96JC6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 196.
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; ORFNames=PSEC0121, UNQ537/PRO1080;
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].
RX PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for
RT their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP 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 protein
RT 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., 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 [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-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT 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 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., 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 [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 project:
RT 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., Chan L.;
RT "A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B
RT 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 complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15544163; DOI=10.1379/csc-52.1;
RA Nakanishi K., Kamiguchi K., Torigoe T., Nabeta C., Hirohashi Y.,
RA Asanuma H., Tobioka H., Koge N., Harada O., Tamura Y., Nagano H., Yano S.,
RA Chiba S., Matsumoto H., Sato N.;
RT "Localization and function in endoplasmic reticulum stress tolerance of
RT 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 OF
RP 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, serves as
RT a cofactor for BiP's interactions with unfolded 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 WITH
RP 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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.
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 multiple
RT 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP FUNCTION, INVOLVEMENT IN PKD6, AND VARIANTS PKD6 ARG-54; PRO-77 AND
RP 206-ARG--TYR-358 DEL.
RX PubMed=29706351; DOI=10.1016/j.ajhg.2018.03.013;
RG Genkyst Study Group;
RG HALT Progression of Polycystic Kidney Disease Group;
RG Consortium for Radiologic Imaging Studies of Polycystic Kidney Disease;
RA Cornec-Le Gall E., Olson R.J., Besse W., Heyer C.M., Gainullin V.G.,
RA Smith J.M., Audrezet M.P., Hopp K., Porath B., Shi B., Baheti S.,
RA Senum S.R., Arroyo J., Madsen C.D., Ferec C., Joly D., Jouret F.,
RA Fikri-Benbrahim O., Charasse C., Coulibaly J.M., Yu A.S., Khalili K.,
RA Pei Y., Somlo S., Le Meur Y., Torres V.E., Harris P.C.;
RT "Monoallelic mutations to DNAJB11 cause atypical autosomal-dominant
RT polycystic kidney disease.";
RL Am. J. Hum. Genet. 102:832-844(2018).
CC -!- FUNCTION: As a co-chaperone for HSPA5 it is required for proper
CC folding, trafficking or degradation of proteins (PubMed:10827079,
CC PubMed:15525676, PubMed:29706351). Binds directly to both unfolded
CC proteins that are substrates for ERAD and nascent unfolded peptide
CC chains, but dissociates from the HSPA5-unfolded protein complex before
CC folding is completed (PubMed:15525676). May help recruiting HSPA5 and
CC other chaperones to the substrate. Stimulates HSPA5 ATPase activity
CC (PubMed:10827079). It is necessary for maturation and correct
CC trafficking of PKD1 (PubMed:29706351). {ECO:0000269|PubMed:10827079,
CC ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:29706351}.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX. Binds to denatured substrates in an ATP-independent manner.
CC Interacts via the J domain with HSPA5 in an ATP-dependent manner.
CC {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15525676,
CC ECO:0000269|PubMed:17976514}.
CC -!- INTERACTION:
CC Q9UBS4; P11021: HSPA5; NbExp=4; IntAct=EBI-713113, EBI-354921;
CC Q9UBS4; P15516: HTN3; NbExp=3; IntAct=EBI-713113, EBI-738783;
CC Q9UBS4; Q8ZQQ2: slrP; Xeno; NbExp=4; IntAct=EBI-713113, EBI-10712653;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15195998,
CC ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}.
CC Note=Associated with the ER membrane in a C-terminally epitope-tagged
CC construct.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10827079,
CC ECO:0000269|PubMed:11584023, ECO:0000269|PubMed:15525676}.
CC -!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
CC thapsigargin and tunicamycin. {ECO:0000269|PubMed:15525676,
CC ECO:0000269|PubMed:15544163}.
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 known.
CC -!- PTM: Thr-188 was reported to be phosphorylated upon DNA damage by ATM
CC or ATR; however as this position has been shown to be in the ER lumen,
CC the in vivo relevance is not proven.
CC -!- DISEASE: Polycystic kidney disease 6 with or without polycystic liver
CC disease (PKD6) [MIM:618061]: A form of polycystic kidney disease, a
CC disorder characterized by progressive formation and enlargement of
CC cysts in both kidneys, typically leading to end-stage renal disease in
CC adult life. Cysts also occur in other organs, particularly the liver.
CC PKD6 inheritance is autosomal dominant. {ECO:0000269|PubMed:29706351}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
CC subcellular location. This result was obtained using an N-terminally
CC GFP-tagged construct which most probably affected signal peptide-driven
CC targeting to the ER. As a consequence, the in vivo revelance of the
CC observed interaction with APOBEC1, a nuclear protein, is dubious. This
CC holds true for the interaction with PWP1. {ECO:0000305}.
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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 CCDS; CCDS3277.1; -.
DR PIR; T52073; T52073.
DR RefSeq; NP_057390.1; NM_016306.5.
DR AlphaFoldDB; Q9UBS4; -.
DR SMR; Q9UBS4; -.
DR BioGRID; 119699; 273.
DR DIP; DIP-29678N; -.
DR IntAct; Q9UBS4; 99.
DR MINT; Q9UBS4; -.
DR STRING; 9606.ENSP00000414398; -.
DR GlyConnect; 1185; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UBS4; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBS4; -.
DR PhosphoSitePlus; Q9UBS4; -.
DR BioMuta; DNAJB11; -.
DR DMDM; 18203497; -.
DR OGP; Q9UBS4; -.
DR REPRODUCTION-2DPAGE; IPI00008454; -.
DR EPD; Q9UBS4; -.
DR jPOST; Q9UBS4; -.
DR MassIVE; Q9UBS4; -.
DR MaxQB; Q9UBS4; -.
DR PaxDb; Q9UBS4; -.
DR PeptideAtlas; Q9UBS4; -.
DR PRIDE; Q9UBS4; -.
DR ProteomicsDB; 84046; -.
DR TopDownProteomics; Q9UBS4; -.
DR Antibodypedia; 2272; 250 antibodies from 29 providers.
DR DNASU; 51726; -.
DR Ensembl; ENST00000265028.8; ENSP00000265028.3; ENSG00000090520.12.
DR Ensembl; ENST00000439351.5; ENSP00000414398.1; ENSG00000090520.12.
DR GeneID; 51726; -.
DR KEGG; hsa:51726; -.
DR MANE-Select; ENST00000265028.8; ENSP00000265028.3; NM_016306.6; NP_057390.1.
DR UCSC; uc003fqi.4; human.
DR CTD; 51726; -.
DR DisGeNET; 51726; -.
DR GeneCards; DNAJB11; -.
DR GeneReviews; DNAJB11; -.
DR HGNC; HGNC:14889; DNAJB11.
DR HPA; ENSG00000090520; Low tissue specificity.
DR MalaCards; DNAJB11; -.
DR MIM; 611341; gene.
DR MIM; 618061; phenotype.
DR neXtProt; NX_Q9UBS4; -.
DR OpenTargets; ENSG00000090520; -.
DR Orphanet; 730; Autosomal dominant polycystic kidney disease.
DR PharmGKB; PA27413; -.
DR VEuPathDB; HostDB:ENSG00000090520; -.
DR eggNOG; KOG0713; Eukaryota.
DR GeneTree; ENSGT00940000155792; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q9UBS4; -.
DR OMA; WDAGFEF; -.
DR OrthoDB; 687505at2759; -.
DR PhylomeDB; Q9UBS4; -.
DR TreeFam; TF105144; -.
DR PathwayCommons; Q9UBS4; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q9UBS4; -.
DR BioGRID-ORCS; 51726; 56 hits in 1093 CRISPR screens.
DR ChiTaRS; DNAJB11; human.
DR GeneWiki; DNAJB11; -.
DR GenomeRNAi; 51726; -.
DR Pharos; Q9UBS4; Tbio.
DR PRO; PR:Q9UBS4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UBS4; protein.
DR Bgee; ENSG00000090520; Expressed in vermiform appendix and 96 other tissues.
DR Genevisible; Q9UBS4; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0051787; F:misfolded protein binding; IDA:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0016556; P:mRNA modification; IEA:Ensembl.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:AgBase.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IMP:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
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 InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Disease variant; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..358
FT /note="DnaJ homolog subfamily B member 11"
FT /id="PRO_0000007260"
FT DOMAIN 25..90
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VARIANT 54
FT /note="P -> R (in PKD6; dbSNP:rs1553849919)"
FT /evidence="ECO:0000269|PubMed:29706351"
FT /id="VAR_081002"
FT VARIANT 77
FT /note="L -> P (in PKD6; dbSNP:rs1553850185)"
FT /evidence="ECO:0000269|PubMed:29706351"
FT /id="VAR_081003"
FT VARIANT 206..358
FT /note="Missing (in PKD6)"
FT /evidence="ECO:0000269|PubMed:29706351"
FT /id="VAR_081004"
FT VARIANT 264
FT /note="I -> V (in dbSNP:rs8147)"
FT /evidence="ECO:0000269|PubMed:16303743, ECO:0000269|Ref.4"
FT /id="VAR_016092"
FT MUTAGEN 53
FT /note="H->Q: Loss of HSPA5-binding, but no effect on
FT interaction with denatured substrates."
FT /evidence="ECO:0000269|PubMed:15525676"
FT MUTAGEN 169
FT /note="C->S: Drastic loss of interaction with denatured
FT substrates."
FT /evidence="ECO:0000269|PubMed:17976514"
FT MUTAGEN 171
FT /note="C->S: Drastic loss of interaction with denatured
FT substrates."
FT /evidence="ECO:0000269|PubMed:17976514"
FT MUTAGEN 193
FT /note="C->S: Drastic loss of interaction with denatured
FT substrates."
FT /evidence="ECO:0000269|PubMed:17976514"
FT MUTAGEN 196
FT /note="C->S: Drastic loss of interaction with denatured
FT substrates."
FT /evidence="ECO:0000269|PubMed:17976514"
FT CONFLICT 247
FT /note="K -> R (in Ref. 8; CAG33377)"
FT /evidence="ECO:0000305"
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
