Q9UBS4Q542Y5Q542Y9Q6IAQ8Q96JC6DJB11_HUMANDnaJ homolog subfamily B member 11APOBEC1-binding protein 2ABBP-2DnaJ protein homolog 9ER-associated DNAJER-associated Hsp40 co-chaperoneEndoplasmic reticulum DNA J domain-containing protein 3ER-resident protein ERdj3ERdj3ERj3pHEDJHuman DnaJ protein 9hDj-9PWP1-interacting protein 4DNAJB11EDJERJ3HDJ9PSEC0121UNQ537/PRO1080Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoMammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.NUCLEOTIDE SEQUENCE [MRNA]HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells.NUCLEOTIDE SEQUENCE [MRNA]FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH HSPA5TISSUE SPECIFICITYGLYCOSYLATIONCharacterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.NUCLEOTIDE SEQUENCE [MRNA]SUBCELLULAR LOCATIONGLYCOSYLATIONhPWP1-interacting protein 4.NUCLEOTIDE SEQUENCE [MRNA]VARIANT VAL-264The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]VARIANT VAL-264Cloning of human full-length CDSs in BD Creator(TM) system donor vector.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing.TISSUE SPECIFICITYA subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.COMPONENT OF A CHAPERONE COMPLEXLocalization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein.SUBCELLULAR LOCATIONINDUCTIONERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates.FUNCTIONSUBCELLULAR LOCATIONINDUCTIONTISSUE SPECIFICITYGLYCOSYLATIONINTERACTION WITH DENATURED SUBSTRATESMUTAGENESIS OF HIS-53Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions.MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196INTERACTION WITH DENATURED SUBSTRATESATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminome analysis of the human mitochondrial proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Monoallelic mutations to DNAJB11 cause atypical autosomal-dominant polycystic kidney disease.FUNCTIONINVOLVEMENT IN PKD6VARIANTS PKD6 ARG-54; PRO-77 AND 206-ARG--TYR-358 DELAs 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).Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 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.Q9UBS4P11021false4Q9UBS4P15516false3Q9UBS4Q8ZQQ2true4Endoplasmic reticulum lumenAssociated with the ER membrane in a C-terminally epitope-tagged construct.Widely expressed.By endoplasmic reticulum stress-inducing agents such as thapsigargin and tunicamycin.Contains high-mannose Endo H-sensitive carbohydrates.Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known.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.Polycystic kidney disease 6 with or without polycystic liver disease
PKD6
A form of polycystic kidney disease, a disorder characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occur in other organs, particularly the liver. PKD6 inheritance is autosomal dominant.The disease is caused by variants affecting the gene represented in this entry.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.ChaperoneDisease variantDisulfide bondEndoplasmic reticulumGlycoproteinPhosphoproteinReference proteomeSignalPRLPIVHQCSCSCSCSKRMAPQNLSTFCLLLLYLIGAVIAGRDFYKILGVPRSASIKDIKKAYRKLALQLHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSSHGDIFSHFFGDFGFMFGGTPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFVEVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHPIFERRGDDLYTNVTISLVESLVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAREGIKQLLKQGSVQKVYNGLQGY
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