Reviewed,
UniProtKB/Swiss-Prot Q9UBS4 (DJB11_HUMAN)
Last modified
July 7, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DnaJ homolog subfamily B member 11 Alternative name(s): ER-associated dnaJ protein 3 ERj3p ERdj3 ER-associated Hsp40 co-chaperone ER-associated DNAJ HEDJ hDj9 PWP1-interacting protein 4 APOBEC1-binding protein 2 Short name=ABBP-2 | ||||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 358 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. Ref.2 Ref.14 |
| Subunit structure | Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, 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. Ref.2 Ref.14 Ref.15 |
| Subcellular location | Endoplasmic reticulum lumen. Note: Associated with the ER membrane in a C-terminally epitope-tagged construct. Ref.2 Ref.14 Ref.3 Ref.13 |
| Tissue specificity | |
| Induction | By ER stress-inducing agents, such as thapsigargin and tunicamycin. Ref.14 Ref.13 |
| Post-translational modification | 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 (Ref.16) 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. Ref.16 |
| Sequence similarities | Contains 1 J domain. |
| Caution | Ref.11 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Coding sequence diversity | Polymorphism |
| Domain | Signal |
| Molecular function | Chaperone |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein folding Inferred from electronic annotation. Source: InterPro |
| Cellular component | endoplasmic reticulum Traceable author statement. Source: UniProtKB endoplasmic reticulum lumenInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | heat shock protein binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | By similarity | ||||||
| Chain | 23 – 358 | 336 | DnaJ homolog subfamily B member 11 | PRO_0000007260 | |||||
Regions | |||||||||
| Domain | 25 – 90 | 66 | J | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 261 | 1 | N-linked (GlcNAc...) | ||||||
Natural variations | |||||||||
| Natural variant | 264 | 1 | I → V: dbSNP rs8147. Ref.4 Ref.6 | VAR_016092 | |||||
Experimental info | |||||||||
| Mutagenesis | 53 | 1 | H → Q: Loss of HSPA5-binding, but no effect on interaction with denatured substrates. Ref.14 | ||||||
| Mutagenesis | 169 | 1 | C → S: Drastic loss of interaction with denatured substrates. Ref.15 | ||||||
| Mutagenesis | 171 | 1 | C → S: Drastic loss of interaction with denatured substrates. Ref.15 | ||||||
| Mutagenesis | 193 | 1 | C → S: Drastic loss of interaction with denatured substrates. Ref.15 | ||||||
| Mutagenesis | 196 | 1 | C → S: Drastic loss of interaction with denatured substrates. Ref.15 | ||||||
| Sequence conflict | 247 | 1 | K → R in CAG33377. Ref.8 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature." Ohtsuka K., Hata M. Cell Stress Chaperones 5:98-112(2000) [PubMed: 11147971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells." Yu M., Haslam R.H.A., Haslam D.B. J. Biol. Chem. 275:24984-24992(2000) [PubMed: 10827079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5, TISSUE SPECIFICITY, GLYCOSYLATION. Tissue: Skeletal muscle. |
| [3] | "Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p." Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M., Zimmermann R. Biol. Chem. 385:389-395(2004) [PubMed: 15195998] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GLYCOSYLATION. Tissue: Placenta. |
| [4] | "hPWP1-interacting protein 4." Honore B. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-264. Tissue: Tonsil. |
| [5] | "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." 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. Gray A.M.Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [6] | "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." 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. Isogai T.DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-264. Tissue: Placenta and Retinoblastoma. |
| [7] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [8] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [9] | 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. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [10] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung. |
| [11] | "A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing." Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J., Chan L. J. Biol. Chem. 276:46445-46452(2001) [PubMed: 11584023] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [12] | "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins." Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. Mol. Biol. Cell 13:4456-4469(2002) [PubMed: 12475965] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX. |
| [13] | "Localization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein." 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. Cell Stress Chaperones 9:253-264(2004) [PubMed: 15544163] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION. |
| [14] | "ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates." Shen Y., Hendershot L.M. Mol. Biol. Cell 16:40-50(2005) [PubMed: 15525676] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, MUTAGENESIS OF HIS-53. |
| [15] | "Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions." Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B. Arch. Biochem. Biophys. 468:147-158(2007) [PubMed: 17976514] [Abstract] Cited for: MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, INTERACTION WITH DENATURED SUBSTRATES. |
| [16] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: POSSIBLE PHOSPHORYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [17] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [18] | "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, MASS SPECTROMETRY. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| AB028859 mRNA. Translation: BAA88307.1. AF228505 mRNA. Translation: AAF61711.1. AJ250137 mRNA. Translation: CAB65118.1. AF277317 mRNA. Translation: AAK69110.1. AY359043 mRNA. Translation: AAQ89402.1. AK075300 mRNA. Translation: BAC11533.1. AK075430 mRNA. Translation: BAC11617.1. BT007063 mRNA. Translation: AAP35712.1. CR457096 mRNA. Translation: CAG33377.1. CH471052 Genomic DNA. Translation: EAW78190.1. BC001144 mRNA. Translation: AAH01144.1. | |
| IPI | IPI00008454. |
| PIR | T52073. |
| RefSeq | NP_057390.1. |
| UniGene | Hs.317192 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HDJ based on UniProtKB P25685. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9UBS4. 6 interactions. |
PTM databases | |
| PhosphoSite | Q9UBS4. |
2-D gel databases | |
| OGP | Q9UBS4. |
| REPRODUCTION-2DPAGE | IPI00008454. |
Proteomic databases | |
| PeptideAtlas | Q9UBS4. |
| PRIDE | Q9UBS4. |
Genome annotation databases | |
| Ensembl | ENSG00000090520. Homo sapiens. [Contig view] |
| GeneID | 51726. |
| KEGG | hsa:51726. |
| UCSC | uc003fqi.1. human. |
Organism-specific databases | |
| GeneCards | GC03P187767. |
| H-InvDB | HIX0003932. |
| HGNC | HGNC:14889. DNAJB11. |
| HPA | HPA010814. HPA017051. |
| MIM | 611341. gene. |
| PharmGKB | PA27413. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q9UBS4. |
| OMA | Q9UBS4. PRAQEKF. |
Gene expression databases | |
| ArrayExpress | Q9UBS4. |
| Bgee | Q9UBS4. |
| CleanEx | HS_DNAJB11. |
| GermOnline | ENSG00000090520. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR002939. DnaJ_C. IPR001623. DnaJ_N. IPR018253. Heat_shock_DnaJ_CS. IPR015609. Hsp40/DnaJ_Rel. IPR003095. Hsp_DnaJ. [Graphical view] |
| Gene3D | G3DSA:1.10.287.110. DnaJ_N. 1 hit. |
| PANTHER | PTHR11821. Hsp40/DnaJ_Rel. 1 hit. |
| Pfam | PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. [Graphical view] |
| PRINTS | PR00625. DNAJPROTEIN. |
| SMART | SM00271. DnaJ. 1 hit. [Graphical view] |
| PROSITE | PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 55780. |
| SOURCE | Search... |
Entry information
| Entry name | DJB11_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9UBS4 Secondary accession number(s): Q542Y5 Q96JC6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


