Q9UBS4 (DJB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DnaJ homolog subfamily B member 11

Alternative name(s):
APOBEC1-binding protein 2
Short name=ABBP-2
DnaJ protein homolog 9
ER-associated DNAJ
ER-associated Hsp40 co-chaperone
ER-associated dnaJ protein 3
Short name=ERdj3
Short name=ERj3p
HEDJ
Human DnaJ protein 9
Short name=hDj-9
PWP1-interacting protein 4

Gene names

Name:	DNAJB11
Synonyms:	EDJ, ERJ3, HDJ9
ORF Names:	PSEC0121, UNQ537/PRO1080

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 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. 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.3 Ref.13 Ref.14
Tissue specificity	Widely expressed. Ref.2 Ref.11 Ref.14
Induction	By endoplasmic reticulum stress-inducing agents such as thapsigargin and tunicamycin. Ref.13 Ref.14
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.
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 Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome mRNA modification Inferred from electronic annotation. Source: Compara protein folding Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: Compara
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
	Modified residue	188	1	Phosphothreonine Ref.16
	Glycosylation	261	1	N-linked (GlcNAc...) Ref.17
Natural variations
	Natural variant	264	1	I → V. Ref.4 Ref.6 Corresponds to variant rs8147 [ dbSNP | Ensembl ].		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

	Sequence		Length	Mass (Da)
	Q9UBS4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 580CC4D66A06B734	FASTA	358	40,514
	10 20 30 40 50 60 MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD 70 80 90 100 110 120 PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT 130 140 150 160 170 180 PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL 190 200 210 220 230 240 GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR 250 260 270 280 290 300 FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW 310 320 330 340 350 KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK VYNGLQGY

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , 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. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [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. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [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. , 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 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, MASS SPECTROMETRY. Tissue: Liver.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_016306.4.
UniGene	Hs.317192.
3D structure databases
ProteinModelPortal	Q9UBS4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29678N.
IntAct	Q9UBS4. 10 interactions.
MINT	MINT-1417807.
STRING	9606.ENSP00000265028.
PTM databases
PhosphoSite	Q9UBS4.
Polymorphism databases
DMDM	18203497.
2D gel databases
OGP	Q9UBS4.
REPRODUCTION-2DPAGE	IPI00008454.
Proteomic databases
PaxDb	Q9UBS4.
PeptideAtlas	Q9UBS4.
PRIDE	Q9UBS4.
Protocols and materials databases
DNASU	51726.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265028; ENSP00000265028; ENSG00000090520. ENST00000439351; ENSP00000414398; ENSG00000090520.
GeneID	51726.
KEGG	hsa:51726.
UCSC	uc003fqi.3. human.
Organism-specific databases
CTD	51726.
GeneCards	GC03P186285.
HGNC	HGNC:14889. DNAJB11.
HPA	HPA010814. HPA017051.
MIM	611341. gene.
neXtProt	NX_Q9UBS4.
PharmGKB	PA27413.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0484.
HOGENOM	HOG000226718.
HOVERGEN	HBG066727.
InParanoid	Q9UBS4.
KO	K09517.
OMA	RDEMEYP.
OrthoDB	EOG4KD6M9.
PhylomeDB	Q9UBS4.
Enzyme and pathway databases
Reactome	REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q9UBS4.
Bgee	Q9UBS4.
CleanEx	HS_DNAJB11.
Genevestigator	Q9UBS4.
GermOnline	ENSG00000090520. Homo sapiens.
Family and domain databases
Gene3D	1.10.287.110. 1 hit.
InterPro	IPR002939. DnaJ_C. IPR001623. DnaJ_domain. IPR018253. DnaJ_domain_CS. IPR008971. HSP40/DnaJ_pept-bd. [Graphical view]
Pfam	PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. [Graphical view]
PRINTS	PR00625. JDOMAIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit. SSF49493. HSP40_DnaJ_pep. 2 hits.
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DNAJB11. human.
GenomeRNAi	51726.
NextBio	55780.
SOURCE	Search...

Entry information

Entry name

DJB11_HUMAN

Accession

Primary (citable) accession number: Q9UBS4
Secondary accession number(s): Q542Y5 , Q542Y9, Q6IAQ8, Q96JC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.