DnaJ homolog subfamily B member 11 precursor

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Reviewed, UniProtKB/Swiss-Prot Q9UBS4 (DJB11_HUMAN)

Last modified July 7, 2009. Version 77. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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

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

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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.

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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	Widely expressed. Ref.2 Ref.14 Ref.11
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.

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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 lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heat shock protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
DOK2	O60496	1	EBI-713113,EBI-1046024

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

By similarity

Chain

23 – 358

336

DnaJ homolog subfamily B member 11

PRO_0000007260

Regions

Domain

25 – 90

Amino acid modifications

Glycosylation

261

N-linked (GlcNAc...)

Natural variations

Natural variant

264

I → V: dbSNP rs8147. Ref.4 Ref.6

VAR_016092

Experimental info

Mutagenesis

H → Q: Loss of HSPA5-binding, but no effect on interaction with denatured substrates. Ref.14

Mutagenesis

169

C → S: Drastic loss of interaction with denatured substrates. Ref.15

Mutagenesis

171

C → S: Drastic loss of interaction with denatured substrates. Ref.15

Mutagenesis

193

C → S: Drastic loss of interaction with denatured substrates. Ref.15

Mutagenesis

196

C → S: Drastic loss of interaction with denatured substrates. Ref.15

Sequence conflict

247

K → R in CAG33377. Ref.8

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9UBS4-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 580CC4D66A06B734
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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

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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: 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.

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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...

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Entry information

Entry name

DJB11_HUMAN

Accession

Primary (citable) accession number: Q9UBS4
Secondary accession number(s): Q542Y5

Q96JC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 1, 2000
Last modified:	July 7, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents