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Q99KV1 (DJB11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily B member 11
Alternative name(s):
APOBEC1-binding protein 2
Short name=ABBP-2
ER-associated DNAJ
ER-associated Hsp40 co-chaperone
Endoplasmic reticulum DNA J domain-containing protein 3
Short name=ER-resident protein ERdj3
Short name=ERdj3
Short name=ERj3p
Gene names
Name:Dnajb11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity.

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 By similarity. Ref.6

Subcellular location

Endoplasmic reticulum lumen Ref.6.

Post-translational modification

Contains high-mannose Endo H-sensitive carbohydrates By similarity.

Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known By similarity.

Sequence similarities

Contains 1 J domain.

Caution

Ref.1 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 358336DnaJ homolog subfamily B member 11
PRO_0000007261

Regions

Domain25 – 9066J

Amino acid modifications

Modified residue1881Phosphothreonine By similarity
Glycosylation2611N-linked (GlcNAc...) Probable

Experimental info

Sequence conflict91F → L in BAC35956. Ref.2
Sequence conflict881T → A in AAH18282. Ref.4
Sequence conflict2171R → L in AAL17676. Ref.1
Sequence conflict2401R → P in AAL17676. Ref.1
Sequence conflict2551G → E in BAC35956. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99KV1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E53CE0B3DF7465B8

FASTA35840,555
        10         20         30         40         50         60 
MAPQNLSTFC LLLLYLIGTV 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 
FRIKVVKHRI FERRGDDLYT NVTVSLVEAL VGFEMDITHL DGHKVHISRD KITRPGAKLW 

       310        320        330        340        350 
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAKEGIK QLLKQGPVQK VYNGLQGY 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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].
Strain: Czech II and FVB/N.
Tissue: Colon and Mammary tumor.
[5]"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.
[6]"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: SUBCELLULAR LOCATION, INTERACTION WITH DENATURED SUBSTRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY054981 mRNA. Translation: AAL17676.1.
AK050500 mRNA. Translation: BAC34293.1.
AK075785 mRNA. Translation: BAC35956.1.
AK075953 mRNA. Translation: BAC36079.1.
AK148511 mRNA. Translation: BAE28593.1.
AK166730 mRNA. Translation: BAE38977.1.
CT027991 Genomic DNA. Translation: CAO78022.1.
BC003999 mRNA. Translation: AAH03999.1.
BC018282 mRNA. Translation: AAH18282.1.
BC040747 mRNA. Translation: AAH40747.1.
CCDSCCDS28070.1.
RefSeqNP_001177733.1. NM_001190804.1.
NP_001177734.1. NM_001190805.1.
NP_080676.3. NM_026400.5.
UniGeneMm.37516.
Mm.477367.

3D structure databases

ProteinModelPortalQ99KV1.
SMRQ99KV1. Positions 18-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212468. 2 interactions.
DIPDIP-60531N.
IntActQ99KV1. 4 interactions.
MINTMINT-1847287.

PTM databases

PhosphoSiteQ99KV1.

2D gel databases

REPRODUCTION-2DPAGEQ99KV1.

Proteomic databases

MaxQBQ99KV1.
PaxDbQ99KV1.
PRIDEQ99KV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004574; ENSMUSP00000004574; ENSMUSG00000004460.
ENSMUST00000166487; ENSMUSP00000126828; ENSMUSG00000004460.
ENSMUST00000178320; ENSMUSP00000137542; ENSMUSG00000004460.
GeneID67838.
KEGGmmu:67838.
UCSCuc007yso.2. mouse.

Organism-specific databases

CTD51726.
MGIMGI:1915088. Dnajb11.

Phylogenomic databases

eggNOGCOG0484.
GeneTreeENSGT00490000043321.
HOGENOMHOG000226718.
HOVERGENHBG066727.
InParanoidQ99KV1.
KOK09517.
OMALFITFDV.
OrthoDBEOG7Z3F59.
PhylomeDBQ99KV1.
TreeFamTF105144.

Gene expression databases

BgeeQ99KV1.
CleanExMM_DNAJB11.
GenevestigatorQ99KV1.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
InterProIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJB11. mouse.
NextBio325665.
PROQ99KV1.
SOURCESearch...

Entry information

Entry nameDJB11_MOUSE
AccessionPrimary (citable) accession number: Q99KV1
Secondary accession number(s): A6X957 expand/collapse secondary AC list , Q543I7, Q8BK79, Q8VCY1, Q8VHB1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot