Q99KV1 (DJB11_MOUSE) 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
ER-associated DNAJ
ER-associated Hsp40 co-chaperone
ER-associated dnaJ protein 3
Short name=ERdj3
Short name=ERj3p

Gene names

Name:

Dnajb11

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Chaperone
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA modification Inferred from direct assay Ref.1. Source: MGI protein folding Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: MGI endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.1. Source: MGI
Molecular_function	unfolded protein binding Inferred from direct assay Ref.1. Source: MGI
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_0000007261
Regions
	Domain	25 – 90	66	J
Amino acid modifications
	Modified residue	188	1	Phosphothreonine By similarity
	Glycosylation	261	1	N-linked (GlcNAc...) Probable
Experimental info
	Sequence conflict	9	1	F → L in BAC35956. Ref.2
	Sequence conflict	88	1	T → A in AAH18282. Ref.4
	Sequence conflict	217	1	R → L in AAL17676. Ref.1
	Sequence conflict	240	1	R → P in AAL17676. Ref.1
	Sequence conflict	255	1	G → E in BAC35956. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99KV1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: E53CE0B3DF7465B8	FASTA	358	40,555
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00320241.
RefSeq	NP_001177733.1. NM_001190804.1. NP_001177734.1. NM_001190805.1. NP_080676.3. NM_026400.5.
UniGene	Mm.37516. Mm.477367.
3D structure databases
ProteinModelPortal	Q99KV1.
SMR	Q99KV1. Positions 18-90, 130-343.
ModBase	Search...
PTM databases
PhosphoSite	Q99KV1.
2D gel databases
REPRODUCTION-2DPAGE	Q99KV1.
Proteomic databases
PaxDb	Q99KV1.
PRIDE	Q99KV1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004574; ENSMUSP00000004574; ENSMUSG00000004460. ENSMUST00000166487; ENSMUSP00000126828; ENSMUSG00000004460. ENSMUST00000178320; ENSMUSP00000137542; ENSMUSG00000004460.
GeneID	67838.
KEGG	mmu:67838.
UCSC	uc007yso.2. mouse.
Organism-specific databases
CTD	51726.
MGI	MGI:1915088. Dnajb11.
Phylogenomic databases
eggNOG	COG0484.
GeneTree	ENSGT00490000043321.
HOGENOM	HOG000226718.
HOVERGEN	HBG066727.
InParanoid	Q99KV1.
KO	K09517.
OMA	RDEMEYP.
OrthoDB	EOG4KD6M9.
Gene expression databases
Bgee	Q99KV1.
CleanEx	MM_DNAJB11.
Genevestigator	Q99KV1.
GermOnline	ENSMUSG00000004460. Mus musculus.
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. mouse.
NextBio	325665.
SOURCE	Search...

Entry information

Entry name

DJB11_MOUSE

Accession

Primary (citable) accession number: Q99KV1
Secondary accession number(s): A6X957 , Q543I7, Q8BK79, Q8VCY1, Q8VHB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program