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Q99KV1

- DJB11_MOUSE

UniProt

Q99KV1 - DJB11_MOUSE

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Protein

DnaJ homolog subfamily B member 11

Gene

Dnajb11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. unfolded protein binding Source: MGI

GO - Biological processi

  1. mRNA modification Source: MGI
  2. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_106572. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
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
Endoplasmic reticulum DNA J domain-containing protein 3
Short name:
ER-resident protein ERdj3
Short name:
ERdj3
Short name:
ERj3p
Gene namesi
Name:Dnajb11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1915088. Dnajb11.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 358336DnaJ homolog subfamily B member 11PRO_0000007261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881PhosphothreonineBy similarity
Glycosylationi261 – 2611N-linked (GlcNAc...)Curated

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ99KV1.
PaxDbiQ99KV1.
PRIDEiQ99KV1.

2D gel databases

REPRODUCTION-2DPAGEQ99KV1.

PTM databases

PhosphoSiteiQ99KV1.

Expressioni

Gene expression databases

BgeeiQ99KV1.
CleanExiMM_DNAJB11.
GenevestigatoriQ99KV1.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi212468. 2 interactions.
DIPiDIP-60531N.
IntActiQ99KV1. 4 interactions.
MINTiMINT-1847287.

Structurei

3D structure databases

ProteinModelPortaliQ99KV1.
SMRiQ99KV1. Positions 18-343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 9066JPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00490000043321.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiQ99KV1.
KOiK09517.
OMAiLFITFDV.
OrthoDBiEOG7Z3F59.
PhylomeDBiQ99KV1.
TreeFamiTF105144.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99KV1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPQNLSTFC LLLLYLIGTV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL
60 70 80 90 100
QLHPDRNPDD PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS
110 120 130 140 150
SHGDIFSHFF GDFGFMFGGT PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF
160 170 180 190 200
VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL GPGRFQMTQE VVCDECPNVK
210 220 230 240 250
LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR FRIKVVKHRI
260 270 280 290 300
FERRGDDLYT NVTVSLVEAL VGFEMDITHL DGHKVHISRD KITRPGAKLW
310 320 330 340 350
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAKEGIK QLLKQGPVQK

VYNGLQGY
Length:358
Mass (Da):40,555
Last modified:June 1, 2001 - v1
Checksum:iE53CE0B3DF7465B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91F → L in BAC35956. (PubMed:16141072)Curated
Sequence conflicti88 – 881T → A in AAH18282. (PubMed:15489334)Curated
Sequence conflicti217 – 2171R → L in AAL17676. (PubMed:11584023)Curated
Sequence conflicti240 – 2401R → P in AAL17676. (PubMed:11584023)Curated
Sequence conflicti255 – 2551G → E in BAC35956. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28070.1.
RefSeqiNP_001177733.1. NM_001190804.1.
NP_001177734.1. NM_001190805.1.
NP_080676.3. NM_026400.5.
UniGeneiMm.37516.
Mm.477367.

Genome annotation databases

EnsembliENSMUST00000004574; ENSMUSP00000004574; ENSMUSG00000004460.
ENSMUST00000166487; ENSMUSP00000126828; ENSMUSG00000004460.
ENSMUST00000178320; ENSMUSP00000137542; ENSMUSG00000004460.
GeneIDi67838.
KEGGimmu:67838.
UCSCiuc007yso.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28070.1.
RefSeqi NP_001177733.1. NM_001190804.1.
NP_001177734.1. NM_001190805.1.
NP_080676.3. NM_026400.5.
UniGenei Mm.37516.
Mm.477367.

3D structure databases

ProteinModelPortali Q99KV1.
SMRi Q99KV1. Positions 18-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212468. 2 interactions.
DIPi DIP-60531N.
IntActi Q99KV1. 4 interactions.
MINTi MINT-1847287.

PTM databases

PhosphoSitei Q99KV1.

2D gel databases

REPRODUCTION-2DPAGE Q99KV1.

Proteomic databases

MaxQBi Q99KV1.
PaxDbi Q99KV1.
PRIDEi Q99KV1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004574 ; ENSMUSP00000004574 ; ENSMUSG00000004460 .
ENSMUST00000166487 ; ENSMUSP00000126828 ; ENSMUSG00000004460 .
ENSMUST00000178320 ; ENSMUSP00000137542 ; ENSMUSG00000004460 .
GeneIDi 67838.
KEGGi mmu:67838.
UCSCi uc007yso.2. mouse.

Organism-specific databases

CTDi 51726.
MGIi MGI:1915088. Dnajb11.

Phylogenomic databases

eggNOGi COG0484.
GeneTreei ENSGT00490000043321.
HOGENOMi HOG000226718.
HOVERGENi HBG066727.
InParanoidi Q99KV1.
KOi K09517.
OMAi LFITFDV.
OrthoDBi EOG7Z3F59.
PhylomeDBi Q99KV1.
TreeFami TF105144.

Enzyme and pathway databases

Reactomei REACT_106572. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi DNAJB11. mouse.
NextBioi 325665.
PROi Q99KV1.
SOURCEi Search...

Gene expression databases

Bgeei Q99KV1.
CleanExi MM_DNAJB11.
Genevestigatori Q99KV1.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
InterProi IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view ]
Pfami PF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view ]
PRINTSi PR00625. JDOMAIN.
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
PROSITEi PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDJB11_MOUSE
AccessioniPrimary (citable) accession number: Q99KV1
Secondary accession number(s): A6X957
, Q543I7, Q8BK79, Q8VCY1, Q8VHB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

PubMed:11584023 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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3