Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DnaJ homolog subfamily B member 9

Gene

Dnajb9

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

Functioni

Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (PubMed:11836248). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (PubMed:22267725). Required for survival of B-cell progenitors and normal antibody production (PubMed:25222125).By similarity3 Publications

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • misfolded protein binding Source: MGI

GO - Biological processi

  • B cell differentiation Source: UniProtKB
  • immunoglobulin production Source: UniProtKB
  • negative regulation of IRE1-mediated unfolded protein response Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
  • ubiquitin-dependent ERAD pathway Source: UniProtKB

Keywordsi

Molecular functionChaperone
Biological processUnfolded protein response

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily B member 9Curated
Alternative name(s):
Endoplasmic reticulum DNA J domain-containing protein 41 Publication
Short name:
ER-resident protein ERdj41 Publication
Short name:
ERdj41 Publication
mDj71 Publication
Gene namesi
Name:Dnajb9Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1351618. Dnajb9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Perinatal death in approximately half of knockout mice (PubMed:24336520). Death is caused by fetal growth restriction, reduced hepatic glycogen stores and hypoglycemia (PubMed:24336520). Surviving adult mice display constitutive endoplasmic reticulum stress in multiple cells and tissues (PubMed:24336520). Elevated endoplasmic reticulum stress in pancreatic beta cells is associated with beta cell loss, hypoinsulinemia and glucose intolerance (PubMed:24336520) Conditional knockout mice lacking Dnajb9 in bone marrow show impaired hematopoiesis: the number of myeloid cells is increased, while the number of erythroid and B lymphoid cells is reduced (PubMed:25222125). B-cell defects cause decreased survival of B-cell precursors, including large and small pre-B, and immature B-cells (PubMed:25222125).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54H → Q: Abolishes ability to stimulate ATPase activity of HSPA5/BiP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000007103224 – 222DnaJ homolog subfamily B member 9Add BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei133PhosphoserineBy similarity1

Post-translational modificationi

Not N-glycosylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QYI6.
PaxDbiQ9QYI6.
PeptideAtlasiQ9QYI6.
PRIDEiQ9QYI6.

PTM databases

iPTMnetiQ9QYI6.
PhosphoSitePlusiQ9QYI6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000014905.
CleanExiMM_DNAJB9.
ExpressionAtlasiQ9QYI6. baseline and differential.
GenevisibleiQ9QYI6. MM.

Interactioni

Subunit structurei

Interacts with HSPA5/BiP; interaction is direct (PubMed:11836248). Interacts with ERN1/IRE1 (via the luminal region) (By similarity). Interacts with DERL1 (PubMed:22267725).By similarity2 Publications

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • misfolded protein binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015049.

Structurei

3D structure databases

ProteinModelPortaliQ9QYI6.
SMRiQ9QYI6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 90JPROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni91 – 222Divergent targeting domainCuratedAdd BLAST132

Domaini

The J domain stimulates the ATPase activity of HSPA5/BiP, while the divergent targeting domain is required for efficient substrate recognition by HSPA5/BiP. The divergent targeting domain specifically recognizes and binds to aggregation-prone sequences.1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0714. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00760000118947.
HOGENOMiHOG000290187.
HOVERGENiHBG051372.
InParanoidiQ9QYI6.
KOiK09515.
OMAiATPQSIF.
OrthoDBiEOG091G15JG.
TreeFamiTF105143.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
InterProiView protein in InterPro
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR036869. J_dom_sf.
PfamiView protein in Pfam
PF00226. DnaJ. 1 hit.
PRINTSiPR00625. JDOMAIN.
SMARTiView protein in SMART
SM00271. DnaJ. 1 hit.
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiView protein in PROSITE
PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9QYI6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPQSVFVF AICILMITEL ILASKSYYDI LGVPKSASER QIKKAFHKLA
60 70 80 90 100
MKYHPDKNKS PDAEAKFREI AEAYETLSDA NSRKEYDTIG HSAFTNGKGQ
110 120 130 140 150
RGNGSPFEQS FNFNFDDLFK DFNFFGQNQN TRSKKHFENH FHTRQDGSSR
160 170 180 190 200
QRHHFQEFSF GGGLFDDMFE DMEKMFSFSG FDTTNRHTVQ TENRFHGSSK
210 220
HCRTVTQRRG NMVTTYTDCS GQ
Length:222
Mass (Da):25,616
Last modified:October 3, 2012 - v2
Checksum:i4A737D704E760069
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133S → F in BAA88305 (PubMed:11147971).Curated1
Sequence conflicti148S → F in BAA88305 (PubMed:11147971).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028857 mRNA. Translation: BAA88305.1.
AK005475 mRNA. Translation: BAB24065.1.
CT010304 mRNA. Translation: CAJ18512.1.
CT010444 Genomic DNA. No translation available.
BC042713 mRNA. Translation: AAH42713.1.
BC096676 mRNA. Translation: AAH96676.1.
CCDSiCCDS25897.1.
RefSeqiNP_038788.2. NM_013760.4.
UniGeneiMm.27432.

Genome annotation databases

EnsembliENSMUST00000015049; ENSMUSP00000015049; ENSMUSG00000014905.
GeneIDi27362.
KEGGimmu:27362.
UCSCiuc007nlo.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiDNJB9_MOUSE
AccessioniPrimary (citable) accession number: Q9QYI6
Secondary accession number(s): Q5D0C3, Q9DAW1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 3, 2012
Last modified: March 28, 2018
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was initially thought to be an integral membrane protein (PubMed:11836248). However, it was later shown that it is a soluble luminal protein localized in the endoplasmic reticulum lumen.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome