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Protein

DnaJ homolog subfamily B member 9

Gene

DNAJB9

Organism
Homo sapiens (Human)
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:18400946). 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. Required for survival of B-cell progenitors and normal antibody production (By similarity).By similarity1 Publication

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processUnfolded protein response

Enzyme and pathway databases

ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.

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
Microvascular endothelial differentiation gene 1 protein1 Publication
Short name:
Mdg-11 Publication
Gene namesi
Name:DNAJB9
Synonyms:MDG11 Publication
ORF Names:UNQ743/PRO14711 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000128590.4.
HGNCiHGNC:6968. DNAJB9.
MIMi602634. gene.
neXtProtiNX_Q9UBS3.

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

Organism-specific databases

DisGeNETi4189.
OpenTargetsiENSG00000128590.
PharmGKBiPA27419.

Polymorphism and mutation databases

BioMutaiDNAJB9.
DMDMi18203496.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000007103124 – 223DnaJ homolog subfamily B member 9Add BLAST200

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei133PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UBS3.
MaxQBiQ9UBS3.
PaxDbiQ9UBS3.
PeptideAtlasiQ9UBS3.
PRIDEiQ9UBS3.

PTM databases

iPTMnetiQ9UBS3.
PhosphoSitePlusiQ9UBS3.

Expressioni

Tissue specificityi

Widely expressed. Expressed at highest level in the liver, placenta and kidney (PubMed:11836248).1 Publication

Gene expression databases

BgeeiENSG00000128590.
CleanExiHS_DNAJB9.
ExpressionAtlasiQ9UBS3. baseline and differential.
GenevisibleiQ9UBS3. HS.

Organism-specific databases

HPAiHPA040967.
HPA041553.

Interactioni

Subunit structurei

Interacts with HSPA5/BiP; interaction is direct (By similarity). Interacts with ERN1/IRE1 (via the luminal region) (By similarity). Interacts with DERL1 (By similarity).By similarity

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi110354. 59 interactors.
IntActiQ9UBS3. 9 interactors.
MINTiQ9UBS3.
STRINGi9606.ENSP00000249356.

Structurei

Secondary structure

1223
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 31Combined sources5
Helixi39 – 52Combined sources14
Turni55 – 57Combined sources3
Helixi61 – 78Combined sources18
Helixi81 – 88Combined sources8
Helixi91 – 94Combined sources4
Beta strandi97 – 99Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CTRNMR-A26-100[»]
ProteinModelPortaliQ9UBS3.
SMRiQ9UBS3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBS3.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni91 – 223Divergent targeting domainBy similarityAdd BLAST133

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.By similarity

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0714. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00760000118947.
HOGENOMiHOG000290187.
HOVERGENiHBG051372.
InParanoidiQ9UBS3.
KOiK09515.
OMAiATPQSIF.
OrthoDBiEOG091G15JG.
PhylomeDBiQ9UBS3.
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.

Q9UBS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPQSIFIF AICILMITEL ILASKSYYDI LGVPKSASER QIKKAFHKLA
60 70 80 90 100
MKYHPDKNKS PDAEAKFREI AEAYETLSDA NRRKEYDTLG HSAFTSGKGQ
110 120 130 140 150
RGSGSSFEQS FNFNFDDLFK DFGFFGQNQN TGSKKRFENH FQTRQDGGSS
160 170 180 190 200
RQRHHFQEFS FGGGLFDDMF EDMEKMFSFS GFDSTNQHTV QTENRFHGSS
210 220
KHCRTVTQRR GNMVTTYTDC SGQ
Length:223
Mass (Da):25,518
Last modified:May 1, 2000 - v1
Checksum:i59E3E57FF8B378BC
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048911136R → H. Corresponds to variant dbSNP:rs17155937Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026908 mRNA. Translation: BAA84703.1.
AF083247 mRNA. Translation: AAD39845.1.
AL080081 mRNA. Translation: CAB45701.1.
AY359045 mRNA. Translation: AAQ89404.1.
BC028912 mRNA. Translation: AAH28912.1.
CCDSiCCDS5752.1.
PIRiT12472.
RefSeqiNP_036460.1. NM_012328.2.
UniGeneiHs.732494.
Hs.741182.

Genome annotation databases

EnsembliENST00000249356; ENSP00000249356; ENSG00000128590.
GeneIDi4189.
KEGGihsa:4189.
UCSCiuc003vfn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiDNJB9_HUMAN
AccessioniPrimary (citable) accession number: Q9UBS3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: March 28, 2018
This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome