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Q13217 (DNJC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 3
Alternative name(s):
Endoplasmic reticulum DNA J domain-containing protein 6
Short name=ER-resident protein ERdj6
Short name=ERdj6
Interferon-induced, double-stranded RNA-activated protein kinase inhibitor
Protein kinase inhibitor of 58 kDa
Short name=Protein kinase inhibitor p58
Gene names
Name:DNAJC3
Synonyms:P58IPK, PRKRI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity. Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with EIF2AK3 By similarity and EIF2AK2. Forms a trimeric complex with DNAJB1 and HSPA8. Interacts with PRKRIR/P52RIPK. Ref.5 Ref.6 Ref.7

Subcellular location

Endoplasmic reticulum By similarity.

Tissue specificity

Widely expressed with high level in the pancreas and testis. Also expressed in cell lines with different levels. Ref.1

Induction

Up-regulated during an endoplasmic reticulum stress via ATF6. Activated in response to infection by influenza virus through the dissociation of DNAJB1. Down-regulated by DNAJB1 and PRKRIR/P52RIPK. Ref.6 Ref.7 Ref.8

Domain

The J domain mediates interaction with HSPA8.

Binding to misfolded proteins is mediated by a hydrophobic patch forming a large groove within the first two TPR repeats By similarity.

Sequence similarities

Contains 1 J domain.

Contains 9 TPR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 504473DnaJ homolog subfamily C member 3
PRO_0000071045

Regions

Repeat37 – 7034TPR 1
Repeat72 – 10433TPR 2
Repeat105 – 13834TPR 3
Repeat154 – 18734TPR 4
Repeat189 – 22133TPR 5
Repeat222 – 25534TPR 6
Repeat268 – 30134TPR 7
Repeat306 – 33934TPR 8
Repeat340 – 37334TPR 9
Domain394 – 46269J
Region375 – 39319Flexible linker

Amino acid modifications

Disulfide bond248 ↔ 258 Ref.10
Disulfide bond313 ↔ 329 Ref.10

Secondary structure

...................................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13217 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E720A1E7F618B912

FASTA50457,580
        10         20         30         40         50         60 
MVAPGSVTSR LGSVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA GQLADALSQF 

        70         80         90        100        110        120 
HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIQL KMDFTAARLQ RGHLLLKQGK 

       130        140        150        160        170        180 
LDEAEDDFKK VLKSNPSENE EKEAQSQLIK SDEMQRLRSQ ALNAFGSGDY TAAIAFLDKI 

       190        200        210        220        230        240 
LEVCVWDAEL RELRAECFIK EGEPRKAISD LKAASKLKND NTEAFYKIST LYYQLGDHEL 

       250        260        270        280        290        300 
SLSEVRECLK LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS 

       310        320        330        340        350        360 
IAEYTVRSKE RICHCFSKDE KPVEAIRVCS EVLQMEPDNV NALKDRAEAY LIEEMYDEAI 

       370        380        390        400        410        420 
QDYETAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG VKRNAKKQEI IKAYRKLALQ 

       430        440        450        460        470        480 
WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR 

       490        500 
SWNSWQGFNP FSSGGPFRFK FHFN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase."
Korth M.J., Lyons C.N., Wambach M., Katze M.G.
Gene 170:181-188(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]NIEHS SNPs program
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Leukocyte.
[5]"The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity."
Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G.
J. Biol. Chem. 271:1702-1707(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
[6]"Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK."
Gale M.J. Jr., Blakely C.M., Hopkins D.A., Melville M.W., Wambach M., Romano P.R., Katze M.G.
Mol. Cell. Biol. 18:859-871(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKRIR, INDUCTION.
[7]"The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity."
Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.
J. Biol. Chem. 274:3797-3803(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNAJB1 AND HSPA8, INDUCTION.
[8]"P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling."
van Huizen R., Martindale J.L., Gorospe M., Holbrook N.J.
J. Biol. Chem. 278:15558-15564(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The crystal structure of the human co-chaperone P58(IPK)."
Svard M., Biterova E.I., Bourhis J.M., Guy J.E.
PLoS ONE 6:E22337-E22337(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-461, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28424 mRNA. Translation: AAC50502.1.
AY795482 Genomic DNA. Translation: AAV40838.1.
AL138955 Genomic DNA. Translation: CAH70090.1.
BC047936 mRNA. Translation: AAH47936.2.
PIRJC4775.
RefSeqNP_006251.1. NM_006260.4.
UniGeneHs.59214.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y4TX-ray3.00A/B/C35-461[»]
2Y4UX-ray3.20A35-461[»]
ProteinModelPortalQ13217.
SMRQ13217. Positions 35-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111597. 8 interactions.
IntActQ13217. 1 interaction.
MINTMINT-1531270.
STRING9606.ENSP00000365991.

PTM databases

PhosphoSiteQ13217.

Polymorphism databases

DMDM73620807.

Proteomic databases

PaxDbQ13217.
PeptideAtlasQ13217.
PRIDEQ13217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000602402; ENSP00000473631; ENSG00000102580.
GeneID5611.
KEGGhsa:5611.
UCSCuc001vmq.3. human.

Organism-specific databases

CTD5611.
GeneCardsGC13P096329.
HGNCHGNC:9439. DNAJC3.
HPAHPA039336.
HPA041326.
MIM601184. gene.
neXtProtNX_Q13217.
PharmGKBPA27420.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000193351.
HOVERGENHBG053820.
InParanoidQ13217.
KOK09523.
OMAQNENDQQ.
OrthoDBEOG70KGPH.
PhylomeDBQ13217.
TreeFamTF105162.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ13217.
BgeeQ13217.
CleanExHS_DNAJC3.
GenevestigatorQ13217.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProIPR001623. DnaJ_domain.
IPR026901. DNAJC3.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR24078:SF1. PTHR24078:SF1. 1 hit.
PfamPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
PROSITEPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJC3. human.
GeneWikiDNAJC3.
GenomeRNAi5611.
NextBio21810.
PROQ13217.
SOURCESearch...

Entry information

Entry nameDNJC3_HUMAN
AccessionPrimary (citable) accession number: Q13217
Secondary accession number(s): Q86WT9, Q8N4N2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM