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Q13217

- DNJC3_HUMAN

UniProt

Q13217 - DNJC3_HUMAN

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Protein
DnaJ homolog subfamily C member 3
Gene
DNAJC3, P58IPK, PRKRI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. protein kinase inhibitor activity Source: ProtInc

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. defense response to virus Source: UniProtKB-KW
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. negative regulation of protein kinase activity Source: GOC
  6. proteolysis involved in cellular protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Antiviral defense, Unfolded protein response

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DNAJC3
Synonyms:P58IPK, PRKRI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:9439. DNAJC3.

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. endoplasmic reticulum Sec complex Source: Ensembl
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 504473DnaJ homolog subfamily C member 3
PRO_0000071045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi248 ↔ 2581 Publication
Disulfide bondi313 ↔ 3291 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ13217.
PaxDbiQ13217.
PeptideAtlasiQ13217.
PRIDEiQ13217.

PTM databases

PhosphoSiteiQ13217.

Expressioni

Tissue specificityi

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

Inductioni

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.3 Publications

Gene expression databases

ArrayExpressiQ13217.
BgeeiQ13217.
CleanExiHS_DNAJC3.
GenevestigatoriQ13217.

Organism-specific databases

HPAiHPA039336.
HPA041326.

Interactioni

Subunit structurei

Interacts with EIF2AK3 By similarity and EIF2AK2. Forms a trimeric complex with DNAJB1 and HSPA8. Interacts with PRKRIR/P52RIPK.3 Publications

Protein-protein interaction databases

BioGridi111597. 8 interactions.
IntActiQ13217. 1 interaction.
MINTiMINT-1531270.
STRINGi9606.ENSP00000365991.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4915
Helixi53 – 6614
Helixi71 – 8313
Helixi87 – 10014
Turni101 – 1033
Helixi105 – 11713
Helixi121 – 13212
Helixi138 – 16730
Helixi170 – 18314
Helixi188 – 20013
Helixi204 – 2074
Helixi208 – 21811
Helixi222 – 23413
Helixi238 – 25114
Helixi256 – 28126
Helixi284 – 29714
Helixi302 – 31716
Turni318 – 3203
Helixi322 – 33514
Helixi340 – 35213
Helixi356 – 36712
Beta strandi370 – 3723
Helixi374 – 39118
Helixi396 – 3983
Helixi409 – 42012
Helixi423 – 4253
Helixi429 – 44820
Helixi451 – 4544

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y4TX-ray3.00A/B/C35-461[»]
2Y4UX-ray3.20A35-461[»]
ProteinModelPortaliQ13217.
SMRiQ13217. Positions 35-455.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati37 – 7034TPR 1
Add
BLAST
Repeati72 – 10433TPR 2
Add
BLAST
Repeati105 – 13834TPR 3
Add
BLAST
Repeati154 – 18734TPR 4
Add
BLAST
Repeati189 – 22133TPR 5
Add
BLAST
Repeati222 – 25534TPR 6
Add
BLAST
Repeati268 – 30134TPR 7
Add
BLAST
Repeati306 – 33934TPR 8
Add
BLAST
Repeati340 – 37334TPR 9
Add
BLAST
Domaini394 – 46269J
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni375 – 39319Flexible linker
Add
BLAST

Domaini

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 similaritiesi

Contains 1 J domain.
Contains 9 TPR repeats.

Keywords - Domaini

Repeat, Signal, TPR repeat

Phylogenomic databases

eggNOGiCOG0484.
HOGENOMiHOG000193351.
HOVERGENiHBG053820.
InParanoidiQ13217.
KOiK09523.
OMAiQNENDQQ.
OrthoDBiEOG70KGPH.
PhylomeDBiQ13217.
TreeFamiTF105162.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProiIPR001623. DnaJ_domain.
IPR026901. DNAJC3.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR24078:SF165. PTHR24078:SF165. 1 hit.
PfamiPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13217-1 [UniParc]FASTAAdd to Basket

« Hide

MVAPGSVTSR LGSVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA    50
GQLADALSQF HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIQL 100
KMDFTAARLQ RGHLLLKQGK LDEAEDDFKK VLKSNPSENE EKEAQSQLIK 150
SDEMQRLRSQ ALNAFGSGDY TAAIAFLDKI LEVCVWDAEL RELRAECFIK 200
EGEPRKAISD LKAASKLKND NTEAFYKIST LYYQLGDHEL SLSEVRECLK 250
LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS 300
IAEYTVRSKE RICHCFSKDE KPVEAIRVCS EVLQMEPDNV NALKDRAEAY 350
LIEEMYDEAI QDYETAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG 400
VKRNAKKQEI IKAYRKLALQ WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS 450
DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR SWNSWQGFNP FSSGGPFRFK 500
FHFN 504
Length:504
Mass (Da):57,580
Last modified:November 1, 1996 - v1
Checksum:iE720A1E7F618B912
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28424 mRNA. Translation: AAC50502.1.
AY795482 Genomic DNA. Translation: AAV40838.1.
AL138955 Genomic DNA. Translation: CAH70090.1.
BC047936 mRNA. Translation: AAH47936.2.
CCDSiCCDS9479.1.
PIRiJC4775.
RefSeqiNP_006251.1. NM_006260.4.
UniGeneiHs.59214.

Genome annotation databases

EnsembliENST00000602402; ENSP00000473631; ENSG00000102580.
GeneIDi5611.
KEGGihsa:5611.
UCSCiuc001vmq.3. human.

Polymorphism databases

DMDMi73620807.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28424 mRNA. Translation: AAC50502.1 .
AY795482 Genomic DNA. Translation: AAV40838.1 .
AL138955 Genomic DNA. Translation: CAH70090.1 .
BC047936 mRNA. Translation: AAH47936.2 .
CCDSi CCDS9479.1.
PIRi JC4775.
RefSeqi NP_006251.1. NM_006260.4.
UniGenei Hs.59214.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y4T X-ray 3.00 A/B/C 35-461 [» ]
2Y4U X-ray 3.20 A 35-461 [» ]
ProteinModelPortali Q13217.
SMRi Q13217. Positions 35-455.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111597. 8 interactions.
IntActi Q13217. 1 interaction.
MINTi MINT-1531270.
STRINGi 9606.ENSP00000365991.

PTM databases

PhosphoSitei Q13217.

Polymorphism databases

DMDMi 73620807.

Proteomic databases

MaxQBi Q13217.
PaxDbi Q13217.
PeptideAtlasi Q13217.
PRIDEi Q13217.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000602402 ; ENSP00000473631 ; ENSG00000102580 .
GeneIDi 5611.
KEGGi hsa:5611.
UCSCi uc001vmq.3. human.

Organism-specific databases

CTDi 5611.
GeneCardsi GC13P096329.
HGNCi HGNC:9439. DNAJC3.
HPAi HPA039336.
HPA041326.
MIMi 601184. gene.
neXtProti NX_Q13217.
PharmGKBi PA27420.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0484.
HOGENOMi HOG000193351.
HOVERGENi HBG053820.
InParanoidi Q13217.
KOi K09523.
OMAi QNENDQQ.
OrthoDBi EOG70KGPH.
PhylomeDBi Q13217.
TreeFami TF105162.

Enzyme and pathway databases

Reactomei REACT_18273. XBP1(S) activates chaperone genes.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSi DNAJC3. human.
GeneWikii DNAJC3.
GenomeRNAii 5611.
NextBioi 21810.
PROi Q13217.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13217.
Bgeei Q13217.
CleanExi HS_DNAJC3.
Genevestigatori Q13217.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProi IPR001623. DnaJ_domain.
IPR026901. DNAJC3.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view ]
PANTHERi PTHR24078:SF165. PTHR24078:SF165. 1 hit.
Pfami PF00226. DnaJ. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view ]
PRINTSi PR00625. JDOMAIN.
SMARTi SM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
PROSITEi PS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiDNJC3_HUMAN
AccessioniPrimary (citable) accession number: Q13217
Secondary accession number(s): Q86WT9, Q8N4N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 130 of the entry and version 1 of the sequence. [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

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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