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Protein

DnaJ homolog subfamily C member 3

Gene

DNAJC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 apoptotic process Source: ParkinsonsUK-UCL
  6. negative regulation of protein kinase activity Source: GOC
  7. negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
  8. 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 lumen Source: Reactome
  3. endoplasmic reticulum Sec complex Source: Ensembl
  4. extracellular vesicular exosome Source: UniProtKB
  5. membrane Source: UniProtKB
  6. smooth endoplasmic reticulum Source: Ensembl
  7. vesicle Source: UniProtKB
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 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 504473DnaJ homolog subfamily C member 3PRO_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

BgeeiQ13217.
CleanExiHS_DNAJC3.
ExpressionAtlasiQ13217. baseline and differential.
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.By similarity3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4915Combined sources
Helixi53 – 6614Combined sources
Helixi71 – 8313Combined sources
Helixi87 – 10014Combined sources
Turni101 – 1033Combined sources
Helixi105 – 11713Combined sources
Helixi121 – 13212Combined sources
Helixi138 – 16730Combined sources
Helixi170 – 18314Combined sources
Helixi188 – 20013Combined sources
Helixi204 – 2074Combined sources
Helixi208 – 21811Combined sources
Helixi222 – 23413Combined sources
Helixi238 – 25114Combined sources
Helixi256 – 28126Combined sources
Helixi284 – 29714Combined sources
Helixi302 – 31716Combined sources
Turni318 – 3203Combined sources
Helixi322 – 33514Combined sources
Helixi340 – 35213Combined sources
Helixi356 – 36712Combined sources
Beta strandi370 – 3723Combined sources
Helixi374 – 39118Combined sources
Helixi396 – 3983Combined sources
Helixi409 – 42012Combined sources
Helixi423 – 4253Combined sources
Helixi429 – 44820Combined sources
Helixi451 – 4544Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni375 – 39319Flexible linkerAdd
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.PROSITE-ProRule annotation
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, TPR repeat

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00720000108760.
HOGENOMiHOG000193351.
HOVERGENiHBG053820.
InParanoidiQ13217.
KOiK09523.
OMAiGVHEYTI.
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_dom.
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

        10         20         30         40         50
MVAPGSVTSR LGSVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA
60 70 80 90 100
GQLADALSQF HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIQL
110 120 130 140 150
KMDFTAARLQ RGHLLLKQGK LDEAEDDFKK VLKSNPSENE EKEAQSQLIK
160 170 180 190 200
SDEMQRLRSQ ALNAFGSGDY TAAIAFLDKI LEVCVWDAEL RELRAECFIK
210 220 230 240 250
EGEPRKAISD LKAASKLKND NTEAFYKIST LYYQLGDHEL SLSEVRECLK
260 270 280 290 300
LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS
310 320 330 340 350
IAEYTVRSKE RICHCFSKDE KPVEAIRVCS EVLQMEPDNV NALKDRAEAY
360 370 380 390 400
LIEEMYDEAI QDYETAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG
410 420 430 440 450
VKRNAKKQEI IKAYRKLALQ WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS
460 470 480 490 500
DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR SWNSWQGFNP FSSGGPFRFK

FHFN
Length:504
Mass (Da):57,580
Last modified:November 1, 1996 - v1
Checksum:iE720A1E7F618B912
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ13217.

Polymorphism databases

DMDMi73620807.

Proteomic databases

MaxQBiQ13217.
PaxDbiQ13217.
PeptideAtlasiQ13217.
PRIDEiQ13217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5611.
GeneCardsiGC13P096329.
HGNCiHGNC:9439. DNAJC3.
HPAiHPA039336.
HPA041326.
MIMi601184. gene.
neXtProtiNX_Q13217.
PharmGKBiPA27420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00720000108760.
HOGENOMiHOG000193351.
HOVERGENiHBG053820.
InParanoidiQ13217.
KOiK09523.
OMAiGVHEYTI.
OrthoDBiEOG70KGPH.
PhylomeDBiQ13217.
TreeFamiTF105162.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiDNAJC3. human.
GeneWikiiDNAJC3.
GenomeRNAii5611.
NextBioi21810.
PROiQ13217.
SOURCEiSearch...

Gene expression databases

BgeeiQ13217.
CleanExiHS_DNAJC3.
ExpressionAtlasiQ13217. baseline and differential.
GenevestigatoriQ13217.

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_dom.
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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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: March 4, 2015
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.