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Q13217

- DNJC3_HUMAN

UniProt

Q13217 - DNJC3_HUMAN

Protein

DnaJ homolog subfamily C member 3

Gene

DNAJC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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: UniProt
    5. membrane Source: UniProtKB

    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

    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

    1
    504
    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.
    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.
    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

    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: October 1, 2014
    This is version 131 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