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UniProtKB/Swiss-Prot entry Q13217


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DNJC3_HUMAN
Primary accession number Q13217
Secondary accession numbers Q86WT9 Q8N4N2
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 76)
Name and origin of the protein
Protein name DnaJ homolog subfamily C member 3 [Precursor]
Synonyms Interferon-induced, double-stranded RNA-activated protein kinase inhibitor
Protein kinase inhibitor of 58 kDa
Protein kinase inhibitor p58
Gene name
Name: DNAJC3
Synonyms: P58IPK, PRKRI
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
DOI=10.1016/0378-1119(95)00883-7; PubMed=8666242 [NCBI, ExPASy, EBI, Israel, Japan]
Korth M.J., Lyons C.N., Wambach M., Katze M.G.;
"Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase.";
Gene 170:181-188(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02379; PubMed=15057823 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Blood;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND INTERACTION WITH EIF2AK2.
DOI=10.1074/jbc.271.3.1702; PubMed=8576172 [NCBI, ExPASy, EBI, Israel, Japan]
Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G.;
"The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity.";
J. Biol. Chem. 271:1702-1707(1996).
[6]
FUNCTION, INTERACTION WITH PRKRIR, AND INDUCTION.
PubMed=9447982 [NCBI, ExPASy, EBI, Israel, Japan]
Gale M.J. Jr., Blakely C.M., Hopkins D.A., Melville M.W., Wambach M., Romano P.R., Katze M.G.;
"Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK.";
Mol. Cell. Biol. 18:859-871(1998).
[7]
FUNCTION, INTERACTION WITH DNAJB1 AND HSPA8, AND INDUCTION.
DOI=10.1074/jbc.274.6.3797; PubMed=9920933 [NCBI, ExPASy, EBI, Israel, Japan]
Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.;
"The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity.";
J. Biol. Chem. 274:3797-3803(1999).
[8]
FUNCTION, AND INDUCTION.
DOI=10.1074/jbc.M212074200; PubMed=12601012 [NCBI, ExPASy, EBI, Israel, Japan]
van Huizen R., Martindale J.L., Gorospe M., Holbrook N.J.;
"P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling.";
J. Biol. Chem. 278:15558-15564(2003).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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.
  • SUBUNIT: Interacts with EIF2AK3 (By similarity) and EIF2AK2. Forms a trimeric complex with DNAJB1 and HSPA8. Interacts with PRKRIR/P52RIPK.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity).
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ13217-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ13217-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_015148, VSP_015149.
  • TISSUE SPECIFICITY: Widely expressed with high level in the pancreas and testis. Also expressed in cell lines with different levels.
  • 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.
  • DOMAIN: The J domain mediates interaction with HSPA8.
  • SIMILARITY: Contains 1 J domain.
  • SIMILARITY: Contains 9 TPR repeats.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dnajc3/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U28424; AAC50502.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY795482; AAV40838.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138955; CAH70090.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033823; AAH33823.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047936; AAH47936.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00006713; -.
IPI00166730; -.
PIR JC4775; JC4775.
RefSeq NP_006251.1; -.
UniGene Hs.656476
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
ModBase Q13217.
Organism-specific databases
GeneCards GC13P095127; -.
H-InvDB HIX0037309; -.
HGNC HGNC:9439; DNAJC3.
GenAtlas DNAJC3.
MIM 601184; gene. [NCBI / EBI]
PharmGKB PA27420; -.
Gene expression databases
ArrayExpress Q13217; -.
Bgee Q13217; -.
CleanEx HS_DNAJC3; -.
GermOnline ENSG00000102580; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0004860; Molecular function: protein kinase inhibitor activity (traceable author statement from ProtInc).
GO:0006986; Biological process: response to unfolded protein (inferred from electronic annotation from UniProtKB-KW).
GO:0009615; Biological process: response to virus (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001623; DnaJ_N.
IPR018253; Heat_shock_DnaJ_CS.
IPR015609; Hsp40/DnaJ_Rel.
IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
IPR019734; TPR_repeat.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
G3DSA:1.25.40.10; TPR-like_helical; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF00515; TPR_1; 6.
Pfam graphical view of domain structure.
SMART SM00271; DnaJ; 1.
SM00028; TPR; 7.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; FALSE_NEG.
PS50076; DNAJ_2; 1.
PS50005; TPR; 8.
PS50293; TPR_REGION; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q13217; -.
PRIDE Q13217; -.
Genome annotation databases
Ensembl ENSG00000102580; Homo sapiens. [Contig view]
GeneID 5611; -.
KEGG hsa:5611; -.
Phylogenomic databases
HOGENOM Q13217; -.
HOVERGEN Q13217; -.
OMA Q13217; ISSKSFM.
Other
NextBio 21810; -.
SOURCE DNAJC3; Homo sapiens.
ProtoNet Q13217.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Antiviral defense; Chaperone; Endoplasmic reticulum; Repeat; Signal; TPR repeat; Unfolded protein response.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   504  473     DnaJ homolog subfamily C member 3. PRO_0000071045
REPEAT   37    70  34     TPR 1. 
REPEAT   72   104  33     TPR 2. 
REPEAT   105   138  34     TPR 3. 
REPEAT   154   187  34     TPR 4. 
REPEAT   189   221  33     TPR 5. 
REPEAT   222   255  34     TPR 6. 
REPEAT   268   301  34     TPR 7. 
REPEAT   306   339  34     TPR 8. 
REPEAT   340   373  34     TPR 9. 
DOMAIN   394   462  69     J. 
VAR_SEQ   132   234        LKSNPSENEEKEAQSQLIKSDEMQRLRSQALNAFGSGDYT AAIAFLDKILEVCVWDAELRELRAECFIKEGEPRKAISDL KAASKLKNDNTEAFYKISTLYYQ -> VFPVPSLLGLQRSLLDDLYLLFWFFLMKKVTFRCLSSAIS ECLPQSLNLMKFNLLISFLLLWTVRLVSCLRSIHYAVGSK TFLISSKSFMVLCFIFKPIVYLS (in isoform 2). VSP_015148
VAR_SEQ   235   504        Missing (in isoform 2). VSP_015149
Sequence information
Length: 504 AA [This is the length of the unprocessed precursor] Molecular weight: 57580 Da [This is the MW of the unprocessed precursor] CRC64: E720A1E7F618B912 [This is a checksum on the sequence]
        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 

Q13217 in FASTA format

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