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Reviewed, UniProtKB/Swiss-Prot Q13217 (DNJC3_HUMAN)

Last modified February 9, 2010. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DnaJ homolog subfamily C member 3
Alternative name(s):
    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) [Complete 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.

Sequence similarities

Contains 1 J domain.

Contains 9 TPR repeats.

Ontologies

Keywords
   Biological processAntiviral defense
Unfolded protein response
   Cellular componentEndoplasmic reticulum
   DomainRepeat
Signal
TPR repeat
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processresponse to unfolded protein

Inferred from electronic annotation. Source: UniProtKB-KW

response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheat shock protein binding

Inferred from electronic annotation. Source: InterPro

protein kinase inhibitor activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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

Sequences

Sequence LengthMass (Da)Tools
Q13217-1 [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: 8666242] [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: 15057823] [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: 15489334] [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: 8576172] [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: 9447982] [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: 9920933] [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: 12601012] [Abstract]
Cited for: FUNCTION, INDUCTION.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+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.
IPIIPI00006713.
PIRJC4775.
RefSeqNP_006251.1.
UniGeneHs.59214

3D structure databases

SMRQ13217. Positions 36-375, 341-458, 391-489.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ13217.

Proteomic databases

PeptideAtlasQ13217.
PRIDEQ13217.

Genome annotation databases

EnsemblENST00000376795; ENSP00000365991; ENSG00000102580; Homo sapiens. [Genome view]
GeneID5611.
KEGGhsa:5611.
UCSCuc001vmp.1. human.
uc001vmq.1. human.

Organism-specific databases

CTD5611.
GeneCardsGC13P095127.
H-InvDBHIX0037309.
HGNCHGNC:9439. DNAJC3.
MIM601184. gene.
PharmGKBPA27420.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09986.
HOGENOMHBG314286.
HOVERGENQ13217.
InParanoidQ13217.
OMAESSDYTA.
OrthoDBEOG92JRBD.
PhylomeDBQ13217.

Enzyme and pathway databases

ReactomeREACT_15380. Diabetes pathways.

Gene expression databases

ArrayExpressQ13217.
BgeeQ13217.
CleanExHS_DNAJC3.
GenevestigatorQ13217.
GermOnlineENSG00000102580. Homo sapiens.

Family and domain databases

InterProIPR001623. DnaJ_N.
IPR015609. Hsp40/DnaJ_Rel.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.10.287.110. DnaJ_N. 1 hit.
G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PANTHERPTHR11821. Hsp40/DnaJ_Rel. 1 hit.
PfamPF00226. DnaJ. 1 hit.
[Graphical view]
SMARTSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
PROSITEPS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21810.
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: February 9, 2010
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 13

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents