ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q96EY1


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DNJA3_HUMAN
Primary accession number Q96EY1
Secondary accession numbers B2RAJ5 O75472 Q8WUJ6 Q8WXJ3 Q96D76 Q96IV1 Q9NYH8
Integrated into Swiss-Prot on May 16, 2003
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 77)
Name and origin of the protein
Protein name DnaJ homolog subfamily A member 3, mitochondrial [Precursor]
Synonyms Tumorous imaginal discs protein Tid56 homolog
DnaJ protein Tid-1
hTid-1
Hepatocellular carcinoma-associated antigen 57
Gene name
Name: DNAJA3
Synonyms: HCA57, TID1
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), TISSUE SPECIFICITY, AND VARIANT ASN-75.
DOI=10.1006/viro.1998.9220; PubMed=9683573 [NCBI, ExPASy, EBI, Israel, Japan]
Schilling B., De-Medina T., Syken J., Vidal M., Munger K.;
"A novel human DnaJ protein, hTid-1, a homolog of the Drosophila tumor suppressor protein Tid56, can interact with the human papillomavirus type 16 E7 oncoprotein.";
Virology 247:74-85(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2.
DOI=10.1074/jbc.M103683200; PubMed=11679576 [NCBI, ExPASy, EBI, Israel, Japan]
Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.;
"hTid-1, a human DnaJ protein, modulates the interferon signaling pathway.";
J. Biol. Chem. 276:49034-49042(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Colon, Lung, Muscle, and Placenta;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-480 (ISOFORM 2).
TISSUE=Hepatoma;
PubMed=12097419 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.;
"Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies.";
J. Immunol. 169:1102-1109(2002).
[6]
CHARACTERIZATION, AND MUTAGENESIS OF HIS-121.
DOI=10.1073/pnas.96.15.8499; PubMed=10411904 [NCBI, ExPASy, EBI, Israel, Japan]
Syken J., De-Medina T., Muenger K.;
"TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions.";
Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[9]
STRUCTURE BY NMR OF 93-303.
RIKEN structural genomics initiative (RSGI);
"Solution structure of J-domain and of zinc finger domain from human DnaJ subfamily A member 3.";
Submitted (OCT-2006) to the PDB data bank.
Comments
  • FUNCTION: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity.
  • SUBUNIT: Interacts with JAK2, HSPA9B and IFN-gammaR2 chain. Interacts with Ras GTPase-activating protein 1 (RASA1).
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsTid-1(L)
    Isoform IDQ96EY1-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsTid-1(S)
    Isoform IDQ96EY1-2
    Features which should be applied to build the isoform sequence: VSP_007425, VSP_007426.
  • TISSUE SPECIFICITY: Widely expressed with highest levels in heart, liver, lung and skeletal muscles. Also expressed in keratinocytes.
  • DOMAIN: Modulation of apoptosis, i.e proapoptotic activity of isoform 1 and antiapoptotic activity of isoform 2, is J domain-dependent.
  • PTM: Tyrosine phosphorylated (By similarity).
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • SIMILARITY: Contains 1 CR-type zinc finger.
  • SIMILARITY: Contains 1 J domain.
  • SEQUENCE CAUTION:
    • Sequence=AAF66245.1; Type=Frameshift; Positions=408, 411;
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
AF061749; AAC29066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF411044; AAL35323.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314218; BAG36892.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007225; AAH07225.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011855; AAH11855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012343; AAH12343.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014062; AAH14062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020248; AAH20248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030145; AAH30145.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032100; AAH32100.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF244136; AAF66245.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00179187; -.
IPI00294610; -.
UniGene Hs.459779
3D structure databases
PDB
2CTT; NMR; -; A=213-303.[ExPASy / RCSB / EBI]
2DN9; NMR; -; A=93-158.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2CTT; -.
2DN9; -.
ModBase Q96EY1.
Protein-protein interaction databases
IntAct Q96EY1; 17.
PTM databases
PhosphoSite Q96EY1; -.
Enzyme and pathway databases
Pathway_Interaction_DB trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
Organism-specific databases
GeneCards GC16P004415; -.
H-InvDB HIX0012782; -.
HIX0059641; -.
HGNC HGNC:11808; DNAJA3.
GenAtlas DNAJA3.
MIM 608382; gene. [NCBI / EBI]
PharmGKB PA27410; -.
Gene expression databases
ArrayExpress Q96EY1; -.
Bgee Q96EY1; -.
CleanEx HS_DNAJA3; -.
GermOnline ENSG00000103423; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from direct assay from UniProtKB).
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0051082; Molecular function: unfolded protein binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006915; Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0008285; Biological process: negative regulation of cell proliferation (inferred from direct assay from UniProtKB).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002939; DnaJ_C.
IPR001623; DnaJ_N.
IPR018253; Heat_shock_DnaJ_CS.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
IPR001305; HSP_DnaJ_cys-rich.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF01556; DnaJ_C; 1.
PF00684; DnaJ_CXXCXGXG; 1.
Pfam graphical view of domain structure.
PRINTS PR00625; DNAJPROTEIN.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PS51188; ZF_CR; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q96EY1; -.
Genome annotation databases
Ensembl ENSG00000103423; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN Q96EY1; -.
Other
NextBio 34071; -.
SOURCE DNAJA3; Homo sapiens.
ProtoNet Q96EY1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Chaperone; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism; Repeat; Transit peptide; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   480        DnaJ homolog subfamily A member 3, mitochondrial. PRO_0000007256
DOMAIN   93   158  66     J. 
REPEAT   236   243  8     CXXCXGXG motif. 
REPEAT   253   260  8     CXXCXGXG motif. 
REPEAT   275   282  8     CXXCXGXG motif. 
REPEAT   289   296  8     CXXCXGXG motif. 
ZN_FING   223   301  79     CR-type. 
METAL   236   236        Zinc 1 (By similarity). 
METAL   239   239        Zinc 1 (By similarity). 
METAL   253   253        Zinc 2 (By similarity). 
METAL   256   256        Zinc 2 (By similarity). 
METAL   275   275        Zinc 2 (By similarity). 
METAL   278   278        Zinc 2 (By similarity). 
METAL   289   289        Zinc 1 (By similarity). 
METAL   292   292        Zinc 1 (By similarity). 
MOD_RES   169   169        Phosphoserine. 
VAR_SEQ   448   453        GSTMDS -> KRSTGN (in isoform 2). VSP_007425
VAR_SEQ   454   480        Missing (in isoform 2). VSP_007426
VARIANT   75    75  1     Y -> N (in dbSNP:rs4785963 [NCBI]). VAR_027965 
MUTAGEN   121   121        H->Q: Loss of modulation of apoptosis. 
CONFLICT   320   320        M -> W (in Ref. 5; AAF66245). 
HELIX   94    98  5      
HELIX   106   119  14      
TURN   122   124  3      
HELIX   131   146  16      
HELIX   148   156  9      
STRAND   222   224  3      
STRAND   237   244  8      
STRAND   254   259  6      
STRAND   261   266  6      
STRAND   269   274  6      
STRAND   276   284  9      
STRAND   290   294  5      
STRAND   296   298  3      
Sequence information
Length: 480 AA [This is the length of the unprocessed precursor] Molecular weight: 52538 Da [This is the MW of the unprocessed precursor] CRC64: D28B7AE270F56004 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS SLTSCGPRAL 

        70         80         90        100        110        120 
LTLRPGVSLT GTKHYPFICT ASFHTSAPLA KEDYYQILGV PRNASQKEIK KAYYQLAKKY 

       130        140        150        160        170        180 
HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV 

       190        200        210        220        230        240 
DPEELFRKIF GEFSSSSFGD FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN 

       250        260        270        280        290        300 
GKGNEPGTKV QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ 

       310        320        330        340        350        360 
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL FISIAQALLG 

       370        380        390        400        410        420 
GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG YGDHYIHIKI RVPKRLTSRQ 

       430        440        450        460        470        480 
QSLILSYAED ETDVEGTVNG VTLTSSGGST MDSSAGSKAR REAGEDEEGF LSKLKKMFTS 

Q96EY1 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!