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DnaJ homolog subfamily A member 3, mitochondrial (DnaJ protein Tid-1) (hTid-1) (Hepatocellular carcinoma-associated antigen 57) (Tumorous imaginal discs protein Tid56 homolog)

 DNJA3_HUMAN             Reviewed;         480 AA.
Q96EY1; B2RAJ5; B4DI33; E7ES32; O75472; Q8WUJ6; Q8WXJ3; Q96D76;
Q96IV1; Q9NYH8;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
25-OCT-2017, entry version 167.
RecName: Full=DnaJ homolog subfamily A member 3, mitochondrial;
AltName: Full=DnaJ protein Tid-1;
Short=hTid-1;
AltName: Full=Hepatocellular carcinoma-associated antigen 57;
AltName: Full=Tumorous imaginal discs protein Tid56 homolog;
Flags: Precursor;
Name=DNAJA3; Synonyms=HCA57, TID1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=9683573; DOI=10.1006/viro.1998.9220;
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), INTERACTION WITH JAK2; HSP70
AND IFN-GAMMAR2, AND VARIANT TYR-75.
PubMed=11679576; DOI=10.1074/jbc.M103683200;
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] (ISOFORMS 1 AND 3), AND VARIANT
TYR-75.
TISSUE=Corpus callosum, and Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
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 GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
TYR-75.
TISSUE=Brain, Colon, Lung, Muscle, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-480 (ISOFORM 2), AND VARIANT TYR-75.
TISSUE=Hepatoma;
PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
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).
[7]
CHARACTERIZATION, AND MUTAGENESIS OF HIS-121.
PubMed=10411904; DOI=10.1073/pnas.96.15.8499;
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
METHYLATION AT ARG-58; ARG-238 AND ARG-293 BY CARM1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23455924; DOI=10.1038/nmeth.2397;
Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P.,
Meierhofer D., Benlasfer N., Valovka T., Timmermann B., Wanker E.E.,
Sauer S., Stelzl U.;
"A Y2H-seq approach defines the human protein methyltransferase
interactome.";
Nat. Methods 10:339-342(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
STRUCTURE BY NMR OF 93-303 IN COMPLEX WITH ZINC IONS.
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.
-!- 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. Isoform 2 may play a role in
neuromuscular junction development as an effector of the MUSK
signaling pathway.
-!- SUBUNIT: Interacts with JAK2, HSPA9B and IFN-gammaR2 chain.
Interacts with Ras GTPase-activating protein 1 (RASA1). Isoform 2
interacts with MUSK (via the cytoplasmic domain) (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q9H614:-; NbExp=3; IntAct=EBI-3952284, EBI-10249899;
Q53TS8:C2CD6; NbExp=3; IntAct=EBI-3952284, EBI-739879;
Q86X55:CARM1; NbExp=2; IntAct=EBI-356767, EBI-2339854;
Q7L5A3:FAM214B; NbExp=3; IntAct=EBI-3952284, EBI-745689;
P15408:FOSL2; NbExp=3; IntAct=EBI-3952284, EBI-3893419;
Q96NE9:FRMD6; NbExp=3; IntAct=EBI-3952284, EBI-741729;
Q96CN9:GCC1; NbExp=3; IntAct=EBI-3952284, EBI-746252;
Q15735:INPP5J; NbExp=3; IntAct=EBI-3952284, EBI-10236940;
O60341:KDM1A; NbExp=2; IntAct=EBI-356767, EBI-710124;
P08581:MET; NbExp=2; IntAct=EBI-3952284, EBI-1039152;
Q9BVI4:NOC4L; NbExp=3; IntAct=EBI-3952284, EBI-395927;
Q9UJX0:OSGIN1; NbExp=3; IntAct=EBI-3952284, EBI-9057006;
Q96LA8:PRMT6; NbExp=2; IntAct=EBI-356767, EBI-912440;
Q61115:Ptch1 (xeno); NbExp=2; IntAct=EBI-356767, EBI-15619523;
P51692:STAT5B; NbExp=2; IntAct=EBI-356767, EBI-1186119;
P42232:Stat5b (xeno); NbExp=3; IntAct=EBI-356767, EBI-617454;
O75716:STK16; NbExp=3; IntAct=EBI-3952284, EBI-749295;
D2IYK5:TCF19; NbExp=3; IntAct=EBI-3952284, EBI-10176552;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cytoplasm, cytosol
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Note=Recruited to the postsynaptic cell membrane of the
neuromuscular junction through interaction with MUSK.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Tid-1(L);
IsoId=Q96EY1-1; Sequence=Displayed;
Name=2; Synonyms=Tid-1(S);
IsoId=Q96EY1-2; Sequence=VSP_007425, VSP_007426;
Name=3;
IsoId=Q96EY1-3; Sequence=VSP_055728, VSP_007425, VSP_007426;
Note=Ref.3 (BAG58345) sequence is in conflict in position:
33:Y->H. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
liver, lung and skeletal muscles. Also expressed in keratinocytes.
{ECO:0000269|PubMed:9683573}.
-!- DOMAIN: Modulation of apoptosis, i.e. proapoptotic activity of
isoform 1 and antiapoptotic activity of isoform 2, is J domain-
dependent.
-!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAF66245.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF66245.1; Type=Frameshift; Positions=408, 411; Evidence={ECO:0000305};
Sequence=AAH12343.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DNAJA3ID40342ch16p13.html";
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EMBL; AF061749; AAC29066.1; -; mRNA.
EMBL; AF411044; AAL35323.1; -; mRNA.
EMBL; AK295391; BAG58345.1; -; mRNA.
EMBL; AK314218; BAG36892.1; -; mRNA.
EMBL; AC012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007225; AAH07225.1; -; mRNA.
EMBL; BC011855; AAH11855.1; -; mRNA.
EMBL; BC012343; AAH12343.1; ALT_INIT; mRNA.
EMBL; BC014062; AAH14062.1; -; mRNA.
EMBL; BC020248; AAH20248.1; -; mRNA.
EMBL; BC030145; AAH30145.1; -; mRNA.
EMBL; BC032100; AAH32100.1; -; mRNA.
EMBL; AF244136; AAF66245.1; ALT_SEQ; mRNA.
CCDS; CCDS10515.1; -. [Q96EY1-1]
CCDS; CCDS45400.1; -. [Q96EY1-2]
CCDS; CCDS66930.1; -. [Q96EY1-3]
RefSeq; NP_001128582.1; NM_001135110.2. [Q96EY1-2]
RefSeq; NP_001273445.1; NM_001286516.1. [Q96EY1-3]
RefSeq; NP_005138.3; NM_005147.5. [Q96EY1-1]
UniGene; Hs.459779; -.
PDB; 2CTT; NMR; -; A=213-303.
PDB; 2DN9; NMR; -; A=93-158.
PDBsum; 2CTT; -.
PDBsum; 2DN9; -.
ProteinModelPortal; Q96EY1; -.
SMR; Q96EY1; -.
BioGrid; 114547; 85.
DIP; DIP-33870N; -.
IntAct; Q96EY1; 65.
MINT; MINT-1151431; -.
STRING; 9606.ENSP00000262375; -.
iPTMnet; Q96EY1; -.
PhosphoSitePlus; Q96EY1; -.
BioMuta; DNAJA3; -.
DMDM; 311033374; -.
EPD; Q96EY1; -.
MaxQB; Q96EY1; -.
PaxDb; Q96EY1; -.
PeptideAtlas; Q96EY1; -.
PRIDE; Q96EY1; -.
DNASU; 9093; -.
Ensembl; ENST00000262375; ENSP00000262375; ENSG00000103423. [Q96EY1-1]
Ensembl; ENST00000355296; ENSP00000347445; ENSG00000103423. [Q96EY1-2]
Ensembl; ENST00000431375; ENSP00000393970; ENSG00000103423. [Q96EY1-3]
Ensembl; ENST00000612103; ENSP00000477570; ENSG00000276726. [Q96EY1-1]
Ensembl; ENST00000614397; ENSP00000479815; ENSG00000276726. [Q96EY1-2]
GeneID; 9093; -.
KEGG; hsa:9093; -.
UCSC; uc002cwk.4; human. [Q96EY1-1]
CTD; 9093; -.
DisGeNET; 9093; -.
EuPathDB; HostDB:ENSG00000103423.13; -.
GeneCards; DNAJA3; -.
H-InvDB; HIX0012782; -.
HGNC; HGNC:11808; DNAJA3.
HPA; CAB016095; -.
HPA; HPA040875; -.
HPA; HPA044229; -.
MIM; 608382; gene.
neXtProt; NX_Q96EY1; -.
OpenTargets; ENSG00000103423; -.
PharmGKB; PA27410; -.
eggNOG; KOG0715; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00890000139473; -.
HOGENOM; HOG000203530; -.
HOVERGEN; HBG051371; -.
InParanoid; Q96EY1; -.
KO; K09504; -.
OMA; DMGGFAD; -.
OrthoDB; EOG091G09C7; -.
PhylomeDB; Q96EY1; -.
TreeFam; TF105152; -.
ChiTaRS; DNAJA3; human.
EvolutionaryTrace; Q96EY1; -.
GeneWiki; DNAJA3; -.
GenomeRNAi; 9093; -.
PRO; PR:Q96EY1; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103423; -.
CleanEx; HS_DNAJA3; -.
ExpressionAtlas; Q96EY1; baseline and differential.
Genevisible; Q96EY1; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IMP:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0030695; F:GTPase regulator activity; IEA:Ensembl.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0005133; F:interferon-gamma receptor binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0006264; P:mitochondrial DNA replication; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0007528; P:neuromuscular junction development; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0006457; P:protein folding; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0009408; P:response to heat; IEA:InterPro.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
CDD; cd06257; DnaJ; 1.
CDD; cd10719; DnaJ_zf; 1.
Gene3D; 1.10.287.110; -; 1.
HAMAP; MF_01152; DnaJ; 1.
InterPro; IPR012724; DnaJ.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
Pfam; PF00684; DnaJ_CXXCXGXG; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 1.
SUPFAM; SSF57938; SSF57938; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51188; ZF_CR; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Cell junction; Cell membrane; Chaperone; Complete proteome; Cytoplasm;
Membrane; Metal-binding; Methylation; Mitochondrion; Phosphoprotein;
Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat;
Synapse; Transit peptide; Zinc; Zinc-finger.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 480 DnaJ homolog subfamily A member 3,
mitochondrial.
/FTId=PRO_0000007256.
DOMAIN 93 158 J.
REPEAT 236 243 CXXCXGXG motif.
REPEAT 253 260 CXXCXGXG motif.
REPEAT 275 282 CXXCXGXG motif.
REPEAT 289 296 CXXCXGXG motif.
ZN_FING 223 301 CR-type.
METAL 236 236 Zinc 1. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 239 239 Zinc 1. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 253 253 Zinc 2. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 256 256 Zinc 2. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 275 275 Zinc 2. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 278 278 Zinc 2. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 289 289 Zinc 1. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
METAL 292 292 Zinc 1. {ECO:0000244|PDB:2CTT,
ECO:0000269|Ref.12}.
MOD_RES 58 58 Omega-N-methylarginine; by CARM1.
{ECO:0000269|PubMed:23455924}.
MOD_RES 134 134 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99M87}.
MOD_RES 238 238 Omega-N-methylarginine; by CARM1.
{ECO:0000269|PubMed:23455924}.
MOD_RES 293 293 Omega-N-methylarginine; by CARM1.
{ECO:0000269|PubMed:23455924}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 3 186 ARCSTRWLLVVVGTPRLPAISGRGARPPREGVVGAWLSRKL
SVPAFASSLTSCGPRALLTLRPGVSLTGTKHNPFICTASFH
TSAPLAKEDYYQILGVPRNASQKEIKKAYYQLAKKYHPDTN
KDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGA
SGSQHSYWKGGPTVDPEELF -> EPQAERPRLCVFPDLLR
PPSAADIETWCQPY (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055728.
VAR_SEQ 448 453 GSTMDS -> KRSTGN (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:11679576,
ECO:0000303|PubMed:12097419,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007425.
VAR_SEQ 454 480 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11679576,
ECO:0000303|PubMed:12097419,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007426.
VARIANT 75 75 N -> Y (in dbSNP:rs4785963).
{ECO:0000269|PubMed:11679576,
ECO:0000269|PubMed:12097419,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_027965.
MUTAGEN 121 121 H->Q: Loss of modulation of apoptosis.
{ECO:0000269|PubMed:10411904}.
CONFLICT 320 320 M -> W (in Ref. 6; AAF66245).
{ECO:0000305}.
HELIX 94 98 {ECO:0000244|PDB:2DN9}.
HELIX 106 119 {ECO:0000244|PDB:2DN9}.
TURN 122 124 {ECO:0000244|PDB:2DN9}.
HELIX 131 146 {ECO:0000244|PDB:2DN9}.
HELIX 148 156 {ECO:0000244|PDB:2DN9}.
STRAND 222 224 {ECO:0000244|PDB:2CTT}.
STRAND 237 244 {ECO:0000244|PDB:2CTT}.
STRAND 254 259 {ECO:0000244|PDB:2CTT}.
STRAND 261 266 {ECO:0000244|PDB:2CTT}.
STRAND 269 274 {ECO:0000244|PDB:2CTT}.
STRAND 276 284 {ECO:0000244|PDB:2CTT}.
STRAND 290 294 {ECO:0000244|PDB:2CTT}.
STRAND 296 298 {ECO:0000244|PDB:2CTT}.
SEQUENCE 480 AA; 52489 MW; 5A57B9020992CF59 CRC64;
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS SLTSCGPRAL
LTLRPGVSLT GTKHNPFICT ASFHTSAPLA KEDYYQILGV PRNASQKEIK KAYYQLAKKY
HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV
DPEELFRKIF GEFSSSSFGD FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN
GKGNEPGTKV QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL FISIAQALLG
GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG YGDHYIHIKI RVPKRLTSRQ
QSLILSYAED ETDVEGTVNG VTLTSSGGST MDSSAGSKAR REAGEDEEGF LSKLKKMFTS


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