DNJA3_HUMAN
ID DNJA3_HUMAN Reviewed; 480 AA.
AC Q96EY1; B2RAJ5; B4DI33; E7ES32; O75472; Q8WUJ6; Q8WXJ3; Q96D76; Q96IV1;
AC Q9NYH8;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=DnaJ homolog subfamily A member 3, mitochondrial;
DE AltName: Full=DnaJ protein Tid-1;
DE Short=hTid-1;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 57;
DE AltName: Full=Tumorous imaginal discs protein Tid56 homolog;
DE Flags: Precursor;
GN Name=DNAJA3; Synonyms=HCA57, TID1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9683573; DOI=10.1006/viro.1998.9220;
RA Schilling B., De-Medina T., Syken J., Vidal M., Munger K.;
RT "A novel human DnaJ protein, hTid-1, a homolog of the Drosophila tumor
RT suppressor protein Tid56, can interact with the human papillomavirus type
RT 16 E7 oncoprotein.";
RL Virology 247:74-85(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND
RP IFN-GAMMAR2, AND VARIANT TYR-75.
RX PubMed=11679576; DOI=10.1074/jbc.m103683200;
RA Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A.,
RA Pestka S.;
RT "hTid-1, a human DnaJ protein, modulates the interferon signaling
RT pathway.";
RL J. Biol. Chem. 276:49034-49042(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP TYR-75.
RC TISSUE=Corpus callosum, and Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-75.
RC TISSUE=Brain, Colon, Lung, Muscle, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-480 (ISOFORM 2), AND VARIANT TYR-75.
RC TISSUE=Hepatoma;
RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA Chen W.-F.;
RT "Large scale identification of human hepatocellular carcinoma-associated
RT antigens by autoantibodies.";
RL J. Immunol. 169:1102-1109(2002).
RN [7]
RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-121.
RX PubMed=10411904; DOI=10.1073/pnas.96.15.8499;
RA Syken J., De-Medina T., Muenger K.;
RT "TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes
RT two mitochondrial modulators of apoptosis with opposing functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP METHYLATION AT ARG-58; ARG-238 AND ARG-293 BY CARM1, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=23455924; DOI=10.1038/nmeth.2397;
RA Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D.,
RA Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U.;
RT "A Y2H-seq approach defines the human protein methyltransferase
RT interactome.";
RL Nat. Methods 10:339-342(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP STRUCTURE BY NMR OF 93-303 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of J-domain and of zinc finger domain from human DnaJ
RT subfamily A member 3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Modulates apoptotic signal transduction or effector
CC structures within the mitochondrial matrix. Affect cytochrome C release
CC from the mitochondria and caspase 3 activation, but not caspase 8
CC activation. Isoform 1 increases apoptosis triggered by both TNF and the
CC DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses
CC apoptosis. Can modulate IFN-gamma-mediated transcriptional activity.
CC Isoform 2 may play a role in neuromuscular junction development as an
CC effector of the MUSK signaling pathway.
CC -!- SUBUNIT: Interacts with JAK2, HSPA9B and IFN-gammaR2 chain. Interacts
CC with Ras GTPase-activating protein 1 (RASA1). Isoform 2 interacts with
CC MUSK (via the cytoplasmic domain) (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96EY1; P54253: ATXN1; NbExp=7; IntAct=EBI-356767, EBI-930964;
CC Q96EY1; Q86X55: CARM1; NbExp=2; IntAct=EBI-356767, EBI-2339854;
CC Q96EY1; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-356767, EBI-7062247;
CC Q96EY1; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-356767, EBI-3867333;
CC Q96EY1; P42858: HTT; NbExp=5; IntAct=EBI-356767, EBI-466029;
CC Q96EY1; O60341: KDM1A; NbExp=2; IntAct=EBI-356767, EBI-710124;
CC Q96EY1; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-356767, EBI-912440;
CC Q96EY1; P51692: STAT5B; NbExp=2; IntAct=EBI-356767, EBI-1186119;
CC Q96EY1; Q61115: Ptch1; Xeno; NbExp=2; IntAct=EBI-356767, EBI-15619523;
CC Q96EY1; P42232: Stat5b; Xeno; NbExp=3; IntAct=EBI-356767, EBI-617454;
CC Q96EY1-1; P42232: Stat5b; Xeno; NbExp=2; IntAct=EBI-4322330, EBI-617454;
CC Q96EY1-2; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-3952284, EBI-739879;
CC Q96EY1-2; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-3952284, EBI-745689;
CC Q96EY1-2; P15408: FOSL2; NbExp=3; IntAct=EBI-3952284, EBI-3893419;
CC Q96EY1-2; Q96NE9: FRMD6; NbExp=6; IntAct=EBI-3952284, EBI-741729;
CC Q96EY1-2; Q96CN9: GCC1; NbExp=3; IntAct=EBI-3952284, EBI-746252;
CC Q96EY1-2; Q15735: INPP5J; NbExp=3; IntAct=EBI-3952284, EBI-10236940;
CC Q96EY1-2; P08581: MET; NbExp=2; IntAct=EBI-3952284, EBI-1039152;
CC Q96EY1-2; Q9BVI4: NOC4L; NbExp=3; IntAct=EBI-3952284, EBI-395927;
CC Q96EY1-2; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-3952284, EBI-9057006;
CC Q96EY1-2; O75716: STK16; NbExp=3; IntAct=EBI-3952284, EBI-749295;
CC Q96EY1-2; D2IYK5: TCF19; NbExp=3; IntAct=EBI-3952284, EBI-10176552;
CC Q96EY1-2; Q9H614; NbExp=3; IntAct=EBI-3952284, EBI-10249899;
CC Q96EY1-2; P42232: Stat5b; Xeno; NbExp=2; IntAct=EBI-3952284, EBI-617454;
CC Q96EY1-3; P54253: ATXN1; NbExp=6; IntAct=EBI-11526226, EBI-930964;
CC Q96EY1-3; P55212: CASP6; NbExp=3; IntAct=EBI-11526226, EBI-718729;
CC Q96EY1-3; O75460-2: ERN1; NbExp=3; IntAct=EBI-11526226, EBI-25852368;
CC Q96EY1-3; P22607: FGFR3; NbExp=3; IntAct=EBI-11526226, EBI-348399;
CC Q96EY1-3; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-11526226, EBI-10226858;
CC Q96EY1-3; P14136: GFAP; NbExp=3; IntAct=EBI-11526226, EBI-744302;
CC Q96EY1-3; P06396: GSN; NbExp=3; IntAct=EBI-11526226, EBI-351506;
CC Q96EY1-3; P54652: HSPA2; NbExp=3; IntAct=EBI-11526226, EBI-356991;
CC Q96EY1-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11526226, EBI-1055254;
CC Q96EY1-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-11526226, EBI-21591415;
CC Q96EY1-3; P19404: NDUFV2; NbExp=3; IntAct=EBI-11526226, EBI-713665;
CC Q96EY1-3; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-11526226, EBI-5280197;
CC Q96EY1-3; P62826: RAN; NbExp=3; IntAct=EBI-11526226, EBI-286642;
CC Q96EY1-3; Q13148: TARDBP; NbExp=6; IntAct=EBI-11526226, EBI-372899;
CC Q96EY1-3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-11526226, EBI-741480;
CC Q96EY1-3; Q9Y649; NbExp=3; IntAct=EBI-11526226, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cytoplasm, cytosol
CC {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Recruited to the postsynaptic cell
CC membrane of the neuromuscular junction through interaction with MUSK.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Tid-1(L);
CC IsoId=Q96EY1-1; Sequence=Displayed;
CC Name=2; Synonyms=Tid-1(S);
CC IsoId=Q96EY1-2; Sequence=VSP_007425, VSP_007426;
CC Name=3;
CC IsoId=Q96EY1-3; Sequence=VSP_055728, VSP_007425, VSP_007426;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
CC liver, lung and skeletal muscles. Also expressed in keratinocytes.
CC {ECO:0000269|PubMed:9683573}.
CC -!- DOMAIN: Modulation of apoptosis, i.e. proapoptotic activity of isoform
CC 1 and antiapoptotic activity of isoform 2, is J domain-dependent.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66245.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF66245.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH12343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DNAJA3ID40342ch16p13.html";
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DR EMBL; AF061749; AAC29066.1; -; mRNA.
DR EMBL; AF411044; AAL35323.1; -; mRNA.
DR EMBL; AK295391; BAG58345.1; -; mRNA.
DR EMBL; AK314218; BAG36892.1; -; mRNA.
DR EMBL; AC012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007225; AAH07225.1; -; mRNA.
DR EMBL; BC011855; AAH11855.1; -; mRNA.
DR EMBL; BC012343; AAH12343.1; ALT_INIT; mRNA.
DR EMBL; BC014062; AAH14062.1; -; mRNA.
DR EMBL; BC020248; AAH20248.1; -; mRNA.
DR EMBL; BC030145; AAH30145.1; -; mRNA.
DR EMBL; BC032100; AAH32100.1; -; mRNA.
DR EMBL; AF244136; AAF66245.1; ALT_SEQ; mRNA.
DR CCDS; CCDS10515.1; -. [Q96EY1-1]
DR CCDS; CCDS45400.1; -. [Q96EY1-2]
DR CCDS; CCDS66930.1; -. [Q96EY1-3]
DR RefSeq; NP_001128582.1; NM_001135110.2. [Q96EY1-2]
DR RefSeq; NP_001273445.1; NM_001286516.1. [Q96EY1-3]
DR RefSeq; NP_005138.3; NM_005147.5. [Q96EY1-1]
DR PDB; 2CTT; NMR; -; A=213-303.
DR PDB; 2DN9; NMR; -; A=93-158.
DR PDB; 6IWS; NMR; -; A=89-159.
DR PDBsum; 2CTT; -.
DR PDBsum; 2DN9; -.
DR PDBsum; 6IWS; -.
DR AlphaFoldDB; Q96EY1; -.
DR SMR; Q96EY1; -.
DR BioGRID; 114547; 332.
DR DIP; DIP-33870N; -.
DR IntAct; Q96EY1; 130.
DR MINT; Q96EY1; -.
DR STRING; 9606.ENSP00000262375; -.
DR GlyGen; Q96EY1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EY1; -.
DR MetOSite; Q96EY1; -.
DR PhosphoSitePlus; Q96EY1; -.
DR BioMuta; DNAJA3; -.
DR DMDM; 311033374; -.
DR EPD; Q96EY1; -.
DR jPOST; Q96EY1; -.
DR MassIVE; Q96EY1; -.
DR MaxQB; Q96EY1; -.
DR PaxDb; Q96EY1; -.
DR PeptideAtlas; Q96EY1; -.
DR PRIDE; Q96EY1; -.
DR ProteomicsDB; 17904; -.
DR ProteomicsDB; 76466; -. [Q96EY1-1]
DR ProteomicsDB; 76467; -. [Q96EY1-2]
DR Antibodypedia; 24319; 277 antibodies from 33 providers.
DR DNASU; 9093; -.
DR Ensembl; ENST00000262375.11; ENSP00000262375.4; ENSG00000103423.14. [Q96EY1-1]
DR Ensembl; ENST00000355296.8; ENSP00000347445.4; ENSG00000103423.14. [Q96EY1-2]
DR Ensembl; ENST00000431375.6; ENSP00000393970.2; ENSG00000103423.14. [Q96EY1-3]
DR Ensembl; ENST00000612103.4; ENSP00000477570.1; ENSG00000276726.4. [Q96EY1-1]
DR Ensembl; ENST00000614397.4; ENSP00000479815.1; ENSG00000276726.4. [Q96EY1-2]
DR GeneID; 9093; -.
DR KEGG; hsa:9093; -.
DR MANE-Select; ENST00000262375.11; ENSP00000262375.4; NM_005147.6; NP_005138.3.
DR UCSC; uc002cwk.4; human. [Q96EY1-1]
DR CTD; 9093; -.
DR DisGeNET; 9093; -.
DR GeneCards; DNAJA3; -.
DR HGNC; HGNC:11808; DNAJA3.
DR HPA; ENSG00000103423; Low tissue specificity.
DR MIM; 608382; gene.
DR neXtProt; NX_Q96EY1; -.
DR OpenTargets; ENSG00000103423; -.
DR PharmGKB; PA27410; -.
DR VEuPathDB; HostDB:ENSG00000103423; -.
DR eggNOG; KOG0715; Eukaryota.
DR GeneTree; ENSGT00940000155280; -.
DR HOGENOM; CLU_017633_0_5_1; -.
DR InParanoid; Q96EY1; -.
DR OMA; DLHCTVT; -.
DR PhylomeDB; Q96EY1; -.
DR TreeFam; TF105152; -.
DR PathwayCommons; Q96EY1; -.
DR SignaLink; Q96EY1; -.
DR BioGRID-ORCS; 9093; 700 hits in 1102 CRISPR screens.
DR ChiTaRS; DNAJA3; human.
DR EvolutionaryTrace; Q96EY1; -.
DR GeneWiki; DNAJA3; -.
DR GenomeRNAi; 9093; -.
DR Pharos; Q96EY1; Tbio.
DR PRO; PR:Q96EY1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96EY1; protein.
DR Bgee; ENSG00000103423; Expressed in gastrocnemius and 95 other tissues.
DR ExpressionAtlas; Q96EY1; baseline and differential.
DR Genevisible; Q96EY1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0030695; F:GTPase regulator activity; IEA:Ensembl.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0106137; F:IkappaB kinase complex binding; IDA:UniProtKB.
DR GO; GO:0005133; F:interferon-gamma receptor binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 1.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell membrane;
KW Chaperone; Cytoplasm; Membrane; Metal-binding; Methylation; Mitochondrion;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..480
FT /note="DnaJ homolog subfamily A member 3, mitochondrial"
FT /id="PRO_0000007256"
FT DOMAIN 93..158
FT /note="J"
FT REPEAT 236..243
FT /note="CXXCXGXG motif"
FT REPEAT 253..260
FT /note="CXXCXGXG motif"
FT REPEAT 275..282
FT /note="CXXCXGXG motif"
FT REPEAT 289..296
FT /note="CXXCXGXG motif"
FT ZN_FING 223..301
FT /note="CR-type"
FT REGION 443..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2CTT"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by CARM1"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99M87"
FT MOD_RES 238
FT /note="Omega-N-methylarginine; by CARM1"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 293
FT /note="Omega-N-methylarginine; by CARM1"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 3..186
FT /note="ARCSTRWLLVVVGTPRLPAISGRGARPPREGVVGAWLSRKLSVPAFASSLTS
FT CGPRALLTLRPGVSLTGTKHNPFICTASFHTSAPLAKEDYYQILGVPRNASQKEIKKAY
FT YQLAKKYHPDTNKDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGASGSQHS
FT YWKGGPTVDPEELF -> EPQAERPRLCVFPDLLRPPSAADIETWCQPY (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055728"
FT VAR_SEQ 448..453
FT /note="GSTMDS -> KRSTGN (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11679576,
FT ECO:0000303|PubMed:12097419, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007425"
FT VAR_SEQ 454..480
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11679576,
FT ECO:0000303|PubMed:12097419, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007426"
FT VARIANT 75
FT /note="N -> Y (in dbSNP:rs1139653)"
FT /evidence="ECO:0000269|PubMed:11679576,
FT ECO:0000269|PubMed:12097419, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027965"
FT MUTAGEN 121
FT /note="H->Q: Loss of modulation of apoptosis."
FT /evidence="ECO:0000269|PubMed:10411904"
FT CONFLICT 320
FT /note="M -> W (in Ref. 6; AAF66245)"
FT /evidence="ECO:0000305"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2DN9"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:2DN9"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2DN9"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6IWS"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:2DN9"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:2DN9"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:2CTT"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2CTT"
FT CONFLICT Q96EY1-3:33
FT /note="Y -> H (in Ref. 3; BAG58345)"
FT /evidence="ECO:0000305"
SQ 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
