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 27-MAR-2024, entry version 208. 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; P08581: MET; NbExp=4; IntAct=EBI-356767, EBI-1039152; 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; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-3952284, EBI-745689; CC Q96EY1-2; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-3952284, EBI-739879; 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="https://atlasgeneticsoncology.org/gene/40342/DNAJA3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7X89; NMR; -; A=89-159. DR PDBsum; 2CTT; -. DR PDBsum; 2DN9; -. DR PDBsum; 6IWS; -. DR PDBsum; 7X89; -. DR AlphaFoldDB; Q96EY1; -. DR SMR; Q96EY1; -. DR BioGRID; 114547; 373. DR DIP; DIP-33870N; -. DR IntAct; Q96EY1; 143. 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 SwissPalm; Q96EY1; -. DR BioMuta; DNAJA3; -. DR DMDM; 311033374; -. DR EPD; Q96EY1; -. DR jPOST; Q96EY1; -. DR MassIVE; Q96EY1; -. DR MaxQB; Q96EY1; -. DR PaxDb; 9606-ENSP00000262375; -. DR PeptideAtlas; Q96EY1; -. DR ProteomicsDB; 17904; -. DR ProteomicsDB; 76466; -. [Q96EY1-1] DR ProteomicsDB; 76467; -. [Q96EY1-2] DR Pumba; Q96EY1; -. DR Antibodypedia; 24319; 312 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 AGR; HGNC:11808; -. 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; CPECAGD; -. DR OrthoDB; 276132at2759; -. DR PhylomeDB; Q96EY1; -. DR TreeFam; TF105152; -. DR PathwayCommons; Q96EY1; -. DR SignaLink; Q96EY1; -. DR BioGRID-ORCS; 9093; 730 hits in 1179 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 97 other cell types or tissues. DR ExpressionAtlas; Q96EY1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IMP: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:HPA. 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: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:0005133; F:type II interferon receptor binding; IDA: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:0043124; P:negative regulation of canonical NF-kappaB signal transduction; 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: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:0060336; P:negative regulation of type II interferon-mediated signaling pathway; 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 type II interferon; 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; cd10747; DnaJ_C; 1. DR CDD; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1. DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2. 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 PANTHER; PTHR44145; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1. DR PANTHER; PTHR44145:SF3; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1. 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; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51188; ZF_CR; 1. DR Genevisible; Q96EY1; HS. 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 //