DNJA1_HUMAN
ID DNJA1_HUMAN Reviewed; 397 AA.
AC P31689; Q5T7Q0; Q86TL9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=DnaJ homolog subfamily A member 1;
DE AltName: Full=DnaJ protein homolog 2;
DE AltName: Full=HSDJ;
DE AltName: Full=Heat shock 40 kDa protein 4;
DE AltName: Full=Heat shock protein J2;
DE Short=HSJ-2;
DE AltName: Full=Human DnaJ protein 2;
DE Short=hDj-2;
DE Flags: Precursor;
GN Name=DNAJA1; Synonyms=DNAJ2, HDJ2, HSJ2, HSPF4;
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).
RX PubMed=8334161; DOI=10.1016/0167-4781(93)90104-l;
RA Oh S., Iwahori A., Kato S.;
RT "Human cDNA encoding DnaJ protein homologue.";
RL Biochim. Biophys. Acta 1174:114-116(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8334160; DOI=10.1016/0167-4781(93)90103-k;
RA Chellaiah A., Davis A., Mohanakumar T.;
RT "Cloning of a unique human homologue of the Escherichia coli DNAJ heat
RT shock protein.";
RL Biochim. Biophys. Acta 1174:111-113(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15595953; DOI=10.1111/j.1365-2605.2004.00492.x;
RA Hu Y., Zhou Z., Huang X., Xu M., Lu L., Xu Z., Li J., Sha J.;
RT "Expression of a novel DnaJA1 alternative splicing in human testis and
RT sperm.";
RL Int. J. Androl. 27:343-349(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [8]
RP FUNCTION, INDUCTION BY HEAT, AND ISOPRENYLATION AT CYS-394.
RX PubMed=9192730; DOI=10.1093/oxfordjournals.jbchem.a021670;
RA Kanazawa M., Terada K., Kato S., Mori M.;
RT "HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein
RT import into mitochondria.";
RL J. Biochem. 121:890-895(1997).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ISOPRENYLATION.
RX PubMed=10816573; DOI=10.1074/jbc.m002021200;
RA Terada K., Mori M.;
RT "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of
RT hsc70.";
RL J. Biol. Chem. 275:24728-24734(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HSPA1B AND BAX,
RP ISOPRENYLATION AT CYS-394, AND MUTAGENESIS OF CYS-394.
RX PubMed=14752510; DOI=10.1038/sj.cdd.4401369;
RA Gotoh T., Terada K., Oyadomari S., Mori M.;
RT "hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced
RT apoptosis by inhibiting translocation of Bax to mitochondria.";
RL Cell Death Differ. 11:390-402(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
RP IDENTIFICATION BY 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 [24]
RP FUNCTION.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [25]
RP INTERACTION WITH RNF207.
RX PubMed=25281747; DOI=10.1074/jbc.m114.592295;
RA Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
RA Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
RT "RING finger protein RNF207, a novel regulator of cardiac excitation.";
RL J. Biol. Chem. 289:33730-33740(2014).
RN [26]
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 [27]
RP STRUCTURE BY NMR OF 1-67, AND FUNCTION.
RX PubMed=24512202; DOI=10.1021/bi401329a;
RA Stark J.L., Mehla K., Chaika N., Acton T.B., Xiao R., Singh P.K.,
RA Montelione G.T., Powers R.;
RT "Structure and function of human DnaJ homologue subfamily a member 1
RT (DNAJA1) and its relationship to pancreatic cancer.";
RL Biochemistry 53:1360-1372(2014).
CC -!- FUNCTION: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates
CC ATP hydrolysis, but not the folding of unfolded proteins mediated by
CC HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport
CC into mitochondria via its role as co-chaperone. Functions as co-
CC chaperone for HSPA1B and negatively regulates the translocation of BAX
CC from the cytosol to mitochondria in response to cellular stress,
CC thereby protecting cells against apoptosis (PubMed:14752510). Promotes
CC apoptosis in response to cellular stress mediated by exposure to
CC anisomycin or UV (PubMed:24512202). {ECO:0000269|PubMed:10816573,
CC ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877,
CC ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}.
CC -!- SUBUNIT: Identified in a complex with HSPA1B and BAX (PubMed:14752510).
CC Interacts with RNF207 (PubMed:25281747). {ECO:0000269|PubMed:14752510,
CC ECO:0000269|PubMed:25281747}.
CC -!- INTERACTION:
CC P31689; Q9GZX7: AICDA; NbExp=6; IntAct=EBI-347834, EBI-3834328;
CC P31689; P42858: HTT; NbExp=17; IntAct=EBI-347834, EBI-466029;
CC P31689; O60260-5: PRKN; NbExp=6; IntAct=EBI-347834, EBI-21251460;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10816573}; Lipid-
CC anchor {ECO:0000305|PubMed:10816573}. Cytoplasm
CC {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000250}.
CC Note=Primarily associated with microsomes. A minor proportion is
CC associated with mitochondria (By similarity). Primarily cytoplasmic. A
CC minor proportion is associated with nuclei. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31689-1; Sequence=Displayed;
CC Name=2; Synonyms=nDnaJA1;
CC IsoId=P31689-2; Sequence=VSP_046566;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is highly expressed in testis
CC and lung, but detected at low levels in thymus, prostate, colon and
CC liver. {ECO:0000269|PubMed:10816573, ECO:0000269|PubMed:15595953}.
CC -!- INDUCTION: Up-regulated by heat shock. {ECO:0000269|PubMed:9192730}.
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DR EMBL; D13388; BAA02656.1; -; mRNA.
DR EMBL; L08069; AAC37517.1; -; mRNA.
DR EMBL; AY186741; AAO31694.1; -; mRNA.
DR EMBL; BT007292; AAP35956.1; -; mRNA.
DR EMBL; AK289623; BAF82312.1; -; mRNA.
DR EMBL; CH471071; EAW58525.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58526.1; -; Genomic_DNA.
DR EMBL; BC008182; AAH08182.1; -; mRNA.
DR CCDS; CCDS6533.1; -. [P31689-1]
DR PIR; S34630; S34630.
DR RefSeq; NP_001530.1; NM_001539.3. [P31689-1]
DR PDB; 2LO1; NMR; -; A=1-70.
DR PDB; 2M6Y; NMR; -; A=1-67.
DR PDB; 6E8M; X-ray; 1.61 A; B=375-387.
DR PDBsum; 2LO1; -.
DR PDBsum; 2M6Y; -.
DR PDBsum; 6E8M; -.
DR AlphaFoldDB; P31689; -.
DR BMRB; P31689; -.
DR SMR; P31689; -.
DR BioGRID; 109534; 375.
DR IntAct; P31689; 165.
DR MINT; P31689; -.
DR STRING; 9606.ENSP00000369127; -.
DR BindingDB; P31689; -.
DR ChEMBL; CHEMBL2189122; -.
DR GlyGen; P31689; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P31689; -.
DR MetOSite; P31689; -.
DR PhosphoSitePlus; P31689; -.
DR SwissPalm; P31689; -.
DR BioMuta; DNAJA1; -.
DR DMDM; 1706474; -.
DR EPD; P31689; -.
DR jPOST; P31689; -.
DR MassIVE; P31689; -.
DR MaxQB; P31689; -.
DR PaxDb; P31689; -.
DR PeptideAtlas; P31689; -.
DR PRIDE; P31689; -.
DR ProteomicsDB; 54799; -. [P31689-1]
DR Antibodypedia; 675; 294 antibodies from 32 providers.
DR DNASU; 3301; -.
DR Ensembl; ENST00000330899.5; ENSP00000369127.3; ENSG00000086061.16. [P31689-1]
DR GeneID; 3301; -.
DR KEGG; hsa:3301; -.
DR MANE-Select; ENST00000330899.5; ENSP00000369127.3; NM_001539.4; NP_001530.1.
DR UCSC; uc003zsd.2; human. [P31689-1]
DR CTD; 3301; -.
DR DisGeNET; 3301; -.
DR GeneCards; DNAJA1; -.
DR HGNC; HGNC:5229; DNAJA1.
DR HPA; ENSG00000086061; Low tissue specificity.
DR MIM; 602837; gene.
DR neXtProt; NX_P31689; -.
DR OpenTargets; ENSG00000086061; -.
DR PharmGKB; PA31536; -.
DR VEuPathDB; HostDB:ENSG00000086061; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000153558; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P31689; -.
DR OMA; GMSAFNG; -.
DR OrthoDB; 1012379at2759; -.
DR PhylomeDB; P31689; -.
DR TreeFam; TF105141; -.
DR PathwayCommons; P31689; -.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR SignaLink; P31689; -.
DR BioGRID-ORCS; 3301; 252 hits in 1075 CRISPR screens.
DR ChiTaRS; DNAJA1; human.
DR GeneWiki; DNAJA1; -.
DR GenomeRNAi; 3301; -.
DR Pharos; P31689; Tchem.
DR PRO; PR:P31689; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P31689; protein.
DR Bgee; ENSG00000086061; Expressed in oocyte and 212 other tissues.
DR Genevisible; P31689; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030957; F:Tat protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
DR GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0051223; P:regulation of protein transport; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; 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; IPR044713; DNJA1/2-like.
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; PTHR43888; PTHR43888; 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; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
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; Chaperone; Cytoplasm;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding; Methylation;
KW Microsome; Mitochondrion; Nucleus; Phosphoprotein; Prenylation;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..394
FT /note="DnaJ homolog subfamily A member 1"
FT /id="PRO_0000071008"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000393941"
FT DOMAIN 6..68
FT /note="J"
FT REPEAT 134..141
FT /note="CXXCXGXG motif"
FT REPEAT 150..157
FT /note="CXXCXGXG motif"
FT REPEAT 177..184
FT /note="CXXCXGXG motif"
FT REPEAT 193..200
FT /note="CXXCXGXG motif"
FT ZN_FING 121..205
FT /note="CR-type"
FT REGION 352..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 394
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 394
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:14752510,
FT ECO:0000269|PubMed:9192730"
FT VAR_SEQ 327..397
FT /note="NFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNG
FT EAYEDDEHHPRGGVQCQTS -> SCNVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15595953"
FT /id="VSP_046566"
FT MUTAGEN 394
FT /note="C->S: Loss of farnesylation."
FT /evidence="ECO:0000269|PubMed:14752510"
FT CONFLICT 274
FT /note="Q -> H (in Ref. 1; BAA02656)"
FT /evidence="ECO:0000305"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:2LO1"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:2LO1"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2LO1"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2LO1"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:2LO1"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2LO1"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2LO1"
SQ SEQUENCE 397 AA; 44868 MW; A899C06F6BB32780 CRC64;
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLSDAKK
RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR ERRGKNVVHQ LSVTLEDLYN
GATRKLALQK NVICDKCEGR GGKKGAVECC PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC
QGHGERISPK DRCKSCNGRK IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII
IVLDQKDHAV FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI
KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK EVEETDEMDQ
VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS
