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DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2)

 DNJA1_HUMAN             Reviewed;         397 AA.
P31689; Q5T7Q0; Q86TL9;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 191.
RecName: Full=DnaJ homolog subfamily A member 1;
AltName: Full=DnaJ protein homolog 2;
AltName: Full=HSDJ;
AltName: Full=Heat shock 40 kDa protein 4;
AltName: Full=Heat shock protein J2;
Short=HSJ-2;
AltName: Full=Human DnaJ protein 2;
Short=hDj-2;
Flags: Precursor;
Name=DNAJA1; Synonyms=DNAJ2, HDJ2, HSJ2, HSPF4;
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).
PubMed=8334161; DOI=10.1016/0167-4781(93)90104-L;
Oh S., Iwahori A., Kato S.;
"Human cDNA encoding DnaJ protein homologue.";
Biochim. Biophys. Acta 1174:114-116(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8334160; DOI=10.1016/0167-4781(93)90103-K;
Chellaiah A., Davis A., Mohanakumar T.;
"Cloning of a unique human homologue of the Escherichia coli DNAJ heat
shock protein.";
Biochim. Biophys. Acta 1174:111-113(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=15595953; DOI=10.1111/j.1365-2605.2004.00492.x;
Hu Y., Zhou Z., Huang X., Xu M., Lu L., Xu Z., Li J., Sha J.;
"Expression of a novel DnaJA1 alternative splicing in human testis and
sperm.";
Int. J. Androl. 27:343-349(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=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).
[8]
FUNCTION, INDUCTION BY HEAT, AND ISOPRENYLATION AT CYS-394.
PubMed=9192730; DOI=10.1093/oxfordjournals.jbchem.a021670;
Kanazawa M., Terada K., Kato S., Mori M.;
"HSDJ, a human homolog of DnaJ, is farnesylated and is involved in
protein import into mitochondria.";
J. Biochem. 121:890-895(1997).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
ISOPRENYLATION.
PubMed=10816573; DOI=10.1074/jbc.M002021200;
Terada K., Mori M.;
"Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones
of hsc70.";
J. Biol. Chem. 275:24728-24734(2000).
[10]
FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HSPA1B AND BAX,
ISOPRENYLATION AT CYS-394, AND MUTAGENESIS OF CYS-394.
PubMed=14752510; DOI=10.1038/sj.cdd.4401369;
Gotoh T., Terada K., Oyadomari S., Mori M.;
"hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced
apoptosis by inhibiting translocation of Bax to mitochondria.";
Cell Death Differ. 11:390-402(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, 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).
[23]
FUNCTION.
PubMed=24318877; DOI=10.1074/jbc.M113.521997;
Rauch J.N., Gestwicki J.E.;
"Binding of human nucleotide exchange factors to heat shock protein 70
(Hsp70) generates functionally distinct complexes in vitro.";
J. Biol. Chem. 289:1402-1414(2014).
[24]
INTERACTION WITH RNF207.
PubMed=25281747; DOI=10.1074/jbc.M114.592295;
Roder K., Werdich A.A., Li W., Liu M., Kim T.Y., Organ-Darling L.E.,
Moshal K.S., Hwang J.M., Lu Y., Choi B.R., MacRae C.A., Koren G.;
"RING finger protein RNF207, a novel regulator of cardiac
excitation.";
J. Biol. Chem. 289:33730-33740(2014).
[25]
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).
[26]
STRUCTURE BY NMR OF 1-67, AND FUNCTION.
PubMed=24512202; DOI=10.1021/bi401329a;
Stark J.L., Mehla K., Chaika N., Acton T.B., Xiao R., Singh P.K.,
Montelione G.T., Powers R.;
"Structure and function of human DnaJ homologue subfamily a member 1
(DNAJA1) and its relationship to pancreatic cancer.";
Biochemistry 53:1360-1372(2014).
-!- FUNCTION: Co-chaperone for HSPA8/Hsc70 (PubMed:10816573).
Stimulates ATP hydrolysis, but not the folding of unfolded
proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a
role in protein transport into mitochondria via its role as co-
chaperone. Functions as co-chaperone for HSPA1B and negatively
regulates the translocation of BAX from the cytosol to
mitochondria in response to cellular stress, thereby protecting
cells against apoptosis (PubMed:14752510). Promotes apoptosis in
response to cellular stress mediated by exposure to anisomycin or
UV (PubMed:24512202). {ECO:0000269|PubMed:10816573,
ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:24512202, ECO:0000269|PubMed:9192730}.
-!- SUBUNIT: Identified in a complex with HSPA1B and BAX
(PubMed:14752510). Interacts with RNF207 (PubMed:25281747).
{ECO:0000269|PubMed:14752510, ECO:0000269|PubMed:25281747}.
-!- INTERACTION:
Q9GZX7:AICDA; NbExp=6; IntAct=EBI-347834, EBI-3834328;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10816573};
Lipid-anchor {ECO:0000305|PubMed:10816573}. Cytoplasm
{ECO:0000269|PubMed:10816573}. Microsome {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000250}.
Note=Primarily associated with microsomes. A minor proportion is
associated with mitochondria (By similarity). Primarily
cytoplasmic. A minor proportion is associated with nuclei.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P31689-1; Sequence=Displayed;
Name=2; Synonyms=nDnaJA1;
IsoId=P31689-2; Sequence=VSP_046566;
-!- TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is highly expressed in
testis and lung, but detected at low levels in thymus, prostate,
colon and liver. {ECO:0000269|PubMed:10816573,
ECO:0000269|PubMed:15595953}.
-!- INDUCTION: Up-regulated by heat shock.
{ECO:0000269|PubMed:9192730}.
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EMBL; D13388; BAA02656.1; -; mRNA.
EMBL; L08069; AAC37517.1; -; mRNA.
EMBL; AY186741; AAO31694.1; -; mRNA.
EMBL; BT007292; AAP35956.1; -; mRNA.
EMBL; AK289623; BAF82312.1; -; mRNA.
EMBL; CH471071; EAW58525.1; -; Genomic_DNA.
EMBL; CH471071; EAW58526.1; -; Genomic_DNA.
EMBL; BC008182; AAH08182.1; -; mRNA.
CCDS; CCDS6533.1; -. [P31689-1]
PIR; S34630; S34630.
RefSeq; NP_001530.1; NM_001539.3. [P31689-1]
UniGene; Hs.445203; -.
UniGene; Hs.707338; -.
PDB; 2LO1; NMR; -; A=1-70.
PDB; 2M6Y; NMR; -; A=1-67.
PDBsum; 2LO1; -.
PDBsum; 2M6Y; -.
ProteinModelPortal; P31689; -.
SMR; P31689; -.
BioGrid; 109534; 160.
IntAct; P31689; 91.
MINT; MINT-5004184; -.
STRING; 9606.ENSP00000369127; -.
BindingDB; P31689; -.
ChEMBL; CHEMBL2189122; -.
iPTMnet; P31689; -.
PhosphoSitePlus; P31689; -.
SwissPalm; P31689; -.
BioMuta; DNAJA1; -.
DMDM; 1706474; -.
EPD; P31689; -.
PaxDb; P31689; -.
PeptideAtlas; P31689; -.
PRIDE; P31689; -.
DNASU; 3301; -.
Ensembl; ENST00000330899; ENSP00000369127; ENSG00000086061. [P31689-1]
GeneID; 3301; -.
KEGG; hsa:3301; -.
UCSC; uc003zsd.2; human. [P31689-1]
CTD; 3301; -.
DisGeNET; 3301; -.
EuPathDB; HostDB:ENSG00000086061.15; -.
GeneCards; DNAJA1; -.
H-InvDB; HIX0007975; -.
HGNC; HGNC:5229; DNAJA1.
HPA; HPA001306; -.
MIM; 602837; gene.
neXtProt; NX_P31689; -.
OpenTargets; ENSG00000086061; -.
PharmGKB; PA31536; -.
eggNOG; KOG0712; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00860000133716; -.
HOGENOM; HOG000226718; -.
HOVERGEN; HBG066727; -.
InParanoid; P31689; -.
KO; K09502; -.
OMA; CDGHGMK; -.
OrthoDB; EOG091G0CAC; -.
PhylomeDB; P31689; -.
TreeFam; TF105141; -.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
GeneWiki; DNAJA1; -.
GenomeRNAi; 3301; -.
PRO; PR:P31689; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000086061; -.
CleanEx; HS_DNAJA1; -.
Genevisible; P31689; HS.
GO; GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; IPI:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030957; F:Tat protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; IEA:Ensembl.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB.
GO; GO:0051223; P:regulation of protein transport; IDA:UniProtKB.
GO; GO:0009408; P:response to heat; IEA:InterPro.
GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:1901998; P:toxin transport; 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; 3.
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; Chaperone;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Lipoprotein;
Membrane; Metal-binding; Methylation; Microsome; Mitochondrion;
Nucleus; Phosphoprotein; Prenylation; Reference proteome; Repeat;
Zinc; Zinc-finger.
CHAIN 1 394 DnaJ homolog subfamily A member 1.
/FTId=PRO_0000071008.
PROPEP 395 397 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000393941.
DOMAIN 6 68 J.
REPEAT 134 141 CXXCXGXG motif.
REPEAT 150 157 CXXCXGXG motif.
REPEAT 177 184 CXXCXGXG motif.
REPEAT 193 200 CXXCXGXG motif.
ZN_FING 121 205 CR-type.
COMPBIAS 75 96 Gly-rich.
METAL 134 134 Zinc 1. {ECO:0000250}.
METAL 137 137 Zinc 1. {ECO:0000250}.
METAL 150 150 Zinc 2. {ECO:0000250}.
METAL 153 153 Zinc 2. {ECO:0000250}.
METAL 177 177 Zinc 2. {ECO:0000250}.
METAL 180 180 Zinc 2. {ECO:0000250}.
METAL 193 193 Zinc 1. {ECO:0000250}.
METAL 196 196 Zinc 1. {ECO:0000250}.
MOD_RES 66 66 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 381 381 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 394 394 Cysteine methyl ester. {ECO:0000305}.
LIPID 394 394 S-farnesyl cysteine.
{ECO:0000269|PubMed:14752510,
ECO:0000269|PubMed:9192730}.
VAR_SEQ 327 397 NFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFD
PNQERRRHYNGEAYEDDEHHPRGGVQCQTS -> SCNVL
(in isoform 2).
{ECO:0000303|PubMed:15595953}.
/FTId=VSP_046566.
MUTAGEN 394 394 C->S: Loss of farnesylation.
{ECO:0000269|PubMed:14752510}.
CONFLICT 274 274 Q -> H (in Ref. 1; BAA02656).
{ECO:0000305}.
HELIX 7 10 {ECO:0000244|PDB:2LO1}.
HELIX 19 33 {ECO:0000244|PDB:2LO1}.
HELIX 35 37 {ECO:0000244|PDB:2LO1}.
STRAND 39 41 {ECO:0000244|PDB:2LO1}.
HELIX 42 54 {ECO:0000244|PDB:2LO1}.
HELIX 58 64 {ECO:0000244|PDB:2LO1}.
TURN 65 67 {ECO:0000244|PDB:2LO1}.
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


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