HUMAN:DNJA1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	DNAJA1 (synonyms: DNAJ2, HDJ2, HSJ2, HSPF4)
Protein Name(s)	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
External Links
UniProt	P31689
EMBL	D13388 L08069 AY186741 BT007292 AK289623 CH471071 CH471071 BC008182
CCDS	CCDS6533.1
PIR	S34630
RefSeq	NP_001530.1
UniGene	Hs.445203
PDB	2LO1 2M6Y
PDBsum	2LO1 2M6Y
ProteinModelPortal	P31689
SMR	P31689
BioGrid	109534
IntAct	P31689
MINT	MINT-5004184
STRING	9606.ENSP00000369127
BindingDB	P31689
ChEMBL	CHEMBL2189122
PhosphoSite	P31689
DMDM	1706474
MaxQB	P31689
PaxDb	P31689
PeptideAtlas	P31689
PRIDE	P31689
DNASU	3301
Ensembl	ENST00000330899
GeneID	3301
KEGG	hsa:3301
UCSC	uc003zsd.1 uc003zse.1
CTD	3301
GeneCards	GC09P033025
H-InvDB	HIX0007975
HGNC	HGNC:5229
HPA	HPA001306
MIM	602837
neXtProt	NX_P31689
PharmGKB	PA31536
eggNOG	COG0484
GeneTree	ENSGT00490000043321
HOGENOM	HOG000226718
HOVERGEN	HBG066727
InParanoid	P31689
KO	K09502
OMA	VLDQKDN
OrthoDB	EOG7XM2XK
PhylomeDB	P31689
TreeFam	TF105141
GeneWiki	DNAJA1
GenomeRNAi	3301
NextBio	13099
PRO	PR:P31689
Proteomes	UP000005640
Bgee	P31689
CleanEx	HS_DNAJA1
ExpressionAtlas	P31689
Genevestigator	P31689
GO	GO:0098554 GO:0005829 GO:0070062 GO:0016020 GO:0005739 GO:0005634 GO:0048471 GO:0005524 GO:0051087 GO:0001664 GO:0030544 GO:0050750 GO:0046872 GO:0031625 GO:0030521 GO:0042769 GO:0043066 GO:0043508 GO:0031397 GO:0043065 GO:0006457 GO:0070585 GO:0051223 GO:0009408 GO:0006986 GO:0030317 GO:0007283
Gene3D	1.10.287.110 2.10.230.10
HAMAP	MF_01152
InterPro	IPR012724 IPR002939 IPR001623 IPR018253 IPR008971 IPR001305
Pfam	PF01556 PF00226 PF00684
PRINTS	PR00625
SMART	SM00271
SUPFAM	SSF46565 SSF49493 SSF57938
PROSITE	PS00636 PS50076 PS51188

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0030957	Tat protein binding	PMID:14752510^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07813	F	has_input:(UniProtKB:Q07812)	Seeded From UniProt	complete
involved_in	GO:1903748	negative regulation of establishment of protein localization to mitochondrion	PMID:14752510^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:1905259) has_regulation_target:(UniProtKB:Q07812)	Seeded From UniProt	complete
involved_in	GO:1905259	negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway	PMID:14752510^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0000235)	Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:21231916^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DMV9	F		Seeded From UniProt	complete
enables	GO:0001671	ATPase activator activity	PMID:24318877^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0055131	C3HC4-type RING finger domain binding	PMID:25281747^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6ZRF8	F		Seeded From UniProt	complete
enables	GO:0001664	G protein-coupled receptor binding	PMID:12150907^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O15354	F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:12150907^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60260	F		Seeded From UniProt	complete
involved_in	GO:0051223	regulation of protein transport	PMID:14752510^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030544	Hsp70 protein binding	PMID:14752510^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:14752510^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0070585	protein localization to mitochondrion	PMID:14752510^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:14752510^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043508	negative regulation of JUN kinase activity	PMID:24512202^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:24512202^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031397	negative regulation of protein ubiquitination	PMID:12150907^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:O15354)	Seeded From UniProt	complete
colocalizes_with	GO:0000151	ubiquitin ligase complex	PMID:12150907^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:21231916^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P17066	F		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:21231916^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DMV8	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:21231916^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21231916^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001531327 PomBase:SPBC1734.11 RGD:71001 SGD:S000005008 TAIR:locus:505006628 UniProtKB:O60884 UniProtKB:P31689 UniProtKB:Q8WW22 UniProtKB:Q94AW8	C		Seeded From UniProt	complete
enables	GO:0050750	low-density lipoprotein particle receptor binding	PMID:15082773^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0015630	microtubule cytoskeleton	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032781	positive regulation of ATPase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0001671	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012724	F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008971 InterPro:IPR012724	P		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012724	P		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001305	F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001305 InterPro:IPR008971 InterPro:IPR012724	F		Seeded From UniProt	complete
part_of	GO:0098554	cytoplasmic side of endoplasmic reticulum membrane	PMID:12150907^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:8334160^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:8334160^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-3371590 Reactome:R-HSA-3371503 Reactome:R-HSA-3371422	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0492 UniProtKB-SubCell:SL-0166	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 Gotoh, T et al. (2004) hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ. 11 390-402 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Hageman, J et al. (2011) The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem. J. 435 127-42 PubMed GONUTS page
↑ Rauch, JN & Gestwicki, JE (2014) Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J. Biol. Chem. 289 1402-14 PubMed GONUTS page
↑ Roder, K et al. (2014) RING finger protein RNF207, a novel regulator of cardiac excitation. J. Biol. Chem. 289 33730-40 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 PubMed GONUTS page
↑ ^6.0 ^6.1 Stark, JL et al. (2014) Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer. Biochemistry 53 1360-72 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Marschang, P et al. (2004) Normal development and fertility of knockout mice lacking the tumor suppressor gene LRP1b suggest functional compensation by LRP1. Mol. Cell. Biol. 24 3782-93 PubMed GONUTS page
↑ ^12.0 ^12.1 Chellaiah, A et al. (1993) Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein. Biochim. Biophys. Acta 1174 111-3 PubMed GONUTS page

[PMID:14752510-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 Gotoh, T et al. (2004) hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ. 11 390-402 PubMed GONUTS page

[PMID:21231916-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Hageman, J et al. (2011) The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem. J. 435 127-42 PubMed GONUTS page

[PMID:24318877-3] Rauch, JN & Gestwicki, JE (2014) Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J. Biol. Chem. 289 1402-14 PubMed GONUTS page

[PMID:25281747-4] Roder, K et al. (2014) RING finger protein RNF207, a novel regulator of cardiac excitation. J. Biol. Chem. 289 33730-40 PubMed GONUTS page

[PMID:12150907-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 PubMed GONUTS page

[PMID:24512202-6] 6.0 ^6.1 Stark, JL et al. (2014) Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer. Biochemistry 53 1360-72 PubMed GONUTS page

[PMID:19946888-7] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19056867-8] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-9] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:21873635-10] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:15082773-11] Marschang, P et al. (2004) Normal development and fertility of knockout mice lacking the tumor suppressor gene LRP1b suggest functional compensation by LRP1. Mol. Cell. Biol. 24 3782-93 PubMed GONUTS page

[PMID:8334160-12] 12.0 ^12.1 Chellaiah, A et al. (1993) Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein. Biochim. Biophys. Acta 1174 111-3 PubMed GONUTS page

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HUMAN:DNJA1

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