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DNAJA1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2LO1, 2M6Y

Identifiers

Aliases

DNAJA1, DJ-2, DjA1, HDJ2, HSDJ, HSJ2, HSPF4, NEDD7, hDJ-2, HSJ-2, DnaJ heat shock protein family (Hsp40) member A1

External IDs

OMIM: 602837; MGI: 1270129; HomoloGene: 55588; GeneCards: DNAJA1; OMA:DNAJA1 - orthologs

Gene location (Human)
👁 Chromosome 9 (human)
Chr.	Chromosome 9 (human)^[1]
👁 Chromosome 9 (human) 👁 Genomic location for DNAJA1 👁 Genomic location for DNAJA1
Band	9p21.1	Start	33,025,273 bp^[1]
Band	9p21.1	End	33,039,907 bp^[1]

Gene location (Mouse)
👁 Chromosome 4 (mouse)
Chr.	Chromosome 4 (mouse)^[2]
👁 Chromosome 4 (mouse) 👁 Genomic location for DNAJA1 👁 Genomic location for DNAJA1
Band	4\|4 A5	Start	40,722,150 bp^[2]
Band	4\|4 A5	End	40,737,149 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

oocyte

bronchial epithelial cell

ganglionic eminence

amniotic fluid

mucosa of paranasal sinus

secondary oocyte

mucosa of sigmoid colon

ventricular zone

beta cell

stromal cell of endometrium

Top expressed in

genital tubercle

tail of embryo

morula

morula

facial motor nucleus

right kidney

ganglionic eminence

blastocyst

dentate gyrus of hippocampal formation granule cell

anterior horn of spinal cord

More reference expression data

BioGPS

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More reference expression data

Gene ontology
Molecular function	chaperone binding heat shock protein binding unfolded protein binding C3HC4-type RING finger domain binding metal ion binding low-density lipoprotein particle receptor binding Hsp70 protein binding protein binding G protein-coupled receptor binding ATP binding ubiquitin protein ligase binding Tat protein binding ATPase activator activity
Cellular component	cytoplasm membrane intracellular membrane-bounded organelle ubiquitin ligase complex mitochondrion cytoplasmic side of endoplasmic reticulum membrane endoplasmic reticulum perinuclear region of cytoplasm extracellular exosome nucleus microtubule cytoskeleton cytosol
Biological process	flagellated sperm motility androgen receptor signaling pathway regulation of protein transport negative regulation of apoptotic process response to heat toxin transport negative regulation of protein ubiquitination response to unfolded protein protein folding spermatogenesis positive regulation of apoptotic process protein localization to mitochondrion negative regulation of JUN kinase activity negative regulation of establishment of protein localization to mitochondrion negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway positive regulation of ATP-dependent activity
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


3301


15502

Ensembl


ENSG00000086061


ENSMUSG00000028410

UniProt


P31689


P63037

RefSeq (mRNA)


NM_001539 NM_001314039


NM_001164671 NM_001164672 NM_008298

RefSeq (protein)


NP_001300968 NP_001530


NP_001158143 NP_001158144 NP_032324

Location (UCSC)

Chr 9: 33.03 – 33.04 Mb

Chr 4: 40.72 – 40.74 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.^[5]^[6]^[7]

Interactions

[edit]

DNAJA1 has been shown to interact with PTTG1.^[8]

References

[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000086061 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028410 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Chellaiah A, Davis A, Mohanakumar T (August 1993). "Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein". Biochim Biophys Acta. 1174 (1): 111–3. doi:10.1016/0167-4781(93)90103-k. PMID 8334160.
^ Ohtsuka K, Hata M (January 2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress & Chaperones. 5 (2): 98–112. doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 12 July 2025). PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (link)
^ "Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1".
^ Pei L (January 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". J. Biol. Chem. 274 (5). UNITED STATES: 3151–8. doi:10.1074/jbc.274.5.3151. ISSN 0021-9258. PMID 9915854.

Oh S, Iwahori A, Kato S (1993). "Human cDNA encoding DnaJ protein homologue". Biochim. Biophys. Acta. 1174 (1): 114–6. doi:10.1016/0167-4781(93)90104-l. PMID 8334161.
Kanazawa M, Terada K, Kato S, Mori M (1997). "HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria". J. Biochem. 121 (5): 890–5. doi:10.1093/oxfordjournals.jbchem.a021670. PMID 9192730.
Davis AR, Alevy YG, Chellaiah A, et al. (1998). "Characterization of HDJ-2, a human 40 kD heat shock protein". Int. J. Biochem. Cell Biol. 30 (11): 1203–21. doi:10.1016/S1357-2725(98)00091-0. PMID 9839446.
Pei L (1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". J. Biol. Chem. 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. PMID 9915854.
Meacham GC, Lu Z, King S, et al. (1999). "The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis". EMBO J. 18 (6): 1492–505. doi:10.1093/emboj/18.6.1492. PMC 1171238. PMID 10075921.
Terada K, Mori M (2000). "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70". J. Biol. Chem. 275 (32): 24728–34. doi:10.1074/jbc.M002021200. PMID 10816573.
Jana NR, Tanaka M, Wang G, Nukina N (2000). "Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity". Hum. Mol. Genet. 9 (13): 2009–18. doi:10.1093/hmg/9.13.2009. PMID 10942430.
Bao YP, Cook LJ, O'Donovan D, et al. (2002). "Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy". J. Biol. Chem. 277 (14): 12263–9. doi:10.1074/jbc.M109633200. PMID 11796717.
Hernández MP, Chadli A, Toft DO (2002). "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor". J. Biol. Chem. 277 (14): 11873–81. doi:10.1074/jbc.M111445200. PMID 11809754.
Imai Y, Soda M, Hatakeyama S, 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 (1): 55–67. doi:10.1016/S1097-2765(02)00583-X. PMID 12150907.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Hanai R, Mashima K (2004). "Characterization of two isoforms of a human DnaJ homologue, HSJ2". Mol. Biol. Rep. 30 (3): 149–53. doi:10.1023/A:1024916223616. PMID 12974469. S2CID 24105834.
Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Marschang P, Brich J, Weeber EJ, 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 (9): 3782–93. doi:10.1128/MCB.24.9.3782-3793.2004. PMC 387731. PMID 15082773.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
Hu Y, Zhou Z, Huang X, et al. (2005). "Expression of a novel DnaJA1 alternative splicing in human testis and sperm". Int. J. Androl. 27 (6): 343–9. doi:10.1111/j.1365-2605.2004.00492.x. PMID 15595953.

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α₁ α₂ β ER TRAP1
Other	Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2

Protein targeting

Ubiquitin
(ubiquitylation)

E1 Ubiquitin-activating enzyme
- UBA1
- UBA2
- UBA3
- UBA5
- UBA6
- UBA7
- ATG7
- NAE1
- SAE1

E2 Ubiquitin-conjugating enzyme
- A
- B
- C
- D1
- D2
- D3
- E1
- E2
- E3
- G1
- G2
- H
- I
- J1
- J2
- K
- L1
- L2
- L3
- L4
- L6
- M
- N
- O
- Q1
- Q2
- R1 (CDC34)
- R2
- S
- V1
- V2
- Z

E3 Ubiquitin ligase
- VHL
- Cullin
- CBL
- MDM2
- FANCL
- UBR1

Ubiquitin-like proteins
(UBL)

SUMO protein (SUMOylation)	E1 SUMO-activating enzyme SAE1 SAE2 E2 SUMO-conjugating enzyme UBC9 E3 SUMO ligase PIAS1 PIAS2 PIAS3 PIAS4
Other	ISG15 URM1 UFM1 NEDD8 (neddylation) FAT10 ATG8 ATG12 FUB1 MUB UBL5 Prokaryotic ubiquitin-like protein

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Interactions

References

Further reading