DNAJC1

DNAJC1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CQQ, 2CQR
Identifiers
Aliases	DNAJC1, DNAJL1, ERdj1, HTJ1, MTJ1, DnaJ heat shock protein family (Hsp40) member C1
External IDs	MGI: 103268 HomoloGene: 7293 GeneCards: DNAJC1
Gene ontology Molecular function • DNA binding • ATPase activator activity • chaperone binding • protein binding Cellular component • integral component of membrane • organelle membrane • cytosol • plasma membrane • nuclear membrane • endoplasmic reticulum membrane • endoplasmic reticulum • membrane • nucleus • intracellular membrane-bounded organelle Biological process • negative regulation of proteolysis • protein folding • regulation of translation • regulation of protein secretion • positive regulation of ATPase activity Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	64215	13418
Ensembl	ENSG00000136770	ENSMUSG00000026740
UniProt	Q96KC8	Q61712
RefSeq (mRNA)	NM_022365	NM_001190817 NM_007869
RefSeq (protein)	NP_071760.2	NP_001177746.1 NP_031895.1
Location (UCSC)	Chr 10: 21.76 – 22 Mb	Chr 2: 18.2 – 18.39 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

DnaJ homolog subfamily C member 1 is a protein that in humans is encoded by the DNAJC1 gene.^[3]

Interactions

DNAJC1 has been shown to interact with Alpha 1-antichymotrypsin.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: DNAJC1 DnaJ (Hsp40) homolog, subfamily C, member 1".
4. Kroczynska B, Evangelista CM, Samant SS, Elguindi EC, Blond SY (2004). "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity". J. Biol. Chem. 279 (12): 11432–43. doi:10.1074/jbc.M310903200. PMC 1553221. PMID 14668352.

Further reading

• Kroczynska B, King-Simmons L, Alloza L, et al. (2006). "BIP co-chaperone MTJ1/ERDJ1 interacts with inter-alpha-trypsin inhibitor heavy chain 4.". Biochem. Biophys. Res. Commun. 338 (3): 1467–77. doi:10.1016/j.bbrc.2005.10.101. PMID 16271702.
• 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.
• Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature. 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Kroczynska B, Evangelista CM, Samant SS, et al. (2004). "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity.". J. Biol. Chem. 279 (12): 11432–43. doi:10.1074/jbc.M310903200. PMC 1553221. PMID 14668352.
• 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.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chevalier M, Rhee H, Elguindi EC, Blond SY (2000). "Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1.". J. Biol. Chem. 275 (26): 19620–7. doi:10.1074/jbc.M001333200. PMC 1534116. PMID 10777498.