DNAJB1

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DNAJB1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDNAJB1, HSPF1, Hdj1, Hsp40, RSPH16B, Sis1, DnaJ heat shock protein family (Hsp40) member B1
External IDsOMIM: 604572 MGI: 1931874 HomoloGene: 55957 GeneCards: DNAJB1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001313964
NM_001300914
NM_006145

NM_018808
NM_001308227

RefSeq (protein)

NP_001287843
NP_001300893
NP_006136

NP_001295156
NP_061278

Location (UCSC)Chr 19: 14.51 – 14.56 MbChr 8: 84.33 – 84.34 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.[5][6][7]

A fusion protein of DNAJB1 and PRKACA drives fibrolemallar hepatocellular carcinoma, a type of rare liver cancer.[8]

Interactions

DNAJB1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000132002 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005483 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hata M, Okumura K, Seto M, Ohtsuka K (December 1996). "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2". Genomics. 38 (3): 446–449. doi:10.1006/geno.1996.0653. PMID 8975727.
  6. ^ Ohtsuka K (November 1993). "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ". Biochemical and Biophysical Research Communications. 197 (1): 235–240. doi:10.1006/bbrc.1993.2466. PMID 8250930.
  7. ^ "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".
  8. ^ Neumayer C, Ng D, Jiang CS, Qureshi A, Lalazar G, Vaughan R, et al. (January 2023). "Oncogenic Addiction of Fibrolamellar Hepatocellular Carcinoma to the Fusion Kinase DNAJB1-PRKACA". Clinical Cancer Research. 29 (1): 271–278. doi:10.1158/1078-0432.CCR-22-1851. PMC 9811160. PMID 36302174.
  9. ^ Oh WK, Song J (August 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells. 16 (1): 84–91. doi:10.1016/S1016-8478(23)13770-8. PMID 14503850.
  10. ^ Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, et al. (June 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Molecular and Cellular Biology. 19 (6): 4535–4545. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.

Further reading