Search by BoMiProt ID - Bomi5232


Primary Information

BoMiProt ID Bomi5232
Protein Name DnaJ homolog subfamily B member 6/MRJ
Organism Bos taurus
Uniprot IDQ0III6
Milk FractionExosomes
Ref Sequence ID NP_776957.2
Aminoacid Length 242
Molecular Weight 26944
FASTA Sequence Download
Gene Name DNAJB6
Gene ID 282215
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells  highest expression in brain and retina and lower levels observed in testis, spleen, heart, liver and kidney.
Protein Function MRJ (DNAJB6), a member of the heat shock protein 40 family, acts as a molecular chaperone for a wide range of cellular processes. 
Biochemical Properties Mammalian relative of DnaJ (MRJ/DNAJB6) is an Hsp40 family member. The Hsp40 family can be categorized into three major types (I, II, and III), all of which share the ∼70-amino acid J-domain.In type-I Hsp40 proteins, the J-domain is at the N-terminus, followed by the glycine/phenylalanine (G/F)-rich region, the zinc finger domain, and the peptide-binding domain in the C-terminus. Type-II is similar to type-I but lacks a zinc finger domain. Type-III members contain only the J-domain, whose location differs between members.
PTMs Omega-N-methylation at Arginine
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
na
Predicted Disorder Regions 77-96, 238-242
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments  MRJ mutations are linked to human diseases, such as muscular dystrophy and neurodegenerative diseases. 
Bibliography 1.Chuang JZ, Zhou H, Zhu M, Li SH, Li XJ, Sung CH. Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently. J Biol Chem. 2002 May 31;277(22):19831-8. doi: 10.1074/jbc.M109613200. Epub 2002 Mar 14. PMID: 11896048. 2.Ko SH, Huang LM, Tarn WY. The Host Heat Shock Protein MRJ/DNAJB6 Modulates Virus Infection. Front Microbiol. 2019 Dec 11;10:2885. doi: 10.3389/fmicb.2019.02885. PMID: 31921062; PMCID: PMC6917656. 3.Heat shock protein 40: structural studies and their functional implications.Li J, Qian X, Sha B.Protein Pept Lett. 2009; 16(6):606-12. 4.The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones.Qiu XB, Shao YM, Miao S, Wang L.Cell Mol Life Sci. 2006 Nov; 63(22):2560-70.