HSC70: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co- chaperones. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with PACRG and TSC2. Interacts with BAG1. Interacts with SV40 VP1. Interacts with DNAJC7. Interacts with HERC5. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Constitutively synthesized. Ubiquitous. Belongs to the heat shock protein 70 family. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Nucleolus; Heat shock protein; Chaperone; RNA-binding
Chromosomal Location of Human Ortholog: 11q24.1
Cellular Component: cytosol; extracellular space; focal adhesion; intracellular; lysosomal lumen; lysosomal membrane; melanosome; membrane; myelin sheath; nucleolus; nucleoplasm; nucleus; plasma membrane; ribonucleoprotein complex; spliceosome; ubiquitin ligase complex
Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; protein binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: ATP metabolic process; axon guidance; cellular response to starvation; chaperone cofactor-dependent protein folding; gene expression; negative regulation of transcription, DNA-dependent; neurotransmitter secretion; nuclear mRNA splicing, via spliceosome; positive regulation of nuclear mRNA splicing, via spliceosome; post-Golgi vesicle-mediated transport; protein folding; protein refolding; protein targeting to lysosome; regulation of cell cycle; regulation of mRNA stability; regulation of protein complex assembly; regulation of protein stability; response to unfolded protein; RNA splicing; synaptic transmission; transcription, DNA-dependent; viral reproduction
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