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: RNA-binding; Heat shock protein; Chaperone; Nucleolus
Cellular Component: extracellular space; neuron projection; focal adhesion; protein complex; terminal button; cytosol; ribonucleoprotein complex; spliceosome; synaptic vesicle; cell soma; membrane; cytoplasm; plasma membrane; nucleolus; melanosome; intracellular; nucleus; myelin sheath; ubiquitin ligase complex
Molecular Function: protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; unfolded protein binding; ATPase activity; ATPase activity, coupled; ADP binding; ATP binding; receptor binding
Biological Process: positive regulation of nuclear mRNA splicing, via spliceosome; protein folding; transcription, DNA-dependent; chaperone cofactor-dependent protein folding; regulation of cell cycle; RNA splicing; protein refolding; mRNA processing; negative regulation of transcription, DNA-dependent
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