HIP One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins. Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90. Interacts (via the C-terminus 303- 319 AA) with GRK5. Belongs to the FAM10 family. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold; Chaperone
Chromosomal Location of Human Ortholog: 15|15 E1
Cellular Component:  cytoplasm; cytosol; protein-containing complex
Molecular Function:  chaperone binding; dATP binding; Hsp70 protein binding; identical protein binding; protein dimerization activity; protein domain specific binding; protein-containing complex binding; unfolded protein binding
Biological Process:  chaperone cofactor-dependent protein refolding; negative regulation of protein refolding; protein homooligomerization; protein homotetramerization; response to bacterium
Reference #:  Q99L47 (UniProtKB)
Alt. Names/Synonyms: 1110007I03Rik; 3110002K08Rik; AW555194; F10A1; Fam10a1; Hip; HOP; Hsc70-interacting protein; Hsp70 interacting protein; HSPABP; HSPABP1; p48; PRO0786; Protein FAM10A1; Protein ST13 homolog; SNC6; St13; suppression of tumorigenicity 13
Gene Symbols: St13
Molecular weight: 41,656 Da
Basal Isoelectric point: 5.19  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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HIP

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene