ID:F10A1_HUMAN DESCRIPTION: RecName: Full=Hsc70-interacting protein; Short=Hip; AltName: Full=Aging-associated protein 2; AltName: Full=Progesterone receptor-associated p48 protein; AltName: Full=Protein FAM10A1; AltName: Full=Putative tumor suppressor ST13; AltName: Full=Renal carcinoma antigen NY-REN-33; AltName: Full=Suppression of tumorigenicity 13 protein; FUNCTION: 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 (By similarity). SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90 (By similarity). Interacts (via the C-terminus 303- 319 AA) with GRK5. INTERACTION: P02649:APOE; NbExp=3; IntAct=EBI-357285, EBI-1222467; P29474:NOS3; NbExp=3; IntAct=EBI-357285, EBI-1391623; P49768:PSEN1; NbExp=3; IntAct=EBI-357285, EBI-297277; SUBCELLULAR LOCATION: Cytoplasm (By similarity). SIMILARITY: Belongs to the FAM10 family. SIMILARITY: Contains 1 STI1 domain. SIMILARITY: Contains 3 TPR repeats.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P50502
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006457 protein folding GO:0051085 chaperone mediated protein folding requiring cofactor GO:0051260 protein homooligomerization GO:0051289 protein homotetramerization GO:0061084 negative regulation of protein refolding