Hsc70-interacting protein (ST13)
The protein contains 369 amino acids for an estimated molecular weight of 41332 Da.
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). (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs710193 |
Biological Process
Chaperone cofactor-dependent protein refolding
Chaperone cofactor-dependent protein refolding
Chaperone-mediated protein folding
Negative regulation of protein refolding
Protein folding
Protein homooligomerization
Protein homotetramerization
Protein-containing complex assembly
Response to bacterium
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Protein complex
Protein-containing complex
Molecular Function
Chaperone binding
DATP binding
Heat shock protein binding
Hsp70 protein binding
Identical protein binding
Protein complex binding
Protein dimerization activity
Protein domain specific binding
Protein-containing complex binding
Protein-macromolecule adaptor activity
Unfolded protein binding
The reference OMIM entry for this protein is 606796
Suppression of tumorigenicity 13; st13
P48
Hsc70-interacting protein; hip
DESCRIPTION
ST13 is an abundant, highly conserved protein that binds the major cytosolic chaperones heat-shock protein 70-kD (HSP70; see 140550) and HSP90 (see 140571) during an intermediate stage of steroid receptor assembly, but is absent from the mature receptor complex.CLONING
Prapapanich et al. (1996) isolated a 48-kD protein that transiently associates with progesterone receptor (607311) during cell-free assembly in rabbit reticulocyte lysate. Using an antibody developed against the purified protein, Prapapanich et al. (1996) cloned ST13 cDNA from a HeLa cell cDNA library. The deduced 369-amino acid protein has a calculated molecular mass of approximately 41 kD and an apparent molecular mass of 48 kD by SDS-PAGE. By Northern blot analysis, Prapapanich et al. (1996) identified 4 ST13 mRNAs, ranging in size from about 1.3 kb to 3.2 kb, with expression in all tissues examined.GENE FUNCTION
Using a yeast 2-hybrid assay, Hohfeld et al. (1995) showed that rat Hip bound Hsc70 (HSPA8; 600816). One Hip oligomer bound the ATPase domains of at least 2 Hsc70 molecules, and binding was dependent on activation of the Hsc70 ATPase by Hsp40 (DNAJB1; 604572). Hip stabilized the ADP-bound form of Hsc70, which had a high affinity for a test protein substrate. Hohfeld et al. (1995) concluded that HIP contributes to interactions of HSC70 with target proteins through its own chaperone activity. Prapapanich et al. (1996) coimmunoprecipitated progesterone receptor assembly complexes with in vitro translated ST13. By Western blot analysis, they identified HSP70 and HSP90 in these complexes. Using subtractive hybridization between cDNA of normal mucosal tissues and mRNA of colorectal carcinoma tissues, Cao et al. (1997) found downregulated expression of ST13 in the cancer tissues. Using a yeast expression system, Nelson et al. (2004) found that human HIP enhanced hormone-dependent activation of a reporter gene by rat glucocorticoid receptor (GCCR; 138040). HIP promoted functional maturation of Gccr by enhancing formation of its ligand-binding domain. HIP did not affect the steady-state levels of Gccr protein, and its activity did not require yeast Hsp70 proteins. N-terminal truncation of HIP reduced its ability to enhance Gccr signaling, likely due to loss of HIP homooligomerization. HOP (STIP1; 605063) also appeared to have an HSP70-independent role in GCCR maturation. Polyglutamine disorders, such as spinal and bulbar muscular atrophy (SBMA, or SMAX1; 313200) and Huntington disease (143100), are caused by an expansion in the glutamine trinucleotide (CAG) repeat in the affected genes, resulting in mutant proteins that aggregate into insoluble inclusions within affected neurons. Howarth et al. (2009) showed that overexpression of human HIP significantly reduced inclusion formation in an in vitro mouse model of SBMA and in a rat primary neuronal model of polyglutamine disease. The activity of denatured luciferase, a measure of protein refolding, was not increased in the presence of HIP alone, but it was increased when HIP was coexpressed with HSP70 or HSC70. Howarth et al. (2009) concluded that HIP may prevent inclusion formation by facilitating the constitutive HSC70 refolding cycle and possibly by preventing aggregation.MAPPING
Zhang et al. (1998) mapped the ST13 gene to chromosome 22q13 by fluorescence in situ hybridization. They noted that colorectal, breast, and ovarian carcinomas frequently show loss of h ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for ST13
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606796 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed