ST13

ST13

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1UZS

Identifiers

Aliases

ST13, AAG2, FAM10A1, FAM10A4, HIP, HOP, HSPABP, HSPABP1, P48, PRO0786, SNC6, ST13 Hsp70 interacting protein

External IDs

OMIM: 606796; MGI: 1917606; HomoloGene: 2921; GeneCards: ST13; OMA:ST13 - orthologs

Gene location (Human)

Chr.	Chromosome 22 (human)^[1]

Band	22q13.2	Start	40,824,535 bp^[1]
Band	22q13.2	End	40,856,639 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 E1	Start	81,247,870 bp^[2]
Band	15\|15 E1	End	81,284,278 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

ganglionic eminence

stromal cell of endometrium

canal of the cervix

gallbladder

right adrenal gland

optic nerve

left adrenal gland

gastric mucosa

popliteal artery

Top expressed in

pineal gland

retinal pigment epithelium

yolk sac

abdominal wall

lens

dorsomedial hypothalamic nucleus

white adipose tissue

left lobe of liver

habenula

medial ganglionic eminence

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	dATP binding unfolded protein binding protein-containing complex binding Hsp70 protein binding protein-macromolecule adaptor activity chaperone binding protein binding protein domain specific binding identical protein binding protein dimerization activity
Cellular component	extracellular exosome cytoplasm cytosol protein-containing complex
Biological process	protein homooligomerization protein folding negative regulation of protein refolding response to bacterium chaperone cofactor-dependent protein refolding protein homotetramerization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


6767


70356

Ensembl


ENSG00000100380


ENSMUSG00000022403

UniProt


P50502


Q99L47

RefSeq (mRNA)


NM_003932 NM_001278589


NM_133726

RefSeq (protein)


NP_001265518 NP_003923


NP_598487

Location (UCSC)

Chr 22: 40.82 – 40.86 Mb

Chr 15: 81.25 – 81.28 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Hsc70-interacting protein also known as suppression of tumorigenicity 13 (ST13) is a protein that in humans is encoded by the ST13 gene.^[5]^[6]^[7]

Function

The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90. This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of this gene is reported to be downregulated in colorectal carcinoma tissue suggesting that is a candidate tumor suppressor gene.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100380 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022403 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Zhang Y, Cai X, Schlegelberger B, Zheng S (Mar 1999). "Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24→q25 by in situ hybridization". Cytogenet Cell Genet. 83 (1–2): 56–7. doi:10.1159/000015125. PMID 9925927. S2CID 37163219.
^ Prapapanich V, Chen S, Nair SC, Rimerman RA, Smith DF (Oct 1996). "Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein". Mol Endocrinol. 10 (4): 420–31. doi:10.1210/mend.10.4.8721986. PMID 8721986.
^ ^a ^b "Entrez Gene: ST13 suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein)".

Prapapanich V, Chen S, Toran EJ, et al. (1996). "Mutational analysis of the hsp70-interacting protein Hip". Mol. Cell. Biol. 16 (11): 6200–7. doi:10.1128/MCB.16.11.6200. PMC 231623. PMID 8887650.
Cao J, Cai X, Zheng L, et al. (1997). "Characterization of colorectal-cancer-related cDNA clones obtained by subtractive hybridization screening". J. Cancer Res. Clin. Oncol. 123 (8): 447–51. doi:10.1007/BF01372549. PMID 9292708. S2CID 42097617.
Mo Y, Zheng S, Shen D (1998). "[Differential expression of HSU17714 gene in colorectal cancer and normal colonic mucosa]". Zhonghua Zhong Liu Za Zhi. 18 (4): 241–3. PMID 9387309.
Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998). "Hop modulates Hsp70/Hsp90 interactions in protein folding". J. Biol. Chem. 273 (6): 3679–86. doi:10.1074/jbc.273.6.3679. PMID 9452498.
Zheng S, Cai X, Cao J, et al. (1998). "Screening and identification of down-regulated genes in colorectal carcinoma by subtractive hybridization: a method to identify putative tumor suppressor genes". Chin. Med. J. 110 (7): 543–7. PMID 9594214.
Chen S, Smith DF (1999). "Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery". J. Biol. Chem. 273 (52): 35194–200. doi:10.1074/jbc.273.52.35194. PMID 9857057.
Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479. S2CID 21839750.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
Morishima Y, Kanelakis KC, Silverstein AM, et al. (2000). "The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system". J. Biol. Chem. 275 (10): 6894–900. doi:10.1074/jbc.275.10.6894. PMID 10702249.
Rajapandi T, Greene LE, Eisenberg E (2000). "The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor". J. Biol. Chem. 275 (29): 22597–604. doi:10.1074/jbc.M002035200. PMID 10781595.
Agarraberes FA, Dice JF (2002). "A molecular chaperone complex at the lysosomal membrane is required for protein translocation". J. Cell Sci. 114 (Pt 13): 2491–9. doi:10.1242/jcs.114.13.2491. PMID 11559757.
Velten M, Gomez-Vrielynck N, Chaffotte A, Ladjimi MM (2002). "Domain structure of the HSC70 cochaperone, HIP". J. Biol. Chem. 277 (1): 259–66. doi:10.1074/jbc.M106881200. PMID 11687574.
Fan GH, Yang W, Sai J, Richmond A (2002). "Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking". J. Biol. Chem. 277 (8): 6590–7. doi:10.1074/jbc.M110588200. PMC 2665275. PMID 11751889.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Nelson GM, Prapapanich V, Carrigan PE, et al. (2005). "The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor". Mol. Endocrinol. 18 (7): 1620–30. doi:10.1210/me.2004-0054. PMID 15071092.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

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