Er

Cytosol/ nucleus

Mitochondria

Hspel, chaperonin 10 Mitochondria

APG-2, Hspl 10, Hsp70RY, Hspa4, Hspl05a, and Hspl05|3

Implicated in peptide llq23 9

transport in the ER

immunoglobulin)

folding

Protein folding, clathrin 11 (q24.1) 9

uncoating, peptide binding

Involved in antigen 5 (q31.1) 18

presentation and radioresistance. Also oncogenic

(overexpression of Mot-2 leads to p53 inactivation and cell transformation).

Tolerance of ischemia 2 (q33.1 )

Cytosol/ nucleus

Binds to Hsc70 to form high-molecular-weight complex; involved in protein folding, thermotolerance, and embryogenesis

Distant member of Hsp70 family

Constitutively expressed; also induced by metabolic stress such as glucose starvation

Leukemia-derived Hsc70 is now being tested as a leukemia vaccine

Belongs to Hsp70 family; Mot-1 and Mot-2 differ by only two amino acid residues at the C-terminus and have different subcellular localizations. Localized to human chromosome 5, band q31, a region that is frequently deleted in myeloid leukemias and myelodysplasia.

Uses same promoter as Hsp60 in humans

Two isoforms in mice; heat-inducible; also induced by human papilloma virus oncoprotein E7

Haas and Wabl (1983); Kaloff and Haas (1995)

Udono and Srivastava (1993)

Dahlseid et al. (1994); Wadhwa et al. (2002); Liu et al. (2003)

Hartman et al. (1992)

Table A.1T.1 Heat-Shock Protein Genes and Products from Human and Mouse", continued

Heat-shock protein

Other names

Subcellular localization

Known functions

Chromosome assignment

(human)

Chromosome assignment

(mouse)

Comments

Reference

Hsp27

Hsp40

Hsp47

Hsp60

HSPB2, Hsp25 in rodents

HSPF1, HDJ1. Has five isoforms (Dnajal, Dnajbl, Dnajb3, Dnajb5, Dnajc4).

BERF-1, |3-enolase repressor factor 1, Cbpl, Cbp2, colligin, gp46, Hsp47, Hsp47, Hsp47, J6, Serpinhl, Serpinh2

HSPD1, Homologous to plant Rubisco binding protein, E. coli GroEL, and 65 kDa major antigen of Mycobacteria bovis BCG (HSP65)

Cytosol

Cytosol

Endoplasmic reticulum (ER)

Mitochondria

Antiapoptotic, cytoprotection

Repair denatured proteins, together with Hsp70/Hsc70

Synthesis/assembly of various collagens, a member of serpin (serine protease inhibitor) superfamily

Cytoprotection; macrophage activator possibly through Toll-like receptors

Dnajbl: 19 (pl3.2) Dnajb3: (?) Dnajb5: 9 (pl3.2) Dnajc4: 11 (ql3)

Dnajal: 4 Dnajbl: 8 Dnajb3: 1 Dnajb5: 4 Dnajc4: 19

Heat-inducible, chaperone activity is independent of ATP; high expression correlated with poor prognosis in cancer

Homologous to bacterial protein DnaJ

Involved in tumor migration and metastasis

Functions along with co-chaperone HsplO; linked with autoimmunity such as rheumatoid arthritis

Arrigo and Landry (1994)

Ohtsuka and Hata (2000)

Bukau and Horwich (1998); Ohashi et al. (2000)

Table A.1T.1 Heat-Shock Protein Genes and Products from Human and Mouse", continued

. . Other names , ,. .. Known functions assignment assignment Comments Reference protein localization ., ° . . ° .

Hsp70

Hsp90a

Hsp90ß

Hsp72. Has three isoforms in mouse (hsp70-l, hsp70-2 and hsp70-3) with three human homologs (hsp70-2, hspA2, hsp70-1) and three rat homologs (hsp70-l, hst70 and hsp70-2)

Hsp90, Hsp86-1, inducible Hsp90, Hsp89, hsp4

Cytosol/ nucleus

Cytosol

Hsp84-1, hsp84, Hsc90 Cytosol

Cytoprotection and anti-apoptotic, Hsp70-2 implicated in spermatogenesis

Protein folding, peptide chaperone, cytoprotection, intracellular signaling (e.g., steroid receptor), cell-cycle control and buffering of harmful mutations

Major cytosol chaperone; protein folding; cytoprotection; intracellular signaling (e.g., steroid receptor); cell-cycle control; and buffering of harmful mutations

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