TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
1.A.33.1.1









Heat shock cognate 70 kDa protein, Hsc70
Eukaryota
Viridiplantae, Streptophyta
Hsc70 of Arabidopsis thaliana
1.A.33.1.2









Heat shock protein-70 homologue, DnaK.  Although DnaK homologues are ubiquitous, a transport function in eukaryotes, but not in prokaryotes has been demonstrated.

Bacteria
Pseudomonadota
DnaK of E. coli
1.A.33.1.3









Heat shock protein 70(1B)
Eukaryota
Metazoa, Chordata
Hsp70(1B) of Homo sapiens (AAH57397)
1.A.33.1.4









DnaK of 611 aas

Bacteria
Bacillota
DnaK of Bacillus subtiiis
1.A.33.1.5









Glucose regulated protein, GRP78 of 654 aas.  GRP78, a member of the ER stress protein family.  It can relocate to the surface of cancer cells, playing a role in promoting cell proliferation and metastasis. GRP78 consists of two major functional domains: the ATPase and protein/peptide-binding domains. The protein/peptide-binding domain of cell-surface GRP78 has served as a novel functional receptor for delivering cytotoxic agents (e.g., a apoptosis-inducing peptide or taxol) across the cell membrane. The ATPase domain of GRP78 (GRP78ATPase) has potential as a transmembrane delivery system of cytotoxic agents including nucleotides (e.g., ATP-based nucleotide triphosphate analogs) (Hughes et al. 2016). It may also play a role in facilitating the assembly of multimeric protein complexes inside the ER (Evensen et al. 2013). It is involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (Evensen et al. 2013). Grp78 as a critical factor in Kras-mutated adenomagenesis. This can be attributed to a critical role for Grp78 in GLUT1 expression and localization, targeting glycolysis and the Warburg effect (Spaan et al. 2023).

).

Eukaryota
Metazoa, Chordata
GRP78 of Homo sapiens
1.A.33.1.6









Lhs1, Hsp70 homolog of 881 aas and 1 N-terminal TMS.  It is a chaperone required for protein translocation and folding in the endoplasmic reticulum via the ERAD pathway ( TC# 3.A.25) (Steel et al. 2004).  The Lhs1-dependent ERAD pathway is influenced by the transmembrane domain context (Sukhoplyasova et al. 2023).

Eukaryota
Fungi, Ascomycota
Lhs1 of Saccharomyces cerevisiae
1.A.33.2.1









MMAR_0617 MOMP (Hsp70 homologue) (van der Woude et al. 2013).

Bacteria
Actinomycetota
MMAR_0617 of Mycobcterium marinum
1.A.33.2.2









Hsp70 homologue of 581 aas.

Bacteria
Actinomycetota
Hsp70 homologue of Mycobacterium tuberculosis
1.A.33.2.3









Hsp70 homologue of 455 aas

Bacteria
Actinomycetota
Hsp70 of Nocardia farcinica