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CDC37 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (378 aa) | |||
NKTR | natural killer-tumor recognition sequence; Component of a putative tumor-recognition complex. Involved in the function of NK cells (1462 aa) | |||
TTC31 | tetratricopeptide repeat domain 31 (519 aa) | |||
TRAP1 | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 aa) | |||
PTGES3 | prostaglandin E synthase 3 (cytosolic); Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor- mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (160 aa) | |||
CAD | carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase; This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) (2225 aa) | |||
ERCC3 | excision repair cross-complementing rodent repair deficiency, complementation group 3; ATP-dependent 3’-5’ DNA helicase, component of the core- TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage (782 aa) | |||
CLPB | ClpB caseinolytic peptidase B homolog (E. coli); May function as a regulatory ATPase and be related to secretion/protein trafficking process (707 aa) | |||
HSPA4L | heat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity) (839 aa) | |||
HSP90B1 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (803 aa) | |||
HSPA4 | heat shock 70kDa protein 4 (840 aa) | |||
PPID | peptidylprolyl isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be i [...] (370 aa) | |||
PPIH | peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone (177 aa) | |||
DNAJA2 | DnaJ (Hsp40) homolog, subfamily A, member 2; Co-chaperone of Hsc70 (412 aa) | |||
HSPH1 | heat shock 105kDa/110kDa protein 1; Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity) (858 aa) | |||
HSP90AB1 | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (724 aa) | |||
HSP90AA1 | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (854 aa) | |||
SUGT1 | SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins (365 aa) | |||
MS4A13 | membrane-spanning 4-domains, subfamily A, member 13; May be involved in signal transduction as a component of a multimeric receptor complex (By similarity) (152 aa) | |||
DNAJA1 | DnaJ (Hsp40) homolog, subfamily A, member 1; Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria (397 aa) | |||
CDC37L1 | cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (By similarity) (337 aa) | |||
DNAJA4 | DnaJ (Hsp40) homolog, subfamily A, member 4 (426 aa) | |||
ENSG00000108825 | PTGES3L-AARSD1 readthrough; Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) (By similarity) (586 aa) | |||
PPIL6 | peptidylprolyl isomerase (cyclophilin)-like 6; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (337 aa) | |||
PTGES3L | prostaglandin E synthase 3 (cytosolic)-like (166 aa) | |||
CPS1 | carbamoyl-phosphate synthase 1, mitochondrial; Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell (1506 aa) |