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PSMA4 | proteasome (prosome, macropain) subunit, alpha type, 4; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity) (261 aa) | |||
PSMA2 | proteasome (prosome, macropain) subunit, alpha type, 2; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation (234 aa) | |||
HSPA8 | heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (646 aa) | |||
HSPA2 | heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (639 aa) | |||
DNAJB6 | DnaJ (Hsp40) homolog, subfamily B, member 6 (326 aa) | |||
DNAJC10 | DnaJ (Hsp40) homolog, subfamily C, member 10 (793 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) | |||
GRPEL1 | GrpE-like 1, mitochondrial (E. coli); Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (217 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) | |||
UBB | ubiquitin B (229 aa) | |||
DNAJB7 | DnaJ (Hsp40) homolog, subfamily B, member 7; Probably acts as a co-chaperone (By similarity) (309 aa) | |||
HSPA6 | heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity) (643 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) | |||
HSPA5 | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (654 aa) | |||
GRPEL2 | GrpE-like 2, mitochondrial (E. coli); Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity) (225 aa) | |||
GSPT2 | G1 to S phase transition 2; Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (628 aa) | |||
DNAJB13 | DnaJ (Hsp40) homolog, subfamily B, member 13; May be involved in inhibiting testis spermatogenesis apoptosis (316 aa) | |||
UBC | ubiquitin C (685 aa) | |||
HSPA1B | heat shock 70kDa protein 1B (641 aa) | |||
HSPA1A | heat shock 70kDa protein 1A (641 aa) | |||
HSPA1L | heat shock 70kDa protein 1-like (641 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) | |||
SPATA13 | spermatogenesis associated 13 (1277 aa) | |||
DNAJA4 | DnaJ (Hsp40) homolog, subfamily A, member 4 (426 aa) | |||
GSPT1 | G1 to S phase transition 1; Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ERF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (637 aa) |