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his-28 | Histone H4. (103 aa) | ||||
his-46 | Histone H4; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. (103 aa) | ||||
hsp-3 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. (661 aa) | ||||
nex-3 | Annexin. (317 aa) | ||||
his-37 | Histone H4. (103 aa) | ||||
his-50 | Histone H4. (103 aa) | ||||
his-31 | Histone H4. (103 aa) | ||||
his-64 | Histone H4. (103 aa) | ||||
hsp-4 | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. (657 aa) | ||||
his-5 | Histone H4. (103 aa) | ||||
his-56 | Histone H4. (103 aa) | ||||
his-60 | Histone H4. (103 aa) | ||||
his-38 | Histone H4. (103 aa) | ||||
his-18 | Histone H4. (103 aa) | ||||
hsp-75 | HATPase_c domain-containing protein. (672 aa) | ||||
act-3 | Actin-1; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. (376 aa) | ||||
act-1 | Actin-1. (376 aa) | ||||
nex-2 | Annexin. (497 aa) | ||||
his-1 | Histone H4. (103 aa) | ||||
his-67 | Histone H4. (103 aa) | ||||
taf-6.1 | TAF domain-containing protein. (470 aa) | ||||
nex-1 | Annexin. (322 aa) | ||||
ubq-2 | Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...] (128 aa) | ||||
his-26 | Histone H4. (103 aa) | ||||
his-10 | Histone H4. (103 aa) | ||||
his-14 | Histone H4. (103 aa) |