Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Combined Automated Annotation using Multiple IEA Methods
ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Integrated structural analysis of the human nuclear pore complex scaffold.
The Structure Inventory of the Nuclear Pore Complex.
Identification of Conserved MEL-28/ELYS Domains with Essential Roles in Nuclear Assembly and Chromosome Segregation.
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MEL-28/ELYS domains required for NPC, kinetochore, and chromatin localization are conserved, and the C-terminal region of human ELYS supports chromatin association.
MAD2 converted to an inhibitory state via interaction with Mad1
MAD2 associates with the Mad1 kinetochore complex
Release of activated MAD2 from kinetochores
Phosphorylation of cohesin by PLK1 at centromeres
PP2A-B56 dephosphorylates centromeric cohesin
ESPL1 (Separase) cleaves centromeric cohesin
Separation of sister chromatids
CDK1 phosphorylates CDCA5 (Sororin) at centromeres
Kinetochore capture of astral microtubules
CDC42:GTP recruits DIAPH2-2 to kinetochores
AURKB phosphorylates DIAPH2-2 at kinetochores
Kinetochore capture of astral microtubules is positively regulated by CDC42:GTP:p-S196-DIAPH2-2
AHCTF1 (ELYS) binds chromatin and Nup107-Nup160 complex
POM121 binds the Nup107-Nup160 complex
POM121 and NDC1 bind the Nup93 complex
EML4 recruits NUDC to mitotic spindle
UniProtKB record for human AHCTF1/ELYS
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Reviewed UniProt record summarizes AHCTF1 as a nuclear pore assembly factor that recruits Nup107-160 and localizes to NPCs, nuclear envelope, chromatin, and kinetochores.
Falcon deep research review of human AHCTF1/ELYS
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Falcon research summarizes AHCTF1/ELYS as a chromatin-binding nucleoporin that seeds post-mitotic NPC reassembly by recruiting the Nup107-160/Y-complex to decondensing chromosomes.
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Falcon research highlights recent literature on ELYS nucleosome binding, VAPB interaction during mitosis, chromatin anchoring at NPCs, and cancer-relevant nuclear architecture contexts.