Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
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
Electronic Gene Ontology annotations created by ARBA machine learning models
Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction.
Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues.
Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C.
The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300.
Golgi localization of Syne-1.
DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation.
Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy.
Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness.
Proteomic characterization of the human sperm nucleus.
LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
Mammalian microtubule P-body dynamics are mediated by nesprin-1.
Outer nuclear membrane protein Kuduk modulates the LINC complex and nuclear envelope architecture.
HENA, heterogeneous network-based data set for Alzheimer's disease.
Structural Analysis of Different LINC Complexes Reveals Distinct Binding Modes.
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies.