Famplex: Default type

[jvwong]

The FamPlex entities (entities.csv) don't necessarily have relationships defined (relations.csv). However, the latter is where the type is set, so the result is some will be missing a type. e.g. IκB.

• Tasks
  • [x] Figure out the overlap between entities vs relations
  • [x] If not a issue with dataset, set a default: e.g. 'protein'

[jvwong]

Entries	Count
entity	779
relations	766

So there are 13 entities with no relationship information.

id	name	summary
E3_Ub_ligase	E3_Ub_ligase	A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
ETC_complex_V	ETC_complex_V	Proton-translocating ATPases responsible for ADENOSINE TRIPHOSPHATE synthesis in the MITOCHONDRIA. They derive energy from the respiratory chain-driven reactions that develop high concentrations of protons within the intermembranous space of the mitochondria.
GAP	GAP	Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
GEF	GEF
GTPase	GTPase	Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.
IKB	IKB
Pertussis_toxin	Pertussis_toxin
Phosphatase	Phosphatase	A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
Protease	Protease	Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
RasGAP	RasGAP	PROTEINS that specifically activate the GTP-phosphohydrolase activity of RAS PROTEINS.
RTK	RTK
TNF	TNF	TNF(Tumour Necrosis Factor) family
Ubiquitin	Ubiquitin	A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.