An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.

Publication

Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4.

Mederos Y Schnitzler M, Rinne S, Skrobek L, Renigunta V, Schlichthoerl G, Derst C, Gudermann T, Daut J, Preisig-Mueller R

The voltage-activated K(+) channel subunit Kv2.1 can form heterotetramers with members of the Kv6 subfamily, generating channels with biophysical properties different from homomeric Kv2.1 channels. The N-terminal tetramerization domain (T1) has been shown previously to play a role in Kv channel assembly, but the mechanisms controlling specific heteromeric assembly are still unclear. In Kv6.x channels the histidine residue of the ... [more]

J. Biol. Chem. Feb. 13, 2009; 284(7);4695-704 [Pubmed: 19074135]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
KCNA1 KCNA1	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Mederos Y Schnitzler M (2009)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

KCNA1

Gene Ontology Biological Process

Gene Ontology Molecular Function

delayed rectifier potassium channel activity [IMP, ISO, ISS]protein binding [IPI]voltage-gated potassium channel activity [IMP, ISO, ISS]

Gene Ontology Cellular Component