KChannelDB: Extraction of mutation data from the literature

2005, KChannelDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation V72S was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation V72S in KCNE3_HUMAN

Point mutation:	V72S
Domain:	TRANSMEM I
General numbering (KChannelDB):	160
Protein:	KCNE3_HUMAN (KCNE)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 72 in KCNE3_HUMAN
Other point mutations / same protein	List of mutations in KCNE3_HUMAN
Family alignments	IsK related channels (minK,MiRP,AMMECR2) Potassium channels 1 TM
Other point mutations / same position	Position 58 in IsK related channels (minK,MiRP,AMMECR2) family Position 58 in Potassium channels 1 TM family
Reference:	A single transmembrane site in the KCNE-encoded proteins controls the specificity of KvLQT1 channel gating. Melman YF, Krumerman A, McDonald TV J Biol Chem 2002 Jul 12;277(28):25187-94.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

V72S

In substituting the hydroxylated residue serine into KCNE3 (V72S) , we observed slow voltage-dependent activation with sigmoidal kinetics and no voltage-independent constitutive current (Fig. 4 a)
Recordings are from CHO cells (obtained as in Fig. 1 ) transfected with KvLQT1 cDNA with V72S KCNE3 (scale bar = 4000 pA) (a) ; V72C KCNE3 (scale bar = 4000 pA) (b) ; V72A KCNE3 (scale bar = 5000 pA) (c) ; V72I KCNE3 (scale bar = 4000 pA) (d) ; V72Y KCNE3 (scale bar = 9000 pA) (e) ; T58S minK (scale bar = 10 , 000 pA) (f) ; T58A minK (scale bar = 5000 pA) (g)
(V72S , n = 7 ; V72A , n = 7 ; V72Y , n = 7 ; V72I , n = 6 ; V72C , and n = 5.) That two sets of isosteric residues (threonine and valine , cysteine and serine) gave dramatically different currents solely with the introduction of a hydroxyl group suggests that this group has an important role in control KvLQT1 gating

F.Horn (kchanneldbcmbi.ru.nl), 17-Aug-2005