dbPTM

KCNE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCNE1_HUMAN
UniProt AC	P15382
Protein Name	Potassium voltage-gated channel subfamily E member 1
Gene Name	KCNE1
Organism	Homo sapiens (Human).
Sequence Length	129
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Apical cell membrane . Membrane raft . Colocalizes with KCNB1 at the plasma membrane (By similarity). Targets to the membrane raft when associated with KCNQ1 (PubMed:20533308).
Protein Description	Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. [PubMed: 19219384 Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr]
Protein Sequence	MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGKLEALYVLMVLGFFGFFTLGIMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNTHLPETKPSP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	N-linked_Glycosylation	---MILSNTTAVTPF ---CCCCCCCCHHHH	37.69	21676880
7	O-linked_Glycosylation	-MILSNTTAVTPFLT -CCCCCCCCHHHHHH	24.31	21669976
7	Phosphorylation	-MILSNTTAVTPFLT -CCCCCCCCHHHHHH	24.31	-
26	N-linked_Glycosylation	ETVQQGGNMSGLARR HHHHCCCCCCCCCCC	28.42	21676880
28	Phosphorylation	VQQGGNMSGLARRSP HHCCCCCCCCCCCCC	34.35	-
34	Phosphorylation	MSGLARRSPRSSDGK CCCCCCCCCCCCCCH	21.07	17081983
102	Phosphorylation	VQARVLESYRSCYVV HHHHHHHHHHCEEEE	22.99	21699843

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
102	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
5	N	Glycosylation	21676880
N-glycosylation at Asn-26 occurs post-translationally, and requires prior cotranslational glycosylation at Asn-5.
26	N	Glycosylation	21676880
N-glycosylation at Asn-26 occurs post-translationally, and requires prior cotranslational glycosylation at Asn-5.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of KCNE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNH2_HUMAN	KCNH2	physical	9230439
TPM3_HUMAN	TPM3	physical	25416956
UBS3A_HUMAN	UBASH3A	physical	25416956

Drug and Disease Associations

Kegg Disease
H00720	Long QT syndrome, including: Romano-Ward syndrome; Jervell and Lange-Nielsen syndrome (JLNS)
OMIM Disease
612347	Jervell and Lange-Nielsen syndrome 2 (JLNS2)
613695	Long QT syndrome 5 (LQT5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00808	Indapamide

Regulatory Network of KCNE1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"O-glycosylation of the cardiac I(Ks) complex."; Chandrasekhar K.D., Lvov A., Terrenoire C., Gao G.Y., Kass R.S.,Kobertz W.R.; J. Physiol. (Lond.) 589:3721-3730(2011). Cited for: GLYCOSYLATION AT ASN-5 AND THR-7, AND MUTAGENESIS OF ASN-5; THR-6;THR-7 AND SER-28.	21669976 [Abstract]
O-linked Glycosylation
Reference	PubMed
"O-glycosylation of the cardiac I(Ks) complex."; Chandrasekhar K.D., Lvov A., Terrenoire C., Gao G.Y., Kass R.S.,Kobertz W.R.; J. Physiol. (Lond.) 589:3721-3730(2011). Cited for: GLYCOSYLATION AT ASN-5 AND THR-7, AND MUTAGENESIS OF ASN-5; THR-6;THR-7 AND SER-28.	21669976 [Abstract]