KCNE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNE2_HUMAN
• UniProt AC: Q9Y6J6
• Protein Name: Potassium voltage-gated channel subfamily E member 2
• Gene Name: KCNE2
• Organism: Homo sapiens (Human).
• Sequence Length: 123
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Colocalizes with KCNB1 at the plasma membrane.
• 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. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with HCN1 and HCN2 and increase potassium current. Interacts with KCNQ1; forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current. [PubMed: 11101505]
• Protein Sequence: MSTLSNFTQTLEDVFRRIFITYMDNWRQNTTAEQEALQAKVDAENFYYVILYLMVMIGMFSFIIVAILVSTVKSKRREHSNDPYHQYIVEDWQEKYKSQILNLEESKATIHENIGAAGFKMSP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSTLSNFTQ ------CCCHHHHHH	37.75	24043423
3	Phosphorylation	-----MSTLSNFTQT -----CCCHHHHHHH	32.67	30206219
5	Phosphorylation	---MSTLSNFTQTLE ---CCCHHHHHHHHH	29.95	24043423
6	N-linked_Glycosylation	--MSTLSNFTQTLED --CCCHHHHHHHHHH	47.28	UniProtKB CARBOHYD
8	Phosphorylation	MSTLSNFTQTLEDVF CCCHHHHHHHHHHHH	25.54	30206219
10	Phosphorylation	TLSNFTQTLEDVFRR CHHHHHHHHHHHHHH	29.11	30206219
21	Phosphorylation	VFRRIFITYMDNWRQ HHHHHHHHHHHHHHC	11.31	24043423
22	Phosphorylation	FRRIFITYMDNWRQN HHHHHHHHHHHHHCC	9.54	24043423
29	N-linked_Glycosylation	YMDNWRQNTTAEQEA HHHHHHCCCHHHHHH	30.72	UniProtKB CARBOHYD
47	Phosphorylation	KVDAENFYYVILYLM HCCHHHHHHHHHHHH	14.38	19369195
48	Phosphorylation	VDAENFYYVILYLMV CCHHHHHHHHHHHHH	4.11	19369195

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

Oops, there are no upstream regulatory protein records of KCNE2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCNE2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KCNE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAC1C_HUMAN	CACNA1C	physical	24681347

Drug and Disease Associations

• Kegg Disease
• H00720: Long QT syndrome, including: Romano-Ward syndrome; Jervell and Lange-Nielsen syndrome (JLNS)
• H00731: Atrial fibrillation
• OMIM Disease
• 613693: Long QT syndrome 6 (LQT6)
• 611493: Atrial fibrillation, familial, 4 (ATFB4)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47 AND TYR-48, AND MASSSPECTROMETRY.
PubMed: 19369195