KCIP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCIP2_HUMAN
• UniProt AC: Q9NS61
• Protein Name: Kv channel-interacting protein 2
• Gene Name: KCNIP2
• Organism: Homo sapiens (Human).
• Sequence Length: 270
• Subcellular Localization: Isoform 1: Cell membrane ; Lipid-anchor . Detected on lipid rafts (By similarity).; Isoform 2: Cell membrane ; Lipid-anchor .; Isoform 6: Cell membrane ; Lipid-anchor .
• Protein Description: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. May be required for the expression of I(To) currents in the heart (By similarity)..
• Protein Sequence: MRGQGRKESLSDSRDLDGSYDQLTGHPPGPTKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRLLDPDSVDDEFELSTVCHRPEGLEQLQEQTKFTRKELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSTYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTVDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQKDENIMRSMQLFDNVI

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
9	Phosphorylation	RGQGRKESLSDSRDL CCCCCCCCCCCCCCC	35.89	-
19	Phosphorylation	DSRDLDGSYDQLTGH CCCCCCCCHHHHCCC	25.79	25307156
20 (in isoform 9)	Phosphorylation	-	17.15	-
20 (in isoform 7)	Phosphorylation	-	17.15	-
20 (in isoform 5)	Phosphorylation	-	17.15	-
20 (in isoform 3)	Phosphorylation	-	17.15	-
20	Phosphorylation	SRDLDGSYDQLTGHP CCCCCCCHHHHCCCC	17.15	25332170
24	Phosphorylation	DGSYDQLTGHPPGPT CCCHHHHCCCCCCCC	28.01	-
31	Phosphorylation	TGHPPGPTKKALKQR CCCCCCCCHHHHHHH	51.60	-
45	S-palmitoylation	RFLKLLPCCGPQALP HHHHHHCCCCCCCCC	4.17	-
46	S-palmitoylation	FLKLLPCCGPQALPS HHHHHCCCCCCCCCC	9.34	-
55 (in isoform 6)	Phosphorylation	-	29.24	25159151
103	Phosphorylation	LQEQTKFTRKELQVL HHHHHCCCHHHHHHH	42.24	18220336
111	Phosphorylation	RKELQVLYRGFKNEC HHHHHHHHHHHCCCC	15.16	18220336
207	Phosphorylation	EMLDIMKSIYDMMGK HHHHHHHHHHHHHHH	14.70	24719451
209	Phosphorylation	LDIMKSIYDMMGKYT HHHHHHHHHHHHHCC	12.60	-
216	Phosphorylation	YDMMGKYTYPALREE HHHHHHCCHHHHHHH	26.89	24719451

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

Oops, there are no upstream regulatory protein records of KCIP2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCIP2_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 KCIP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCND3_HUMAN	KCND3	physical	12928444
KCND2_HUMAN	KCND2	physical	20498229
KCNE4_HUMAN	KCNE4	physical	20498229
KCND2_HUMAN	KCND2	physical	10676964
KCIP2_HUMAN	KCNIP2	physical	15358149
KCIP1_HUMAN	KCNIP1	physical	26186194
AN13A_HUMAN	ANKRD13A	physical	26186194
S10A7_HUMAN	S100A7	physical	26186194
KCIP1_HUMAN	KCNIP1	physical	28514442
S10A7_HUMAN	S100A7	physical	28514442
AN13A_HUMAN	ANKRD13A	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• 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

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND TYR-111, ANDMASS SPECTROMETRY.
PubMed: 18220336