UniProt ID | KCIP2_RAT | |
---|---|---|
UniProt AC | Q9JM59 | |
Protein Name | Kv channel-interacting protein 2 | |
Gene Name | Kcnip2 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 270 | |
Subcellular Localization |
Cell membrane Lipid-anchor . Detected on lipid rafts. |
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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. [PubMed: 16820361 In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. Essential for the expression of I(To) currents in the heart (By similarity Required for normal protein levels of KCND2 in the heart ventricle (By similarity] | |
Protein Sequence | MRGQGRKESLSESRDLDGSYDQLTGHPPGPSKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRPLDPDSVEDEFELSTVCHRPEGLEQLQEQTKFTRRELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLSWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQQDENIMRSMQLFDNVI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Phosphorylation | RGQGRKESLSESRDL CCCCCCCCCCCCCCC | 39.98 | 25403869 | |
11 | Phosphorylation | QGRKESLSESRDLDG CCCCCCCCCCCCCCC | 42.69 | 24972320 | |
19 | Phosphorylation | ESRDLDGSYDQLTGH CCCCCCCCCHHHCCC | 25.79 | 30240740 | |
20 | Phosphorylation | SRDLDGSYDQLTGHP CCCCCCCCHHHCCCC | 17.15 | 22673903 | |
45 | S-palmitoylation | RFLKLLPCCGPQALP HHHHHHCCCCCCCCC | 4.17 | 12006572 | |
46 | S-palmitoylation | FLKLLPCCGPQALPS HHHHHCCCCCCCCCC | 9.34 | 12006572 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of KCIP2_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KCIP2_RAT !! |
* 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 KCIP2_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of KCIP2_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Palmitoylation | |
Reference | PubMed |
"Palmitoylation of KChIP splicing variants is required for efficientcell surface expression of Kv4.3 channels."; Takimoto K., Yang E.-K., Conforti L.; J. Biol. Chem. 277:26904-26911(2002). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULARLOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-45 AND CYS-46, ANDMUTAGENESIS OF 45-CYS-CYS-46. |