| UniProt ID | COR1C_MOUSE | |
|---|---|---|
| UniProt AC | Q9WUM4 | |
| Protein Name | Coronin-1C | |
| Gene Name | Coro1c | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 474 | |
| Subcellular Localization | Cell membrane. Cell projection, lamellipodium. Cytoplasm, cytoskeleton. Localize in a diffuse and punctate pattern in the cytosol and are highly enriched in F-actin-rich areas.. | |
| Protein Description | May be involved in cytokinesis, motility, and signal transduction.. | |
| Protein Sequence | MRRVVRQSKFRHVFGQAVKNDQCYDDIRVSRVTWDSSFCAVNPRFVAIIIEASGGGAFLVLPLHKTGRIDKSYPTVCGHTGPVLDIDWCPHNDQVIASGSEDCTVMVWQIPENGLTLSLTEPVVILEGHSKRVGIVAWHPTARNVLLSAGCDNAIIIWNVGTGEALINLDDMHSDMIYNVSWSRNGSLICTASKDKKVRVIDPRKQEIVAEKEKAHEGARPMRAIFLADGNVFTTGFSRMSERQLALWNPKNMQEPIALHEMDTSNGVLLPFYDPDTSIIYLCGKGDSSIRYFEITDESPYVHYLNTFSSKEPQRGMGYMPKRGLDVNKCEIARFFKLHERKCEPIIMTVPRKSDLFQDDLYPDTAGPEAALEAEEWFEGKNADPILISLKHGYIPGKNRDLKVVKKNILDSKPAANKKSELSCAPKKPTDTASVQNEAKLDEILKEIKSIKETICSQDERISKLEQQLAKMAA | |
| 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 |
|---|---|---|---|---|---|
| 23 | Glutathionylation | QAVKNDQCYDDIRVS HHHCCCCCCCCEEEE | 4.48 | 24333276 | |
| 23 | S-nitrosylation | QAVKNDQCYDDIRVS HHHCCCCCCCCEEEE | 4.48 | 21278135 | |
| 23 | S-nitrosocysteine | QAVKNDQCYDDIRVS HHHCCCCCCCCEEEE | 4.48 | - | |
| 39 | S-nitrosocysteine | VTWDSSFCAVNPRFV EEECCCCCCCCCCEE | 4.46 | - | |
| 39 | S-nitrosylation | VTWDSSFCAVNPRFV EEECCCCCCCCCCEE | 4.46 | 21278135 | |
| 39 | S-palmitoylation | VTWDSSFCAVNPRFV EEECCCCCCCCCCEE | 4.46 | 28526873 | |
| 187 | Phosphorylation | VSWSRNGSLICTASK EEECCCCCEEEEECC | 20.36 | 24759943 | |
| 193 | Phosphorylation | GSLICTASKDKKVRV CCEEEEECCCCCEEE | 24.20 | - | |
| 296 | Phosphorylation | SIRYFEITDESPYVH EEEEEEECCCCCCEE | 26.90 | 25367039 | |
| 299 | Phosphorylation | YFEITDESPYVHYLN EEEECCCCCCEEEEE | 25.08 | 25367039 | |
| 301 | Phosphorylation | EITDESPYVHYLNTF EECCCCCCEEEEEEC | 14.78 | 22817900 | |
| 304 | Phosphorylation | DESPYVHYLNTFSSK CCCCCEEEEEECCCC | 7.51 | 25367039 | |
| 307 | Phosphorylation | PYVHYLNTFSSKEPQ CCEEEEEECCCCCCC | 23.46 | 25367039 | |
| 322 | Acetylation | RGMGYMPKRGLDVNK CCCCCCCCCCCCCCH | 42.44 | 6569473 | |
| 329 | Acetylation | KRGLDVNKCEIARFF CCCCCCCHHHHHHHH | 32.85 | 22826441 | |
| 330 | S-nitrosylation | RGLDVNKCEIARFFK CCCCCCHHHHHHHHH | 3.74 | 20925432 | |
| 330 | S-nitrosocysteine | RGLDVNKCEIARFFK CCCCCCHHHHHHHHH | 3.74 | - | |
| 330 | Glutathionylation | RGLDVNKCEIARFFK CCCCCCHHHHHHHHH | 3.74 | 24333276 | |
| 343 | S-palmitoylation | FKLHERKCEPIIMTV HHHCCCCCEEEEEEC | 10.61 | 28526873 | |
| 343 | Glutathionylation | FKLHERKCEPIIMTV HHHCCCCCEEEEEEC | 10.61 | 24333276 | |
| 391 | Ubiquitination | DPILISLKHGYIPGK CCEEEEEECCCCCCC | 28.35 | 27667366 | |
| 391 | Acetylation | DPILISLKHGYIPGK CCEEEEEECCCCCCC | 28.35 | 23806337 | |
| 394 | Phosphorylation | LISLKHGYIPGKNRD EEEEECCCCCCCCCC | 12.03 | 25367039 | |
| 413 | Acetylation | KKNILDSKPAANKKS HHHHHCCCCCCCCCC | 38.04 | 23806337 | |
| 419 | Acetylation | SKPAANKKSELSCAP CCCCCCCCCCCCCCC | 49.31 | 23806337 | |
| 419 | Succinylation | SKPAANKKSELSCAP CCCCCCCCCCCCCCC | 49.31 | 23806337 | |
| 424 | Glutathionylation | NKKSELSCAPKKPTD CCCCCCCCCCCCCCC | 13.53 | 24333276 | |
| 427 | Malonylation | SELSCAPKKPTDTAS CCCCCCCCCCCCCHH | 53.51 | 26320211 | |
| 434 | Phosphorylation | KKPTDTASVQNEAKL CCCCCCHHHHCHHHH | 26.74 | 30387612 | |
| 446 | Acetylation | AKLDEILKEIKSIKE HHHHHHHHHHHHHHH | 64.15 | 23236377 | |
| 456 | Glutathionylation | KSIKETICSQDERIS HHHHHHHCCHHHHHH | 3.79 | 24333276 | |
| 456 | S-nitrosylation | KSIKETICSQDERIS HHHHHHHCCHHHHHH | 3.79 | 21278135 | |
| 456 | S-nitrosocysteine | KSIKETICSQDERIS HHHHHHHCCHHHHHH | 3.79 | - | |
| 463 | Phosphorylation | CSQDERISKLEQQLA CCHHHHHHHHHHHHH | 37.09 | 22355754 | |
| 464 | Acetylation | SQDERISKLEQQLAK CHHHHHHHHHHHHHH | 54.38 | 22826441 | |
| 471 | Ubiquitination | KLEQQLAKMAA---- HHHHHHHHHHC---- | 37.35 | 27667366 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of COR1C_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COR1C_MOUSE !! | ||||||
* 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 COR1C_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASSSPECTROMETRY. | |
