| UniProt ID | CERU_MOUSE | |
|---|---|---|
| UniProt AC | Q61147 | |
| Protein Name | Ceruloplasmin | |
| Gene Name | Cp | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 1061 | |
| Subcellular Localization | Secreted. Colocalizes with GCP1 in secretory intracellular compartments.. | |
| Protein Description | Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).. | |
| Protein Sequence | MKFLLLSTFIFLYSSLALARDKHYFIGITEAVWDYASGTEEKKLISVDTEQSNFYLQNGPDRIGRKYKKALYFEYTDGTFSKTIDKPAWLGFLGPVIKAEVEDKVYVHLKNLASRIYTFHAHGVTYTKEYEGAVYPDNTTDFQRADDKVLPGQQYVYVLHANEPSPGEGDSNCVTRIYHSHVDAPKDIASGLIGPLILCKKGSLYKEKEKNIDQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAADRVKWYLFGMGNEVDVHSAFFHGQALTSRNYQTDIINLFPATLIDAYMVAQNPGVWMLSCQNLNHLKAGLQAFFQVRDCNKPSPEDNIQDRHVRHYYIAAEEVIWNYAPSGTDIFTGENLTALESDSRVFFEQGATRIGGSYKKMAYREYTDGSFTNRKQRGPDEEHLGILGPVIWAEVGDTIKVTFHNKGQHPLSIQPMGVSFTAENEGTYYGPPGRSSQQAASHVAPKETFTYEWTVPKEMGPTYADPVCLSKMYYSGVDPTKDIFTGLIGPMKICKKGSLLADGRQKDVDKEFYLFPTVFDENESLLLDDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLNMCLGESIVWYLFSAGNEADVHGIYFSGNTYLSKGERRDTANLFPHKSLTLLMNPDTKGTFDVECLTTDHYTGGMKQKYTVNQCQRQFEDFTVYLGERTYYVAAVEVEWDYSPSRAWEKELHHLQEQNVSNVFLDKEEFFIGSKYKKVVYRQFTDSSFREQVKRRAEDEHLGILGPPIHANVGDKVKVVFKNMATRPYSIHAHGVKTESSTVVPTLPGEVRTYTWQIPERSGAGREDSACIPWAYYSTVDRVKDLYSGLIGPLIVCRKSYVKVFSPKKKMEFFLLFLVFDENESWYLDDNIKTYSEHPEKVNKDNEEFLESNKMHAINGKMFGNLQGLTMHVKDEVNWYVMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDLFPGTYQTLEMFPQTPGTWLLHCHVTDHVHAGMATTYTVLPVEQETKSG | |
| 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 |
|---|---|---|---|---|---|
| 138 | N-linked_Glycosylation | EGAVYPDNTTDFQRA CCCCCCCCCCCCCCC | 40.13 | 16944957 | |
| 221 | Phosphorylation | QEFVLMFSVVDENLS CEEEEEEEEECCCCC | 13.78 | - | |
| 226 | N-linked_Glycosylation | MFSVVDENLSWYLED EEEEECCCCCCHHCC | 34.61 | - | |
| 259 | Phosphorylation | FQESNRMYSINGYTF HHHHHCEEEECCEEC | 11.80 | - | |
| 264 | Phosphorylation | RMYSINGYTFGSLPG CEEEECCEECCCCCC | 8.39 | - | |
| 396 | N-linked_Glycosylation | TDIFTGENLTALESD CCCCCCCCCEECCCC | 44.00 | - | |
| 542 | Ubiquitination | YSGVDPTKDIFTGLI HCCCCCCCCCCCCCC | 54.97 | - | |
| 557 | Acetylation | GPMKICKKGSLLADG CCEEEECCCCEECCC | 49.69 | 23576753 | |
| 583 | N-linked_Glycosylation | FPTVFDENESLLLDD CCEECCCCCCEEECC | 46.10 | - | |
| 676 | Ubiquitination | TANLFPHKSLTLLMN CCCCCCCCEEEEEEC | 47.61 | - | |
| 713 | S-palmitoylation | QKYTVNQCQRQFEDF CEEEHHHHHHHHCCE | 2.80 | 26165157 | |
| 757 | N-linked_Glycosylation | LHHLQEQNVSNVFLD HHHHHHCCCCCEECC | 38.13 | 16944957 | |
| 921 | N-linked_Glycosylation | LFLVFDENESWYLDD EEEEECCCCCEECCC | 50.90 | - |
| 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 CERU_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CERU_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 CERU_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CERU_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; Bernhard O.K., Kapp E.A., Simpson R.J.; J. Proteome Res. 6:987-995(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757, AND MASSSPECTROMETRY. | |
| "Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757, AND MASSSPECTROMETRY. | |
