UniProt ID | APOH_MOUSE | |
---|---|---|
UniProt AC | Q01339 | |
Protein Name | Beta-2-glycoprotein 1 | |
Gene Name | Apoh | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 345 | |
Subcellular Localization | Secreted. | |
Protein Description | Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.. | |
Protein Sequence | MVSPVLALFSAFLCHVAIAGRICPKPDDLPFATVVPLKTSYDPGEQIVYSCKPGYVSRGGMRRFTCPLTGMWPINTLRCVPRVCPFAGILENGIVRYTSFEYPKNISFACNPGFFLNGTSSSKCTEEGKWSPDIPACARITCPPPPVPKFALLKDYRPSAGNNSLYQDTVVFKCLPHFAMIGNDTVMCTEQGNWTRLPECLEVKCPFPPRPENGYVNYPAKPVLLYKDKATFGCHETYKLDGPEEAECTKTGTWSFLPTCRESCKLPVKKATVLYQGMRVKIQEQFKNGMMHGDKIHFYCKNKEKKCSYTVEAHCRDGTIEIPSCFKEHSSLAFWKTDASELTPC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
23 | S-palmitoylation | VAIAGRICPKPDDLP HHHHCCCCCCCCCCC | 3.23 | 28526873 | |
33 | O-linked_Glycosylation | PDDLPFATVVPLKTS CCCCCCEEEEEECCC | 23.55 | - | |
55 | Phosphorylation | VYSCKPGYVSRGGMR EEEECCCEECCCCCC | 12.09 | 23737553 | |
57 | Phosphorylation | SCKPGYVSRGGMRRF EECCCEECCCCCCEE | 19.41 | 23737553 | |
79 | S-palmitoylation | WPINTLRCVPRVCPF CCCCCCCCCCCCCCC | 5.78 | 26165157 | |
84 | S-palmitoylation | LRCVPRVCPFAGILE CCCCCCCCCCCCHHH | 2.12 | 26165157 | |
105 | N-linked_Glycosylation | TSFEYPKNISFACNP CCEECCCCEEEEECC | 30.54 | 17330941 | |
117 | N-linked_Glycosylation | CNPGFFLNGTSSSKC ECCCEECCCCCCCCC | 46.68 | 16944957 | |
162 | N-linked_Glycosylation | DYRPSAGNNSLYQDT CCCCCCCCCCCCCCE | 34.33 | 16944957 | |
183 | N-linked_Glycosylation | PHFAMIGNDTVMCTE CCEEEECCCEEEECC | 30.75 | 17330941 | |
193 | N-linked_Glycosylation | VMCTEQGNWTRLPEC EEECCCCCEEECCCC | 36.32 | 17330941 | |
260 | S-palmitoylation | TWSFLPTCRESCKLP CEEECCCCHHHCCCC | 4.25 | 28526873 | |
319 | Phosphorylation | EAHCRDGTIEIPSCF EEEECCCEEECCCCC | 21.52 | - | |
324 | Phosphorylation | DGTIEIPSCFKEHSS CCEEECCCCCCCCCC | 37.54 | - |
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 APOH_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APOH_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 APOH_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of APOH_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-105; ASN-117; ASN-162;ASN-183 AND ASN-193, AND MASS SPECTROMETRY. | |
"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-117 AND ASN-162, AND MASSSPECTROMETRY. |