UniProt ID | APLP2_MOUSE | |
---|---|---|
UniProt AC | Q06335 | |
Protein Name | Amyloid-like protein 2 | |
Gene Name | Aplp2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 707 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Nucleus . |
|
Protein Description | May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein (By similarity). Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts.. | |
Protein Sequence | MAATGTAAAAATGKLLVLLLLGLTAPAAALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCLGTKEEVLQYCQEIYPELQITNVMEANQPVNIDSWCRRDKRQCKSHIVIPFKCLVGEFVSDVLLVPDNCQFFHQERMEVCEKHQRWHTLVKEACLTEGLTLYSYGMLLPCGVDQFHGTEYVCCPQTKTVDSDSTMSKEEEEEEEDEEDEEEDYDLDKSEFPTEADLEDFTEAAADEEEEDEEEGEEVVEDRDYYYDPFKGDDYNEENPTEPSSEGTISDKEIVHDVKVPPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKTERQTLIQHFQAMVKALEKEAASEKQQLVETHLARVEAMLNDRRRIALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRADMDQFTSSISENPVDVRVSSEESEEIPPFHPLHPFPSLSENEDTQPELYHPMKKGSGMAEQDGGLIGAEEKVINSKNKMDENMVIDETLDVKEMIFNAERVGGLEEEPESVGPLREDFSLSSNALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQMQI | |
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 |
---|---|---|---|---|---|
208 | Phosphorylation | VCCPQTKTVDSDSTM EECCCCEECCCCCCC | 32.69 | 23737553 | |
211 | Phosphorylation | PQTKTVDSDSTMSKE CCCEECCCCCCCCHH | 29.17 | 25195567 | |
213 | Phosphorylation | TKTVDSDSTMSKEEE CEECCCCCCCCHHHH | 29.93 | 25521595 | |
214 | Phosphorylation | KTVDSDSTMSKEEEE EECCCCCCCCHHHHH | 30.38 | 25521595 | |
216 | Phosphorylation | VDSDSTMSKEEEEEE CCCCCCCCHHHHHHH | 36.68 | 25521595 | |
485 | N-linked_Glycosylation | HVIEERRNQSLSLLY HHHHHHHCCCHHHHH | 41.85 | - | |
533 | Phosphorylation | NPVDVRVSSEESEEI CCCEEEECCCCCCCC | 22.82 | 19060867 | |
534 | Phosphorylation | PVDVRVSSEESEEIP CCEEEECCCCCCCCC | 42.39 | 21183079 | |
537 | Phosphorylation | VRVSSEESEEIPPFH EEECCCCCCCCCCCC | 36.16 | 19060867 | |
665 | Phosphorylation | VMLRKRQYGTISHGI HHHHHCCCCCCCCCE | 21.92 | 30635358 | |
667 | Phosphorylation | LRKRQYGTISHGIVE HHHCCCCCCCCCEEE | 17.86 | 30635358 | |
669 | Phosphorylation | KRQYGTISHGIVEVD HCCCCCCCCCEEEEC | 18.59 | 30635358 | |
680 | Phosphorylation | VEVDPMLTPEERHLN EEECCCCCHHHHHHH | 23.54 | 20415495 | |
688 | Ubiquitination | PEERHLNKMQNHGYE HHHHHHHHHHHCCCC | 48.50 | - | |
694 | Phosphorylation | NKMQNHGYENPTYKY HHHHHCCCCCCCHHH | 12.65 | 26032504 | |
698 | Phosphorylation | NHGYENPTYKYLEQM HCCCCCCCHHHHHHH | 44.20 | 26643407 | |
699 | Phosphorylation | HGYENPTYKYLEQMQ CCCCCCCHHHHHHHC | 10.01 | 25263469 | |
700 | Ubiquitination | GYENPTYKYLEQMQI CCCCCCHHHHHHHCC | 45.92 | - |
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 APLP2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APLP2_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 APLP2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of APLP2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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