UniProt ID | ENTP2_MOUSE | |
---|---|---|
UniProt AC | O55026 | |
Protein Name | Ectonucleoside triphosphate diphosphohydrolase 2 | |
Gene Name | Entpd2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 495 | |
Subcellular Localization |
Isoform Long: Cell membrane Multi-pass membrane protein. |
|
Protein Description | In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity).. | |
Protein Sequence | MAGKLVSLVPPLLLAAVGLAGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNISSCPFSQCSFNGVFQPPVAGNFIAFSAFYYTVDFLKTVMGLPVGTLKQLEDATETTCNQTWAELQARVPGQQTRLPDYCAVAMFIHQLLSRGYRFDERSFRGVVFEKKAADTAVGWALGYMLNLTNLIPADLPGLRKGTHFSSWVALLLLFTVLILAALVLLLRQVRSAKSPGAL | |
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 |
---|---|---|---|---|---|
64 | N-linked_Glycosylation | KWPADKENDTGIVGQ EEECCCCCCCCCCCC | 58.86 | - | |
129 | N-linked_Glycosylation | TAGMRLLNLTSPEAT CHHCHHHCCCCHHHH | 45.95 | 19349973 | |
294 | N-linked_Glycosylation | GQRPQTFNSSATVSL CCCCCCCCCCCEEEE | 38.14 | - | |
319 | N-linked_Glycosylation | DLVSGLFNISSCPFS HHHHHHCCCCCCCCC | 37.97 | - | |
378 | N-linked_Glycosylation | DATETTCNQTWAELQ HHCHHHHHHHHHHHH | 39.98 | - | |
443 | N-linked_Glycosylation | WALGYMLNLTNLIPA HHHHHHHHHHHCCCC | 28.43 | - |
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 ENTP2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ENTP2_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 ENTP2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ENTP2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-129, AND MASSSPECTROMETRY. |