| UniProt ID | P3IP1_HUMAN | |
|---|---|---|
| UniProt AC | Q96FE7 | |
| Protein Name | Phosphoinositide-3-kinase-interacting protein 1 | |
| Gene Name | PIK3IP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 263 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
| Protein Description | Negative regulator of hepatic phosphatidylinositol 3-kinase (PI3K) activity.. | |
| Protein Sequence | MLLAWVQAFLVSNMLLAEAYGSGGCFWDNGHLYREDQTSPAPGLRCLNWLDAQSGLASAPVSGAGNHSYCRNPDEDPRGPWCYVSGEAGVPEKRPCEDLRCPETTSQALPAFTTEIQEASEGPGADEVQVFAPANALPARSEAAAVQPVIGISQRVRMNSKEKKDLGTLGYVLGITMMVIIIAIGAGIILGYSYKRGKDLKEQHDQKVCEREMQRITLPLSAFTNPTCEIVDEKTVVVHTSQTPVDPQEGTTPLMGQAGTPGA | |
| 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 |
|---|---|---|---|---|---|
| 38 | O-linked_Glycosylation | HLYREDQTSPAPGLR CEECCCCCCCCCCCC | 49.34 | OGP | |
| 39 | O-linked_Glycosylation | LYREDQTSPAPGLRC EECCCCCCCCCCCCH | 17.27 | 22171320 | |
| 66 | N-linked_Glycosylation | APVSGAGNHSYCRNP CCCCCCCCCCCCCCC | 22.01 | 22171320 | |
| 85 | Phosphorylation | RGPWCYVSGEAGVPE CCCCCEEECCCCCCC | 12.39 | 29759185 | |
| 113 | O-linked_Glycosylation | SQALPAFTTEIQEAS HHHHCHHCHHHHHHH | 26.14 | OGP | |
| 120 | O-linked_Glycosylation | TTEIQEASEGPGADE CHHHHHHHCCCCCCE | 42.19 | OGP | |
| 141 | Phosphorylation | ANALPARSEAAAVQP CCCCCCCCHHHHHHC | 33.42 | 29759185 | |
| 141 | O-linked_Glycosylation | ANALPARSEAAAVQP CCCCCCCCHHHHHHC | 33.42 | OGP | |
| 171 | Phosphorylation | KDLGTLGYVLGITMM CCHHHHHHHHHHHHH | 8.80 | 22817900 | |
| 192 | Phosphorylation | GAGIILGYSYKRGKD HHHHHHHCHHHCCCC | 12.84 | 22817900 | |
| 194 | Phosphorylation | GIILGYSYKRGKDLK HHHHHCHHHCCCCHH | 9.02 | 22817900 | |
| 198 | Ubiquitination | GYSYKRGKDLKEQHD HCHHHCCCCHHHHHH | 65.01 | - |
| 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 P3IP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of P3IP1_HUMAN !! | ||||||
* 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 P3IP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of P3IP1_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT SER-39 AND ASN-66, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY. | |
| O-linked Glycosylation | |
| Reference | PubMed |
| "Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT SER-39 AND ASN-66, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY. | |
