| UniProt ID | AIF1L_HUMAN | |
|---|---|---|
| UniProt AC | Q9BQI0 | |
| Protein Name | Allograft inflammatory factor 1-like | |
| Gene Name | AIF1L | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 150 | |
| Subcellular Localization |
Cytoplasm, cytoskeleton . Cell projection, ruffle membrane Peripheral membrane protein Cytoplasmic side . Colocalizes with F-actin. Partially relocates to membrane ruffles in response to invading bacteria. |
|
| Protein Description | Actin-binding protein that promotes actin bundling. May neither bind calcium nor depend on calcium for function.. | |
| Protein Sequence | MSGELSNRFQGGKAFGLLKARQERRLAEINREFLCDQKYSDEENLPEKLTAFKEKYMEFDLNNEGEIDLMSLKRMMEKLGVPKTHLEMKKMISEVTGGVSDTISYRDFVNMMLGKRSAVLKLVMMFEGKANESSPKPVGPPPERDIASLP | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSGELSNRF ------CCCCCCHHC | 40.76 | 21406692 | |
| 2 | Acetylation | ------MSGELSNRF ------CCCCCCHHC | 40.76 | 21406692 | |
| 2 (in isoform 2) | Phosphorylation | - | 40.76 | 24719451 | |
| 6 | Phosphorylation | --MSGELSNRFQGGK --CCCCCCHHCCCCH | 22.96 | 21406692 | |
| 6 (in isoform 2) | Phosphorylation | - | 22.96 | 27251275 | |
| 8 | Methylation | MSGELSNRFQGGKAF CCCCCCHHCCCCHHH | 23.14 | 115368561 | |
| 13 (in isoform 4) | Ubiquitination | - | 47.57 | 21890473 | |
| 13 (in isoform 3) | Ubiquitination | - | 47.57 | 21890473 | |
| 13 (in isoform 1) | Ubiquitination | - | 47.57 | 21890473 | |
| 13 (in isoform 2) | Ubiquitination | - | 47.57 | 21890473 | |
| 13 | Ubiquitination | SNRFQGGKAFGLLKA CHHCCCCHHHHHHHH | 47.57 | 32015554 | |
| 13 | Acetylation | SNRFQGGKAFGLLKA CHHCCCCHHHHHHHH | 47.57 | 90925 | |
| 19 | Ubiquitination | GKAFGLLKARQERRL CHHHHHHHHHHHHHH | 46.71 | - | |
| 38 | Ubiquitination | REFLCDQKYSDEENL HHHHHCCCCCCCCCC | 33.21 | 32015554 | |
| 40 | Phosphorylation | FLCDQKYSDEENLPE HHHCCCCCCCCCCHH | 45.65 | - | |
| 48 | Ubiquitination | DEENLPEKLTAFKEK CCCCCHHHHHHHHHH | 49.55 | 29967540 | |
| 56 | Phosphorylation | LTAFKEKYMEFDLNN HHHHHHHHHCCCCCC | 11.72 | 25690035 | |
| 64 | Ubiquitination | MEFDLNNEGEIDLMS HCCCCCCCCCCCHHH | 58.07 | 32015554 | |
| 74 | Ubiquitination | IDLMSLKRMMEKLGV CCHHHHHHHHHHHCC | 34.67 | 29967540 | |
| 84 | Phosphorylation | EKLGVPKTHLEMKKM HHHCCCHHHHHHHHH | 26.14 | 23403867 | |
| 133 | Phosphorylation | FEGKANESSPKPVGP HCCCCCCCCCCCCCC | 52.31 | 30266825 | |
| 134 | Phosphorylation | EGKANESSPKPVGPP CCCCCCCCCCCCCCC | 30.66 | 30266825 | |
| 148 | Phosphorylation | PPERDIASLP----- CCCCCCCCCC----- | 41.32 | 28102081 | |
| 159 (in isoform 2) | Phosphorylation | - | 21406692 | ||
| 160 (in isoform 2) | Phosphorylation | - | 24719451 |
| 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 AIF1L_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AIF1L_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 AIF1L_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of AIF1L_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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