UniProt ID | AFI1_YEAST | |
---|---|---|
UniProt AC | Q99222 | |
Protein Name | ARF3-interacting protein 1 | |
Gene Name | AFI1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 893 | |
Subcellular Localization | Cytoplasm, perinuclear region. Cytoplasm, cell cortex. Enriched at the nuclear envelope and at the plasma membrane, especially in daughter cells and at the bud neck. | |
Protein Description | Involved in actin patch polarization. Required for maintaining a proper budding pattern in yeast cells. Required for proper polarized localization of the ADP-ribosylation factor ARF3 at the plasma membrane.. | |
Protein Sequence | MLRRELNNSISNRSIENESFPFERPNVSYIISAEFDNKLGPILKHQYPKDIPGFNQFSHEQRNGNTSVSMNLASLMIPSSIERNPGKQDITVFTLYYNKFTQNYQLFPVPKDPRFSFNLHHREQSDGSVTNSIYYDAENHQDAKNNRYTIVLEDDELECQEVQNNQKAIDNEPLFFINVANTVLDTTNDRGAVIKSIAIGTPLKTFFAFKNIIVLVLDLYMKAPTQAAATDILLDCFNMLNSIDLTLINDIHSKSSIQEVLHSIHDESIITKVFLDPDSTLKKLFCINGFDTKDKYGNIVTFHDQLIQYHFTRFQPKTLPPFLLKIPLQFNMIRREPIYIENDYNELVLKFLDKFVPYLLKAGQKVNAWKLVINSTKLSKEDLCAFILSLANITATYASDPQSYFKGNAALIFPYMDISLVDGLRAYVASNSDFVGCFAIIGTANPIFRYQLDIWDYYYDVDEGVFYENNSPEKEKPDTVAEVKIGPNPLRKIFNRPHFSTNAVNESQVNLGQKLFSLLIDEYHDSDTIMSVLRRLNVLQLENLLDALKRREIPPNIALKDEYIMFYKDFFIFPEFFDYFTLHSIELLSNLDNCLFSLGNTCQLFSTEQIYSQLSQILDIVKELFRMVSVSRTNIEKFLNACLNYSPFKILPTAQLHGDNISRWSFESEVRQGFDNFNSYMGIEKDPHGVIVSAIDLFTQIYSFDILAFFLTFITKESGQDLPFTKSLSRRRTYLTRIAQSSSLRQFLQLSTRPNIRILGGNGQGTGNSNYPEFTNASSVISPKLRASPLLERRASKICYAITKLLYRLECHPIGMALLKKYLHNQLREAYLESKRHFISKKGDSTNTSSTIASSSFAGASVPLSSNESGMLNGLKQINEQQESTLETTQKED | |
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 |
---|---|---|---|---|---|
9 | Phosphorylation | LRRELNNSISNRSIE CHHHHHHCCCCCCCC | 26.73 | 28889911 | |
14 | Phosphorylation | NNSISNRSIENESFP HHCCCCCCCCCCCCC | 38.21 | 27214570 | |
101 | Phosphorylation | TLYYNKFTQNYQLFP EEEEECCCCCEEEEC | 19.95 | 29734811 | |
104 | Phosphorylation | YNKFTQNYQLFPVPK EECCCCCEEEECCCC | 9.22 | 29734811 | |
125 | Phosphorylation | NLHHREQSDGSVTNS ECCCCCCCCCCEEEE | 38.90 | 23749301 | |
128 | Phosphorylation | HREQSDGSVTNSIYY CCCCCCCCEEEEEEE | 30.66 | 23749301 | |
130 | Phosphorylation | EQSDGSVTNSIYYDA CCCCCCEEEEEEEEC | 25.58 | 23749301 | |
132 | Phosphorylation | SDGSVTNSIYYDAEN CCCCEEEEEEEECCC | 11.55 | 23749301 | |
144 | Ubiquitination | AENHQDAKNNRYTIV CCCCCCHHCCCEEEE | 64.15 | 23749301 | |
255 | Phosphorylation | INDIHSKSSIQEVLH HCCCCCCHHHHHHHH | 35.37 | 27017623 | |
256 | Phosphorylation | NDIHSKSSIQEVLHS CCCCCCHHHHHHHHH | 31.84 | 27017623 | |
280 | Phosphorylation | VFLDPDSTLKKLFCI EEECCCCHHHHHHEE | 50.40 | 27017623 | |
404 | Phosphorylation | YASDPQSYFKGNAAL ECCCHHHHHCCCEEE | 12.22 | 28132839 | |
741 | Phosphorylation | YLTRIAQSSSLRQFL HHHHHHHCHHHHHHH | 16.93 | 30377154 |
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 AFI1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AFI1_YEAST !! |
* 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 AFI1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY. |