| UniProt ID | ASI1_YEAST | |
|---|---|---|
| UniProt AC | P54074 | |
| Protein Name | Protein ASI1 | |
| Gene Name | ASI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 624 | |
| Subcellular Localization |
Nucleus inner membrane Multi-pass membrane protein . |
|
| Protein Description | Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals.. | |
| Protein Sequence | MNSSTSSENVFINSFSYLNQTSQAVISGNSTFANVINFPYRLGLSFIGAVNLQYEQTVKSEEIPPTLRSVFDTIGFFFSPYAIFCFVIAIVLNRFVVFYAVLNNGSRRTLPLWLSNVFHVSAVVVLAMVSLGPLTLGKDFKILGDPAFAQEKFLLNIFYAFAYSYCVETIFTIMRNSSPLEGTDYSLFELSIQFYTMTNNNTKFLDSPDYIIDCSMAILSRILIHLVEIFRLRNYRLLFSTIMNLCHICYLGIRVKQGGWKSLPFSVKFRHFPKLFSVSIICLSLLIFKLSCLIRWDPFGKSRNSCELLQFYPLSRNWKKYLNYTGEEDFSAMATKFALLLCSGTELMEKGIRREFPAINIPDNVNEKFFISGYLNELSKPYKENTSISFPKKNSSILKQRFFLMFPKSIIWIMKKLVGQVFFGFRDNKDEDIPDNDPSKMLKITKTNSLNNSAGHKEDIELELLNTSDDEYSEDYEPSEVESLGDSDEENLEEDSLIFNETRDALLDLFSSEDNEVHTDYNWIMSTSRILQQKLLSDKTLTRASILDTKLSEVDETFGTESDFDLSCAVCKVNERNTVLWPCRCFAICEDCRISLGLRGFSTCVCCRSKVHGYCKVHPVSDSK | |
| 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 | N-linked_Glycosylation | ------MNSSTSSEN ------CCCCCCCCC | 44.67 | 16735580 | |
| 19 | N-linked_Glycosylation | INSFSYLNQTSQAVI ECEEHHHCCCCCEEC | 34.55 | 16735580 | |
| 29 | N-linked_Glycosylation | SQAVISGNSTFANVI CCEECCCCCHHHHHC | 30.96 | 16735580 | |
| 447 | Phosphorylation | KMLKITKTNSLNNSA HHHHEEECCCCCCCC | 22.76 | 28889911 | |
| 449 | Phosphorylation | LKITKTNSLNNSAGH HHEEECCCCCCCCCC | 37.39 | 28889911 | |
| 562 | Phosphorylation | DETFGTESDFDLSCA CHHHCCCCCCCEEEE | 43.33 | 27214570 |
| 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 ASI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASI1_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 ASI1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function inconcert to maintain the latent properties of transcription factorsStp1 and Stp2."; Zargari A., Boban M., Heessen S., Andreasson C., Thyberg J.,Ljungdahl P.O.; J. Biol. Chem. 282:594-605(2007). Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-2; ASN-19 ANDASN-29, AND INTERACTION WITH ASI3. | |
| "Asi1 is an inner nuclear membrane protein that restricts promoteraccess of two latent transcription factors."; Boban M., Zargari A., Andreasson C., Heessen S., Thyberg J.,Ljungdahl P.O.; J. Cell Biol. 173:695-707(2006). Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-2; ASN-19 ANDASN-29, TOPOLOGY, AND MUTAGENESIS OF CYS-583 AND CYS-585. | |