UniProt ID | PPB_YEAST | |
---|---|---|
UniProt AC | P11491 | |
Protein Name | Repressible alkaline phosphatase | |
Gene Name | PHO8 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 566 | |
Subcellular Localization |
Repressible alkaline phosphatase: Vacuole membrane Single-pass membrane protein. The full-length version is found in lysosome-like vacuoles. Soluble alkaline phosphatase: Cytoplasm. The truncated version of the protein is soluble. |
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Protein Description | Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase. [PubMed: 1848184] | |
Protein Sequence | MMTHTLPSEQTRLVPGSDSSSRPKKRRISKRSKIIVSTVVCIGLLLVLVQLAFPSSFALRSASHKKKNVIFFVTDGMGPASLSMARSFNQHVNDLPIDDILTLDEHFIGSSRTRSSDSLVTDSAAGATAFACALKSYNGAIGVDPHHRPCGTVLEAAKLAGYLTGLVVTTRITDATPASFSSHVDYRWQEDLIATHQLGEYPLGRVVDLLMGGGRSHFYPQGEKASPYGHHGARKDGRDLIDEAQSNGWQYVGDRKNFDSLLKSHGENVTLPFLGLFADNDIPFEIDRDEKEYPSLKEQVKVALGALEKASNEDKDSNGFFLMVEGSRIDHAGHQNDPASQVREVLAFDEAFQYVLEFAENSDTETVLVSTSDHETGGLVTSRQVTASYPQYVWYPQVLANATHSGEFLKRKLVDFVHEHKGASSKIENFIKHEILEKDLGIYDYTDSDLETLIHLDDNANAIQDKLNDMVSFRAQIGWTTHGHSAVDVNIYAYANKKATWSYVLNNLQGNHENTEVGQFLENFLELNLNEVTDLIRDTKHTSDFDATEIASEVQHYDEYYHELTN | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MMTHTLPSEQ -----CCCCCCCCCC | 15.48 | 27017623 | |
5 | Phosphorylation | ---MMTHTLPSEQTR ---CCCCCCCCCCCC | 31.06 | 27017623 | |
8 | Phosphorylation | MMTHTLPSEQTRLVP CCCCCCCCCCCCCCC | 45.51 | 29136822 | |
11 | Phosphorylation | HTLPSEQTRLVPGSD CCCCCCCCCCCCCCC | 23.17 | 29136822 | |
17 | Phosphorylation | QTRLVPGSDSSSRPK CCCCCCCCCCCCCCC | 28.40 | 22369663 | |
19 | Phosphorylation | RLVPGSDSSSRPKKR CCCCCCCCCCCCCCC | 31.73 | 22369663 | |
20 | Phosphorylation | LVPGSDSSSRPKKRR CCCCCCCCCCCCCCH | 35.04 | 22369663 | |
21 | Phosphorylation | VPGSDSSSRPKKRRI CCCCCCCCCCCCCHH | 57.46 | 22369663 | |
113 | Phosphorylation | HFIGSSRTRSSDSLV HHCCCCCCCCCCCCC | 36.53 | 22369663 | |
115 | Phosphorylation | IGSSRTRSSDSLVTD CCCCCCCCCCCCCCC | 37.57 | 22890988 | |
116 | Phosphorylation | GSSRTRSSDSLVTDS CCCCCCCCCCCCCCC | 28.11 | 22890988 | |
118 | Phosphorylation | SRTRSSDSLVTDSAA CCCCCCCCCCCCCHH | 27.04 | 22890988 | |
121 | Phosphorylation | RSSDSLVTDSAAGAT CCCCCCCCCCHHHHH | 29.54 | 22369663 | |
123 | Phosphorylation | SDSLVTDSAAGATAF CCCCCCCCHHHHHHH | 15.62 | 22369663 | |
128 | Phosphorylation | TDSAAGATAFACALK CCCHHHHHHHHHHHH | 22.76 | 22890988 | |
135 | Ubiquitination | TAFACALKSYNGAIG HHHHHHHHHCCCCCC | 32.16 | 17644757 | |
268 | N-linked_Glycosylation | LLKSHGENVTLPFLG HHHHCCCCCEECEEE | 36.34 | - | |
401 | N-linked_Glycosylation | WYPQVLANATHSGEF CHHHHHCCCCCCHHH | 41.01 | - | |
432 | Acetylation | SKIENFIKHEILEKD HHHHHHHHHHHHHCC | 30.92 | 24489116 |
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 PPB_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PPB_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 PPB_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PPB_YEAST | PHO8 | physical | 19497047 | |
SVP26_YEAST | SVP26 | physical | 19497047 | |
PDX3_YEAST | PDX3 | genetic | 21623372 | |
COX9_YEAST | COX9 | genetic | 21623372 | |
COPA_YEAST | COP1 | genetic | 27708008 | |
RSP5_YEAST | RSP5 | genetic | 27708008 | |
RPN12_YEAST | RPN12 | genetic | 27708008 | |
CDC23_YEAST | CDC23 | genetic | 27708008 | |
MAK11_YEAST | MAK11 | genetic | 27708008 | |
PRI2_YEAST | PRI2 | genetic | 27708008 | |
NEP1_YEAST | EMG1 | genetic | 27708008 | |
TAD3_YEAST | TAD3 | genetic | 27708008 | |
HAS1_YEAST | HAS1 | genetic | 27708008 | |
SYA_YEAST | ALA1 | genetic | 27708008 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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 THR-121; SER-123 ANDTHR-128, AND MASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASSSPECTROMETRY. |