Tag | Content |
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CPLM ID | CPLM-003938 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Repressible alkaline phosphatase |
Protein Synonyms/Alias | Membrane-bound repressible alkaline phosphatase; Soluble alkaline phosphatase; Farnesyl diphosphatase |
Gene Name | PHO8 |
Gene Synonyms/Alias | YDR481C; D8035.24 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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432 | SKIENFIKHEILEKD | acetylation | [1] |
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Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional 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. |
Sequence Annotation | ACT_SITE 123 123 Phosphoserine intermediate (By METAL 75 75 Magnesium (By similarity). METAL 75 75 Zinc 2 (By similarity). METAL 174 174 Magnesium (By similarity). METAL 176 176 Magnesium (By similarity). METAL 325 325 Magnesium (By similarity). METAL 330 330 Zinc 1 (By similarity). METAL 334 334 Zinc 1 (By similarity). METAL 373 373 Zinc 2 (By similarity). METAL 374 374 Zinc 2 (By similarity). METAL 484 484 Zinc 1 (By similarity). MOD_RES 123 123 Phosphoserine. CARBOHYD 268 268 N-linked (GlcNAc...). CARBOHYD 401 401 N-linked (GlcNAc...). |
Keyword | Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase; Magnesium; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Vacuole; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 566 AA |
Protein Sequence | MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ LAFPSSFALR 60 SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI LTLDEHFIGS SRTRSSDSLV 120 TDSAAGATAF ACALKSYNGA IGVDPHHRPC GTVLEAAKLA GYLTGLVVTT RITDATPASF 180 SSHVDYRWQE DLIATHQLGE YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL 240 IDEAQSNGWQ YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV 300 KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE AFQYVLEFAE 360 NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA NATHSGEFLK RKLVDFVHEH 420 KGASSKIENF IKHEILEKDL GIYDYTDSDL ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT 480 THGHSAVDVN IYAYANKKAT WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK 540 HTSDFDATEI ASEVQHYDEY YHELTN 566 |
Gene Ontology | GO:0000329; C:fungal-type vacuole membrane; IDA:SGD. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0004035; F:alkaline phosphatase activity; IDA:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0019204; F:nucleotide phosphatase activity; IDA:SGD. GO:0046496; P:nicotinamide nucleotide metabolic process; IMP:SGD. GO:0006470; P:protein dephosphorylation; IDA:SGD. |
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