UniProt ID | PHO84_YEAST | |
---|---|---|
UniProt AC | P25297 | |
Protein Name | Inorganic phosphate transporter PHO84 | |
Gene Name | PHO84 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 587 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | High-affinity transporter for external inorganic phosphate. Is not an essential protein, since a constitutive, low affinity pI transporter exists in yeast.. | |
Protein Sequence | MSSVNKDTIHVAERSLHKEHLTEGGNMAFHNHLNDFAHIEDPLERRRLALESIDDEGFGWQQVKTISIAGVGFLTDSYDIFAINLGITMMSYVYWHGSMPGPSQTLLKVSTSVGTVIGQFGFGTLADIVGRKRIYGMELIIMIVCTILQTTVAHSPAINFVAVLTFYRIVMGIGIGGDYPLSSIITSEFATTKWRGAIMGAVFANQAWGQISGGIIALILVAAYKGELEYANSGAECDARCQKACDQMWRILIGLGTVLGLACLYFRLTIPESPRYQLDVNAKLELAAAAQEQDGEKKIHDTSDEDMAINGLERASTAVESLDNHPPKASFKDFCRHFGQWKYGKILLGTAGSWFTLDVAFYGLSLNSAVILQTIGYAGSKNVYKKLYDTAVGNLILICAGSLPGYWVSVFTVDIIGRKPIQLAGFIILTALFCVIGFAYHKLGDHGLLALYVICQFFQNFGPNTTTFIVPGECFPTRYRSTAHGISAASGKVGAIIAQTALGTLIDHNCARDGKPTNCWLPHVMEIFALFMLLGIFTTLLIPETKRKTLEEINELYHDEIDPATLNFRNKNNDIESSSPSQLQHEA | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSVNKDTI ------CCCCCHHHH | 42.89 | 22369663 | |
3 | Phosphorylation | -----MSSVNKDTIH -----CCCCCHHHHH | 28.54 | 22369663 | |
6 | Ubiquitination | --MSSVNKDTIHVAE --CCCCCHHHHHHHH | 54.84 | 17644757 | |
8 | Phosphorylation | MSSVNKDTIHVAERS CCCCCHHHHHHHHHH | 18.00 | 22369663 | |
15 | Phosphorylation | TIHVAERSLHKEHLT HHHHHHHHHCHHHCC | 26.74 | 17330950 | |
18 | Ubiquitination | VAERSLHKEHLTEGG HHHHHHCHHHCCCCC | 52.72 | 22817900 | |
22 | Phosphorylation | SLHKEHLTEGGNMAF HHCHHHCCCCCCCCC | 34.20 | 28889911 | |
64 | Ubiquitination | GFGWQQVKTISIAGV CCCCCEEEEEEEEEE | 35.48 | 17644757 | |
108 | Ubiquitination | GPSQTLLKVSTSVGT CCCHHEEEEECCCHH | 36.93 | 17644757 | |
132 | Ubiquitination | LADIVGRKRIYGMEL HHHHHCCCCCCCHHH | 36.90 | 17644757 | |
283 | Ubiquitination | YQLDVNAKLELAAAA CCCCHHHHHHHHHHH | 36.97 | 17644757 | |
297 | Ubiquitination | AQEQDGEKKIHDTSD HHHHCCCCCCCCCCH | 63.66 | 22817900 | |
298 | Ubiquitination | QEQDGEKKIHDTSDE HHHCCCCCCCCCCHH | 40.76 | 22817900 | |
302 | Phosphorylation | GEKKIHDTSDEDMAI CCCCCCCCCHHHHHH | 24.74 | 17330950 | |
303 | Phosphorylation | EKKIHDTSDEDMAIN CCCCCCCCHHHHHHH | 45.09 | 17330950 | |
316 | Phosphorylation | INGLERASTAVESLD HHHHHHHHHHHHHHH | 24.10 | 17330950 | |
317 | Phosphorylation | NGLERASTAVESLDN HHHHHHHHHHHHHHC | 33.46 | 17330950 | |
321 | Phosphorylation | RASTAVESLDNHPPK HHHHHHHHHHCCCCC | 34.13 | 17330950 | |
328 | Ubiquitination | SLDNHPPKASFKDFC HHHCCCCCCCHHHHH | 62.20 | 17644757 | |
332 | Ubiquitination | HPPKASFKDFCRHFG CCCCCCHHHHHHHCC | 47.61 | 17644757 | |
492 | Ubiquitination | GISAASGKVGAIIAQ CCHHCCCCHHHHHHH | 34.69 | 17644757 | |
546 | Ubiquitination | TLLIPETKRKTLEEI HHHCHHHHHHHHHHH | 50.68 | 17644757 | |
548 | Ubiquitination | LIPETKRKTLEEINE HCHHHHHHHHHHHHH | 60.04 | 17644757 | |
571 | Ubiquitination | ATLNFRNKNNDIESS HHCCCCCCCCCCCCC | 53.52 | 22817900 | |
577 | Phosphorylation | NKNNDIESSSPSQLQ CCCCCCCCCCHHHHC | 36.13 | 22369663 | |
578 | Phosphorylation | KNNDIESSSPSQLQH CCCCCCCCCHHHHCC | 33.21 | 22369663 | |
579 | Phosphorylation | NNDIESSSPSQLQHE CCCCCCCCHHHHCCC | 37.54 | 22369663 | |
581 | Phosphorylation | DIESSSPSQLQHEA- CCCCCCHHHHCCCC- | 45.53 | 22369663 |
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 PHO84_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHO84_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 PHO84_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 THR-22; THR-302; SER-303;SER-316; THR-317; SER-321; SER-577; SER-578; SER-579 AND SER-581, ANDMASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-321 ANDSER-578, 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 THR-302; SER-303; SER-316;THR-317; SER-321; SER-577; SER-579 AND SER-581, AND MASS SPECTROMETRY. | |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302; SER-303; THR-317;SER-321 AND SER-579, UBIQUITINATION AT LYS-6 AND LYS-298, AND MASSSPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302; SER-303; THR-317;SER-321 AND SER-579, UBIQUITINATION AT LYS-6 AND LYS-298, AND MASSSPECTROMETRY. |