UniProt ID | BAP2_YEAST | |
---|---|---|
UniProt AC | P38084 | |
Protein Name | Leu/Val/Ile amino-acid permease | |
Gene Name | BAP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 609 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
Protein Description | Permease for leucine, valine and isoleucine. Also transports cysteine, methionine, phenyalanine, tyrosine and tryptophan.. | |
Protein Sequence | MLSSEDFGSSGKKETSPDSISIRSFSAGNNFQSSSSEKTYSKQKSGSDKLIHRFADSFKRAEGSTTRTKQINENTSDLEDGVESITSDSKLKKSMKSRHVVMMSLGTGIGTGLLVANAKGLHYGGPAALIIGYILVSFVTYFMIQAAGEMAVTYPTLPANFNAYSSIFISKSFGFATVWLYCFQWLTVLPLELITASMTIQFWNDKINPDIYILIFYVFLVFIHFFGVKAYGETEFIFNCCKILMIAGFIILSIVINCGGAGNDGYIGATYWHNPGAFAGDTSIGRFKNVCYILVTAYFSFGGMELFALSVQEQSNPRKSTPVAAKRSIYRIVVIYLLTMILIGFNVPYNDDQLMGAGGSATHASPYVLAASIHGVKIVPHIINAVILISVVSVANSSLYAGPRLICSLAQQGYAPKFLDYVDREGRPLRALIVCCVFGVIAFVAASSKEEIVFTWLAAIAGLSELFTWTSIMLSHLRFRQAMKVQGRSLDELGYKATTGIWGSIYGVFFNILVFVAQFWVALAPLGNGGKCDAESFFQNYLAFPIWLAFYFGYMVYNRDFTLLNPLDKIDLDFHRRIYDPELMRQEDEENKEKLRNMSLMRKAYHFWC | |
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 | -----MLSSEDFGSS -----CCCCCCCCCC | 30.31 | 22369663 | |
4 | Phosphorylation | ----MLSSEDFGSSG ----CCCCCCCCCCC | 36.90 | 22369663 | |
9 | Phosphorylation | LSSEDFGSSGKKETS CCCCCCCCCCCCCCC | 35.59 | 29136822 | |
10 | Phosphorylation | SSEDFGSSGKKETSP CCCCCCCCCCCCCCC | 55.82 | 23749301 | |
12 | Ubiquitination | EDFGSSGKKETSPDS CCCCCCCCCCCCCCC | 49.76 | 23749301 | |
13 | Ubiquitination | DFGSSGKKETSPDSI CCCCCCCCCCCCCCE | 70.52 | 23749301 | |
15 | Phosphorylation | GSSGKKETSPDSISI CCCCCCCCCCCCEEE | 55.21 | 22369663 | |
16 | Phosphorylation | SSGKKETSPDSISIR CCCCCCCCCCCEEEE | 28.00 | 22369663 | |
19 | Phosphorylation | KKETSPDSISIRSFS CCCCCCCCEEEEEEC | 22.94 | 22369663 | |
21 | Phosphorylation | ETSPDSISIRSFSAG CCCCCCEEEEEECCC | 18.85 | 22369663 | |
24 | Phosphorylation | PDSISIRSFSAGNNF CCCEEEEEECCCCCC | 23.14 | 22369663 | |
26 | Phosphorylation | SISIRSFSAGNNFQS CEEEEEECCCCCCCC | 36.19 | 22369663 | |
33 | Phosphorylation | SAGNNFQSSSSEKTY CCCCCCCCCCCCCCC | 28.22 | 27017623 | |
34 | Phosphorylation | AGNNFQSSSSEKTYS CCCCCCCCCCCCCCC | 27.40 | 27017623 | |
35 | Phosphorylation | GNNFQSSSSEKTYSK CCCCCCCCCCCCCCC | 48.00 | 23749301 | |
38 | Ubiquitination | FQSSSSEKTYSKQKS CCCCCCCCCCCCCCC | 55.50 | 23749301 | |
41 | Phosphorylation | SSSEKTYSKQKSGSD CCCCCCCCCCCCCCH | 33.57 | 19779198 | |
42 | Ubiquitination | SSEKTYSKQKSGSDK CCCCCCCCCCCCCHH | 51.86 | 22817900 | |
57 | Phosphorylation | LIHRFADSFKRAEGS HHHHHHHHHHHCCCC | 29.27 | 30377154 | |
59 | Ubiquitination | HRFADSFKRAEGSTT HHHHHHHHHCCCCCC | 55.43 | 23749301 | |
69 | Ubiquitination | EGSTTRTKQINENTS CCCCCCCCCCCCCCC | 45.98 | 23749301 | |
75 | Phosphorylation | TKQINENTSDLEDGV CCCCCCCCCCCHHHH | 19.89 | 22369663 | |
76 | Phosphorylation | KQINENTSDLEDGVE CCCCCCCCCCHHHHH | 52.35 | 22369663 | |
84 | Phosphorylation | DLEDGVESITSDSKL CCHHHHHHHHCCHHH | 28.85 | 22369663 | |
86 | Phosphorylation | EDGVESITSDSKLKK HHHHHHHHCCHHHHH | 35.44 | 22369663 | |
87 | Phosphorylation | DGVESITSDSKLKKS HHHHHHHCCHHHHHH | 37.91 | 22369663 | |
89 | Phosphorylation | VESITSDSKLKKSMK HHHHHCCHHHHHHHH | 39.39 | 22369663 | |
111 | Phosphorylation | SLGTGIGTGLLVANA ECCCCCCCCHHHHCC | 23.80 | 24909858 | |
489 | Phosphorylation | AMKVQGRSLDELGYK HHHCCCCCHHHHCCC | 47.17 | 28889911 | |
579 | Phosphorylation | LDFHRRIYDPELMRQ CCHHHHHCCHHHHHC | 24.51 | 19779198 | |
599 | Phosphorylation | KEKLRNMSLMRKAYH HHHHHHHHHHHHHHH | 23.67 | 19795423 | |
609 | S-palmitoylation | RKAYHFWC------- HHHHHHCC------- | 3.80 | 16751107 |
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 BAP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BAP2_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 BAP2_YEAST !! |
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 SER-3; SER-4; THR-15;SER-16; SER-19; SER-21; SER-24 AND SER-76, AND MASS 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 SER-16 AND SER-19, AND MASSSPECTROMETRY. | |
"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-15 AND SER-24, AND MASSSPECTROMETRY. |