UniProt ID | YAT2_YEAST | |
---|---|---|
UniProt AC | P40017 | |
Protein Name | Carnitine O-acetyltransferase YAT2 | |
Gene Name | YAT2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 923 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Involved in the shutteling of acetyl-CoA in the cell.. | |
Protein Sequence | MSSGSTIVSSDKSGRTFKHEEELPKLPLPKLCDTLQRLKESLEPLYYADGYYQHPLDPEQIEKLSSIIRDFEENPVSEKLQSKLQSYHDTRDCYLDELHLDINNQTSTREIQDDVLPRNPFLVLADDALPNITQADRSAVLVHSAARFISALKQDLLPPDINATNGKPLSMAPFLNLFGTTRSPVFQRGEVENFDLNKPYTASDLEDPDYSSDEDDNDEPTQKDFDDRKRKHEEDIFTGNGITIKRHPDSKHILIISRGQYYTLEVLDSTNKIIYTAAELTTIFNHIIKDSSGIEKSTALGSLTSHSFRNWKYARKRLQKRYPNELHRIDSALFVLVLDESQEETTNDGDDTADISQMFNRTITERDKKCTSANCKRVFYGTSIINSKGHQVGSCVSRWYDKLQLVVTADAKATVIWDSFTCDGSVVLRFTSEIYTESVLRLARDVNAGDPQFSLWPNVTQMDPETKKLMTATISADGGGPSEIDPKLVVNKIDWSFSNILNTHVHLSETKLADLISKYDIVRASIPLGRRSAQRLGVKPDSMVQVALQIAHYALYGRMVFGLEPVSTRGFKNSRSSFINIQSQALLELCQLFISSSIDGTDKLDKFIQTCETHNNMVKHAKSGVGYEKHFNALKYLFKFHDHFGIHLSGDESSAAKDLFENPLVLPFSQPELIVANCGNAATTTFGITPAVPHGFGIGYIIKDDQVDLTVTSQFRQGDRLMFMLSWVLGEIRSYWRMSRGTSHNKTGVKISPVVDKLYEMDNAVNNPPKRNGHTVNGSRKTSSSSQVNLNRYGGFFDLEGHIDSRNISKTPSMKNLQKTFNGLTMSADNDHSSSAVSVPTEKEKLNTGHEILQIQPREVASNGLEADDETDIEIVAGNADGTSSSASSATSLNSKKRNVINSRFDIDFDRSRVGRKVATLDQ | |
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 | Acetylation | ------MSSGSTIVS ------CCCCCEEEC | 43.32 | 22814378 | |
2 | Phosphorylation | ------MSSGSTIVS ------CCCCCEEEC | 43.32 | 30377154 | |
5 | Phosphorylation | ---MSSGSTIVSSDK ---CCCCCEEECCCC | 19.53 | 30377154 | |
9 | Phosphorylation | SSGSTIVSSDKSGRT CCCCEEECCCCCCCC | 29.03 | 28889911 | |
200 | Phosphorylation | NFDLNKPYTASDLED CCCCCCCCCHHHCCC | 19.29 | 22369663 | |
201 | Phosphorylation | FDLNKPYTASDLEDP CCCCCCCCHHHCCCC | 28.36 | 22369663 | |
203 | Phosphorylation | LNKPYTASDLEDPDY CCCCCCHHHCCCCCC | 34.62 | 22369663 | |
210 | Phosphorylation | SDLEDPDYSSDEDDN HHCCCCCCCCCCCCC | 18.57 | 22369663 | |
211 | Phosphorylation | DLEDPDYSSDEDDND HCCCCCCCCCCCCCC | 38.40 | 22369663 | |
212 | Phosphorylation | LEDPDYSSDEDDNDE CCCCCCCCCCCCCCC | 38.50 | 22369663 | |
221 | Phosphorylation | EDDNDEPTQKDFDDR CCCCCCCCCCCCHHH | 46.32 | 22369663 | |
251 | 2-Hydroxyisobutyrylation | IKRHPDSKHILIISR EEECCCCCEEEEEEC | 41.88 | - | |
368 | Acetylation | RTITERDKKCTSANC HHCCHHHHCCCCCCC | 56.84 | 25381059 | |
747 | Phosphorylation | RGTSHNKTGVKISPV CCCCCCCCCCEECCH | 53.15 | 28889911 | |
752 | Phosphorylation | NKTGVKISPVVDKLY CCCCCEECCHHHHHH | 13.11 | 22369663 | |
779 | Phosphorylation | NGHTVNGSRKTSSSS CCCCCCCCCCCCCCC | 25.96 | 30377154 | |
782 | Phosphorylation | TVNGSRKTSSSSQVN CCCCCCCCCCCCCEE | 32.50 | 22369663 | |
783 | Phosphorylation | VNGSRKTSSSSQVNL CCCCCCCCCCCCEEE | 31.12 | 22369663 | |
784 | Phosphorylation | NGSRKTSSSSQVNLN CCCCCCCCCCCEEEE | 38.96 | 22369663 | |
785 | Phosphorylation | GSRKTSSSSQVNLNR CCCCCCCCCCEEEEC | 25.26 | 22369663 | |
786 | Phosphorylation | SRKTSSSSQVNLNRY CCCCCCCCCEEEECC | 39.84 | 22369663 | |
805 | Phosphorylation | DLEGHIDSRNISKTP ECCCCCCCCCCCCCC | 26.99 | 27214570 | |
809 | Phosphorylation | HIDSRNISKTPSMKN CCCCCCCCCCCCHHH | 33.74 | 22369663 | |
811 | Phosphorylation | DSRNISKTPSMKNLQ CCCCCCCCCCHHHHH | 17.50 | 22369663 | |
813 | Phosphorylation | RNISKTPSMKNLQKT CCCCCCCCHHHHHHH | 47.85 | 22369663 | |
820 | Phosphorylation | SMKNLQKTFNGLTMS CHHHHHHHHCCEEEC | 14.90 | 22369663 | |
825 | Phosphorylation | QKTFNGLTMSADNDH HHHHCCEEECCCCCC | 15.52 | 29734811 | |
827 | Phosphorylation | TFNGLTMSADNDHSS HHCCEEECCCCCCCC | 27.51 | 22369663 | |
833 | Phosphorylation | MSADNDHSSSAVSVP ECCCCCCCCCCCCCC | 28.93 | 22369663 | |
834 | Phosphorylation | SADNDHSSSAVSVPT CCCCCCCCCCCCCCC | 20.92 | 22369663 | |
835 | Phosphorylation | ADNDHSSSAVSVPTE CCCCCCCCCCCCCCH | 35.39 | 22369663 | |
838 | Phosphorylation | DHSSSAVSVPTEKEK CCCCCCCCCCCHHHH | 23.30 | 22369663 | |
841 | Phosphorylation | SSAVSVPTEKEKLNT CCCCCCCCHHHHCCC | 58.49 | 29734811 | |
903 | Phosphorylation | KKRNVINSRFDIDFD CCCCCHHCCCCCCCC | 24.17 | 27214570 | |
920 | Phosphorylation | RVGRKVATLDQ---- HCCCEEEECCC---- | 33.58 | 30377154 |
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 YAT2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YAT2_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 YAT2_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 SER-784; SER-786 ANDSER-833, 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 THR-782 AND SER-786, ANDMASS SPECTROMETRY. |