UniProt ID | AKR1_YEAST | |
---|---|---|
UniProt AC | P39010 | |
Protein Name | Palmitoyltransferase AKR1 | |
Gene Name | AKR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 764 | |
Subcellular Localization |
Early endosome membrane Multi-pass membrane protein. Golgi apparatus membrane Multi-pass membrane protein. |
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Protein Description | Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis of alpha-factor receptor STE2.. | |
Protein Sequence | MVNELENVPRASTLTNEEQTVDPSNNDSQEDISLGDSNEITSLASLKAIRSGNEEESGNEQVNHNDEAEEDPLLTRYHTACQRGDLATVKEMIHGKLLEVNNDGDSTEHITGLHWASINNRLSVVDFLVSQGADVNARAGALHATPLHWAARYGYVYIVDFLLKHGADPTMTDDQGFNLLHLSVNSSNIMLVLYVLFNVVSKGLLDIDCRDPKGRTSLLWAAYQGDSLTVAELLKFGASIKIADTEGFTPLHWGTVKGQPHVLKYLIQDGADFFQKTDTGKDCFAIAQEMNTVYSLREALTHSGFDYHGYPIKKWFKKSQHAKLVTFITPFLFLGIAFALFSHINPLFVIIVLFLLAIATNKGLNKFVLPSYGRMGVHNVTLLRSPLLSGVFFGTLLWVTIVWFFKVMPRTFSDEQYTNILMLVILVSVFYLFGQLVIMDPGCLPEETDHENVRQTISNLLEIGKFDTKNFCIETWIRKPLRSKFSPLNNAVVARFDHYCPWIFNDVGLKNHKAFIFFITLMESGIFTFLALCLEYFDELEDAHEDTSQKNGKCFILGASDLCSGLIYDRFVFLILLWALLQSIWVASLIFVQAFQICKGMTNTEFNVLMKESKSIGPDGLSFNENFNTTPEGFAPSIDPGEESNDTVLAPVPGSTIRKPRTCFGVCYAVTGMDQWLAVIKETIGIKDSTGHNVYSITSRIPTNYGWKRNVKDFWLTSDINAPLWRRILYPPSGSKALLNGIEVDYFKLYKLPNKDVEQGNDMV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
12 | Phosphorylation | LENVPRASTLTNEEQ CCCCCCCHHCCCCCC | 25.81 | 19795423 | |
13 | Phosphorylation | ENVPRASTLTNEEQT CCCCCCHHCCCCCCC | 36.29 | 19795423 | |
15 | Phosphorylation | VPRASTLTNEEQTVD CCCCHHCCCCCCCCC | 40.44 | 19795423 | |
20 | Phosphorylation | TLTNEEQTVDPSNND HCCCCCCCCCCCCCC | 30.10 | 19795423 | |
24 | Phosphorylation | EEQTVDPSNNDSQED CCCCCCCCCCCCHHC | 43.75 | 19795423 | |
28 | Phosphorylation | VDPSNNDSQEDISLG CCCCCCCCHHCCCCC | 37.28 | 19795423 | |
33 | Phosphorylation | NDSQEDISLGDSNEI CCCHHCCCCCCCHHH | 38.32 | 19795423 | |
37 | Phosphorylation | EDISLGDSNEITSLA HCCCCCCCHHHHHHH | 34.27 | 19795423 | |
41 | Phosphorylation | LGDSNEITSLASLKA CCCCHHHHHHHHHHH | 16.12 | 19795423 | |
42 | Phosphorylation | GDSNEITSLASLKAI CCCHHHHHHHHHHHH | 27.83 | 21440633 | |
45 | Phosphorylation | NEITSLASLKAIRSG HHHHHHHHHHHHHCC | 35.38 | 21440633 | |
51 | Phosphorylation | ASLKAIRSGNEEESG HHHHHHHCCCCCCCC | 39.60 | 22369663 | |
57 | Phosphorylation | RSGNEEESGNEQVNH HCCCCCCCCCCCCCC | 50.64 | 22369663 | |
75 | Phosphorylation | AEEDPLLTRYHTACQ HHCCCCHHHHHHHHH | 36.54 | 22369663 | |
79 | Phosphorylation | PLLTRYHTACQRGDL CCHHHHHHHHHCCCH | 21.86 | 27214570 | |
90 | Acetylation | RGDLATVKEMIHGKL CCCHHHHHHHHCCEE | 36.89 | 24489116 | |
264 | Acetylation | KGQPHVLKYLIQDGA CCCCHHHHHHHHCCC | 36.60 | 24489116 | |
465 | Acetylation | SNLLEIGKFDTKNFC HHHHHHCCCCCCCCC | 45.81 | 24489116 | |
484 | Ubiquitination | IRKPLRSKFSPLNNA HCCHHHHCCCCCCCC | 43.35 | 23749301 | |
484 | Acetylation | IRKPLRSKFSPLNNA HCCHHHHCCCCCCCC | 43.35 | 24489116 | |
755 | Ubiquitination | KLYKLPNKDVEQGND EEEECCCCCHHCCCC | 62.30 | 23749301 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of AKR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of AKR1_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 AKR1_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-51 AND SER-57, AND MASSSPECTROMETRY. | |
"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-51 AND SER-57, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, 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 SER-51 AND SER-57, AND MASSSPECTROMETRY. |