UniProt ID | ACK1_YEAST | |
---|---|---|
UniProt AC | Q07622 | |
Protein Name | Activator of C kinase protein 1 | |
Gene Name | ACK1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 623 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MVNQGQPQPNLYDKHINMFPPARARESSHKLGNANSDRHGLPAQNIVPAPYPVDDSIVELTPAIPFTSPSSSSSLSLPLSALNFTDGNADGGQLGTPVTINSNNGMDIFNSKPTGEIGYANNGTNSTGSRYELPFNFSSTKESLGSPAVQDASISSGNRISESVRDNSAPPPYEESESRILQEKVYRTEEKAPIRPLNNNPVPPQKINQPPTGSAKTDDNGSSGGEDKLSSYSPEALAFYQVYKKTITDSSKFTPEIQMQWCETLLTYAFNEDFISQYNINAEKLKRSLKPEEMLKNQKVILEHSFKVLTKLITLKWPPAMYLMGTLYSHQPYLPIKNKNIVIKNDEKALEYYCKAAKLNNSDACYRAGVCFEYQRGTSSLDPSPTKEQCIKKAFQYYQHGAEVCSNSACMYKLGMSHLYGLNMQKTDVLLAIKWFDKAAQKGDSPQTLYELGKIYEFSVLPPEIQNLLFANGIRKDSQLAIKYYQQCAKDFEYPLAQWKLGNCYEFGDLGLPVVAKKSIYWYSKAAAAQPKGNPMAMLSLSGWYLTGAPNILKPNNKEAFNWALKSSKCSDGKLARTEFALGFYYEKGVGCEVDLDLAKQYYQRAARMGFRKAVDALRSLTN | |
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 |
---|---|---|---|---|---|
127 | Phosphorylation | ANNGTNSTGSRYELP ECCCCCCCCCCEECC | 41.04 | 21551504 | |
141 | Ubiquitination | PFNFSSTKESLGSPA CCCCCCCCHHHCCCC | 47.45 | 23749301 | |
143 | Phosphorylation | NFSSTKESLGSPAVQ CCCCCCHHHCCCCCC | 39.32 | 17563356 | |
146 | Phosphorylation | STKESLGSPAVQDAS CCCHHHCCCCCCCCC | 18.25 | 28152593 | |
153 | Phosphorylation | SPAVQDASISSGNRI CCCCCCCCCCCCCCC | 31.15 | 28889911 | |
155 | Phosphorylation | AVQDASISSGNRISE CCCCCCCCCCCCCCH | 29.69 | 28889911 | |
156 | Phosphorylation | VQDASISSGNRISES CCCCCCCCCCCCCHH | 38.12 | 28889911 | |
163 | Phosphorylation | SGNRISESVRDNSAP CCCCCCHHHCCCCCC | 18.70 | 29136822 | |
168 | Phosphorylation | SESVRDNSAPPPYEE CHHHCCCCCCCCCCH | 46.58 | 29136822 | |
184 | Ubiquitination | ESRILQEKVYRTEEK HHHHHHHHHHCCCCC | 31.44 | 23749301 | |
191 | Ubiquitination | KVYRTEEKAPIRPLN HHHCCCCCCCCCCCC | 53.91 | 23749301 | |
216 | Ubiquitination | QPPTGSAKTDDNGSS CCCCCCCCCCCCCCC | 54.93 | 23749301 | |
217 | Phosphorylation | PPTGSAKTDDNGSSG CCCCCCCCCCCCCCC | 48.58 | 21551504 | |
222 | Phosphorylation | AKTDDNGSSGGEDKL CCCCCCCCCCCCCCH | 31.87 | 21551504 | |
230 | Phosphorylation | SGGEDKLSSYSPEAL CCCCCCHHHCCHHHH | 32.73 | 30377154 | |
231 | Phosphorylation | GGEDKLSSYSPEALA CCCCCHHHCCHHHHH | 39.81 | 30377154 | |
232 | Phosphorylation | GEDKLSSYSPEALAF CCCCHHHCCHHHHHH | 25.52 | 30377154 | |
233 | Phosphorylation | EDKLSSYSPEALAFY CCCHHHCCHHHHHHH | 20.43 | 30377154 | |
240 | Phosphorylation | SPEALAFYQVYKKTI CHHHHHHHHHHHHHC | 7.46 | 30377154 | |
243 | Phosphorylation | ALAFYQVYKKTITDS HHHHHHHHHHHCCCH | 7.40 | 30377154 | |
310 | Phosphorylation | EHSFKVLTKLITLKW HHHHHHHHHHHHCCC | 27.13 | 19779198 | |
314 | Phosphorylation | KVLTKLITLKWPPAM HHHHHHHHCCCCHHH | 32.49 | 19795423 | |
406 | Phosphorylation | QHGAEVCSNSACMYK HHHHHHCCCCHHHHH | 38.71 | 28889911 | |
408 | Phosphorylation | GAEVCSNSACMYKLG HHHHCCCCHHHHHHC | 13.42 | 28889911 | |
417 | Phosphorylation | CMYKLGMSHLYGLNM HHHHHCCHHHHCCCC | 14.45 | 30377154 | |
420 | Phosphorylation | KLGMSHLYGLNMQKT HHCCHHHHCCCCCCC | 17.72 | 27214570 | |
427 | Phosphorylation | YGLNMQKTDVLLAIK HCCCCCCCHHHHHHH | 17.91 | 30377154 | |
540 | Phosphorylation | GNPMAMLSLSGWYLT CCCCEEEEECCEECC | 13.85 | 21551504 | |
542 | Phosphorylation | PMAMLSLSGWYLTGA CCEEEEECCEECCCC | 24.73 | 21551504 | |
622 | Phosphorylation | VDALRSLTN------ HHHHHHHCC------ | 39.88 | 20377248 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACK1_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 ACK1_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-155, 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-143, 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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-184, AND MASSSPECTROMETRY. |