| UniProt ID | KICH_YEAST | |
|---|---|---|
| UniProt AC | P20485 | |
| Protein Name | Choline kinase | |
| Gene Name | CKI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 582 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Responsible for phosphatidylcholine synthesis via the CDP-choline pathway. Also exhibits ethanolamine kinase activity but at 14% efficiency compared with choline.. | |
| Protein Sequence | MVQESRPGSVRSYSVGYQARSRSSSQRRHSLTRQRSSQRLIRTISIESDVSNITDDDDLRAVNEGVAGVQLDVSETANKGPRRASATDVTDSLGSTSSEYIEIPFVKETLDASLPSDYLKQDILNLIQSLKISKWYNNKKIQPVAQDMNLVKISGAMTNAIFKVEYPKLPSLLLRIYGPNIDNIIDREYELQILARLSLKNIGPSLYGCFVNGRFEQFLENSKTLTKDDIRNWKNSQRIARRMKELHVGVPLLSSERKNGSACWQKINQWLRTIEKVDQWVGDPKNIENSLLCENWSKFMDIVDRYHKWLISQEQGIEQVNKNLIFCHNDAQYGNLLFTAPVMNTPSLYTAPSSTSLTSQSSSLFPSSSNVIVDDIINPPKQEQSQDSKLVVIDFEYAGANPAAYDLANHLSEWMYDYNNAKAPHQCHADRYPDKEQVLNFLYSYVSHLRGGAKEPIDEEVQRLYKSIIQWRPTVQLFWSLWAILQSGKLEKKEASTAITREEIGPNGKKYIIKTEPESPEEDFVENDDEPEAGVSIDTFDYMAYGRDKIAVFWGDLIGLGIITEEECKNFSSFKFLDTSYL | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MVQESRPGSVRS ---CCCCCCCCCCEE | 27.04 | 30377154 | |
| 9 | Phosphorylation | VQESRPGSVRSYSVG CCCCCCCCCEEECCE | 19.62 | 28889911 | |
| 12 | Phosphorylation | SRPGSVRSYSVGYQA CCCCCCEEECCEEEE | 21.43 | 22890988 | |
| 13 | Phosphorylation | RPGSVRSYSVGYQAR CCCCCEEECCEEEEC | 9.23 | 22890988 | |
| 14 | Phosphorylation | PGSVRSYSVGYQARS CCCCEEECCEEEECC | 15.43 | 22369663 | |
| 17 | Phosphorylation | VRSYSVGYQARSRSS CEEECCEEEECCCCH | 9.24 | 22890988 | |
| 25 | Phosphorylation | QARSRSSSQRRHSLT EECCCCHHHHHHCHH | 29.02 | 28889911 | |
| 30 | Phosphorylation | SSSQRRHSLTRQRSS CHHHHHHCHHHHHHH | 29.62 | 28889911 | |
| 37 | Phosphorylation | SLTRQRSSQRLIRTI CHHHHHHHHHHHHEE | 22.85 | 28889911 | |
| 43 | Phosphorylation | SSQRLIRTISIESDV HHHHHHHEEEEECCH | 16.45 | 22890988 | |
| 45 | Phosphorylation | QRLIRTISIESDVSN HHHHHEEEEECCHHC | 21.49 | 21082442 | |
| 48 | Phosphorylation | IRTISIESDVSNITD HHEEEEECCHHCCCC | 41.46 | 22890988 | |
| 51 | Phosphorylation | ISIESDVSNITDDDD EEEECCHHCCCCHHH | 27.75 | 19795423 | |
| 54 | Phosphorylation | ESDVSNITDDDDLRA ECCHHCCCCHHHHHH | 37.31 | 19795423 | |
| 85 | Phosphorylation | NKGPRRASATDVTDS CCCCCCCCCCCCCCC | 29.86 | 22369663 | |
| 87 | Phosphorylation | GPRRASATDVTDSLG CCCCCCCCCCCCCCC | 28.62 | 22369663 | |
| 90 | Phosphorylation | RASATDVTDSLGSTS CCCCCCCCCCCCCCC | 23.76 | 22369663 | |
| 92 | Phosphorylation | SATDVTDSLGSTSSE CCCCCCCCCCCCCCC | 25.84 | 22369663 | |
| 95 | Phosphorylation | DVTDSLGSTSSEYIE CCCCCCCCCCCCEEE | 30.34 | 22369663 | |
| 96 | Phosphorylation | VTDSLGSTSSEYIEI CCCCCCCCCCCEEEC | 34.18 | 22369663 | |
| 97 | Phosphorylation | TDSLGSTSSEYIEIP CCCCCCCCCCEEECC | 23.91 | 22369663 | |
| 98 | Phosphorylation | DSLGSTSSEYIEIPF CCCCCCCCCEEECCC | 34.21 | 22369663 | |
| 100 | Phosphorylation | LGSTSSEYIEIPFVK CCCCCCCEEECCCCC | 13.05 | 22369663 | |
| 131 | Acetylation | LNLIQSLKISKWYNN HHHHHHHCCHHHHCC | 50.62 | 24489116 | |
| 168 | Ubiquitination | IFKVEYPKLPSLLLR EEECCCCCCCHHHHH | 72.61 | 24961812 | |
| 168 | Acetylation | IFKVEYPKLPSLLLR EEECCCCCCCHHHHH | 72.61 | 24489116 | |
| 198 | Phosphorylation | LQILARLSLKNIGPS HHHHHHHHHCCCCHH | 31.57 | 28889911 | |
| 236 | Phosphorylation | DIRNWKNSQRIARRM HHHHHHHHHHHHHHH | 19.67 | 28889911 | |
| 273 | Phosphorylation | KINQWLRTIEKVDQW HHHHHHHHHHHHHHH | 31.17 | 28889911 | |
| 276 | Acetylation | QWLRTIEKVDQWVGD HHHHHHHHHHHHHCC | 47.46 | 24489116 | |
| 454 | Ubiquitination | SHLRGGAKEPIDEEV HHHCCCCCCCCCHHH | 68.26 | 23749301 | |
| 515 | Phosphorylation | GKKYIIKTEPESPEE CCEEEEECCCCCCHH | 46.49 | 24961812 | |
| 519 | Phosphorylation | IIKTEPESPEEDFVE EEECCCCCCHHHCCC | 48.61 | 24961812 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 30 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 30 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 85 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 85 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KICH_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 KICH_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-45; SER-51; THR-54;SER-85; SER-95; THR-96; SER-97 AND SER-98, 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-85; THR-90 AND SER-92,AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-85, AND MASSSPECTROMETRY. | |
| "Phosphorylation of Saccharomyces cerevisiae choline kinase on Ser30and Ser85 by protein kinase A regulates phosphatidylcholine synthesisby the CDP-choline pathway."; Yu Y., Sreenivas A., Ostrander D.B., Carman G.M.; J. Biol. Chem. 277:34978-34986(2002). Cited for: PHOSPHORYLATION AT SER-30 AND SER-85, AND MUTAGENESIS OF SER-30 ANDSER-85. | |