UniProt ID | UTR1_YEAST | |
---|---|---|
UniProt AC | P21373 | |
Protein Name | NAD(+) kinase | |
Gene Name | UTR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 530 | |
Subcellular Localization | ||
Protein Description | Specifically phosphorylates NAD in the presence of ATP, dATP, or CTP as phosphoryl donors.. | |
Protein Sequence | MKENDMNNGVDKWVNEEDGRNDHHNNNNNLMKKAMMNNEQIDRTQDIDNAKEMLRKISSESSSRRSSLLNKDSSLVNGNANSGGGTSINGTRGSSKSSNTHFQYASTAYGVRMLSKDISNTKVELDVENLMIVTKLNDVSLYFLTRELVEWVLVHFPRVTVYVDSELKNSKKFAAGELCEDSKCRESRIKYWTKDFIREHDVFFDLVVTLGGDGTVLFVSSIFQRHVPPVMSFSLGSLGFLTNFKFEHFREDLPRIMNHKIKTNLRLRLECTIYRRHRPEVDPNTGKKICVVEKLSTHHILNEVTIDRGPSPFLSMLELYGDGSLMTVAQADGLIAATPTGSTAYSLSAGGSLVCPTVNAIALTPICPHALSFRPIILPESINLKVKVSMKSRAPAWAAFDGKDRIELQKGDFITICASPYAFPTVEASPDEFINSISRQLNWNVREQQKSFTHILSQKNQEKYAHEANKVRNQAEPLEVIRDKYSLEADATKENNNGSDDESDDESVNCEACKLKPSSVPKPSQARFSV | |
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 |
---|---|---|---|---|---|
58 | Phosphorylation | KEMLRKISSESSSRR HHHHHHHHCCCHHHH | 30.96 | 20377248 | |
59 | Phosphorylation | EMLRKISSESSSRRS HHHHHHHCCCHHHHH | 44.99 | 20377248 | |
61 | Phosphorylation | LRKISSESSSRRSSL HHHHHCCCHHHHHHH | 35.25 | 20377248 | |
62 | Phosphorylation | RKISSESSSRRSSLL HHHHCCCHHHHHHHC | 24.66 | 20377248 | |
63 | Phosphorylation | KISSESSSRRSSLLN HHHCCCHHHHHHHCC | 40.78 | 20377248 | |
66 | Phosphorylation | SESSSRRSSLLNKDS CCCHHHHHHHCCCCC | 24.99 | 20377248 | |
67 | Phosphorylation | ESSSRRSSLLNKDSS CCHHHHHHHCCCCCC | 34.76 | 19823750 | |
73 | Phosphorylation | SSLLNKDSSLVNGNA HHHCCCCCCCCCCCC | 27.47 | 20377248 | |
74 | Phosphorylation | SLLNKDSSLVNGNAN HHCCCCCCCCCCCCC | 46.61 | 22369663 | |
82 | Phosphorylation | LVNGNANSGGGTSIN CCCCCCCCCCCCCCC | 36.08 | 22369663 | |
86 | Phosphorylation | NANSGGGTSINGTRG CCCCCCCCCCCCCCC | 29.70 | 22369663 | |
87 | Phosphorylation | ANSGGGTSINGTRGS CCCCCCCCCCCCCCC | 19.82 | 22369663 | |
91 | Phosphorylation | GGTSINGTRGSSKSS CCCCCCCCCCCCCCC | 27.63 | 22369663 | |
94 | Phosphorylation | SINGTRGSSKSSNTH CCCCCCCCCCCCCCC | 31.16 | 22369663 | |
95 | Phosphorylation | INGTRGSSKSSNTHF CCCCCCCCCCCCCCC | 39.10 | 22369663 | |
96 | Ubiquitination | NGTRGSSKSSNTHFQ CCCCCCCCCCCCCCC | 60.65 | 17644757 | |
97 | Phosphorylation | GTRGSSKSSNTHFQY CCCCCCCCCCCCCCH | 30.67 | 22369663 | |
98 | Phosphorylation | TRGSSKSSNTHFQYA CCCCCCCCCCCCCHH | 49.86 | 22369663 | |
100 | Phosphorylation | GSSKSSNTHFQYAST CCCCCCCCCCCHHHH | 26.47 | 22369663 | |
104 | Phosphorylation | SSNTHFQYASTAYGV CCCCCCCHHHHHHHH | 11.11 | 22369663 | |
106 | Phosphorylation | NTHFQYASTAYGVRM CCCCCHHHHHHHHHH | 14.50 | 22369663 | |
107 | Phosphorylation | THFQYASTAYGVRML CCCCHHHHHHHHHHE | 18.74 | 22369663 | |
109 | Phosphorylation | FQYASTAYGVRMLSK CCHHHHHHHHHHEEC | 19.08 | 22369663 | |
165 | Phosphorylation | RVTVYVDSELKNSKK CEEEEECHHHCCCCC | 34.48 | 27017623 | |
451 | Phosphorylation | NVREQQKSFTHILSQ CHHHHHHHHHHHHHH | 30.92 | 22369663 | |
453 | Phosphorylation | REQQKSFTHILSQKN HHHHHHHHHHHHHHH | 18.33 | 22369663 | |
470 | Ubiquitination | KYAHEANKVRNQAEP HHHHHHHHHHCCCCC | 50.01 | 23749301 | |
499 | Phosphorylation | TKENNNGSDDESDDE CCCCCCCCCCCCCCC | 43.97 | 21440633 | |
503 | Phosphorylation | NNGSDDESDDESVNC CCCCCCCCCCCCCCC | 58.31 | 21440633 | |
507 | Phosphorylation | DDESDDESVNCEACK CCCCCCCCCCCHHCC | 26.14 | 21551504 | |
518 | Phosphorylation | EACKLKPSSVPKPSQ HHCCCCCCCCCCCCC | 42.24 | 20377248 | |
519 | Phosphorylation | ACKLKPSSVPKPSQA HCCCCCCCCCCCCCC | 51.47 | 20377248 | |
524 | Phosphorylation | PSSVPKPSQARFSV- CCCCCCCCCCCCCC- | 42.47 | 21440633 | |
529 | Phosphorylation | KPSQARFSV------ CCCCCCCCC------ | 22.74 | 21440633 |
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 UTR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UTR1_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 UTR1_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-74; SER-97; SER-98;THR-100; SER-499; SER-503 AND SER-518, 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-59; SER-67; SER-97 ANDSER-98, AND MASS SPECTROMETRY. | |
"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-63 AND SER-67, AND MASSSPECTROMETRY. |