| UniProt ID | VIP1_YEAST | |
|---|---|---|
| UniProt AC | Q06685 | |
| Protein Name | Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase | |
| Gene Name | VIP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1146 | |
| Subcellular Localization | Cytoplasm . Cytoplasm, cytoskeleton . | |
| Protein Description | Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. [PubMed: 17412958 Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity Required for maintaining cellular integrity, normal growth and interactions with the ARP complex] | |
| Protein Sequence | MSGIKKEPIESDEVPQQETKNNLPSAPSEMSPLFLNKNTQKAMQSIAPILEGFSPKTSASENMSLKLPPPGIQDDHSEENLTVHDTLQRTISTALGNGNNTNTVTTSGLKKADSESKSEADPEGLSNSNIVNDADNINSISKTGSPHLPQGTMDAEQTNMGTNSVPTSSASSRKSSTSHPKPRLPKVGKIGVCAMDAKVLSKPMRHILNRLIEHGEFETVIFGDKVILDERIENWPTCDFLISFFSSGFPLDKAIKYVKLRKPFIINDLIMQKILWDRRLCLQVLEAYNVPTPPRLEISRDGGPRANEELRAKLREHGVEVKPVEEPEWKMVDDDTLEVDGKTMTKPFVEKPVDGEDHNIYIYYHSKNGGGGRRLFRKVGNKSSEFDPTLVHPRTEGSYIYEQFMDTDNFEDVKAYTIGENFCHAETRKSPVVDGIVRRNTHGKEVRYITELSDEEKTIAGKVSKAFSQMICGFDLLRVSGKSYVIDVNGFSFVKDNKAYYDSCANILRSTFIEAKKKMDMEKKNLPIIREEKEQKWVFKGLAIIIRHADRTPKQKFKHSFTSPIFISLLKGHKEEVVIRNVNDLKIVLQALRIALDEKAGNPAKIKVLANALEKKLNFPGTKIQLKPVLNKENEVEKVQFILKWGGEPTHSAKYQATELGEQMRQDFDLLNKSILQNIKIFSSSERRVLHTAQYWTRALFGADELGSDEISIRKDLLDDSNAAKDLMDKVKKKLKPLLREGKEAPPQFAWPSKMPEPYLVIKRVVELMNYHKKIMDNNFAKKDVNSMQTRWCTSEDPSLFKERWDKLFKEFNNAEKVDPSKISELYDTMKYDALHNRQFLENIFDPGLPNEAIADELGSHSLVDRYPINVLAKNNFKIIDSHSMNNSGKNSSNSVGSLGWVLESGKTSTARNPKSSSQFDEPRFMQLRELYKLAKVLFDFICPKEYGISDAEKLDIGLLTSLPLAKQILNDIGDMKNRETPACVAYFTKESHIYTLLNIIYESGIPMRIARNALPELDYLSQITFELYESTDASGQKSHSIRLKMSPGCHTQDPLDVQLDDRHYISCIPKISLTKHLDMDYVQQKLRNKFTRVIMPPKFTPVNITSPNLSFQKRKTRRKSVSVEKLKRPASSGSSSSTSVNKTLD | |
| 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 | Phosphorylation | ------MSGIKKEPI ------CCCCCCCCC | 61.60 | 24961812 | |
| 5 | Acetylation | ---MSGIKKEPIESD ---CCCCCCCCCCCC | 55.39 | 24489116 | |
| 6 | Acetylation | --MSGIKKEPIESDE --CCCCCCCCCCCCC | 67.79 | 24489116 | |
| 11 | Phosphorylation | IKKEPIESDEVPQQE CCCCCCCCCCCCHHH | 39.53 | 21551504 | |
| 25 | Phosphorylation | ETKNNLPSAPSEMSP HHHCCCCCCCHHCCC | 56.85 | 21126336 | |
| 28 | Phosphorylation | NNLPSAPSEMSPLFL CCCCCCCHHCCCCCC | 45.72 | 22890988 | |
| 30 | Oxidation | LPSAPSEMSPLFLNK CCCCCHHCCCCCCCC | 6.16 | 15665377 | |
| 31 | Phosphorylation | PSAPSEMSPLFLNKN CCCCHHCCCCCCCCC | 17.88 | 25521595 | |
| 37 | Acetylation | MSPLFLNKNTQKAMQ CCCCCCCCCHHHHHH | 64.62 | 22865919 | |
| 39 | Phosphorylation | PLFLNKNTQKAMQSI CCCCCCCHHHHHHHH | 32.81 | 28889911 | |
| 45 | Phosphorylation | NTQKAMQSIAPILEG CHHHHHHHHHHHHCC | 13.97 | 19823750 | |
| 54 | Phosphorylation | APILEGFSPKTSASE HHHHCCCCCCCCCCC | 36.02 | 25521595 | |
| 58 | Phosphorylation | EGFSPKTSASENMSL CCCCCCCCCCCCCCC | 35.60 | 30377154 | |
| 64 | Phosphorylation | TSASENMSLKLPPPG CCCCCCCCCCCCCCC | 33.65 | 30377154 | |
| 77 | Phosphorylation | PGIQDDHSEENLTVH CCCCCCCCCCCCCHH | 54.31 | 22369663 | |
| 82 | Phosphorylation | DHSEENLTVHDTLQR CCCCCCCCHHHHHHH | 27.63 | 22369663 | |
| 86 | Phosphorylation | ENLTVHDTLQRTIST CCCCHHHHHHHHHHH | 15.20 | 29136822 | |
| 90 | Phosphorylation | VHDTLQRTISTALGN HHHHHHHHHHHHHCC | 13.30 | 28889911 | |
| 92 | Phosphorylation | DTLQRTISTALGNGN HHHHHHHHHHHCCCC | 13.65 | 23749301 | |
| 93 | Phosphorylation | TLQRTISTALGNGNN HHHHHHHHHHCCCCC | 23.27 | 30377154 | |
| 114 | Phosphorylation | SGLKKADSESKSEAD CCCCCCCCCCCCCCC | 48.94 | 30377154 | |
| 118 | Phosphorylation | KADSESKSEADPEGL CCCCCCCCCCCCCCC | 47.50 | 21440633 | |
| 139 | Phosphorylation | NDADNINSISKTGSP CCHHHCCCCCCCCCC | 25.17 | 22369663 | |
| 141 | Phosphorylation | ADNINSISKTGSPHL HHHCCCCCCCCCCCC | 24.80 | 22369663 | |
| 143 | Phosphorylation | NINSISKTGSPHLPQ HCCCCCCCCCCCCCC | 35.78 | 22369663 | |
| 145 | Phosphorylation | NSISKTGSPHLPQGT CCCCCCCCCCCCCCC | 17.87 | 25521595 | |
| 152 | Phosphorylation | SPHLPQGTMDAEQTN CCCCCCCCCCHHHCC | 13.46 | 22369663 | |
| 158 | Phosphorylation | GTMDAEQTNMGTNSV CCCCHHHCCCCCCCC | 20.76 | 22890988 | |
| 162 | Phosphorylation | AEQTNMGTNSVPTSS HHHCCCCCCCCCCCC | 17.35 | 22890988 | |
| 164 | Phosphorylation | QTNMGTNSVPTSSAS HCCCCCCCCCCCCCC | 29.34 | 22890988 | |
| 167 | Phosphorylation | MGTNSVPTSSASSRK CCCCCCCCCCCCCCC | 32.91 | 22890988 | |
| 168 | Phosphorylation | GTNSVPTSSASSRKS CCCCCCCCCCCCCCC | 20.17 | 22890988 | |
| 169 | Phosphorylation | TNSVPTSSASSRKSS CCCCCCCCCCCCCCC | 34.35 | 22890988 | |
| 171 | Phosphorylation | SVPTSSASSRKSSTS CCCCCCCCCCCCCCC | 32.40 | 22890988 | |
| 172 | Phosphorylation | VPTSSASSRKSSTSH CCCCCCCCCCCCCCC | 43.36 | 22890988 | |
| 198 | Acetylation | GVCAMDAKVLSKPMR EEECCCHHHHCHHHH | 39.17 | 24489116 | |
| 288 | Phosphorylation | CLQVLEAYNVPTPPR HHHHHHHCCCCCCCC | 13.81 | 27017623 | |
| 495 | Acetylation | VNGFSFVKDNKAYYD ECCCEEEECCHHHHH | 54.28 | 24489116 | |
| 498 | Acetylation | FSFVKDNKAYYDSCA CEEEECCHHHHHHHH | 48.15 | 24489116 | |
| 558 | Acetylation | RTPKQKFKHSFTSPI CCHHHHHCCCCCCHH | 45.43 | 24489116 | |
| 574 | Acetylation | ISLLKGHKEEVVIRN HHHHCCCCEEEEEEC | 65.32 | 24489116 | |
| 615 | Ubiquitination | VLANALEKKLNFPGT HHHHHHHHHHCCCCC | 64.51 | 21427232 | |
| 627 | Acetylation | PGTKIQLKPVLNKEN CCCCCEEEECCCCCC | 19.39 | 24489116 | |
| 632 | Acetylation | QLKPVLNKENEVEKV EEEECCCCCCCCEEE | 58.73 | 24489116 | |
| 638 | Acetylation | NKENEVEKVQFILKW CCCCCCEEEEEEEEC | 46.65 | 24489116 | |
| 644 | Acetylation | EKVQFILKWGGEPTH EEEEEEEECCCCCCC | 38.69 | 24489116 | |
| 654 | Acetylation | GEPTHSAKYQATELG CCCCCCHHHHHHHHH | 40.69 | 24489116 | |
| 725 | Acetylation | LDDSNAAKDLMDKVK CCCCHHHHHHHHHHH | 49.32 | 24489116 | |
| 810 | Acetylation | ERWDKLFKEFNNAEK HHHHHHHHHHHCCCC | 72.35 | 24489116 | |
| 821 | Phosphorylation | NAEKVDPSKISELYD CCCCCCHHHHHHHHH | 37.85 | 27017623 | |
| 824 | Phosphorylation | KVDPSKISELYDTMK CCCHHHHHHHHHHHH | 25.86 | 26447709 | |
| 827 | Phosphorylation | PSKISELYDTMKYDA HHHHHHHHHHHHHHH | 12.81 | 26447709 | |
| 829 | Phosphorylation | KISELYDTMKYDALH HHHHHHHHHHHHHHH | 11.29 | 26447709 | |
| 882 | Phosphorylation | NNFKIIDSHSMNNSG CCEEEECCCCCCCCC | 13.67 | 23749301 | |
| 884 | Phosphorylation | FKIIDSHSMNNSGKN EEEECCCCCCCCCCC | 27.45 | 21440633 | |
| 888 | Phosphorylation | DSHSMNNSGKNSSNS CCCCCCCCCCCCCCC | 46.25 | 21440633 | |
| 892 | Phosphorylation | MNNSGKNSSNSVGSL CCCCCCCCCCCCHHH | 34.09 | 27017623 | |
| 893 | Phosphorylation | NNSGKNSSNSVGSLG CCCCCCCCCCCHHHH | 42.38 | 28889911 | |
| 895 | Phosphorylation | SGKNSSNSVGSLGWV CCCCCCCCCHHHHHH | 29.78 | 25752575 | |
| 961 | Phosphorylation | KLDIGLLTSLPLAKQ HCCHHHHHHHHHHHH | 33.01 | 30377154 | |
| 962 | Phosphorylation | LDIGLLTSLPLAKQI CCHHHHHHHHHHHHH | 28.14 | 30377154 | |
| 1086 | Acetylation | DMDYVQQKLRNKFTR CHHHHHHHHHHCCCE | 32.11 | 24489116 | |
| 1101 | Phosphorylation | VIMPPKFTPVNITSP EECCCCCCCCCCCCC | 32.24 | 22890988 | |
| 1106 | Phosphorylation | KFTPVNITSPNLSFQ CCCCCCCCCCCCCCH | 32.69 | 22369663 | |
| 1107 | Phosphorylation | FTPVNITSPNLSFQK CCCCCCCCCCCCCHH | 14.16 | 22369663 | |
| 1111 | Phosphorylation | NITSPNLSFQKRKTR CCCCCCCCCHHCCCC | 32.07 | 22890988 | |
| 1121 | Phosphorylation | KRKTRRKSVSVEKLK HCCCCCCCCCHHHCC | 20.15 | 28889911 | |
| 1123 | Phosphorylation | KTRRKSVSVEKLKRP CCCCCCCCHHHCCCC | 31.48 | 27214570 | |
| 1132 | Phosphorylation | EKLKRPASSGSSSST HHCCCCCCCCCCCCC | 37.60 | 22890988 | |
| 1133 | Phosphorylation | KLKRPASSGSSSSTS HCCCCCCCCCCCCCC | 44.81 | 22890988 | |
| 1135 | Phosphorylation | KRPASSGSSSSTSVN CCCCCCCCCCCCCCC | 29.06 | 22890988 | |
| 1136 | Phosphorylation | RPASSGSSSSTSVNK CCCCCCCCCCCCCCC | 31.65 | 22890988 | |
| 1137 | Phosphorylation | PASSGSSSSTSVNKT CCCCCCCCCCCCCCC | 39.06 | 22369663 | |
| 1138 | Phosphorylation | ASSGSSSSTSVNKTL CCCCCCCCCCCCCCC | 27.01 | 22890988 | |
| 1139 | Phosphorylation | SSGSSSSTSVNKTLD CCCCCCCCCCCCCCC | 38.35 | 22890988 | |
| 1140 | Phosphorylation | SGSSSSTSVNKTLD- CCCCCCCCCCCCCC- | 26.16 | 22369663 | |
| 1143 | Acetylation | SSSTSVNKTLD---- CCCCCCCCCCC---- | 48.59 | 22865919 |
| 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 VIP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VIP1_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 VIP1_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-31; SER-77; THR-82;SER-92; SER-139; SER-141; THR-143; SER-145; SER-895; THR-1106 ANDSER-1107, 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-143; SER-145; SER-1137;THR-1139 AND SER-1140, AND MASS SPECTROMETRY. | |
| "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-54, AND MASSSPECTROMETRY. | |
| "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-31 AND SER-1107, ANDMASS SPECTROMETRY. | |
