UniProt ID | GIP2_YEAST | |
---|---|---|
UniProt AC | P40036 | |
Protein Name | GLC7-interacting protein 2 | |
Gene Name | GIP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 548 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MYIKAEQKPQQFERKNEKLDRNKNQQLPDLETDFKGYRVNSDLYNKERDGSTEETLNSLKFLHKPQRVTQMRANRFPEEEVQRNTDLNKRIFSAGNDENVDNESGWSKIAAAKNHTSVESLNGSTRPPFKIELPPLSPKSTVPKSFQAEYPEAKSPGNDMNFEYDEEILIPFAPPVYKKSGELLKSSLKRRSKSLPTTPGIRSGNGVQARDGSPMLIRSKSVHFDQAAPVKYFAEDESPINVNKTEQHDNCLSFKHKPVNLMVDPEEETKMLSSGLETTSIDDDLTTVAPKGFAHPAKISNPNNGKGTNNTKLRKSKRFQNLLKNRTDMPPSKSNKKFVNGGGAHEISDRNSKNYHVVGLYSKNFPILSNKNPKSLKLNIFINLSQNKKVFLQELSLYIHRDNNYFSNSSSFYNIPNSHNGNDCNGVAKGYNAGCTRLIAGRILVKNIFYDKRVVVRYTWDSWRTTHEVECVYISDGDGILPGTNMDIFHFIIDDVSKVDPRGKLEFCIHYSTRNDYEREEYWDNNNGNNYKVDVVMDGFNDPFAAAA | |
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 |
---|---|---|---|---|---|
41 | Phosphorylation | FKGYRVNSDLYNKER CCCCCCCHHHCCCCC | 26.57 | 22369663 | |
44 | Phosphorylation | YRVNSDLYNKERDGS CCCCHHHCCCCCCCC | 29.22 | 19779198 | |
51 | Phosphorylation | YNKERDGSTEETLNS CCCCCCCCHHHHHHH | 36.61 | 22369663 | |
52 | Phosphorylation | NKERDGSTEETLNSL CCCCCCCHHHHHHHH | 43.29 | 22369663 | |
55 | Phosphorylation | RDGSTEETLNSLKFL CCCCHHHHHHHHHHH | 25.63 | 22369663 | |
104 | Phosphorylation | DENVDNESGWSKIAA CCCCCCCCHHHHHHH | 52.39 | 30377154 | |
116 | Phosphorylation | IAAAKNHTSVESLNG HHHHCCCCCHHHCCC | 43.81 | 22369663 | |
117 | Phosphorylation | AAAKNHTSVESLNGS HHHCCCCCHHHCCCC | 19.14 | 22369663 | |
120 | Phosphorylation | KNHTSVESLNGSTRP CCCCCHHHCCCCCCC | 25.61 | 22369663 | |
124 | Phosphorylation | SVESLNGSTRPPFKI CHHHCCCCCCCCEEE | 21.85 | 22369663 | |
125 | Phosphorylation | VESLNGSTRPPFKIE HHHCCCCCCCCEEEE | 48.90 | 22369663 | |
137 | Phosphorylation | KIELPPLSPKSTVPK EEECCCCCCCCCCCH | 35.74 | 22369663 | |
155 | Phosphorylation | AEYPEAKSPGNDMNF ECCCCCCCCCCCCCC | 45.12 | 22369663 | |
164 | Phosphorylation | GNDMNFEYDEEILIP CCCCCCCCCCCEEEC | 25.23 | 30377154 | |
186 | Phosphorylation | KSGELLKSSLKRRSK CCHHHHHHHHHHHHC | 40.65 | 19547744 | |
192 | Phosphorylation | KSSLKRRSKSLPTTP HHHHHHHHCCCCCCC | 30.54 | 29136822 | |
194 | Phosphorylation | SLKRRSKSLPTTPGI HHHHHHCCCCCCCCC | 40.61 | 22369663 | |
197 | Phosphorylation | RRSKSLPTTPGIRSG HHHCCCCCCCCCCCC | 51.41 | 22369663 | |
198 | Phosphorylation | RSKSLPTTPGIRSGN HHCCCCCCCCCCCCC | 19.99 | 22369663 | |
203 | Phosphorylation | PTTPGIRSGNGVQAR CCCCCCCCCCCCCCC | 34.39 | 24961812 | |
213 | Phosphorylation | GVQARDGSPMLIRSK CCCCCCCCCEEEEEE | 16.07 | 22369663 | |
219 | Phosphorylation | GSPMLIRSKSVHFDQ CCCEEEEEEEEECCC | 23.45 | 22369663 | |
221 | Phosphorylation | PMLIRSKSVHFDQAA CEEEEEEEEECCCCC | 23.28 | 22369663 | |
238 | Phosphorylation | KYFAEDESPINVNKT EEEECCCCCCCCCCC | 43.32 | 21440633 | |
245 | Phosphorylation | SPINVNKTEQHDNCL CCCCCCCCCCCCCCC | 35.36 | 19779198 | |
273 | Phosphorylation | EEETKMLSSGLETTS HHHHHHHHCCCCCCC | 20.89 | 29136822 | |
274 | Phosphorylation | EETKMLSSGLETTSI HHHHHHHCCCCCCCC | 43.36 | 29136822 | |
278 | Phosphorylation | MLSSGLETTSIDDDL HHHCCCCCCCCCCCC | 30.77 | 29136822 | |
279 | Phosphorylation | LSSGLETTSIDDDLT HHCCCCCCCCCCCCC | 17.82 | 24961812 | |
280 | Phosphorylation | SSGLETTSIDDDLTT HCCCCCCCCCCCCCC | 31.29 | 29136822 | |
286 | Phosphorylation | TSIDDDLTTVAPKGF CCCCCCCCCCCCCCC | 26.64 | 29136822 | |
287 | Phosphorylation | SIDDDLTTVAPKGFA CCCCCCCCCCCCCCC | 23.20 | 29136822 | |
300 | Phosphorylation | FAHPAKISNPNNGKG CCCCCCCCCCCCCCC | 45.59 | 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 GIP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GIP2_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 GIP2_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PP12_YEAST | GLC7 | physical | 11805837 | |
GYS2_YEAST | GSY2 | physical | 11805837 | |
PHSG_YEAST | GPH1 | physical | 11805837 | |
MDHM_YEAST | MDH1 | physical | 11805837 | |
GDE_YEAST | GDB1 | physical | 11805837 | |
POP2_YEAST | POP2 | genetic | 17322879 | |
SLX5_YEAST | SLX5 | genetic | 27708008 | |
FYV10_YEAST | FYV10 | genetic | 27708008 | |
ELF1_YEAST | ELF1 | genetic | 27708008 | |
TBP6_YEAST | YTA6 | genetic | 27708008 |
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-51; SER-137; SER-194;SER-219; SER-221 AND SER-238, 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-194, 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-221, AND MASSSPECTROMETRY. |