GIP2_YEAST - dbPTM
GIP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
41PhosphorylationFKGYRVNSDLYNKER
CCCCCCCHHHCCCCC
26.5722369663
44PhosphorylationYRVNSDLYNKERDGS
CCCCHHHCCCCCCCC
29.2219779198
51PhosphorylationYNKERDGSTEETLNS
CCCCCCCCHHHHHHH
36.6122369663
52PhosphorylationNKERDGSTEETLNSL
CCCCCCCHHHHHHHH
43.2922369663
55PhosphorylationRDGSTEETLNSLKFL
CCCCHHHHHHHHHHH
25.6322369663
104PhosphorylationDENVDNESGWSKIAA
CCCCCCCCHHHHHHH
52.3930377154
116PhosphorylationIAAAKNHTSVESLNG
HHHHCCCCCHHHCCC
43.8122369663
117PhosphorylationAAAKNHTSVESLNGS
HHHCCCCCHHHCCCC
19.1422369663
120PhosphorylationKNHTSVESLNGSTRP
CCCCCHHHCCCCCCC
25.6122369663
124PhosphorylationSVESLNGSTRPPFKI
CHHHCCCCCCCCEEE
21.8522369663
125PhosphorylationVESLNGSTRPPFKIE
HHHCCCCCCCCEEEE
48.9022369663
137PhosphorylationKIELPPLSPKSTVPK
EEECCCCCCCCCCCH
35.7422369663
155PhosphorylationAEYPEAKSPGNDMNF
ECCCCCCCCCCCCCC
45.1222369663
164PhosphorylationGNDMNFEYDEEILIP
CCCCCCCCCCCEEEC
25.2330377154
186PhosphorylationKSGELLKSSLKRRSK
CCHHHHHHHHHHHHC
40.6519547744
192PhosphorylationKSSLKRRSKSLPTTP
HHHHHHHHCCCCCCC
30.5429136822
194PhosphorylationSLKRRSKSLPTTPGI
HHHHHHCCCCCCCCC
40.6122369663
197PhosphorylationRRSKSLPTTPGIRSG
HHHCCCCCCCCCCCC
51.4122369663
198PhosphorylationRSKSLPTTPGIRSGN
HHCCCCCCCCCCCCC
19.9922369663
203PhosphorylationPTTPGIRSGNGVQAR
CCCCCCCCCCCCCCC
34.3924961812
213PhosphorylationGVQARDGSPMLIRSK
CCCCCCCCCEEEEEE
16.0722369663
219PhosphorylationGSPMLIRSKSVHFDQ
CCCEEEEEEEEECCC
23.4522369663
221PhosphorylationPMLIRSKSVHFDQAA
CEEEEEEEEECCCCC
23.2822369663
238PhosphorylationKYFAEDESPINVNKT
EEEECCCCCCCCCCC
43.3221440633
245PhosphorylationSPINVNKTEQHDNCL
CCCCCCCCCCCCCCC
35.3619779198
273PhosphorylationEEETKMLSSGLETTS
HHHHHHHHCCCCCCC
20.8929136822
274PhosphorylationEETKMLSSGLETTSI
HHHHHHHCCCCCCCC
43.3629136822
278PhosphorylationMLSSGLETTSIDDDL
HHHCCCCCCCCCCCC
30.7729136822
279PhosphorylationLSSGLETTSIDDDLT
HHCCCCCCCCCCCCC
17.8224961812
280PhosphorylationSSGLETTSIDDDLTT
HCCCCCCCCCCCCCC
31.2929136822
286PhosphorylationTSIDDDLTTVAPKGF
CCCCCCCCCCCCCCC
26.6429136822
287PhosphorylationSIDDDLTTVAPKGFA
CCCCCCCCCCCCCCC
23.2029136822
300PhosphorylationFAHPAKISNPNNGKG
CCCCCCCCCCCCCCC
45.5921440633

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIP2_YEAST !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP12_YEASTGLC7physical
11805837
GYS2_YEASTGSY2physical
11805837
PHSG_YEASTGPH1physical
11805837
MDHM_YEASTMDH1physical
11805837
GDE_YEASTGDB1physical
11805837
POP2_YEASTPOP2genetic
17322879
SLX5_YEASTSLX5genetic
27708008
FYV10_YEASTFYV10genetic
27708008
ELF1_YEASTELF1genetic
27708008
TBP6_YEASTYTA6genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GIP2_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP