GID7_YEAST - dbPTM
GID7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GID7_YEAST
UniProt AC P25569
Protein Name Glucose-induced degradation protein 7
Gene Name GID7
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 745
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Has a role in the negative regulation of gluconeogenesis. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase)..
Protein Sequence MSHTNKIAYVLNNDTEETASPSSVGCFDKKQLTKLLIHTLKELGYDSAANQLLLESGGYQNESNHIQTFFKLIKTGQFHLINWQIVCSLPLAHSSPLRSEWLQRLLIPTPTPATTSLFDHMLLQLQYLQQLMSSVNSSTCSDAEIATLRNYVEIMILVNRQIFLEFFHPVTNSASHKGPHTALPVLYLRKILKNFIEIWDSLLVSNDQFLNEENIFNPETTLRELSTYLTNPKLTAQLNLERDHLIDAISKYIDPNELVPKGRLLHLLKQAIKYQQSQDIFNIIDPDDDASFSSPPHRINLLQDNFSHDLTVTFQEWKTIQDTTDEIWFLTFSPNGKYLASATSESSRGYFITVYDVEQDFKIYKTCVSLSQSVLYLMFSPDSRYLVACPFSEDVTIYDMNATSLPDASATDSFLLYPSTRLSPMDSFKLDTTTYPDDTESSASSSSRPANANSNQSRVWCCDAFHTAERAGWMVVGSPDREAIVHSLTTKESLFSLKGRTCIALGHDENISGRKSIDPAKVLYKPTSSNGNWQYVEDDETFPRVHDVKISYDDKYVLLMTHQGVIDVYDFSGFPSKEELSKQTVDPKNFLIPRIARLDVGKNMTCISLPLNTTHQGFHRQQISESQHLVLVSLQDNELQMWDYKENILIQKYFGQKQQHFIIRSCFAYGNKLVMSGSEDGKIYIWDRIRGNLVSVLSGHSTVMSNSTKPMGKNCNVVASNPADKEMFASGGDDGKIKIWKISRN
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
15PhosphorylationAYVLNNDTEETASPS
EEECCCCCCCCCCCC		37.5321440633
20PhosphorylationNDTEETASPSSVGCF
CCCCCCCCCCCCCCC		32.5023749301
269AcetylationGRLLHLLKQAIKYQQ
HHHHHHHHHHHHHHH		44.0024489116
274PhosphorylationLLKQAIKYQQSQDIF
HHHHHHHHHHCCCHH		12.9829136822
277PhosphorylationQAIKYQQSQDIFNII
HHHHHHHCCCHHCCC		17.8129136822
291PhosphorylationIDPDDDASFSSPPHR
CCCCCCCCCCCCCHH		32.4329136822
293PhosphorylationPDDDASFSSPPHRIN
CCCCCCCCCCCHHEE		39.1729136822
294PhosphorylationDDDASFSSPPHRINL
CCCCCCCCCCHHEEC		40.2017563356
423PhosphorylationLYPSTRLSPMDSFKL
ECCCCCCCCCCCCCC		18.1928889911
439PhosphorylationTTTYPDDTESSASSS
CCCCCCCCCCCCCCC		45.1823749301
441PhosphorylationTYPDDTESSASSSSR
CCCCCCCCCCCCCCC		33.0423749301
442PhosphorylationYPDDTESSASSSSRP
CCCCCCCCCCCCCCC		26.4128889911
444PhosphorylationDDTESSASSSSRPAN
CCCCCCCCCCCCCCC		32.4717563356
445PhosphorylationDTESSASSSSRPANA
CCCCCCCCCCCCCCC		31.8619779198
447PhosphorylationESSASSSSRPANANS
CCCCCCCCCCCCCCC		44.2023749301
457PhosphorylationANANSNQSRVWCCDA
CCCCCCCCCEEECHH		32.8127017623
493PhosphorylationHSLTTKESLFSLKGR
EECCCHHHHHHCCCC		35.9528889911
725UbiquitinationVASNPADKEMFASGG
EECCHHCHHHHHCCC		53.8623749301
725AcetylationVASNPADKEMFASGG
EECCHHCHHHHHCCC		53.8624489116
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 GID7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GID7_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 GID7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXT7_YEASTHXT7physical
11805837
GID8_YEASTGID8physical
11805837
RMD5_YEASTRMD5physical
11805837
FYV10_YEASTFYV10physical
11805837
VID30_YEASTVID30physical
11805837
VID28_YEASTVID28physical
11805837
VATA_YEASTVMA1physical
11805837
MOH1_YEASTMOH1physical
11805837
SHS1_YEASTSHS1physical
11805837
GID4_YEASTVID24physical
11805837
CTF19_YEASTCTF19physical
11805837
UME1_YEASTUME1physical
11805837
GID7_YEASTGID7physical
18467557
SCS7_YEASTSCS7genetic
27708008
MDM12_YEASTMDM12genetic
27708008
ALDH6_YEASTALD6physical
25172955
MDHC_YEASTMDH2physical
25172955
ADH1_YEASTADH1physical
25172955
RS15_YEASTRPS15physical
25172955
SSB2_YEASTSSB2physical
25172955
RS3_YEASTRPS3physical
25172955
RS7B_YEASTRPS7Bphysical
25172955
GID8_YEASTGID8physical
25172955
RS17A_YEASTRPS17Aphysical
25172955
RLA0_YEASTRPP0physical
25172955
HSP60_YEASTHSP60physical
25172955
EF3A_YEASTYEF3physical
25172955
RSSA2_YEASTRPS0Bphysical
25172955
PDC1_YEASTPDC1physical
25172955
HSP72_YEASTSSA2physical
25172955
PMG1_YEASTGPM1physical
25172955
ALF_YEASTFBA1physical
25172955
RS5_YEASTRPS5physical
25172955
G3P2_YEASTTDH2physical
25172955
RS14B_YEASTRPS14Bphysical
25172955
FYV10_YEASTFYV10physical
25172955
VID28_YEASTVID28physical
25172955
ENO2_YEASTENO2physical
25172955
G3P3_YEASTTDH3physical
25172955
CBS_YEASTCYS4physical
25172955
PDC6_YEASTPDC6physical
25172955
VID30_YEASTVID30physical
25172955
RL7A_YEASTRPL7Aphysical
25172955
METK2_YEASTSAM2physical
25172955
RL12A_YEASTRPL12Bphysical
25172955
RL12B_YEASTRPL12Bphysical
25172955
EF2_YEASTEFT2physical
25172955
EXG2_YEASTEXG2physical
25172955
RMD5_YEASTRMD5physical
25172955
RS13_YEASTRPS13physical
25172955
RL4B_YEASTRPL4Bphysical
25172955
SSB1_YEASTSSB1physical
25172955
YD176_YEASTYDL176Wphysical
25172955
COPA_YEASTCOP1physical
25172955
CDC48_YEASTCDC48physical
25172955
RL13A_YEASTRPL13Aphysical
25172955
MPG1_YEASTPSA1physical
25172955
PGK_YEASTPGK1physical
25172955
MCM7_YEASTMCM7physical
25172955
RS6A_YEASTRPS6Bphysical
25172955
RS6B_YEASTRPS6Bphysical
25172955
GID4_YEASTVID24physical
25172955
KPYK1_YEASTCDC19physical
25172955
HSP71_YEASTSSA1physical
25172955
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GID7_YEAST

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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-291 AND SER-293, ANDMASS 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-294 AND SER-444, ANDMASS SPECTROMETRY.

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