VID27_YEAST - dbPTM
VID27_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VID27_YEAST
UniProt AC P40157
Protein Name Vacuolar import and degradation protein 27
Gene Name VID27
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 782
Subcellular Localization Cytoplasm .
Protein Description Has a role in the negative regulation of gluconeogenesis. Required for vacuolar catabolite degradation of fructose-1,6-bisphosphatase (FBPase)..
Protein Sequence MNILKKFMESGNKPELITIPSGQFNLLRSKNSPKAALECIYNNATLSVRKIGKFDYELAVYRVEDDSEGGTGDEAENFEDDTISVLSTQSKKKEEEWSVEISDKIMFHKTWDKQGNVALVWENLRGDEQDEKVQFVVAADVSFSDVEQFIQTVYRCQFEVRNKKSSLTASADDLKEIEHRSTRLFVQDDDDELDSSSDDFQDAKDTSFEHEKESEILERTPSPLKKVPEGEYCCLVMSSLYMYDPIQEKFILQEPVVKVAIIDTGKYEFWLAIEGKDNRLGTQVAPNINPTFELATDAFLFNYTLQNITLSYMLKFKDLDKCIQFRFAWVKCLWMTLNKETWTDVPEKEKDYILDSSSVPLEKQFDDILHIDDRSNEERDKESSESENDSEDEDDENDHSKRIISSEAFEEPRRATSKGNSSLTVAFRNNRSYVTRDNRIGVFKTDDEDDSLEFVAAIKNISNLGGKSIDPHKPMLYMEDRNLILTDGENENKLYKMDIERGKVIEEWSTGDKNVVQYGPTKKFDQMTPEQTIVGVSQKGVFKIDPRINGKNKIAVDESKDYVGKYNFSSIGTTESGYIAIGSEKGDIKLYDRLGIRAKTAIPSLGQAIKFITTSADGKWLLATCESTLLLMDLKIKDGKNAGNIGFLKSFPASENVKTYVLKIRPEHSASILTYTKKPIRFTKAYFNTGIGQQEQTIVTSTGPYAISWSLKGILNQDGSNNYPYRIRRYNADVVADNFEFGSDKKVIVALKDDVSLSKVKSFKQPSKGVLMPSASLQDFYG
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
41PhosphorylationKAALECIYNNATLSV
HHHHHHHHCCCCEEE		17.6428889911
67PhosphorylationVYRVEDDSEGGTGDE
EEEEECCCCCCCCCC		50.9227214570
71PhosphorylationEDDSEGGTGDEAENF
ECCCCCCCCCCHHHC		52.9323749301
82PhosphorylationAENFEDDTISVLSTQ
HHHCCCCCEEEEECC		27.7230377154
84PhosphorylationNFEDDTISVLSTQSK
HCCCCCEEEEECCCC		21.0630377154
87PhosphorylationDDTISVLSTQSKKKE
CCCEEEEECCCCCCC		23.4227017623
88PhosphorylationDTISVLSTQSKKKEE
CCEEEEECCCCCCCC		32.4730377154
90PhosphorylationISVLSTQSKKKEEEW
EEEEECCCCCCCCCE		46.6728889911
144PhosphorylationVAADVSFSDVEQFIQ
EEECCCHHHHHHHHH		32.9919779198
152PhosphorylationDVEQFIQTVYRCQFE
HHHHHHHHHHHHHEE		18.0619779198
154PhosphorylationEQFIQTVYRCQFEVR
HHHHHHHHHHHEEEC		14.7319779198
165PhosphorylationFEVRNKKSSLTASAD
EEECCCCCCCEECHH		31.9929136822
166PhosphorylationEVRNKKSSLTASADD
EECCCCCCCEECHHH		38.3229136822
168PhosphorylationRNKKSSLTASADDLK
CCCCCCCEECHHHHH		22.1022369663
170PhosphorylationKKSSLTASADDLKEI
CCCCCEECHHHHHHC		27.3122369663
175UbiquitinationTASADDLKEIEHRST
EECHHHHHHCCHHCC		64.7424961812
195PhosphorylationDDDDELDSSSDDFQD
CCCCCCCCCCCCCCH		44.3522369663
196PhosphorylationDDDELDSSSDDFQDA
CCCCCCCCCCCCCHH		37.1422369663
197PhosphorylationDDELDSSSDDFQDAK
CCCCCCCCCCCCHHH		45.1922369663
206PhosphorylationDFQDAKDTSFEHEKE
CCCHHHHCCCCHHHH		34.3122890988
207PhosphorylationFQDAKDTSFEHEKES
CCHHHHCCCCHHHHH		38.4825521595
214PhosphorylationSFEHEKESEILERTP
CCCHHHHHHHHHCCC		40.7922369663
220PhosphorylationESEILERTPSPLKKV
HHHHHHCCCCCCCCC		20.8122369663
222PhosphorylationEILERTPSPLKKVPE
HHHHCCCCCCCCCCC		42.1022369663
356PhosphorylationEKDYILDSSSVPLEK
HCCEEECCCCCCHHH		22.5228889911
357PhosphorylationKDYILDSSSVPLEKQ
CCEEECCCCCCHHHH		34.7124961812
358PhosphorylationDYILDSSSVPLEKQF
CEEECCCCCCHHHHH		31.5421440633
375PhosphorylationILHIDDRSNEERDKE
EECCCCCCHHHHHHH		56.4322369663
383PhosphorylationNEERDKESSESENDS
HHHHHHHCCCCCCCC		45.1819795423
384PhosphorylationEERDKESSESENDSE
HHHHHHCCCCCCCCC		46.3519795423
386PhosphorylationRDKESSESENDSEDE
HHHHCCCCCCCCCCC		43.5819795423
390PhosphorylationSSESENDSEDEDDEN
CCCCCCCCCCCCCCC		59.5425521595
405PhosphorylationDHSKRIISSEAFEEP
HHHHHCCCHHHHCCH		21.5427214570
406PhosphorylationHSKRIISSEAFEEPR
HHHHCCCHHHHCCHH		23.6428889911
421PhosphorylationRATSKGNSSLTVAFR
HHCCCCCCCEEEEEE		35.0822369663
422PhosphorylationATSKGNSSLTVAFRN
HCCCCCCCEEEEEEC		31.8722369663
424PhosphorylationSKGNSSLTVAFRNNR
CCCCCCEEEEEECCC		16.2529688323
451PhosphorylationKTDDEDDSLEFVAAI
ECCCCCCCHHHHHHH		41.9627017623
462PhosphorylationVAAIKNISNLGGKSI
HHHHHHHHHCCCCCC		35.0830377154
486PhosphorylationEDRNLILTDGENENK
ECCCEEEECCCCCCE		34.6625752575
537PhosphorylationEQTIVGVSQKGVFKI
CCEEEEEECCCEEEE		21.9019779198
756PhosphorylationVALKDDVSLSKVKSF
EEECCCCCHHHCCCC		33.6428889911
762PhosphorylationVSLSKVKSFKQPSKG
CCHHHCCCCCCCCCC		40.4430377154
774PhosphorylationSKGVLMPSASLQDFY
CCCCCCCCCCHHHHC		19.2730377154
776PhosphorylationGVLMPSASLQDFYG-
CCCCCCCCHHHHCC-		30.7930377154
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 VID27_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VID27_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 VID27_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPB_YEASTCCT2physical
16429126
TCPE_YEASTCCT5physical
16429126
TCPZ_YEASTCCT6physical
16429126
TCPQ_YEASTCCT8physical
16429126
ILV6_YEASTILV6physical
16429126
TBB_YEASTTUB2physical
16429126
YAJ9_YEASTYAR029Wgenetic
27708008
MRM2_YEASTMRM2genetic
27708008
CSM1_YEASTCSM1genetic
27708008
YFF2_YEASTYFL052Wgenetic
27708008
YGZ2_YEASTYGL242Cgenetic
27708008
STF2_YEASTSTF2genetic
27708008
THIK_YEASTPOT1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
SCS7_YEASTSCS7genetic
27708008
PABC_YEASTABZ2genetic
27708008
MET22_YEASTMET22genetic
27708008
KTR1_YEASTKTR1genetic
27708008
GID4_YEASTVID24physical
29040005
VID30_YEASTVID30physical
29040005
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VID27_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 TYR-41; SER-170; SER-195;SER-196; SER-207; SER-405; SER-421 AND THR-486, 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-222, AND MASSSPECTROMETRY.
"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-170, AND MASSSPECTROMETRY.

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