F26_YEAST - dbPTM
F26_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F26_YEAST
UniProt AC P32604
Protein Name Fructose-2,6-bisphosphatase
Gene Name FBP26
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 452
Subcellular Localization
Protein Description This is predominantly if not solely a fructose-2,6-bisphosphatase..
Protein Sequence MGYSTISNDNDIKVCVIMVGLPARGKSFISQKIIRYLSWLSIKAKCFNVGNYRRDVSGNVPMDAEFFNFENTDNFKLRELAAQNAIKDIVNFFTKEDGSVAVFDATNSTRKRRKWLKDICEKNNIQPMFLESWSNDHELIINNAKDIGSTSPDYENSEPHVAEADFLERIRQYERFYEPLDPQKDKDMTFIKLVNIIEEVVINKIRTYLESRIVFYVMNIRPKPKYIWLSRHGESIYNVEKKIGGDSSLSERGFQYAKKLEQLVKESAGEINLTVWTSTLKRTQQTANYLPYKKLQWKALDELDAGVCDGMTYEEIEKEYPEDFKARDNDKYEYRYRGGESYRDVVIRLEPVIMELERQENVLIITHQAVLRCIYAYFMNVPQEESPWMSIPLHTLIKLEPRAYGTKVTKIKANIPAVSTYKEKGTSQVGELSQSSTKLHQLLNDSPLEDKF
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
3Phosphorylation-----MGYSTISNDN
-----CCCCCCCCCC		11.0128889911
5Phosphorylation---MGYSTISNDNDI
---CCCCCCCCCCCC		21.6830377154
7Phosphorylation-MGYSTISNDNDIKV
-CCCCCCCCCCCCEE		37.9130377154
76UbiquitinationFENTDNFKLRELAAQ
CCCCCCHHHHHHHHH		53.5417644757
87UbiquitinationLAAQNAIKDIVNFFT
HHHHHHHHHHHHHHC		38.7017644757
95UbiquitinationDIVNFFTKEDGSVAV
HHHHHHCCCCCCEEE		48.9617644757
111UbiquitinationDATNSTRKRRKWLKD
ECCCCHHHHHHHHHH		57.5517644757
145UbiquitinationELIINNAKDIGSTSP
EEEECCCHHCCCCCC		52.5917644757
149PhosphorylationNNAKDIGSTSPDYEN
CCCHHCCCCCCCCCC		26.5022369663
150PhosphorylationNAKDIGSTSPDYENS
CCHHCCCCCCCCCCC		38.7822369663
151PhosphorylationAKDIGSTSPDYENSE
CHHCCCCCCCCCCCC		19.9222369663
154PhosphorylationIGSTSPDYENSEPHV
CCCCCCCCCCCCCCC		22.0122369663
157PhosphorylationTSPDYENSEPHVAEA
CCCCCCCCCCCCHHH		40.3322369663
204UbiquitinationIEEVVINKIRTYLES
HHHHHHHHHHHHHHH		23.5723749301
235PhosphorylationWLSRHGESIYNVEKK
EEECCCCEEEEEEHH		34.6628889911
237PhosphorylationSRHGESIYNVEKKIG
ECCCCEEEEEEHHHC		23.5728889911
241UbiquitinationESIYNVEKKIGGDSS
CEEEEEEHHHCCCCC		45.4617644757
242UbiquitinationSIYNVEKKIGGDSSL
EEEEEEHHHCCCCCH		32.8317644757
281UbiquitinationTVWTSTLKRTQQTAN
EEEHHHCHHHHHHHH		54.1917644757
293UbiquitinationTANYLPYKKLQWKAL
HHHCCCCCCCCHHHH		45.1017644757
294UbiquitinationANYLPYKKLQWKALD
HHCCCCCCCCHHHHH		39.8117644757
412UbiquitinationGTKVTKIKANIPAVS
CCCCEEEEECCCCCE		36.6217644757
422UbiquitinationIPAVSTYKEKGTSQV
CCCCEECCCCCCCCC		53.7017644757
424UbiquitinationAVSTYKEKGTSQVGE
CCEECCCCCCCCCHH		64.4417644757
426PhosphorylationSTYKEKGTSQVGELS
EECCCCCCCCCHHHC		27.3622369663
427PhosphorylationTYKEKGTSQVGELSQ
ECCCCCCCCCHHHCH		31.3822369663
433PhosphorylationTSQVGELSQSSTKLH
CCCCHHHCHHHHHHH		24.5822369663
435PhosphorylationQVGELSQSSTKLHQL
CCHHHCHHHHHHHHH		36.2822369663
436PhosphorylationVGELSQSSTKLHQLL
CHHHCHHHHHHHHHH		23.1722369663
437PhosphorylationGELSQSSTKLHQLLN
HHHCHHHHHHHHHHC		42.7622369663
438UbiquitinationELSQSSTKLHQLLND
HHCHHHHHHHHHHCC		46.0117644757
446PhosphorylationLHQLLNDSPLEDKF-
HHHHHCCCCCCCCC-		30.2522369663
451UbiquitinationNDSPLEDKF------
CCCCCCCCC------		43.5317644757
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 F26_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F26_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 F26_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YL345_YEASTYLR345Wphysical
16554755
YL345_YEASTYLR345Wphysical
16429126
YL345_YEASTYLR345Wphysical
18719252
COQ7_YEASTCAT5genetic
21623372
ARO1_YEASTARO1genetic
21623372
SLX5_YEASTSLX5genetic
27708008
YJ68_YEASTYJR098Cgenetic
27708008
UPS1_YEASTUPS1genetic
27708008
BUL2_YEASTBUL2genetic
27708008
NDI1_YEASTNDI1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
YAR1_YEASTYAR1genetic
27708008
BRR1_YEASTBRR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F26_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-151; SER-433; SER-435;SER-436 AND SER-446, 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-151 AND SER-446, ANDMASS 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-446, AND MASSSPECTROMETRY.

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