BUD8_YEAST - dbPTM
BUD8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUD8_YEAST
UniProt AC P41698
Protein Name Bud site selection protein 8
Gene Name BUD8
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 603
Subcellular Localization Cell membrane
Multi-pass membrane protein . Found at presumptive bud sites, bud tips, and the distal poles of daughter cells.
Protein Description May be involved in positioning the distal bud pole signal..
Protein Sequence MIQSDEDNLDSSETTASTSYSGTSSVSSRLQLRTSLFFENLNGAHGNPDAETEMATVAYETTSRGQGFAVYINNERFSQIMGASTSSSSSSNSSSITQFHDTQDNNIPSNTTVRPTSLRRDNEDTVPLRNVTPSQNAAVRPERAVNSPSSQRLSCALTISTSVLMGEDVEGSPIEQEHSRVVSSLYSSLANRGNDESKNGTPPRPTSIEPNETTEHSFFSYHYDDTLEPDVEEAVRLTKNKTSNVNFISSTGSKGEGETEDEVIDQYEPVNESKFIPHKLKIPEKAGSIKSSTSDDSHSPGAPGTSARKIKIPQSPSLIGNILIPSHNSDSSNESSPKDHIGHNNEEKFSSKSTRKPSTSLEEEGPPIGLPSIPVLRSVSGPSKWTKTPLRLESGNSTKSDPFSRYEGHKTPSPLTKMNKKKNKTLPEHGQPLVLAPIKSQSSESDTGQNSIIEKPARSIRRKQQEKTDNRKEDRHDAENIDLEARMPIQHIDTASIHSFDSGQNGFRDVYSIENIIVILLCCSIVPPLFFIIGCSSRRKLVSDYRLMRLLMNKEHRAALLQGFIWDVDLRWFRMFCLILGAAETVIVMAGIAIGFGVGITRE
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
11PhosphorylationSDEDNLDSSETTAST
CCCCCCCCCCCCCCC		32.9930377154
19PhosphorylationSETTASTSYSGTSSV
CCCCCCCCCCCCCCH		18.1430377154
20PhosphorylationETTASTSYSGTSSVS
CCCCCCCCCCCCCHH		15.9430377154
24PhosphorylationSTSYSGTSSVSSRLQ
CCCCCCCCCHHHHHH		32.0630377154
28PhosphorylationSGTSSVSSRLQLRTS
CCCCCHHHHHHHEEH		34.5530377154
92N-linked_GlycosylationTSSSSSSNSSSITQF
CCCCCCCCCCCCEEE		48.10-
110N-linked_GlycosylationQDNNIPSNTTVRPTS
CCCCCCCCCEECCCC		34.12-
125PhosphorylationLRRDNEDTVPLRNVT
CCCCCCCCCCCCCCC		20.1821440633
132PhosphorylationTVPLRNVTPSQNAAV
CCCCCCCCCCCCCCC		22.2923749301
134PhosphorylationPLRNVTPSQNAAVRP
CCCCCCCCCCCCCCH		27.0523749301
147PhosphorylationRPERAVNSPSSQRLS
CHHHHCCCCCHHHHH		21.4028889911
149PhosphorylationERAVNSPSSQRLSCA
HHHCCCCCHHHHHEE		38.6328889911
150PhosphorylationRAVNSPSSQRLSCAL
HHCCCCCHHHHHEEE		23.7823749301
183PhosphorylationQEHSRVVSSLYSSLA
HHHHHHHHHHHHHHH		16.2719779198
184PhosphorylationEHSRVVSSLYSSLAN
HHHHHHHHHHHHHHH		21.5125752575
187PhosphorylationRVVSSLYSSLANRGN
HHHHHHHHHHHHCCC		24.9527017623
188PhosphorylationVVSSLYSSLANRGND
HHHHHHHHHHHCCCC		20.2525752575
201PhosphorylationNDESKNGTPPRPTSI
CCCCCCCCCCCCCCC		39.2421440633
207PhosphorylationGTPPRPTSIEPNETT
CCCCCCCCCCCCCCC		27.8621440633
211N-linked_GlycosylationRPTSIEPNETTEHSF
CCCCCCCCCCCCCCE		46.59-
217PhosphorylationPNETTEHSFFSYHYD
CCCCCCCCEEEEECC		23.0419779198
240N-linked_GlycosylationEAVRLTKNKTSNVNF
HHHHHHCCCCCCCEE		47.83-
242PhosphorylationVRLTKNKTSNVNFIS
HHHHCCCCCCCEEEE		34.6221551504
243PhosphorylationRLTKNKTSNVNFISS
HHHCCCCCCCEEEEC		40.1521551504
250PhosphorylationSNVNFISSTGSKGEG
CCCEEEECCCCCCCC		31.7821440633
251PhosphorylationNVNFISSTGSKGEGE
CCEEEECCCCCCCCC		38.3922369663
253PhosphorylationNFISSTGSKGEGETE
EEEECCCCCCCCCCC		37.2622369663
259PhosphorylationGSKGEGETEDEVIDQ
CCCCCCCCCCCCHHC		60.6427214570
271N-linked_GlycosylationIDQYEPVNESKFIPH
HHCCCCCCHHHCCCC		59.55-
288PhosphorylationKIPEKAGSIKSSTSD
CCCCCCCCCCCCCCC		31.5320377248
291PhosphorylationEKAGSIKSSTSDDSH
CCCCCCCCCCCCCCC		36.8622369663
292PhosphorylationKAGSIKSSTSDDSHS
CCCCCCCCCCCCCCC		27.2521440633
293PhosphorylationAGSIKSSTSDDSHSP
CCCCCCCCCCCCCCC		43.1820377248
294PhosphorylationGSIKSSTSDDSHSPG
CCCCCCCCCCCCCCC		41.1720377248
297PhosphorylationKSSTSDDSHSPGAPG
CCCCCCCCCCCCCCC		30.7521440633
299PhosphorylationSTSDDSHSPGAPGTS
CCCCCCCCCCCCCCC		29.0522369663
317PhosphorylationIKIPQSPSLIGNILI
CCCCCCCCCCCCEEC		37.5521551504
326PhosphorylationIGNILIPSHNSDSSN
CCCEECCCCCCCCCC		28.4519795423
329PhosphorylationILIPSHNSDSSNESS
EECCCCCCCCCCCCC		33.1819795423
331PhosphorylationIPSHNSDSSNESSPK
CCCCCCCCCCCCCCC		34.5819795423
332PhosphorylationPSHNSDSSNESSPKD
CCCCCCCCCCCCCCC		50.0019795423
333N-linked_GlycosylationSHNSDSSNESSPKDH
CCCCCCCCCCCCCCC		58.06-
335PhosphorylationNSDSSNESSPKDHIG
CCCCCCCCCCCCCCC		57.0819795423
336PhosphorylationSDSSNESSPKDHIGH
CCCCCCCCCCCCCCC		29.7719795423
358PhosphorylationSKSTRKPSTSLEEEG
CCCCCCCCCCCHHCC		33.3920377248
359PhosphorylationKSTRKPSTSLEEEGP
CCCCCCCCCCHHCCC		45.9517287358
360PhosphorylationSTRKPSTSLEEEGPP
CCCCCCCCCHHCCCC		37.8119779198
396N-linked_GlycosylationPLRLESGNSTKSDPF
CEEECCCCCCCCCCC		56.64-
411PhosphorylationSRYEGHKTPSPLTKM
CCCCCCCCCCHHHHH		24.2728889911
413PhosphorylationYEGHKTPSPLTKMNK
CCCCCCCCHHHHHHH		37.4628889911
423N-linked_GlycosylationTKMNKKKNKTLPEHG
HHHHHHCCCCCCCCC		51.96-
440PhosphorylationLVLAPIKSQSSESDT
EEEEEECCCCCCCCC		35.6919795423
442PhosphorylationLAPIKSQSSESDTGQ
EEEECCCCCCCCCCC		43.0719795423
443PhosphorylationAPIKSQSSESDTGQN
EEECCCCCCCCCCCC		33.2223749301
445PhosphorylationIKSQSSESDTGQNSI
ECCCCCCCCCCCCCC		42.2819795423
447PhosphorylationSQSSESDTGQNSIIE
CCCCCCCCCCCCCCC		50.3623749301
451PhosphorylationESDTGQNSIIEKPAR
CCCCCCCCCCCHHHH		19.6323749301
455UbiquitinationGQNSIIEKPARSIRR
CCCCCCCHHHHHHHH		33.3023749301
468PhosphorylationRRKQQEKTDNRKEDR
HHHHHHCCCCCHHHH		37.4417287358
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 BUD8_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUD8_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 BUD8_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUD9_YEASTBUD9physical
11118203
STE20_YEASTSTE20physical
11489916
RRP14_YEASTRRP14physical
11489916
BUD9_YEASTBUD9genetic
12221111
BUD9_YEASTBUD9genetic
8657162
AXL2_YEASTAXL2genetic
12221111
BUD3_YEASTBUD3genetic
12221111
BUD4_YEASTBUD4genetic
12221111
RAS2_YEASTRAS2genetic
9055077
STE11_YEASTSTE11genetic
9055077
STE12_YEASTSTE12genetic
9055077
AXL1_YEASTAXL1genetic
12221111
RSR1_YEASTRSR1genetic
12221111
SHO1_YEASTSHO1physical
18591427
BUD9_YEASTBUD9genetic
11877459
RAX2_YEASTRAX2physical
20678480
MPC2_YEASTMPC2genetic
27708008
INO4_YEASTINO4genetic
27708008
YPS5_YEASTYPS5genetic
27708008
NMA2_YEASTNMA2genetic
27708008
RS23A_YEASTRPS23Agenetic
27708008
RS23B_YEASTRPS23Agenetic
27708008
TRS65_YEASTTRS65genetic
27708008
ELP2_YEASTELP2genetic
27708008
MVB12_YEASTMVB12genetic
27708008
YOR1_YEASTYOR1genetic
27708008
WSS1_YEASTWSS1genetic
27708008
TDA11_YEASTTDA11genetic
27708008
SOL3_YEASTSOL3genetic
27708008
INP51_YEASTINP51genetic
27708008
CTK1_YEASTCTK1genetic
27708008
OPY2_YEASTOPY2genetic
27708008
VPS4_YEASTVPS4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUD8_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-184 AND SER-253, 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 THR-359, 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 THR-468, AND MASSSPECTROMETRY.

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