BUD6_YEAST - dbPTM
BUD6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUD6_YEAST
UniProt AC P41697
Protein Name Bud site selection protein 6
Gene Name BUD6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 788
Subcellular Localization
Protein Description Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton..
Protein Sequence MKMAVDDPTYGTPKIKRTASSSSSIETTVTKLLMSTKHLLQVLTQWSKGTTSGRLVSDAYVQLGNDFKVVSKFFMHAKVDMSDVGDVPMALRRVLEVTLREPPSDETLNKHLPKIREIIVTLLDKLKVKQAILKNMQQEHRISVKSHHQQNPSFTSNLSLGSEGTREGTPLSSRKSSIVRDQRQSDSVENSYGEKVNSTSTGTPSAQSAEATLTKPRTNIKQNLKSNNAPNASDDDDALSQLKKGTNLQRRASKRYSAYHMAKLTNQSTTEAAAAAGLMTTPSPSMLHLEETVRKSKLYGNNNNDDDRNINSAENKGKSIDDVSKASPLAKTPLPIENVRASPRRLSSVVTTSPDKAMNGTCPVFLRIGDKTKKCHVQLPTTKNALRLLFIERFAYSPGANSFPDIYIMDPQYGVFYELEELNLLDIKEGFVIELKLEENPNNTIKEFIDTVKMEISNSQNDIIRHLKEMSFGSAISGKQTEVLPQPGLEANKHDLVGQNKKDDDKTIKDIQYELGKIKQVHNINRSNINETIFNILRKVDNFKSLSFSAKNSSNRMYMEKSQTELGDLSDTLLSKVDDLQDVIEIMRKDVAERRSQPAKKKLETVSKDLENAQADVLKLQEFIDTEKPHWKKTWEAELDKVCEEQQFLTLQEELILDLKEDLGKALETFDLIKLCCEEQEKNPSRSKSNPILPIMRPGTFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKLKASNEFDDELENFVGNSNLKKSGGFEEVERIRKQKDEANLRAYFGPGFT
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
9PhosphorylationKMAVDDPTYGTPKIK
CCCCCCCCCCCCCCC		41.3924961812
10PhosphorylationMAVDDPTYGTPKIKR
CCCCCCCCCCCCCCC		25.1228132839
12PhosphorylationVDDPTYGTPKIKRTA
CCCCCCCCCCCCCCC		15.8221440633
18PhosphorylationGTPKIKRTASSSSSI
CCCCCCCCCCCCCCH		26.3721440633
20PhosphorylationPKIKRTASSSSSIET
CCCCCCCCCCCCHHH		30.0921551504
21PhosphorylationKIKRTASSSSSIETT
CCCCCCCCCCCHHHH		31.6019779198
22PhosphorylationIKRTASSSSSIETTV
CCCCCCCCCCHHHHH		26.1328889911
23PhosphorylationKRTASSSSSIETTVT
CCCCCCCCCHHHHHH		36.9623749301
24PhosphorylationRTASSSSSIETTVTK
CCCCCCCCHHHHHHH		26.7927717283
27PhosphorylationSSSSSIETTVTKLLM
CCCCCHHHHHHHHHH		25.5427017623
28PhosphorylationSSSSIETTVTKLLMS
CCCCHHHHHHHHHHC		17.2527017623
30PhosphorylationSSIETTVTKLLMSTK
CCHHHHHHHHHHCHH		17.5527017623
82PhosphorylationMHAKVDMSDVGDVPM
HEEECCHHHCCCHHH		25.3625704821
143PhosphorylationMQQEHRISVKSHHQQ
HHHHHCCCCCCCCCC		24.3720377248
146PhosphorylationEHRISVKSHHQQNPS
HHCCCCCCCCCCCCC		24.8524961812
153PhosphorylationSHHQQNPSFTSNLSL
CCCCCCCCCCCCEEC		49.0225704821
155PhosphorylationHQQNPSFTSNLSLGS
CCCCCCCCCCEECCC		22.5024961812
156PhosphorylationQQNPSFTSNLSLGSE
CCCCCCCCCEECCCC		33.4924961812
159PhosphorylationPSFTSNLSLGSEGTR
CCCCCCEECCCCCCC		34.6328889911
162PhosphorylationTSNLSLGSEGTREGT
CCCEECCCCCCCCCC		37.8419779198
165PhosphorylationLSLGSEGTREGTPLS
EECCCCCCCCCCCCC		22.8428889911
169PhosphorylationSEGTREGTPLSSRKS
CCCCCCCCCCCCCCC		19.1228889911
172PhosphorylationTREGTPLSSRKSSIV
CCCCCCCCCCCCHHC		29.3328889911
173PhosphorylationREGTPLSSRKSSIVR
CCCCCCCCCCCHHCC		51.9519779198
177PhosphorylationPLSSRKSSIVRDQRQ
CCCCCCCHHCCCHHH		28.3021551504
185PhosphorylationIVRDQRQSDSVENSY
HCCCHHHCCCCCCCC		33.7620377248
187PhosphorylationRDQRQSDSVENSYGE
CCHHHCCCCCCCCCC		36.2628889911
191PhosphorylationQSDSVENSYGEKVNS
HCCCCCCCCCCCCCC		22.4721440633
198PhosphorylationSYGEKVNSTSTGTPS
CCCCCCCCCCCCCCC		27.0729688323
199PhosphorylationYGEKVNSTSTGTPSA
CCCCCCCCCCCCCCC		25.7129688323
200PhosphorylationGEKVNSTSTGTPSAQ
CCCCCCCCCCCCCCC		25.3524961812
201PhosphorylationEKVNSTSTGTPSAQS
CCCCCCCCCCCCCCH		45.2024961812
203PhosphorylationVNSTSTGTPSAQSAE
CCCCCCCCCCCCHHH		17.7328152593
205PhosphorylationSTSTGTPSAQSAEAT
CCCCCCCCCCHHHHH		38.4921551504
208PhosphorylationTGTPSAQSAEATLTK
CCCCCCCHHHHHHCC		28.0024961812
215AcetylationSAEATLTKPRTNIKQ
HHHHHHCCCCCCHHH		35.3024489116
221AcetylationTKPRTNIKQNLKSNN
CCCCCCHHHHHHCCC		34.8925381059
226PhosphorylationNIKQNLKSNNAPNAS
CHHHHHHCCCCCCCC		38.1828889911
233PhosphorylationSNNAPNASDDDDALS
CCCCCCCCCCHHHHH		48.4922369663
240PhosphorylationSDDDDALSQLKKGTN
CCCHHHHHHHHHCHH		34.8825521595
259PhosphorylationASKRYSAYHMAKLTN
HHHHHHHHHHHHHCC		6.0319779198
265PhosphorylationAYHMAKLTNQSTTEA
HHHHHHHCCCCHHHH		30.4219779198
270PhosphorylationKLTNQSTTEAAAAAG
HHCCCCHHHHHHHHC		28.9519779198
280PhosphorylationAAAAGLMTTPSPSML
HHHHCCCCCCCHHHH		40.3720377248
281PhosphorylationAAAGLMTTPSPSMLH
HHHCCCCCCCHHHHC		14.0620377248
283PhosphorylationAGLMTTPSPSMLHLE
HCCCCCCCHHHHCHH		27.7522369663
285PhosphorylationLMTTPSPSMLHLEET
CCCCCCHHHHCHHHH		38.0120377248
292PhosphorylationSMLHLEETVRKSKLY
HHHCHHHHHHHHHCC		19.0820377248
296PhosphorylationLEETVRKSKLYGNNN
HHHHHHHHHCCCCCC		19.8225704821
312PhosphorylationDDDRNINSAENKGKS
CCCCCHHHHHHCCCC		32.9127214570
319PhosphorylationSAENKGKSIDDVSKA
HHHHCCCCHHHHHHC		39.6622369663
324PhosphorylationGKSIDDVSKASPLAK
CCCHHHHHHCCCCCC		29.5122369663
327PhosphorylationIDDVSKASPLAKTPL
HHHHHHCCCCCCCCC		24.9622369663
332PhosphorylationKASPLAKTPLPIENV
HCCCCCCCCCCHHHC		25.1723749301
342PhosphorylationPIENVRASPRRLSSV
CHHHCCCCCCCCCCE		14.3622369663
347PhosphorylationRASPRRLSSVVTTSP
CCCCCCCCCEEECCC		21.1922369663
348PhosphorylationASPRRLSSVVTTSPD
CCCCCCCCEEECCCC		25.7922369663
351PhosphorylationRRLSSVVTTSPDKAM
CCCCCEEECCCCHHH		21.2822369663
352PhosphorylationRLSSVVTTSPDKAMN
CCCCEEECCCCHHHC		27.0122369663
353PhosphorylationLSSVVTTSPDKAMNG
CCCEEECCCCHHHCC		23.0322369663
361PhosphorylationPDKAMNGTCPVFLRI
CCHHHCCCCCEEEEE		14.5019779198
554PhosphorylationSFSAKNSSNRMYMEK
CEECCCCCCCEEEEH		37.5420377248
558PhosphorylationKNSSNRMYMEKSQTE
CCCCCCEEEEHHHHH		10.0120377248
562PhosphorylationNRMYMEKSQTELGDL
CCEEEEHHHHHHHHH		29.0920377248
575PhosphorylationDLSDTLLSKVDDLQD
HHHHHHHHHCHHHHH		33.4720377248
608AcetylationKKLETVSKDLENAQA
HHHHHHHHHHHHHHH		63.0925381059
682UbiquitinationLCCEEQEKNPSRSKS
HHHHHHHHCCCCCCC		74.0723749301
687PhosphorylationQEKNPSRSKSNPILP
HHHCCCCCCCCCCCC		44.7822369663
689PhosphorylationKNPSRSKSNPILPIM
HCCCCCCCCCCCCCC		49.4322369663
700PhosphorylationLPIMRPGTFNQVREQ
CCCCCCCCHHHHHHH		23.3022369663
714PhosphorylationQVMVAVQSLNPDHDS
HHHHHHHHCCCCCHH		24.4228889911
742PhosphorylationMERKLKASNEFDDEL
HHHHHHHCCCCHHHH		34.9930377154
774UbiquitinationVERIRKQKDEANLRA
HHHHHHHCCHHHHHH		61.6524961812
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 BUD6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUD6_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 BUD6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWE1_YEASTSWE1genetic
12686605
YGB5_YEASTYGL015Cphysical
10688190
GIC2_YEASTGIC2physical
10938101
PEA2_YEASTPEA2physical
9632790
STE11_YEASTSTE11physical
9632790
BUD6_YEASTBUD6physical
9247651
GIC2_YEASTGIC2genetic
10938101
PROF_YEASTPFY1genetic
14657240
KAR9_YEASTKAR9genetic
15492045
DYHC_YEASTDYN1genetic
15492045
MLC1_YEASTMLC1physical
16554755
YO304_YEASTBIL1physical
16554755
MYO2_YEASTMYO2physical
16554755
YGB5_YEASTYGL015Cphysical
11283351
MSL1_YEASTMSL1genetic
17615297
LIC4_YEASTATC1genetic
17615297
LTE1_YEASTLTE1genetic
17615297
BUD6_YEASTBUD6physical
18467557
HSP71_YEASTSSA1physical
19536198
SLT2_YEASTSLT2genetic
18931302
NBP2_YEASTNBP2genetic
18931302
YPT6_YEASTYPT6genetic
18931302
SGF73_YEASTSGF73genetic
18931302
SLX5_YEASTSLX5genetic
18931302
BNI1_YEASTBNI1genetic
20534809
LTE1_YEASTLTE1genetic
22558355
BIM1_YEASTBIM1physical
22608510
BUD6_YEASTBUD6physical
23161908
BNR1_YEASTBNR1physical
23671312
BNI1_YEASTBNI1physical
23671312
GET2_YEASTGET2genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
CDC24_YEASTCDC24genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CDC10_YEASTCDC10genetic
27708008
UAP1_YEASTQRI1genetic
27708008
COG3_YEASTCOG3genetic
27708008
GNA1_YEASTGNA1genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
RHO3_YEASTRHO3genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRP24_YEASTPRP24genetic
27708008
CAP_YEASTSRV2genetic
27708008
PROF_YEASTPFY1genetic
27708008
MDM10_YEASTMDM10genetic
27708008
PAU8_YEASTPAU8genetic
27708008
PAU11_YEASTPAU8genetic
27708008
PAU9_YEASTPAU8genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
PET18_YEASTPET18genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
PP2A1_YEASTPPH21genetic
27708008
RAD57_YEASTRAD57genetic
27708008
RUB1_YEASTRUB1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
NBP2_YEASTNBP2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
SHE9_YEASTSHE9genetic
27708008
UBP9_YEASTUBP9genetic
27708008
BEM2_YEASTBEM2genetic
27708008
YGB0_YEASTMPO1genetic
27708008
MAN1_YEASTAMS1genetic
27708008
PEX31_YEASTPEX31genetic
27708008
CG21_YEASTCLB1genetic
27708008
SMI1_YEASTSMI1genetic
27708008
TCD1_YEASTTCD1genetic
27708008
SLT2_YEASTSLT2genetic
27708008
INP51_YEASTINP51genetic
27708008
ICE2_YEASTICE2genetic
27708008
YJE3_YEASTYJL043Wgenetic
27708008
BCK1_YEASTBCK1genetic
27708008
HS150_YEASTHSP150genetic
27708008
YJR1_YEASTYJL171Cgenetic
27708008
YJ00_YEASTYJR030Cgenetic
27708008
HSL1_YEASTHSL1genetic
27708008
LDB18_YEASTLDB18genetic
27708008
GTR1_YEASTGTR1genetic
27708008
MMT1_YEASTMMT1genetic
27708008
ICY1_YEASTICY1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
MDM12_YEASTMDM12genetic
27708008
YO098_YEASTYOL098Cgenetic
27708008
HST3_YEASTHST3genetic
27708008
MKK1_YEASTMKK1genetic
27708008
DGK1_YEASTDGK1genetic
27708008
FIT2_YEASTFIT2genetic
27708008
YP066_YEASTRGL1genetic
27708008
BEM4_YEASTBEM4genetic
27708008
NIP80_YEASTNIP100genetic
27708008
ATG13_YEASTATG13genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUD6_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-20; SER-22; SER-172;SER-233; SER-327; SER-342; SER-347; THR-351; SER-353 AND SER-689, 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-233; SER-285; SER-319;SER-327; SER-342 AND SER-347, 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-342, 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-233; SER-327 ANDSER-342, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348 AND SER-353, ANDMASS SPECTROMETRY.

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