BUD9_YEAST - dbPTM
BUD9_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUD9_YEAST
UniProt AC P53226
Protein Name Bud site selection protein 9
Gene Name BUD9
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 547
Subcellular Localization Cell membrane
Multi-pass membrane protein . Found at the necks of large-budded cells and the proximal poles of daughter cells.
Protein Description May be involved in positioning the proximal bud pole signal..
Protein Sequence MTKITRDVSITTENSKSTSGSATASSASLPENDHPIFHQPRARIRSGSLFIEGSDSFPSSEVKSYNVYIDDSKYSEILKGDTNSSSTDGKQVFEDARDDNFHQESHRDLEDSILDLVRRDPEVAAFPLPPPNSNERNRNSSNGSSAETNLNGHSSSGTISTSVLLNMGSAEKHAGTTRGDHMESSSMKSFEKLGTRPSSLFYPPPEGTAPYQGPRATVSGNKSTRQTQGTYSFPSMRYGVDLVSPVEGAVDVAKSRVPNSTLNGTFPDKAFIPHEFQIPKKAWNRIPANKSTSLKTPRNHSLLIDILKPFEAADLANDQRSSSAVLKNTVHSNGQYNPTNETSGTRMQDQRQKNTNEIDLEKIPNPQVPLGIAMDTMRSPNQLHEKEYESNIEAGLASGVGKGDNSIKQHQYKKIPQEIDRDQQLSFQMETMPIQRIDSSSIRSFDSRIYGFSEIYSIPRVITTLCICLFVPPLFFFFSINGNNGVSNYRLMRMIMNYEHRIGLLKGFEWDIDVQWFRTLCFVLGCIEMLAIFASIGIGFGVGIIRE
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
9PhosphorylationTKITRDVSITTENSK
CCEEEEEEEEECCCC		20.6421440633
12PhosphorylationTRDVSITTENSKSTS
EEEEEEEECCCCCCC		31.3427717283
15PhosphorylationVSITTENSKSTSGSA
EEEEECCCCCCCCCC		23.0428889911
17PhosphorylationITTENSKSTSGSATA
EEECCCCCCCCCCCC		27.8519795423
18PhosphorylationTTENSKSTSGSATAS
EECCCCCCCCCCCCC		40.6219795423
19PhosphorylationTENSKSTSGSATASS
ECCCCCCCCCCCCCC		37.5319795423
21PhosphorylationNSKSTSGSATASSAS
CCCCCCCCCCCCCCC		23.3919795423
23PhosphorylationKSTSGSATASSASLP
CCCCCCCCCCCCCCC		28.8619795423
25PhosphorylationTSGSATASSASLPEN
CCCCCCCCCCCCCCC		23.2919795423
26PhosphorylationSGSATASSASLPEND
CCCCCCCCCCCCCCC		21.2919795423
28PhosphorylationSATASSASLPENDHP
CCCCCCCCCCCCCCC		46.5419795423
46PhosphorylationQPRARIRSGSLFIEG
CCCCEECCCCEEEEC		30.2928152593
48PhosphorylationRARIRSGSLFIEGSD
CCEECCCCEEEECCC		22.7328889911
64PhosphorylationFPSSEVKSYNVYIDD
CCHHHCEEEEEEECC		27.4121440633
83N-linked_GlycosylationEILKGDTNSSSTDGK
HHHCCCCCCCCCCCC		44.63-
84PhosphorylationILKGDTNSSSTDGKQ
HHCCCCCCCCCCCCH		27.9721440633
85PhosphorylationLKGDTNSSSTDGKQV
HCCCCCCCCCCCCHH		39.0521440633
87PhosphorylationGDTNSSSTDGKQVFE
CCCCCCCCCCCHHHH		51.2021440633
112PhosphorylationSHRDLEDSILDLVRR
HHHHHHHHHHHHHHC		18.7123607784
133PhosphorylationFPLPPPNSNERNRNS
CCCCCCCCCCCCCCC		45.9329734811
139N-linked_GlycosylationNSNERNRNSSNGSSA
CCCCCCCCCCCCCCC		54.03-
142N-linked_GlycosylationERNRNSSNGSSAETN
CCCCCCCCCCCCCCC		54.94-
176PhosphorylationSAEKHAGTTRGDHME
CHHHCCCCCCCCCCC		17.6924961812
177PhosphorylationAEKHAGTTRGDHMES
HHHCCCCCCCCCCCH		31.5624961812
184PhosphorylationTRGDHMESSSMKSFE
CCCCCCCHHHCCCHH		21.8224961812
185PhosphorylationRGDHMESSSMKSFEK
CCCCCCHHHCCCHHH		22.5828889911
186PhosphorylationGDHMESSSMKSFEKL
CCCCCHHHCCCHHHH		39.2425704821
189PhosphorylationMESSSMKSFEKLGTR
CCHHHCCCHHHHCCC		29.9624930733
195PhosphorylationKSFEKLGTRPSSLFY
CCHHHHCCCCHHHCC		50.2521440633
198PhosphorylationEKLGTRPSSLFYPPP
HHHCCCCHHHCCCCC		36.0621440633
199PhosphorylationKLGTRPSSLFYPPPE
HHCCCCHHHCCCCCC		25.7721440633
221N-linked_GlycosylationPRATVSGNKSTRQTQ
CCEEECCCCCCCCCC		27.83-
259N-linked_GlycosylationVAKSRVPNSTLNGTF
HHHHCCCCCCCCCCC		44.78-
263N-linked_GlycosylationRVPNSTLNGTFPDKA
CCCCCCCCCCCCCCC		47.77-
289N-linked_GlycosylationAWNRIPANKSTSLKT
HHHCCCCCCCCCCCC		33.19-
299N-linked_GlycosylationTSLKTPRNHSLLIDI
CCCCCCCCCEEHHHH		30.24-
301PhosphorylationLKTPRNHSLLIDILK
CCCCCCCEEHHHHHC		28.5528889911
321PhosphorylationDLANDQRSSSAVLKN
HHCCCCCCCHHHHHH		24.0221551504
340N-linked_GlycosylationNGQYNPTNETSGTRM
CCCCCCCCCCCCCCH		52.37-
379PhosphorylationIAMDTMRSPNQLHEK
EEHHCCCCHHHHCHH		19.8521440633
386UbiquitinationSPNQLHEKEYESNIE
CHHHHCHHHHHHHHH		55.6523749301
406PhosphorylationGVGKGDNSIKQHQYK
CCCCCCCCHHHHHHC		35.5825704821
439PhosphorylationMPIQRIDSSSIRSFD
CCCCCCCHHHCCCCC		24.5027214570
440PhosphorylationPIQRIDSSSIRSFDS
CCCCCCHHHCCCCCC		26.4919795423
441PhosphorylationIQRIDSSSIRSFDSR
CCCCCHHHCCCCCCC		26.4419795423
444PhosphorylationIDSSSIRSFDSRIYG
CCHHHCCCCCCCCCC		31.5619795423
447PhosphorylationSSIRSFDSRIYGFSE
HHCCCCCCCCCCHHH		20.6819795423
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 BUD9_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUD9_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 BUD9_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUD8_YEASTBUD8physical
11118203
MAL31_YEASTMAL31physical
16093310
RAX2_YEASTRAX2physical
20678480
VPS8_YEASTVPS8genetic
27708008
SGF29_YEASTSGF29genetic
27708008
SCW4_YEASTSCW4genetic
27708008
BGL2_YEASTBGL2genetic
27708008
DOG1_YEASTDOG1genetic
27708008
MPM1_YEASTMPM1genetic
27708008
ATG36_YEASTATG36genetic
27708008
ELM1_YEASTELM1genetic
27708008
RAD52_YEASTRAD52genetic
27708008
CPT1_YEASTCPT1genetic
27708008
SRO7_YEASTSRO7genetic
27708008
FUN26_YEASTFUN26genetic
27708008
CALX_YEASTCNE1genetic
27708008
PLPHP_YEASTYBL036Cgenetic
27708008
PP2C4_YEASTPTC4genetic
27708008
NPL4_YEASTNPL4genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
THRC_YEASTTHR4genetic
27708008
IMG2_YEASTIMG2genetic
27708008
RL35A_YEASTRPL35Agenetic
27708008
RL35B_YEASTRPL35Agenetic
27708008
BAP3_YEASTBAP3genetic
27708008
UBC5_YEASTUBC5genetic
27708008
CYPH_YEASTCPR1genetic
27708008
TRM82_YEASTTRM82genetic
27708008
PEX5_YEASTPEX5genetic
27708008
SGPL_YEASTDPL1genetic
27708008
RMT2_YEASTRMT2genetic
27708008
PCL6_YEASTPCL6genetic
27708008
IES1_YEASTIES1genetic
27708008
GAT1_YEASTGAT1genetic
27708008
YFF4_YEASTYFL054Cgenetic
27708008
PDE1_YEASTPDE1genetic
27708008
KEL2_YEASTKEL2genetic
27708008
GLPK_YEASTGUT1genetic
27708008
YIH7_YEASTYIL077Cgenetic
27708008
FLX1_YEASTFLX1genetic
27708008
YIQ5_YEASTYIL165Cgenetic
27708008
SNX4_YEASTSNX4genetic
27708008
TAX4_YEASTTAX4genetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
MNN11_YEASTMNN11genetic
27708008
ELO1_YEASTELO1genetic
27708008
ECM25_YEASTECM25genetic
27708008
CBF1_YEASTCBF1genetic
27708008
SFC1_YEASTSFC1genetic
27708008
PGLR_YEASTPGU1genetic
27708008
YJ9S_YEASTYJR154Wgenetic
27708008
EF1G2_YEASTTEF4genetic
27708008
APN1_YEASTAPN1genetic
27708008
ALY1_YEASTALY1genetic
27708008
OSW2_YEASTOSW2genetic
27708008
ERG3_YEASTERG3genetic
27708008
ALAM_YEASTALT1genetic
27708008
ICT1_YEASTICT1genetic
27708008
PUT1_YEASTPUT1genetic
27708008
MDL1_YEASTMDL1genetic
27708008
MCP2_YEASTMCP2genetic
27708008
CSR1_YEASTCSR1genetic
27708008
SST2_YEASTSST2genetic
27708008
YMD7_YEASTYML037Cgenetic
27708008
PUR92_YEASTADE17genetic
27708008
YIM1_YEASTYIM1genetic
27708008
ARK1_YEASTARK1genetic
27708008
SWS2_YEASTSWS2genetic
27708008
CTU2_YEASTNCS2genetic
27708008
SSK2_YEASTSSK2genetic
27708008
CSN10_YEASTRRI2genetic
27708008
GSP2_YEASTGSP2genetic
27708008
HST2_YEASTHST2genetic
27708008
ALDH6_YEASTALD6genetic
27708008
ELP3_YEASTELP3genetic
27708008
INA17_YEASTINA17genetic
27708008
MKK2_YEASTMKK2genetic
27708008
KES1_YEASTKES1genetic
27708008
RLF2_YEASTRLF2genetic
27708008
MED1_YEASTMED1genetic
27708008
MTNA_YEASTMRI1genetic
27708008
CST26_YEASTCST26genetic
26711260
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUD9_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-46 AND SER-48, AND MASSSPECTROMETRY.

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