BUD21_YEAST - dbPTM
BUD21_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUD21_YEAST
UniProt AC Q08492
Protein Name Bud site selection protein 21
Gene Name BUD21
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 214
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in bud site selection maybe via the regulation of expression of bipolar budding components..
Protein Sequence MSNGHVKFDADESQASASAVTDRQDDVLVISKKDKEVHSSSDEESDDDDAPQEEGLHSGKSEVESQITQREEAIRLEQSQLRSKRRKQNELYAKQKKSVNETEVTDEVIAELPEELLKNIDQKDEGSTQYSSSRHVTFDKLDESDENEEALAKAIKTKKRKTLKNLRKDSVKRGKFRVQLLSTTQDSKTLPPKKESSIIRSKDRWLNRKALNKG
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
13PhosphorylationVKFDADESQASASAV
CCCCCCHHHHHHHHH		31.4328889911
16PhosphorylationDADESQASASAVTDR
CCCHHHHHHHHHCCC		18.3428889911
18PhosphorylationDESQASASAVTDRQD
CHHHHHHHHHCCCCC		22.3019779198
21PhosphorylationQASASAVTDRQDDVL
HHHHHHHCCCCCCEE		25.7719779198
32AcetylationDDVLVISKKDKEVHS
CCEEEEECCCCCCCC		54.5925381059
39PhosphorylationKKDKEVHSSSDEESD
CCCCCCCCCCCCCCC		36.3917287358
40PhosphorylationKDKEVHSSSDEESDD
CCCCCCCCCCCCCCC		27.2517287358
41PhosphorylationDKEVHSSSDEESDDD
CCCCCCCCCCCCCCC		52.6417287358
45PhosphorylationHSSSDEESDDDDAPQ
CCCCCCCCCCCCCCC		44.2717287358
65PhosphorylationSGKSEVESQITQREE
CCHHHHHHHHHHHHH		31.8728889911
79PhosphorylationEAIRLEQSQLRSKRR
HHHHHHHHHHHHHHH		23.0830377154
127PhosphorylationIDQKDEGSTQYSSSR
CCCCCCCCCCCCCCC		15.4128889911
128PhosphorylationDQKDEGSTQYSSSRH
CCCCCCCCCCCCCCC		42.2423749301
131PhosphorylationDEGSTQYSSSRHVTF
CCCCCCCCCCCCEEE		16.4230377154
132PhosphorylationEGSTQYSSSRHVTFD
CCCCCCCCCCCEEEC		26.8520377248
133PhosphorylationGSTQYSSSRHVTFDK
CCCCCCCCCCEEECC		22.0620377248
137PhosphorylationYSSSRHVTFDKLDES
CCCCCCEEECCCCCC		21.7122890988
144PhosphorylationTFDKLDESDENEEAL
EECCCCCCCCCHHHH		50.3022369663
183PhosphorylationFRVQLLSTTQDSKTL
EEEEEEECCCCCCCC		28.5727017623
184PhosphorylationRVQLLSTTQDSKTLP
EEEEEECCCCCCCCC		27.3127017623
187PhosphorylationLLSTTQDSKTLPPKK
EEECCCCCCCCCCCC		20.0927017623
196PhosphorylationTLPPKKESSIIRSKD
CCCCCCHHHHHHCHH		35.4030377154
197PhosphorylationLPPKKESSIIRSKDR
CCCCCHHHHHHCHHH		24.1130377154
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 BUD21_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUD21_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 BUD21_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMS1_YEASTBMS1physical
12150911
DHR1_YEASTECM16physical
12150911
ENP1_YEASTENP1physical
12150911
IMP3_YEASTIMP3physical
12150911
UTP7_YEASTUTP7physical
12150911
NAT10_YEASTKRE33physical
12150911
KRR1_YEASTKRR1physical
12150911
MPP10_YEASTMPP10physical
12150911
UTP17_YEASTNAN1physical
12150911
NOP14_YEASTNOP14physical
12150911
NOP56_YEASTNOP56physical
12150911
RL4B_YEASTRPL4Bphysical
12150911
RL7B_YEASTRPL7Bphysical
12150911
RS8A_YEASTRPS8Aphysical
12150911
RS8B_YEASTRPS8Aphysical
12150911
RRP12_YEASTRRP12physical
12150911
RRP5_YEASTRRP5physical
12150911
RRP9_YEASTRRP9physical
12150911
PSA1_YEASTSCL1physical
12150911
UTP20_YEASTUTP20physical
12150911
UTP4_YEASTUTP4physical
12150911
UTP22_YEASTUTP22physical
12150911
UTP8_YEASTUTP8physical
12150911
UTP10_YEASTUTP10physical
12150911
UTP13_YEASTUTP13physical
12150911
UTP15_YEASTUTP15physical
12150911
MPP10_YEASTMPP10physical
12068309
NOP56_YEASTNOP56physical
16554755
NOP58_YEASTNOP58physical
16554755
RRP9_YEASTRRP9physical
16554755
BMS1_YEASTBMS1physical
16429126
IMP3_YEASTIMP3physical
16429126
NAT10_YEASTKRE33physical
16429126
MPP10_YEASTMPP10physical
16429126
RRP5_YEASTRRP5physical
16429126
RRP9_YEASTRRP9physical
16429126
NOP56_YEASTNOP56physical
16429126
UTP10_YEASTUTP10physical
16429126
UTP15_YEASTUTP15physical
16429126
UTP20_YEASTUTP20physical
16429126
UTP7_YEASTUTP7physical
16429126
DHR1_YEASTECM16physical
16429126
ENP1_YEASTENP1physical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
UTP13_YEASTUTP13physical
16429126
UTP18_YEASTUTP18physical
16429126
UTP22_YEASTUTP22physical
16429126
RRP12_YEASTRRP12physical
16429126
UTP17_YEASTNAN1physical
16429126
UTP4_YEASTUTP4physical
16429126
UTP8_YEASTUTP8physical
16429126
RU1C_YEASTYHC1genetic
19061648
RS8A_YEASTRPS8Agenetic
19061648
RS8B_YEASTRPS8Agenetic
19061648
IF2A_YEASTSUI2genetic
19061648
NMD5_YEASTNMD5genetic
19061648
SRS2_YEASTSRS2genetic
21459050
YCU1_YEASTYCR051Wgenetic
27708008
ATG15_YEASTATG15genetic
27708008
RRP8_YEASTRRP8genetic
27708008
ELM1_YEASTELM1genetic
27708008
RCN1_YEASTRCN1genetic
27708008
TOF2_YEASTTOF2genetic
27708008
AIF1_YEASTAIF1genetic
27708008
MOD5_YEASTMOD5genetic
27708008
KA120_YEASTKAP120genetic
27708008
PRM4_YEASTPRM4genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUD21_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-65 AND SER-144, AND MASSSPECTROMETRY.
"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-144, 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 SER-39; SER-40; SER-41 ANDSER-45, AND MASS 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-144, AND MASSSPECTROMETRY.

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