BUL2_YEAST - dbPTM
BUL2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUL2_YEAST
UniProt AC Q03758
Protein Name Ubiquitin ligase-binding protein BUL2
Gene Name BUL2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 920
Subcellular Localization Cytoplasm .
Protein Description Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other permeases such as PMA1. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription and pressure-induced differential regulation of the 2 tryptophan permeases TAT1 and TAT2..
Protein Sequence MTFTFSTSSRKNGRPPLKSVSTEDNIHLLRKRRQQQLSSNSTDNSLHPNSGQTPRASDSQDDDIRSASTTNLDRLRQEREENSLEMDCTQSRLSHRANMLVDVLPSFEMYNALHRHIPQGNVDPDRHDFPPSYQEVRTQRMTILPSNDNSVERSQLTAVPGSENACNNATAHSLTNLHPLQTQHLTINSTRSGGQSLHSSSDTNISQIPFEDDLNDSDNIFIDKLYTLPKLSTPIEIDIRITKTASIPHERPEEQSILKEYTSGDIIHGYCLIENRSSQPLKFEMFYVTLEAYISVIDRQKGKRTLKRFLRMVDLSASWSYTNITPSTGINIVPGERDFDDAIIGLSNSRELKPNTKYKKFFMFKLPTQLLDVTCKQEQFSHCLLPPSFGIDKYKNNCKYSGIKVNSVLGCGHLGTKGSPILTLDMADDNLSINYTIDAKIVGKDKRTSKLNIMKEKEYNLRVMPFPFAGVTNQQNEKTCLRQLKNLESLIEDRFEALNKIFKKLELNEAISNVDIHDTDISGTLDGNEDLDSDEILRRKLDQLHINNRIDDTASQSPSYDSKNMAPKENLVETELRYKFKNKNKSNSSLFSHFLSSSETGSSSTGPHVYNSGLIVLSVKKPQSTLPYWSPSLLRKTNKFEAKSEQEKENWQRLMGMLPEGVKTPLTKLDVHLTCIQSNNSAGHKPPEISSVTTEFVVITAKSDNSIPIKFCTELLMNENRLNKLKTKFLTYQKKVHEYRKKFEENHAKLNELYNRNRDHFTPKELLFTNFISDQINNDIDSLAGLKVNIIDLHDIFKKQIHTFEEENEDIISKKGSSNPPSASSSNNNFLQATFSNGASTATKFTQQIVHEWEKVKPLQYKRDVTVNLKLNPNIKETLVPNLETCLCCRFYCVRVNIKFDNHLGSMKVDIPVDVKKLQI
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
2Phosphorylation------MTFTFSTSS
------CCEEECCCC		31.2330377154
19PhosphorylationNGRPPLKSVSTEDNI
CCCCCCCCCCHHHHH		29.0522890988
21PhosphorylationRPPLKSVSTEDNIHL
CCCCCCCCHHHHHHH		32.9225521595
22PhosphorylationPPLKSVSTEDNIHLL
CCCCCCCHHHHHHHH		45.2422369663
41PhosphorylationQQQLSSNSTDNSLHP
HHHHHCCCCCCCCCC		38.8023749301
57PhosphorylationSGQTPRASDSQDDDI
CCCCCCCCCCCCCCH		38.7928889911
59PhosphorylationQTPRASDSQDDDIRS
CCCCCCCCCCCCHHH		32.7729136822
66PhosphorylationSQDDDIRSASTTNLD
CCCCCHHHCCCCCHH		27.2322890988
68PhosphorylationDDDIRSASTTNLDRL
CCCHHHCCCCCHHHH		36.6922369663
69PhosphorylationDDIRSASTTNLDRLR
CCHHHCCCCCHHHHH		21.3022890988
70PhosphorylationDIRSASTTNLDRLRQ
CHHHCCCCCHHHHHH		31.1522890988
162PhosphorylationQLTAVPGSENACNNA
HCEECCCCCCCCCCC		22.9321440633
182PhosphorylationTNLHPLQTQHLTINS
CCCCCCCCEEEEEEC		26.1628889911
192PhosphorylationLTINSTRSGGQSLHS
EEEECCCCCCCCCCC		47.5728889911
200PhosphorylationGGQSLHSSSDTNISQ
CCCCCCCCCCCCCCC		22.8330377154
201PhosphorylationGQSLHSSSDTNISQI
CCCCCCCCCCCCCCC		52.0130377154
203PhosphorylationSLHSSSDTNISQIPF
CCCCCCCCCCCCCCC		36.0819779198
407PhosphorylationYSGIKVNSVLGCGHL
CCCCEEEEEECCCCC		23.0021440633
448PhosphorylationIVGKDKRTSKLNIMK
EECCCCCCCCCCCCC		35.6319823750
449PhosphorylationVGKDKRTSKLNIMKE
ECCCCCCCCCCCCCC		38.9019823750
489PhosphorylationRQLKNLESLIEDRFE
HHHHCHHHHHHHHHH		37.5024930733
540UbiquitinationSDEILRRKLDQLHIN
HHHHHHHHHHHHCCC		50.4023749301
555PhosphorylationNRIDDTASQSPSYDS
CCCCCCCCCCCCCCC		33.0323749301
557PhosphorylationIDDTASQSPSYDSKN
CCCCCCCCCCCCCCC		17.2017330950
559PhosphorylationDTASQSPSYDSKNMA
CCCCCCCCCCCCCCC		46.9830377154
560PhosphorylationTASQSPSYDSKNMAP
CCCCCCCCCCCCCCC		27.8523749301
562PhosphorylationSQSPSYDSKNMAPKE
CCCCCCCCCCCCCHH		20.0730377154
563UbiquitinationQSPSYDSKNMAPKEN
CCCCCCCCCCCCHHH		48.0923749301
568UbiquitinationDSKNMAPKENLVETE
CCCCCCCHHHHHHHH		50.0922817900
578PhosphorylationLVETELRYKFKNKNK
HHHHHHHHHHCCCCC		33.1421440633
630PhosphorylationQSTLPYWSPSLLRKT
CCCCCCCCHHHHHHC		9.9621440633
632PhosphorylationTLPYWSPSLLRKTNK
CCCCCCHHHHHHCCC		34.2221440633
664PhosphorylationMLPEGVKTPLTKLDV
CCCCCCCCCCCCCEE		22.5628889911
798AcetylationIDLHDIFKKQIHTFE
EEHHHHHHHHCCCCH		44.0724489116
817PhosphorylationDIISKKGSSNPPSAS
HHHHCCCCCCCCCCC		35.5028889911
818PhosphorylationIISKKGSSNPPSASS
HHHCCCCCCCCCCCC		63.1228889911
834PhosphorylationNNNFLQATFSNGAST
CCCCEEEEECCCCCH		18.0324961812
836PhosphorylationNFLQATFSNGASTAT
CCEEEEECCCCCHHH		29.9628889911
840PhosphorylationATFSNGASTATKFTQ
EEECCCCCHHHHHHH		21.7024961812
841PhosphorylationTFSNGASTATKFTQQ
EECCCCCHHHHHHHH		37.5024961812
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 BUL2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUL2_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 BUL2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCK1_YEASTMCK1genetic
10958669
ROG1_YEASTROG1genetic
10958669
PFD6_YEASTYKE2genetic
17314980
RSP5_YEASTRSP5genetic
18434603
MCFS2_YEASTEHT1genetic
20093466
PYC2_YEASTPYC2genetic
20093466
DCC1_YEASTDCC1genetic
20093466
HIM1_YEASTHIM1genetic
20093466
RLA4_YEASTRPP2Bgenetic
20093466
CGR1_YEASTCGR1genetic
20093466
YG5Q_YEASTYGR273Cgenetic
20093466
DCOR_YEASTSPE1genetic
20093466
RL22A_YEASTRPL22Agenetic
20093466
BUL1_YEASTBUL1genetic
20093466
NST1_YEASTNST1genetic
20093466
NCBP2_YEASTCBC2genetic
20093466
ELP3_YEASTELP3genetic
20093466
AXL1_YEASTAXL1genetic
20093466
MEP3_YEASTMEP3genetic
20093466
HRR25_YEASTHRR25physical
20489023
XRN1_YEASTXRN1physical
20489023
MRM1_YEASTMRM1physical
20489023
NOP4_YEASTNOP4physical
20489023
RPM2_YEASTRPM2physical
20489023
RRP5_YEASTRRP5physical
20489023
RSP5_YEASTRSP5physical
20489023
UTP22_YEASTUTP22physical
20489023
NAT5_YEASTNAT5genetic
10958669
YN97_YEASTYNR068Cgenetic
22307975
BUL1_YEASTBUL1genetic
22307975
BSC5_YEASTBSC5genetic
22307975
KIN3_YEASTKIN3physical
22875988
NNF1_YEASTNNF1physical
22875988
VPS20_YEASTVPS20physical
22875988
YO223_YEASTDSC3physical
22875988
YN97_YEASTYNR068Cgenetic
25001409
BSC5_YEASTBSC5genetic
25001409
SMD1_YEASTSMD1genetic
27708008
SNF5_YEASTSNF5genetic
27708008
THRC_YEASTTHR4genetic
27708008
CDC37_YEASTCDC37genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SNU56_YEASTSNU56genetic
27708008
NSE3_YEASTNSE3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SDA1_YEASTSDA1genetic
27708008
RRP4_YEASTRRP4genetic
27708008
DED1_YEASTDED1genetic
27708008
GEM1_YEASTGEM1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
MCFS2_YEASTEHT1genetic
27708008
YG2A_YEASTYGR067Cgenetic
27708008
YG5Q_YEASTYGR273Cgenetic
27708008
DCOR_YEASTSPE1genetic
27708008
MMS22_YEASTMMS22genetic
27708008
BUL1_YEASTBUL1genetic
27708008
KIN4_YEASTKIN4genetic
27708008
ELP3_YEASTELP3genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
MDL2_YEASTMDL2genetic
27708008
AXL1_YEASTAXL1genetic
27708008
MEP3_YEASTMEP3genetic
27708008
PMP1_YEASTPMP1physical
26404137
ROD1_YEASTROD1genetic
28965784
ALY1_YEASTALY1genetic
24942738
ALY2_YEASTALY2genetic
24942738
UBP2_YEASTUBP2genetic
29129641
ATR_YEASTMEC1physical
29129641
SMC1_YEASTSMC1physical
29129641
SMC3_YEASTSMC3physical
29129641
CDC48_YEASTCDC48physical
29129641
RSP5_YEASTRSP5physical
29129641
LCD1_YEASTLCD1physical
29129641
RRP5_YEASTRRP5physical
29129641
UTP20_YEASTUTP20physical
29129641
VPS10_YEASTPEP1physical
29129641
NOP58_YEASTNOP58physical
29129641
UTP17_YEASTNAN1physical
29129641
SC160_YEASTSCP160physical
29129641
BMS1_YEASTBMS1physical
29129641
MAK21_YEASTMAK21physical
29129641
UTP14_YEASTUTP14physical
29129641
GDE1_YEASTGDE1physical
29129641
NCBP1_YEASTSTO1physical
29129641
RPB2_YEASTRPB2physical
29129641
TR120_YEASTTRS120physical
29129641
UTP12_YEASTDIP2physical
29129641
UTP21_YEASTUTP21physical
29129641
PWP2_YEASTPWP2physical
29129641
SPT16_YEASTSPT16physical
29129641
RRP44_YEASTDIS3physical
29129641
NOP14_YEASTNOP14physical
29129641
RPN1_YEASTRPN1physical
29129641
SEC24_YEASTSEC24physical
29129641
STV1_YEASTSTV1physical
29129641
RPN2_YEASTRPN2physical
29129641
UTP4_YEASTUTP4physical
29129641
PRP43_YEASTPRP43physical
29129641
NOP4_YEASTNOP4physical
29129641
MPP10_YEASTMPP10physical
29129641
NOC2_YEASTNOC2physical
29129641
NOP2_YEASTNOP2physical
29129641
EF2_YEASTEFT2physical
29129641
HSC82_YEASTHSC82physical
29129641
PESC_YEASTNOP7physical
29129641
MNN1_YEASTMNN1physical
29129641
6P21_YEASTPFK26physical
29129641
6P22_YEASTPFK27physical
29129641
KRI1_YEASTKRI1physical
29129641
MAK5_YEASTMAK5physical
29129641
LEUC_YEASTLEU1physical
29129641
DBP4_YEASTHCA4physical
29129641
PWP1_YEASTPWP1physical
29129641
ESF1_YEASTESF1physical
29129641
PUF6_YEASTPUF6physical
29129641
RRP6_YEASTRRP6physical
29129641
CDC16_YEASTCDC16physical
29129641
VTC4_YEASTVTC4physical
29129641
TCPQ_YEASTCCT8physical
29129641
TCPA_YEASTTCP1physical
29129641
TCPE_YEASTCCT5physical
29129641
ENP1_YEASTENP1physical
29129641
TCPG_YEASTCCT3physical
29129641
HAS1_YEASTHAS1physical
29129641
NOP12_YEASTNOP12physical
29129641
UTP7_YEASTUTP7physical
29129641
TCPH_YEASTCCT7physical
29129641
CBF5_YEASTCBF5physical
29129641
TCPZ_YEASTCCT6physical
29129641
TCPD_YEASTCCT4physical
29129641
NOP56_YEASTNOP56physical
29129641
RPN3_YEASTRPN3physical
29129641
NOC4_YEASTNOC4physical
29129641
PDC1_YEASTPDC1physical
29129641
VPS45_YEASTVPS45physical
29129641
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUL2_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-21 AND THR-22, 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 THR-22, AND MASSSPECTROMETRY.

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