UPC2_YEAST - dbPTM
UPC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UPC2_YEAST
UniProt AC Q12151
Protein Name Sterol uptake control protein 2
Gene Name UPC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 913
Subcellular Localization Nucleus .
Protein Description Transcription factor that is involved in activation of anaerobic genes such as DAN/TIR cell wall mannoprotein genes and YML083c. Appears to bind to anaerobic response elements (AR1) with the consensus sequence 5'-TCGTTYAG-3' present in the promoter regions of DAN/TIR genes. Involved in sterol uptake and regulation of the sterol biosynthesis. Binds to sterol regulatory elements (SRE) with the consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters. May be involved in down-regulation of CWP2 during anaerobic adaptation..
Protein Sequence MSEVGIQNHKKAVTKPRRREKVIELIEVDGKKVSTTSTGKRKFHNKSKNGCDNCKRRRVKCDEGKPACRKCTNMKLECQYTPIHLRKGRGATVVKYVTRKADGSVESDSSVDLPPTIKKEQTPFNDIQSAVKASGSSNDSFPSSASTTKSESEEKSSAPIEDKNNMTPLSMGLQGTINKKDMMNNFFSQNGTIGFGSPERLNSGIDGLLLPPLPSGNMGAFQLQQQQQVQQQSQPQTQAQQASGTPNERYGSFDLAGSPALQSTGMSLSNSLSGMLLCNRIPSGQNYTQQQLQYQLHQQLQLQQHQQVQLQQYQQLRQEQHQQVQQQQQEQLQQYQQHFLQQQQQVLLQQEQQPNDEEGGVQEENSKKVKEGPLQSQTSETTLNSDAATLQADALSQLSKMGLSLKSLSTFPTAGIGGVSYDFQELLGIKFPINNGNSRATKASNAEEALANMQEHHERAAASVKENDGQLSDTKSPAPSNNAQGGSASIMEPQAADAVSTMAPISMIERNMNRNSNISPSTPSAVLNDRQEMQDSISSLGNLTKAALENNEPTISLQTSQTENEDDASRQDMTSKINNEADRSSVSAGTSNIAKLLDLSTKGNLNLIDMKLFHHYCTKVWPTITAAKVSGPEIWRDYIPELAFDYPFLMHALLAFSATHLSRTETGLEQYVSSHRLDALRLLREAVLEISENNTDALVASALILIMDSLANASGNGTVGNQSLNSMSPSAWIFHVKGAATILTAVWPLSERSKFHNIISVDLSDLGDVINPDVGTITELVCFDESIADLYPVGLDSPYLITLAYLDKLHREKNQGDFILRVFTFPALLDKTFLALLMTGDLGAMRIMRSYYKLLRGFATEVKDKVWFLEGVTQVLPQDVDEYSGGGGMHMMLDFLGGGLPSMTTTNFSDFSL
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
10AcetylationEVGIQNHKKAVTKPR
CCCCHHHHHCCCCCC		50.4025381059
95AcetylationGRGATVVKYVTRKAD
CCCCEEEEEEEECCC		29.6625381059
104PhosphorylationVTRKADGSVESDSSV
EEECCCCCCCCCCCC		24.2129734811
107PhosphorylationKADGSVESDSSVDLP
CCCCCCCCCCCCCCC		40.4120377248
109PhosphorylationDGSVESDSSVDLPPT
CCCCCCCCCCCCCCC		41.3520377248
110PhosphorylationGSVESDSSVDLPPTI
CCCCCCCCCCCCCCC		25.3320377248
122PhosphorylationPTIKKEQTPFNDIQS
CCCCCCCCCHHHHHH		30.8222369663
144PhosphorylationSNDSFPSSASTTKSE
CCCCCCCCCCCCCCC		26.8623749301
147PhosphorylationSFPSSASTTKSESEE
CCCCCCCCCCCCCCC		37.6521440633
150PhosphorylationSSASTTKSESEEKSS
CCCCCCCCCCCCCCC		44.2420377248
152PhosphorylationASTTKSESEEKSSAP
CCCCCCCCCCCCCCC		59.1420377248
156PhosphorylationKSESEEKSSAPIEDK
CCCCCCCCCCCCCCC		34.7028889911
157PhosphorylationSESEEKSSAPIEDKN
CCCCCCCCCCCCCCC		49.4828889911
167PhosphorylationIEDKNNMTPLSMGLQ
CCCCCCCCCCHHHCC		24.1728889911
170PhosphorylationKNNMTPLSMGLQGTI
CCCCCCCHHHCCCCC		16.4128889911
176PhosphorylationLSMGLQGTINKKDMM
CHHHCCCCCCHHHHH		14.3928889911
197PhosphorylationNGTIGFGSPERLNSG
CCCCCCCCHHHCCCC		22.7127017623
376PhosphorylationVKEGPLQSQTSETTL
CCCCCCCCCCCCCCC		43.0121551504
378PhosphorylationEGPLQSQTSETTLNS
CCCCCCCCCCCCCCC		33.5027017623
379PhosphorylationGPLQSQTSETTLNSD
CCCCCCCCCCCCCCC		25.8827017623
381PhosphorylationLQSQTSETTLNSDAA
CCCCCCCCCCCCCHH		36.0321551504
382PhosphorylationQSQTSETTLNSDAAT
CCCCCCCCCCCCHHH		21.6427017623
385PhosphorylationTSETTLNSDAATLQA
CCCCCCCCCHHHHHH		31.5727017623
407PhosphorylationKMGLSLKSLSTFPTA
HCCCCHHHHCCCCCC		32.6119779198
410PhosphorylationLSLKSLSTFPTAGIG
CCHHHHCCCCCCCCC		38.6419779198
463PhosphorylationHHERAAASVKENDGQ
HHHHHHHHHHHCCCC		29.0623749301
472PhosphorylationKENDGQLSDTKSPAP
HHCCCCCCCCCCCCC		35.0325521595
476PhosphorylationGQLSDTKSPAPSNNA
CCCCCCCCCCCCCCC		28.5219779198
487PhosphorylationSNNAQGGSASIMEPQ
CCCCCCCCCCCCCCC		26.1827017623
506PhosphorylationVSTMAPISMIERNMN
HHHCCCHHHHHHHCC		16.7927017623
516PhosphorylationERNMNRNSNISPSTP
HHHCCCCCCCCCCCH		32.1028889911
519PhosphorylationMNRNSNISPSTPSAV
CCCCCCCCCCCHHHH		19.6321082442
521PhosphorylationRNSNISPSTPSAVLN
CCCCCCCCCHHHHHC		46.2730377154
522PhosphorylationNSNISPSTPSAVLND
CCCCCCCCHHHHHCC		25.3321440633
524PhosphorylationNISPSTPSAVLNDRQ
CCCCCCHHHHHCCHH		30.9723749301
556PhosphorylationENNEPTISLQTSQTE
HCCCCCEEEECCCCC		19.5321440633
559PhosphorylationEPTISLQTSQTENED
CCCEEEECCCCCCCC		28.2623749301
560PhosphorylationPTISLQTSQTENEDD
CCEEEECCCCCCCCH		23.3423749301
562PhosphorylationISLQTSQTENEDDAS
EEEECCCCCCCCHHH		40.3121440633
569PhosphorylationTENEDDASRQDMTSK
CCCCCHHHHHHHHHH		37.1523749301
584PhosphorylationINNEADRSSVSAGTS
HHCHHHHHHCCCCCH		35.3223749301
585PhosphorylationNNEADRSSVSAGTSN
HCHHHHHHCCCCCHH		22.4521551504
587PhosphorylationEADRSSVSAGTSNIA
HHHHHHCCCCCHHHH		23.9521440633
590PhosphorylationRSSVSAGTSNIAKLL
HHHCCCCCHHHHHHH		20.5127717283
591PhosphorylationSSVSAGTSNIAKLLD
HHCCCCCHHHHHHHC		25.8927717283
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 UPC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UPC2_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 UPC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATN2_YEASTENA2genetic
10073572
HSP26_YEASTHSP26physical
16554755
BUL2_YEASTBUL2physical
16554755
ERG2_YEASTERG2genetic
16702413
ERG6_YEASTERG6genetic
16702413
ERG28_YEASTERG28genetic
16702413
ELO3_YEASTELO3genetic
15638242
TCD2_YEASTTCD2genetic
19060182
BEM2_YEASTBEM2genetic
19060182
YFE0_YEASTYFL040Wgenetic
19060182
RAS2_YEASTRAS2genetic
19060182
LAM4_YEASTYHR080Cgenetic
19060182
ECM15_YEASTECM15genetic
19060182
AIM44_YEASTAIM44genetic
19060182
CYK2_YEASTHOF1genetic
19060182
FNTB_YEASTRAM1genetic
19060182
TVP18_YEASTTVP18genetic
19060182
SCY1_YEASTSCY1genetic
19060182
DET1_YEASTDET1genetic
19060182
MOT3_YEASTMOT3genetic
19060182
UBP13_YEASTUBP13genetic
20093466
SIF2_YEASTSIF2genetic
20093466
TPS1_YEASTTPS1genetic
20093466
AIM4_YEASTAIM4genetic
20093466
THRC_YEASTTHR4genetic
20093466
BRE1_YEASTBRE1genetic
20093466
MED5_YEASTNUT1genetic
20093466
EIF2A_YEASTYGR054Wgenetic
20093466
PEF1_YEASTPEF1genetic
20093466
CHO2_YEASTCHO2genetic
20093466
FYV4_YEASTFYV4genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
PIR5_YEASTYJL160Cgenetic
20093466
DCOR_YEASTSPE1genetic
20093466
IME1_YEASTIME1genetic
20959818
KCS1_YEASTKCS1genetic
21127252
FUS3_YEASTFUS3genetic
21127252
RDS1_YEASTRDS1genetic
21127252
PP2C1_YEASTPTC1genetic
21127252
IPMK_YEASTARG82genetic
21127252
KIN82_YEASTKIN82genetic
21127252
TOD6_YEASTTOD6genetic
21127252
KCC4_YEASTKCC4genetic
21127252
KIN3_YEASTKIN3genetic
21127252
SEC22_YEASTSEC22genetic
23891562
YPT6_YEASTYPT6genetic
23891562
ERG26_YEASTERG26genetic
23891562
ECM22_YEASTECM22physical
18675371
UPC2_YEASTUPC2physical
25655993
STE12_YEASTSTE12genetic
26448198
DEP1_YEASTDEP1genetic
27708008
TPS1_YEASTTPS1genetic
27708008
AIM4_YEASTAIM4genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
THRC_YEASTTHR4genetic
27708008
CHAC_YEASTGCG1genetic
27708008
MED5_YEASTNUT1genetic
27708008
HOS2_YEASTHOS2genetic
27708008
IMB5_YEASTKAP114genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
ATG26_YEASTATG26genetic
27708008
ECM22_YEASTECM22genetic
27708008
GIS4_YEASTGIS4genetic
27708008
FET3_YEASTFET3genetic
27708008
YNO3_YEASTYNL143Cgenetic
27708008
YO098_YEASTYOL098Cgenetic
27708008
INO4_YEASTINO4genetic
27708008
ERFD_YEASTSHR5genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UPC2_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 THR-122; SER-519; THR-522;SER-560; SER-584 AND SER-585, AND MASS 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-122, AND MASSSPECTROMETRY.

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