UGPA1_YEAST - dbPTM
UGPA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UGPA1_YEAST
UniProt AC P32861
Protein Name UTP--glucose-1-phosphate uridylyltransferase
Gene Name UGP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 499
Subcellular Localization
Protein Description Plays a central role as a glucosyl donor in cellular metabolic pathways..
Protein Sequence MSTKKHTKTHSTYAFESNTNSVAASQMRNALNKLADSSKLDDAARAKFENELDSFFTLFRRYLVEKSSRTTLEWDKIKSPNPDEVVKYEIISQQPENVSNLSKLAVLKLNGGLGTSMGCVGPKSVIEVREGNTFLDLSVRQIEYLNRQYDSDVPLLLMNSFNTDKDTEHLIKKYSANRIRIRSFNQSRFPRVYKDSLLPVPTEYDSPLDAWYPPGHGDLFESLHVSGELDALIAQGREILFVSNGDNLGATVDLKILNHMIETGAEYIMELTDKTRADVKGGTLISYDGQVRLLEVAQVPKEHIDEFKNIRKFTNFNTNNLWINLKAVKRLIESSNLEMEIIPNQKTITRDGHEINVLQLETACGAAIRHFDGAHGVVVPRSRFLPVKTCSDLLLVKSDLFRLEHGSLKLDPSRFGPNPLIKLGSHFKKVSGFNARIPHIPKIVELDHLTITGNVFLGKDVTLRGTVIIVCSDGHKIDIPNGSILENVVVTGNLQILEH
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
2Acetylation------MSTKKHTKT
------CCCCCCCCC		49.2722814378
7Phosphorylation-MSTKKHTKTHSTYA
-CCCCCCCCCCCCEE		46.6628889911
8AcetylationMSTKKHTKTHSTYAF
CCCCCCCCCCCCEEE		43.9124489116
9PhosphorylationSTKKHTKTHSTYAFE
CCCCCCCCCCCEEEE		23.3922369663
11PhosphorylationKKHTKTHSTYAFESN
CCCCCCCCCEEEECC		28.4822369663
12PhosphorylationKHTKTHSTYAFESNT
CCCCCCCCEEEECCC		15.9725521595
13PhosphorylationHTKTHSTYAFESNTN
CCCCCCCEEEECCCC		16.5922369663
17PhosphorylationHSTYAFESNTNSVAA
CCCEEEECCCCHHHH		42.3622369663
19PhosphorylationTYAFESNTNSVAASQ
CEEEECCCCHHHHHH		37.8422369663
21PhosphorylationAFESNTNSVAASQMR
EEECCCCHHHHHHHH		15.8722890988
25PhosphorylationNTNSVAASQMRNALN
CCCHHHHHHHHHHHH		18.1222890988
33AcetylationQMRNALNKLADSSKL
HHHHHHHHHHCHHCC		45.9924489116
33UbiquitinationQMRNALNKLADSSKL
HHHHHHHHHHCHHCC		45.9923749301
37PhosphorylationALNKLADSSKLDDAA
HHHHHHCHHCCCHHH		24.6219823750
38PhosphorylationLNKLADSSKLDDAAR
HHHHHCHHCCCHHHH		37.4723749301
39AcetylationNKLADSSKLDDAARA
HHHHCHHCCCHHHHH		60.9424489116
39UbiquitinationNKLADSSKLDDAARA
HHHHCHHCCCHHHHH		60.9423749301
392-HydroxyisobutyrylationNKLADSSKLDDAARA
HHHHCHHCCCHHHHH		60.94-
66AcetylationFRRYLVEKSSRTTLE
HHHHHHHHCCCCEEE		46.3724489116
67PhosphorylationRRYLVEKSSRTTLEW
HHHHHHHCCCCEEEC		16.1428889911
70PhosphorylationLVEKSSRTTLEWDKI
HHHHCCCCEEECCCC		37.3728889911
76AcetylationRTTLEWDKIKSPNPD
CCEEECCCCCCCCHH		53.7822865919
78AcetylationTLEWDKIKSPNPDEV
EEECCCCCCCCHHHE		66.6524489116
79PhosphorylationLEWDKIKSPNPDEVV
EECCCCCCCCHHHEE		33.1222369663
87AcetylationPNPDEVVKYEIISQQ
CCHHHEEEEEEECCC		42.2024489116
88PhosphorylationNPDEVVKYEIISQQP
CHHHEEEEEEECCCC		10.7622369663
92PhosphorylationVVKYEIISQQPENVS
EEEEEEECCCCCCCC		28.5527017623
99PhosphorylationSQQPENVSNLSKLAV
CCCCCCCCCHHHEEE		43.5727017623
102PhosphorylationPENVSNLSKLAVLKL
CCCCCCHHHEEEEEE		29.8528889911
103AcetylationENVSNLSKLAVLKLN
CCCCCHHHEEEEEEC		43.5624489116
116PhosphorylationLNGGLGTSMGCVGPK
ECCCCCCCCCCCCCC		16.0428889911
165AcetylationMNSFNTDKDTEHLIK
EECCCCCCCHHHHHH		65.5924489116
172AcetylationKDTEHLIKKYSANRI
CCHHHHHHHHCCCCE		52.6024489116
183PhosphorylationANRIRIRSFNQSRFP
CCCEEEEECCHHCCC		26.6117563356
267PhosphorylationMIETGAEYIMELTDK
HHHHCCHHHHHHCCC		12.6728889911
272PhosphorylationAEYIMELTDKTRADV
CHHHHHHCCCCCCCC		23.3428889911
275PhosphorylationIMELTDKTRADVKGG
HHHHCCCCCCCCCCC		33.6226447709
280AcetylationDKTRADVKGGTLISY
CCCCCCCCCCEEEEE		52.7724489116
280UbiquitinationDKTRADVKGGTLISY
CCCCCCCCCCEEEEE		52.7723749301
283PhosphorylationRADVKGGTLISYDGQ
CCCCCCCEEEEECCE		29.5927017623
287PhosphorylationKGGTLISYDGQVRLL
CCCEEEEECCEEEEE		19.6627017623
301AcetylationLEVAQVPKEHIDEFK
EEEECCCHHHHHHHH		64.1724489116
308AcetylationKEHIDEFKNIRKFTN
HHHHHHHHCHHHHCC		49.7924489116
3082-HydroxyisobutyrylationKEHIDEFKNIRKFTN
HHHHHHHHCHHHHCC		49.79-
326AcetylationNNLWINLKAVKRLIE
CCEEEEHHHHHHHHH		46.8024489116
346AcetylationMEIIPNQKTITRDGH
EEECCCCCEECCCCE		48.8424489116
346UbiquitinationMEIIPNQKTITRDGH
EEECCCCCEECCCCE		48.8424961812
369MethylationTACGAAIRHFDGAHG
HHHHHHHHHCCCCCE		21.5023865587
388AcetylationRSRFLPVKTCSDLLL
HHHCCCCCCHHHEEE		41.7024489116
391PhosphorylationFLPVKTCSDLLLVKS
CCCCCCHHHEEEECC		36.2021440633
397AcetylationCSDLLLVKSDLFRLE
HHHEEEECCCCEECC		37.9224489116
397UbiquitinationCSDLLLVKSDLFRLE
HHHEEEECCCCEECC		37.9223749301
407PhosphorylationLFRLEHGSLKLDPSR
CEECCCCCEECCHHH		25.0028889911
409AcetylationRLEHGSLKLDPSRFG
ECCCCCEECCHHHCC		53.1724489116
409UbiquitinationRLEHGSLKLDPSRFG
ECCCCCEECCHHHCC		53.1723749301
422AcetylationFGPNPLIKLGSHFKK
CCCCCCEECCCCCEE		55.2524489116
425PhosphorylationNPLIKLGSHFKKVSG
CCCEECCCCCEECCC		35.8721440633
428AcetylationIKLGSHFKKVSGFNA
EECCCCCEECCCCCC		47.0125381059
429UbiquitinationKLGSHFKKVSGFNAR
ECCCCCEECCCCCCC		40.4623749301
431PhosphorylationGSHFKKVSGFNARIP
CCCCEECCCCCCCCC		46.6921440633
450PhosphorylationIVELDHLTITGNVFL
EEECEEEEEECCEEC		17.0519779198
452PhosphorylationELDHLTITGNVFLGK
ECEEEEEECCEECCC		19.9119779198
459UbiquitinationTGNVFLGKDVTLRGT
ECCEECCCCEEECCE		51.6923749301
462PhosphorylationVFLGKDVTLRGTVII
EECCCCEEECCEEEE		22.3726447709
466PhosphorylationKDVTLRGTVIIVCSD
CCEEECCEEEEEECC		11.3326447709
472PhosphorylationGTVIIVCSDGHKIDI
CEEEEEECCCCEEEC		35.4128889911
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 UGPA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UGPA1_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 UGPA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UGPA1_YEASTUGP1physical
11967834
FBRL_YEASTNOP1physical
16554755
NOP14_YEASTNOP14physical
16554755
SAS10_YEASTSAS10physical
16554755
MPP10_YEASTMPP10physical
16554755
YGZ2_YEASTYGL242Cphysical
16554755
UGPA2_YEASTYHL012Wgenetic
18408719
UGPA2_YEASTYHL012Wgenetic
16941010
UGPA1_YEASTUGP1physical
17010990
PDC6_YEASTPDC6genetic
21623372
METC_YEASTIRC7genetic
21623372
ATP5E_YEASTATP15genetic
21623372
AATC_YEASTAAT2genetic
21623372
NDH2_YEASTNDE2genetic
21623372
MAL31_YEASTMAL31genetic
21623372
TAL1_YEASTTAL1genetic
21623372
ETR1_YEASTETR1genetic
21623372
PYC2_YEASTPYC2genetic
21623372
SCS7_YEASTSCS7genetic
21623372
INP53_YEASTINP53genetic
21623372
INO1_YEASTINO1genetic
21623372
THI6_YEASTTHI6genetic
21623372
CRC1_YEASTCRC1genetic
21623372
DGAT2_YEASTDGA1genetic
21623372
ELO1_YEASTELO1genetic
21623372
CEM1_YEASTCEM1genetic
21623372
SPSY_YEASTSPE4genetic
21623372
GCY1_YEASTGCY1genetic
21623372
ATPO_YEASTATP5genetic
21623372
QCR10_YEASTQCR10genetic
21623372
ERG2_YEASTERG2genetic
21623372
HTD2_YEASTHTD2genetic
21623372
TREA_YEASTNTH1genetic
21623372
UBR1_YEASTUBR1genetic
22670231
TCPZ_YEASTCCT6genetic
27708008
BUD31_YEASTBUD31genetic
27708008
SLH1_YEASTSLH1genetic
27708008
CYPB_YEASTCPR2genetic
27708008
TOR1_YEASTTOR1genetic
27708008
LOT6_YEASTLOT6genetic
27708008
YAP4_YEASTCIN5genetic
27708008
AGC1_YEASTAGC1genetic
27708008
MED8_YEASTMED8genetic
27708008
NSE4_YEASTNSE4genetic
27708008
RPB1_YEASTRPO21genetic
27708008
SLU7_YEASTSLU7genetic
27708008
GPI11_YEASTGPI11genetic
27708008
FCF1_YEASTFCF1genetic
27708008
SYF1_YEASTSYF1genetic
27708008
GPI19_YEASTGPI19genetic
27708008
PANK_YEASTCAB1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
RRP41_YEASTSKI6genetic
27708008
MED6_YEASTMED6genetic
27708008
RRP4_YEASTRRP4genetic
27708008
IPI1_YEASTIPI1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NOC3_YEASTNOC3genetic
27708008
LST8_YEASTLST8genetic
27708008
NOP2_YEASTNOP2genetic
27708008
BRX1_YEASTBRX1genetic
27708008
MED7_YEASTMED7genetic
27708008
RPB2_YEASTRPB2genetic
27708008
SYA_YEASTALA1genetic
27708008
GPI2_YEASTGPI2genetic
27708008
NAB3_YEASTNAB3genetic
27708008
ARP7_YEASTARP7genetic
27708008
CHS3_YEASTCHS3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
IPT1_YEASTIPT1genetic
27708008
PP2C2_YEASTPTC2genetic
27708008
SWI4_YEASTSWI4genetic
27708008
CGR1_YEASTCGR1genetic
27708008
CHS6_YEASTCHS6genetic
27708008
CHS5_YEASTCHS5genetic
27708008
ROM2_YEASTROM2genetic
27708008
MKS1_YEASTMKS1genetic
27708008
NOP12_YEASTNOP12genetic
27708008
RTG1_YEASTRTG1genetic
27708008
RRP6_YEASTRRP6genetic
27708008
LDB19_YEASTLDB19genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UGPA1_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-9; SER-11; THR-12;TYR-13; SER-79; SER-102; SER-116 AND SER-391, 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-9 AND SER-183, 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 THR-9; SER-11; THR-12;SER-17; THR-19 AND SER-21, 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-11, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.

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