MPG1_YEAST - dbPTM
MPG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPG1_YEAST
UniProt AC P41940
Protein Name Mannose-1-phosphate guanyltransferase
Gene Name PSA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 361
Subcellular Localization Cytoplasm .
Protein Description Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint..
Protein Sequence MKGLILVGGYGTRLRPLTLTVPKPLVEFGNRPMILHQIEALANAGVTDIVLAVNYRPEVMVETLKKYEKEYGVNITFSVETEPLGTAGPLKLAEDVLKKDNSPFFVLNSDVICEYPFKELADFHKAHGGKGTIVATKVDEPSKYGVIVHDIATPNLIDRFVEKPKEFVGNRINAGLYILNPEVIDLIEMKPTSIEKETFPILVEEKQLYSFDLEGFWMDVGQPKDFLSGTVLYLNSLAKRQPKKLATGANIVGNALIDPTAKISSTAKIGPDVVIGPNVTIGDGVRITRSVVLCNSTIKNHSLVKSTIVGWNSTVGQWCRLEGVTVLGDDVEVKDEIYINGGKVLPHKSISDNVPKEAIIM
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
10PhosphorylationGLILVGGYGTRLRPL
CEEEECCCCCCEEEE		14.9222369663
12PhosphorylationILVGGYGTRLRPLTL
EEECCCCCCEEEEEE		20.3222369663
18PhosphorylationGTRLRPLTLTVPKPL
CCCEEEEEEECCCCC		24.0622369663
20PhosphorylationRLRPLTLTVPKPLVE
CEEEEEEECCCCCEE		29.5322369663
98AcetylationKLAEDVLKKDNSPFF
HHHHHHHCCCCCCEE		58.9124489116
982-HydroxyisobutyrylationKLAEDVLKKDNSPFF
HHHHHHHCCCCCCEE		58.91-
98SuccinylationKLAEDVLKKDNSPFF
HHHHHHHCCCCCCEE		58.9123954790
118AcetylationVICEYPFKELADFHK
EEEECCHHHHHHHHH		47.5225381059
125AcetylationKELADFHKAHGGKGT
HHHHHHHHHHCCCCE		41.9124489116
1252-HydroxyisobutyrylationKELADFHKAHGGKGT
HHHHHHHHHHCCCCE		41.91-
125UbiquitinationKELADFHKAHGGKGT
HHHHHHHHHHCCCCE		41.9122817900
130SuccinylationFHKAHGGKGTIVATK
HHHHHCCCCEEEEEE		58.4323954790
1302-HydroxyisobutyrylationFHKAHGGKGTIVATK
HHHHHCCCCEEEEEE		58.43-
130UbiquitinationFHKAHGGKGTIVATK
HHHHHCCCCEEEEEE		58.4323749301
132PhosphorylationKAHGGKGTIVATKVD
HHHCCCCEEEEEECC		18.7619823750
136PhosphorylationGKGTIVATKVDEPSK
CCCEEEEEECCCHHH		22.2421440633
137AcetylationKGTIVATKVDEPSKY
CCEEEEEECCCHHHC		37.6424489116
1372-HydroxyisobutyrylationKGTIVATKVDEPSKY
CCEEEEEECCCHHHC		37.64-
137UbiquitinationKGTIVATKVDEPSKY
CCEEEEEECCCHHHC		37.6423749301
137SuccinylationKGTIVATKVDEPSKY
CCEEEEEECCCHHHC		37.6423954790
142PhosphorylationATKVDEPSKYGVIVH
EEECCCHHHCCEEEE		36.1421440633
143AcetylationTKVDEPSKYGVIVHD
EECCCHHHCCEEEEE		57.6624489116
143UbiquitinationTKVDEPSKYGVIVHD
EECCCHHHCCEEEEE		57.6623749301
153PhosphorylationVIVHDIATPNLIDRF
EEEEECCCCCHHHHH		17.0322369663
163UbiquitinationLIDRFVEKPKEFVGN
HHHHHHHCCHHHCCC		56.9722817900
163AcetylationLIDRFVEKPKEFVGN
HHHHHHHCCHHHCCC		56.9724489116
1632-HydroxyisobutyrylationLIDRFVEKPKEFVGN
HHHHHHHCCHHHCCC		56.97-
165UbiquitinationDRFVEKPKEFVGNRI
HHHHHCCHHHCCCCC		74.8922817900
165AcetylationDRFVEKPKEFVGNRI
HHHHHCCHHHCCCCC		74.8924489116
1652-HydroxyisobutyrylationDRFVEKPKEFVGNRI
HHHHHCCHHHCCCCC		74.89-
190UbiquitinationVIDLIEMKPTSIEKE
HEEEEECCCCCCCCC		32.1424961812
196UbiquitinationMKPTSIEKETFPILV
CCCCCCCCCCCCEEE		61.4523749301
228PhosphorylationGQPKDFLSGTVLYLN
CCCCCHHHHHHHHHH		32.2021440633
230PhosphorylationPKDFLSGTVLYLNSL
CCCHHHHHHHHHHHH		12.1722369663
239AcetylationLYLNSLAKRQPKKLA
HHHHHHHHCCCCCCC		57.7824489116
239UbiquitinationLYLNSLAKRQPKKLA
HHHHHHHHCCCCCCC		57.7823749301
243UbiquitinationSLAKRQPKKLATGAN
HHHHCCCCCCCCCCC		52.6722817900
244UbiquitinationLAKRQPKKLATGANI
HHHCCCCCCCCCCCE		50.4623749301
247PhosphorylationRQPKKLATGANIVGN
CCCCCCCCCCCEECC		47.4621440633
262AcetylationALIDPTAKISSTAKI
HHCCCCCCCCCCCCC		45.6724489116
262UbiquitinationALIDPTAKISSTAKI
HHCCCCCCCCCCCCC		45.6724961812
268AcetylationAKISSTAKIGPDVVI
CCCCCCCCCCCCEEE		48.5624489116
268UbiquitinationAKISSTAKIGPDVVI
CCCCCCCCCCCCEEE		48.5623749301
280PhosphorylationVVIGPNVTIGDGVRI
EEECCCCEECCCCEE		26.3628889911
290PhosphorylationDGVRITRSVVLCNST
CCCEEECEEEECCCC		14.1322369663
296PhosphorylationRSVVLCNSTIKNHSL
CEEEECCCCCCCCCE		30.4322369663
297PhosphorylationSVVLCNSTIKNHSLV
EEEECCCCCCCCCEE		23.2122369663
299MethylationVLCNSTIKNHSLVKS
EECCCCCCCCCEEEE		49.0120137074
299AcetylationVLCNSTIKNHSLVKS
EECCCCCCCCCEEEE		49.0124489116
299UbiquitinationVLCNSTIKNHSLVKS
EECCCCCCCCCEEEE		49.0123749301
305UbiquitinationIKNHSLVKSTIVGWN
CCCCCEEEEEEECCC		47.3723749301
306PhosphorylationKNHSLVKSTIVGWNS
CCCCEEEEEEECCCC		18.8421440633
343UbiquitinationEIYINGGKVLPHKSI
EEEECCCEECCCCCC		41.8322817900
348UbiquitinationGGKVLPHKSISDNVP
CCEECCCCCCCCCCC		47.7723749301
348AcetylationGGKVLPHKSISDNVP
CCEECCCCCCCCCCC		47.7724489116
349PhosphorylationGKVLPHKSISDNVPK
CEECCCCCCCCCCCH		25.0422369663
351PhosphorylationVLPHKSISDNVPKEA
ECCCCCCCCCCCHHH		30.1722369663
356AcetylationSISDNVPKEAIIM--
CCCCCCCHHHCCC--		56.3422865919
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 MPG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPG1_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 MPG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE2_YEASTPDE2genetic
10974101
GRP78_YEASTKAR2physical
16554755
NAP1_YEASTNAP1physical
16554755
CDC31_YEASTCDC31physical
16554755
ACAC_YEASTACC1physical
16429126
GCN20_YEASTGCN20physical
16429126
GFA1_YEASTGFA1physical
16429126
HSP60_YEASTHSP60physical
16429126
THDH_YEASTILV1physical
16429126
RL18A_YEASTRPL18Aphysical
16429126
RL18B_YEASTRPL18Aphysical
16429126
RUVB2_YEASTRVB2physical
16429126
TBA3_YEASTTUB3physical
16429126
CARB_YEASTCPA2physical
16429126
RL36B_YEASTRPL36Bphysical
16429126
RPN2_YEASTRPN2physical
16429126
RS14A_YEASTRPS14Aphysical
16429126
PRS6B_YEASTRPT3physical
16429126
HSP7F_YEASTSSE1physical
16429126
TSA1_YEASTTSA1physical
16429126
SYV_YEASTVAS1physical
16429126
YO098_YEASTYOL098Cphysical
16429126
CLU_YEASTCLU1physical
16429126
RL4A_YEASTRPL4Aphysical
16429126
RPN1_YEASTRPN1physical
16429126
TCPQ_YEASTCCT8physical
16429126
KPYK1_YEASTCDC19physical
16429126
RSSA2_YEASTRPS0Bphysical
16429126
RS24A_YEASTRPS24Bphysical
16429126
RS24B_YEASTRPS24Bphysical
16429126
PRS7_YEASTRPT1physical
16429126
SMC3_YEASTSMC3physical
16429126
RL10_YEASTRPL10physical
16429126
RL13B_YEASTRPL13Bphysical
16429126
RL28_YEASTRPL28physical
16429126
RL2A_YEASTRPL2Aphysical
16429126
RL2B_YEASTRPL2Aphysical
16429126
RL7A_YEASTRPL7Aphysical
16429126
RL8B_YEASTRPL8Bphysical
16429126
RRP5_YEASTRRP5physical
16429126
TBB_YEASTTUB2physical
16429126
SYEC_YEASTGUS1physical
16429126
RPA2_YEASTRPA135physical
16429126
COPB2_YEASTSEC27physical
16429126
YG3A_YEASTYGR130Cphysical
18467557
TSR2_YEASTTSR2physical
18467557
MAL13_YEASTMAL13physical
18467557
COPB_YEASTSEC26physical
18467557
LKHA4_YEASTLAP2physical
18467557
ATX1_YEASTATX1physical
18467557
EF2_YEASTEFT2physical
18467557
SMT3_YEASTSMT3physical
18719252
ATP5E_YEASTATP15genetic
21623372
ELO2_YEASTELO2genetic
21623372
LTHAD_YEASTSRY1genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
PHSG_YEASTGPH1genetic
21623372
ETR1_YEASTETR1genetic
21623372
CYS3_YEASTCYS3genetic
21623372
PYR1_YEASTURA2genetic
21623372
IDH1_YEASTIDH1genetic
21623372
LEUC_YEASTLEU1genetic
21623372
PLB1_YEASTPLB1genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
AVT4_YEASTAVT4genetic
21623372
6PGD1_YEASTGND1genetic
21623372
DHOM_YEASTHOM6genetic
21623372
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPG1_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-153; THR-280 ANDSER-351, AND MASS SPECTROMETRY.

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