MDG1_YEAST - dbPTM
MDG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MDG1_YEAST
UniProt AC P53885
Protein Name Signal transduction protein MDG1
Gene Name MDG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 366
Subcellular Localization Cell membrane
Peripheral membrane protein .
Protein Description Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells..
Protein Sequence MQSSLPQFTFKWPKGPEAIILTGTFDDWKGTLPMVKDPSGAFEITLPVTFDSPSSKFYFKFIVDGQWLPSKDYKVNIDEGVENNFITEEDVIKQRENGSSTLVPESAGLAVSKNAPLIEPEAEKRAKKLRKFKIKRVIKTNKQTGERSIFSQEVVELPDSEDETQQVNKTGKNADGLSGTTTIIENNVGVNEEKAIKPYEENHPKVNLVKSEGYVTDGLGKTQSSESRLYELSAEDLEKEEEEEDEDKGGGKDTSTSADAEASEDQNKEPLSKSAKFEKPEEKVPVSSITSHAKETSVKPTGKVATETQTYETKQGAPTAAAKKIEAKKATRPSKPKGTKETPNKGVQKNPAKNGGFFKKLAQLLK
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
3Phosphorylation-----MQSSLPQFTF
-----CCCCCCCCEE		32.3230377154
54PhosphorylationPVTFDSPSSKFYFKF
EEEECCCCCCEEEEE		50.5427017623
71AcetylationDGQWLPSKDYKVNID
CCCCCCCCCCEEECC		64.2424489116
106PhosphorylationSSTLVPESAGLAVSK
CCCCCCCHHCEEECC		22.9027214570
124UbiquitinationLIEPEAEKRAKKLRK
CCCHHHHHHHHHHHH		65.7823749301
127UbiquitinationPEAEKRAKKLRKFKI
HHHHHHHHHHHHHCE		57.2722817900
128UbiquitinationEAEKRAKKLRKFKIK
HHHHHHHHHHHHCEE		53.1722817900
148PhosphorylationNKQTGERSIFSQEVV
CCCCCCCCCCEEEEE		24.5522890988
151PhosphorylationTGERSIFSQEVVELP
CCCCCCCEEEEEECC		24.6222890988
160PhosphorylationEVVELPDSEDETQQV
EEEECCCCCCHHHHH		45.0322369663
164PhosphorylationLPDSEDETQQVNKTG
CCCCCCHHHHHHCCC		36.3025521595
169UbiquitinationDETQQVNKTGKNADG
CHHHHHHCCCCCCCC		60.8523749301
170PhosphorylationETQQVNKTGKNADGL
HHHHHHCCCCCCCCC		48.4622369663
172AcetylationQQVNKTGKNADGLSG
HHHHCCCCCCCCCCC		54.9524489116
172UbiquitinationQQVNKTGKNADGLSG
HHHHCCCCCCCCCCC		54.9523749301
178PhosphorylationGKNADGLSGTTTIIE
CCCCCCCCCCEEEEE		39.3522369663
180PhosphorylationNADGLSGTTTIIENN
CCCCCCCCEEEEECC		19.8622369663
181PhosphorylationADGLSGTTTIIENNV
CCCCCCCEEEEECCC		21.3722369663
182PhosphorylationDGLSGTTTIIENNVG
CCCCCCEEEEECCCC		21.5722369663
194AcetylationNVGVNEEKAIKPYEE
CCCCCHHHCCCCCHH		49.5924489116
194UbiquitinationNVGVNEEKAIKPYEE
CCCCCHHHCCCCCHH		49.5922817900
197UbiquitinationVNEEKAIKPYEENHP
CCHHHCCCCCHHHCC		46.5422817900
205UbiquitinationPYEENHPKVNLVKSE
CCHHHCCCEEEEEEC		35.8822817900
210UbiquitinationHPKVNLVKSEGYVTD
CCCEEEEEECCCCCC		46.0523749301
211PhosphorylationPKVNLVKSEGYVTDG
CCEEEEEECCCCCCC		28.8622890988
214PhosphorylationNLVKSEGYVTDGLGK
EEEEECCCCCCCCCC		8.9822890988
216PhosphorylationVKSEGYVTDGLGKTQ
EEECCCCCCCCCCCC		18.8322890988
221UbiquitinationYVTDGLGKTQSSESR
CCCCCCCCCCCCHHH		48.7323749301
222PhosphorylationVTDGLGKTQSSESRL
CCCCCCCCCCCHHHH		31.7022369663
224PhosphorylationDGLGKTQSSESRLYE
CCCCCCCCCHHHHEE		41.1122369663
225PhosphorylationGLGKTQSSESRLYEL
CCCCCCCCHHHHEEE		29.7622369663
227PhosphorylationGKTQSSESRLYELSA
CCCCCCHHHHEEECH		29.5425521595
230PhosphorylationQSSESRLYELSAEDL
CCCHHHHEEECHHHH		17.4522369663
233PhosphorylationESRLYELSAEDLEKE
HHHHEEECHHHHHHH		20.0622369663
254PhosphorylationDKGGGKDTSTSADAE
CCCCCCCCCCHHHHH		37.0722890988
255PhosphorylationKGGGKDTSTSADAEA
CCCCCCCCCHHHHHH		30.4222369663
256PhosphorylationGGGKDTSTSADAEAS
CCCCCCCCHHHHHHC		29.9922890988
257PhosphorylationGGKDTSTSADAEASE
CCCCCCCHHHHHHCC		24.7422369663
263PhosphorylationTSADAEASEDQNKEP
CHHHHHHCCCCCCCC		32.9622369663
268UbiquitinationEASEDQNKEPLSKSA
HHCCCCCCCCCCCCC		55.8924961812
272PhosphorylationDQNKEPLSKSAKFEK
CCCCCCCCCCCCCCC		34.9722369663
273UbiquitinationQNKEPLSKSAKFEKP
CCCCCCCCCCCCCCC		63.2124961812
279UbiquitinationSKSAKFEKPEEKVPV
CCCCCCCCCCHHCCH		61.9424961812
283UbiquitinationKFEKPEEKVPVSSIT
CCCCCCHHCCHHHHH		50.6123749301
287PhosphorylationPEEKVPVSSITSHAK
CCHHCCHHHHHCCCC		15.2322369663
288PhosphorylationEEKVPVSSITSHAKE
CHHCCHHHHHCCCCC		30.0722369663
290PhosphorylationKVPVSSITSHAKETS
HCCHHHHHCCCCCCC		19.1922369663
291PhosphorylationVPVSSITSHAKETSV
CCHHHHHCCCCCCCC		21.5622369663
294UbiquitinationSSITSHAKETSVKPT
HHHHCCCCCCCCCCC		56.9824961812
296PhosphorylationITSHAKETSVKPTGK
HHCCCCCCCCCCCCC		37.8125005228
297PhosphorylationTSHAKETSVKPTGKV
HCCCCCCCCCCCCCE		29.2725752575
299UbiquitinationHAKETSVKPTGKVAT
CCCCCCCCCCCCEEE		36.3124961812
301PhosphorylationKETSVKPTGKVATET
CCCCCCCCCCEEEEE		43.8724909858
303UbiquitinationTSVKPTGKVATETQT
CCCCCCCCEEEEEEE		31.0423749301
306PhosphorylationKPTGKVATETQTYET
CCCCCEEEEEEEEEC		42.4228889911
308PhosphorylationTGKVATETQTYETKQ
CCCEEEEEEEEECCC		23.1228889911
310PhosphorylationKVATETQTYETKQGA
CEEEEEEEEECCCCC		30.6428889911
314UbiquitinationETQTYETKQGAPTAA
EEEEEECCCCCCCHH		34.4923749301
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 MDG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MDG1_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 MDG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM1_YEASTMCM1genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC48_YEASTCDC48genetic
27708008
RPB1_YEASTRPO21genetic
27708008
PDC2_YEASTPDC2genetic
27708008
ERF3_YEASTSUP35genetic
27708008
TCPA_YEASTTCP1genetic
27708008
SMC5_YEASTSMC5genetic
27708008
RPB2_YEASTRPB2genetic
27708008
APC5_YEASTAPC5genetic
27708008
SYA_YEASTALA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MDG1_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-160; THR-164; SER-178;THR-182; SER-225; SER-227; SER-288; THR-290 AND SER-291, AND MASSSPECTROMETRY.
"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-288 AND SER-291, ANDMASS SPECTROMETRY.

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