YRO2_YEAST - dbPTM
YRO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YRO2_YEAST
UniProt AC P38079
Protein Name Protein YRO2
Gene Name YRO2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 344
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MSDYVELLKRGGNEAIKINPPTGADFHITSRGSDWLFTVFCVNLLFGVILVPLMFRKPVKDRFVYYTAIAPNLFMSIAYFTMASNLGWIPVRAKYNHVQTSTQKEHPGYRQIFYARYVGWFLAFPWPIIQMSLLGGTPLWQIAFNVGMTEIFTVCWLIAACVHSTYKWGYYTIGIGAAIVVCISLMTTTFNLVKARGKDVSNVFITFMSVIMFLWLIAYPTCFGITDGGNVLQPDSATIFYGIIDLLILSILPVLFMPLANYLGIERLGLIFDEEPAEHVGPVAEKKMPSPASFKSSDSDSSIKEKLKLKKKHKKDKKKAKKAKKAKKAKKAQEEEEDVATDSE
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
17UbiquitinationRGGNEAIKINPPTGA
CCCCCCEEECCCCCC		43.4024961812
22PhosphorylationAIKINPPTGADFHIT
CEEECCCCCCCEEEE		46.3822369663
29PhosphorylationTGADFHITSRGSDWL
CCCCEEEECCCCHHH		12.1022369663
30PhosphorylationGADFHITSRGSDWLF
CCCEEEECCCCHHHH		33.7622369663
94AcetylationGWIPVRAKYNHVQTS
CCEEHHHHCCCCCCC		35.7024489116
104AcetylationHVQTSTQKEHPGYRQ
CCCCCCCCCCCCHHH		59.0622865919
286AcetylationHVGPVAEKKMPSPAS
HCCCCCCCCCCCCCH		44.6324489116
286UbiquitinationHVGPVAEKKMPSPAS
HCCCCCCCCCCCCCH		44.6322817900
287UbiquitinationVGPVAEKKMPSPASF
CCCCCCCCCCCCCHH		47.7722817900
290PhosphorylationVAEKKMPSPASFKSS
CCCCCCCCCCHHCCC		29.6022369663
293PhosphorylationKKMPSPASFKSSDSD
CCCCCCCHHCCCCCC		36.2722369663
295UbiquitinationMPSPASFKSSDSDSS
CCCCCHHCCCCCCHH		46.7023749301
296PhosphorylationPSPASFKSSDSDSSI
CCCCHHCCCCCCHHH		37.0522369663
297PhosphorylationSPASFKSSDSDSSIK
CCCHHCCCCCCHHHH		41.5522369663
299PhosphorylationASFKSSDSDSSIKEK
CHHCCCCCCHHHHHH		41.1422369663
301PhosphorylationFKSSDSDSSIKEKLK
HCCCCCCHHHHHHHH		37.6022369663
302PhosphorylationKSSDSDSSIKEKLKL
CCCCCCHHHHHHHHH		42.5422369663
304UbiquitinationSDSDSSIKEKLKLKK
CCCCHHHHHHHHHHH		51.2323749301
306UbiquitinationSDSSIKEKLKLKKKH
CCHHHHHHHHHHHHH		46.0122817900
308UbiquitinationSSIKEKLKLKKKHKK
HHHHHHHHHHHHHHH		70.1322817900
341PhosphorylationEEEEDVATDSE----
HHHHHHCCCCC----		39.6525521595
343PhosphorylationEEDVATDSE------
HHHHCCCCC------		40.6325521595
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 YRO2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YRO2_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 YRO2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC27_YEASTCDC27physical
16554755
YRA1_YEASTYRA1physical
16554755
ZRT1_YEASTZRT1genetic
20093466
TBP7_YEASTYTA7genetic
20093466
MKAR_YEASTIFA38physical
16093310
ATG22_YEASTATG22physical
16093310
STT3_YEASTSTT3physical
16093310
ERG7_YEASTERG7physical
16093310
SPC1_YEASTSPC1physical
16093310
GAP1_YEASTGAP1physical
16093310
ELO3_YEASTELO3physical
16093310
ALG11_YEASTALG11physical
16093310
TIM23_YEASTTIM23physical
16093310
ERP4_YEASTERP4physical
16093310
SEC63_YEASTSEC63physical
16093310
YRO2_YEASTYRO2physical
16093310
VMA21_YEASTVMA21genetic
27708008
TBP7_YEASTYTA7genetic
27708008
NKP2_YEASTNKP2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YRO2_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-293; SER-299; SER-301;SER-302; THR-341 AND SER-343, 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 SER-301, AND MASSSPECTROMETRY.
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341 AND SER-343, ANDMASS SPECTROMETRY.
"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 THR-341 AND SER-343, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-286, AND MASSSPECTROMETRY.

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