MRH1_YEAST - dbPTM
MRH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRH1_YEAST
UniProt AC Q12117
Protein Name Protein MRH1
Gene Name MRH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 320
Subcellular Localization Cell membrane
Multi-pass membrane protein. Mitochondrion. Bud. Localized primarily to the plasma membrane. Also found at the buds.
Protein Description
Protein Sequence MSTFETLIKRGGNEAIKINPPTGADFHITSRGSDWFWTCFCCYLLFGLILTFLMFRKPVNDRFFYLTGIAPNFFMCIAYFTMASNLGWIPVKAKYNHVQTSTQKEHPGYRQIFYSRFVGWFLALPWPIIQICMLAGTPFWQMAFNVCITEFFTVCWLIAACVHSTYKWGYYTIGLGAAIVVSISVMTTSYNLVKQRDNDIRLTFLVFFSIIMFLWIIAYPTCFGITDGGNVLQPDSAGIFYGIIDLILMCFIPTLLVPIANHFGADKLGYHFGPSDAEAVMAPKAPVASPRPAATPNLSKDKKKKSKKSKKSKKSKKSEE
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
9AcetylationSTFETLIKRGGNEAI
CHHHHHHHCCCCCCE		48.3725381059
17UbiquitinationRGGNEAIKINPPTGA
CCCCCCEEECCCCCC		43.4024961812
22PhosphorylationAIKINPPTGADFHIT
CEEECCCCCCCEEEC		46.3822369663
29PhosphorylationTGADFHITSRGSDWF
CCCCEEECCCCCHHH		12.1022369663
30PhosphorylationGADFHITSRGSDWFW
CCCEEECCCCCHHHH		33.7622369663
94AcetylationGWIPVKAKYNHVQTS
CCEEEEHHCCCCCCC		40.6525381059
270PhosphorylationFGADKLGYHFGPSDA
CCCCCCCCCCCCCHH		12.3821440633
275PhosphorylationLGYHFGPSDAEAVMA
CCCCCCCCHHHHHHC		50.2421440633
284UbiquitinationAEAVMAPKAPVASPR
HHHHHCCCCCCCCCC		56.6424961812
289PhosphorylationAPKAPVASPRPAATP
CCCCCCCCCCCCCCC		22.9822369663
295PhosphorylationASPRPAATPNLSKDK
CCCCCCCCCCCCHHH		18.1522369663
299PhosphorylationPAATPNLSKDKKKKS
CCCCCCCCHHHHHHH		45.5122369663
300UbiquitinationAATPNLSKDKKKKSK
CCCCCCCHHHHHHHH		76.3923749301
300AcetylationAATPNLSKDKKKKSK
CCCCCCCHHHHHHHH		76.3924489116
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 MRH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRH1_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 MRH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EMI1_YEASTEMI1genetic
20093466
PT122_YEASTPET122genetic
20093466
HAP2_YEASTHAP2genetic
20093466
YIP5_YEASTYIP5genetic
20093466
RL24A_YEASTRPL24Agenetic
20093466
CBP4_YEASTCBP4genetic
20093466
PACC_YEASTRIM101genetic
20093466
FYV4_YEASTFYV4genetic
20093466
COX23_YEASTCOX23genetic
20093466
YIQ6_YEASTYIL166Cgenetic
20093466
FLX1_YEASTFLX1genetic
20093466
COPE_YEASTSEC28genetic
20093466
DOT5_YEASTDOT5genetic
20093466
MRX5_YEASTYJL147Cgenetic
20093466
YJN2_YEASTYJL132Wgenetic
20093466
DNM1_YEASTDNM1genetic
20093466
PPR1_YEASTPPR1genetic
20093466
COX12_YEASTCOX12genetic
20093466
APTH1_YEASTYLR118Cgenetic
20093466
NKP2_YEASTNKP2genetic
20093466
BCH1_YEASTBCH1genetic
20093466
AEP2_YEASTAEP2genetic
20093466
SCW10_YEASTSCW10genetic
20093466
SWS2_YEASTSWS2genetic
20093466
ATP23_YEASTATP23genetic
20093466
CY1_YEASTCYT1genetic
20093466
COQ7_YEASTCAT5genetic
20093466
MNE1_YEASTMNE1genetic
20093466
HAP5_YEASTHAP5genetic
20093466
COX10_YEASTCOX10genetic
20093466
PRPD_YEASTPDH1genetic
20093466
MSS18_YEASTMSS18genetic
20093466
CTF4_YEASTCTF4genetic
20093466
SRO7_YEASTSRO7genetic
23891562
YRO2_YEASTYRO2genetic
25503505
SCW10_YEASTSCW10genetic
27708008
HAP3_YEASTHAP3genetic
27708008
YPQ3_YEASTRTC2genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
MBA1_YEASTMBA1genetic
27708008
SWC5_YEASTSWC5genetic
27708008
NTM1_YEASTTAE1genetic
27708008
CHK1_YEASTCHK1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RV161_YEASTRVS161genetic
27708008
THRC_YEASTTHR4genetic
27708008
YD186_YEASTYDL186Wgenetic
27708008
DTD_YEASTDTD1genetic
27708008
UBP5_YEASTUBP5genetic
27708008
XRN1_YEASTXRN1genetic
27708008
MTO1_YEASTMTO1genetic
27708008
ASK10_YEASTASK10genetic
27708008
CBP4_YEASTCBP4genetic
27708008
TBP7_YEASTYTA7genetic
27708008
SNF6_YEASTSNF6genetic
27708008
COX23_YEASTCOX23genetic
27708008
DOT5_YEASTDOT5genetic
27708008
YIQ6_YEASTYIL166Cgenetic
27708008
YJN2_YEASTYJL132Wgenetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
DNM1_YEASTDNM1genetic
27708008
PPR1_YEASTPPR1genetic
27708008
COX12_YEASTCOX12genetic
27708008
NKP2_YEASTNKP2genetic
27708008
ATP18_YEASTATP18genetic
27708008
MSC1_YEASTMSC1genetic
27708008
AIM34_YEASTAIM34genetic
27708008
MSS1_YEASTMSS1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
ATP23_YEASTATP23genetic
27708008
HMI1_YEASTHMI1genetic
27708008
CY1_YEASTCYT1genetic
27708008
COQ7_YEASTCAT5genetic
27708008
MNE1_YEASTMNE1genetic
27708008
COX10_YEASTCOX10genetic
27708008
PRPD_YEASTPDH1genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
MSS18_YEASTMSS18genetic
27708008
CTF4_YEASTCTF4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MRH1_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-289 AND THR-295, ANDMASS 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-289 AND THR-295, ANDMASS SPECTROMETRY.
"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 SER-289; THR-295 ANDSER-299, AND MASS SPECTROMETRY.
"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 SER-289 AND THR-295, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND THR-295, ANDMASS 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-289 AND THR-295, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND THR-295, 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 SER-289 AND THR-295, ANDMASS SPECTROMETRY.

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