NRM1_YEAST - dbPTM
NRM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRM1_YEAST
UniProt AC P53718
Protein Name Transcription factor NRM1
Gene Name NRM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 249
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Negative regulatory component of the MBF complex involved in cell-cycle-dependent transcription..
Protein Sequence MSIMKQRLPLGEFSSSKINKLAIANIADASEPRNHGENNVGTVCLPSIKSLMVSPEVYENTKSLPVPLMRSSGGGMACASKSSCQDGISTKTTSRDYSELSKKLQIRLQFAYYKYKTKQTDKNFTDLKSKHSITRPSKVATHSKSEPLTRRRKLVLSQGHYKTPARSKIKTPSSICSHDNTSSFTSFRGVSESSSTTADMNVADTTTPIRNNINTKHSNSHNRTLYQRQETPTSIKAAKSLIHLFTSNQ
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
14PhosphorylationRLPLGEFSSSKINKL
CCCCCCCCHHHHHHH		29.4221440633
15PhosphorylationLPLGEFSSSKINKLA
CCCCCCCHHHHHHHH		40.7621440633
20AcetylationFSSSKINKLAIANIA
CCHHHHHHHHHHHHC		42.6524489116
54PhosphorylationSIKSLMVSPEVYENT
HHHHHCCCHHHHCCC		11.0227017623
63PhosphorylationEVYENTKSLPVPLMR
HHHCCCCCCCCCCEE		35.5525752575
71PhosphorylationLPVPLMRSSGGGMAC
CCCCCEECCCCCCCC		21.2630377154
82PhosphorylationGMACASKSSCQDGIS
CCCCCCCCCCCCCCC		33.5730377154
132PhosphorylationTDLKSKHSITRPSKV
CCHHHHHCCCCCCCC		29.4121551504
134PhosphorylationLKSKHSITRPSKVAT
HHHHHCCCCCCCCCC		39.2721551504
137PhosphorylationKHSITRPSKVATHSK
HHCCCCCCCCCCCCC		36.1521551504
144AcetylationSKVATHSKSEPLTRR
CCCCCCCCCCCCHHH		51.7622865919
145PhosphorylationKVATHSKSEPLTRRR
CCCCCCCCCCCHHHC		47.6817287358
149PhosphorylationHSKSEPLTRRRKLVL
CCCCCCCHHHCHHHH		32.6127017623
157PhosphorylationRRRKLVLSQGHYKTP
HHCHHHHCCCCCCCC		27.0021440633
183PhosphorylationCSHDNTSSFTSFRGV
CCCCCCCCCCCEECC		30.4227017623
197PhosphorylationVSESSSTTADMNVAD
CCCCCCCCCCCCCCC		23.7025371407
207PhosphorylationMNVADTTTPIRNNIN
CCCCCCCCCCCCCCC		20.8628132839
215PhosphorylationPIRNNINTKHSNSHN
CCCCCCCCCCCCCCC		26.7427214570
218PhosphorylationNNINTKHSNSHNRTL
CCCCCCCCCCCCCCE		41.4027214570
220PhosphorylationINTKHSNSHNRTLYQ
CCCCCCCCCCCCEEE		25.7524961812
224PhosphorylationHSNSHNRTLYQRQET
CCCCCCCCEEECCCC		34.8224961812
231PhosphorylationTLYQRQETPTSIKAA
CEEECCCCCCHHHHH		24.4317287358
233PhosphorylationYQRQETPTSIKAAKS
EECCCCCCHHHHHHH		50.9717287358
234PhosphorylationQRQETPTSIKAAKSL
ECCCCCCHHHHHHHH		24.2428889911
240PhosphorylationTSIKAAKSLIHLFTS
CHHHHHHHHHHHHHC		28.0321440633
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 NRM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRM1_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 NRM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWD3_YEASTSWD3genetic
19269370
KCS1_YEASTKCS1genetic
19269370
MNN10_YEASTMNN10genetic
19269370
UBP3_YEASTUBP3genetic
19269370
AAKG_YEASTSNF4genetic
19269370
ADK_YEASTADO1genetic
19269370
NPR1_YEASTNPR1genetic
19269370
CLA4_YEASTCLA4genetic
19269370
MBP1_YEASTMBP1physical
23382076
SWI6_YEASTSWI6physical
23382076
RSP5_YEASTRSP5genetic
27708008
VTI1_YEASTVTI1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRM1_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-14; SER-63; SER-145 ANDSER-240, AND MASS 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-145, AND MASSSPECTROMETRY.

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