RLM1_YEAST - dbPTM
RLM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLM1_YEAST
UniProt AC Q12224
Protein Name Transcription factor RLM1
Gene Name RLM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 676
Subcellular Localization Nucleus .
Protein Description May function as a transcription factor downstream of MPK1 that is subject to activation by the MPK1 mitogen-activated protein kinase pathway. Binds to the DNA sequence 5'-CTA[TA](4)TAG-3'. At least some RML1 target genes are involved in cell wall biosynthesis..
Protein Sequence MGRRKIEIQRISDDRNRAVTFIKRKAGLFKKAHELSVLCQVDIAVIILGSNNTFYEFSSVDTNDLIYHYQNDKNLLHEVKDPSDYGDFHKSASVNINQDLLRSSMSNKPSKSNVKGMNQSENDDDENNDEDDDDHGNFERNSNMHSNKKASDKNIPSAHMKLLSPTALISKMDGSEQNKRHPENALPPLQHLKRLKPDPLQISRTPQQQQQQNISRPYHSSMYNLNQPSSSSSSPSTMDFPKLPSFQNSSFNGRPPPISISPNKFSKPFTNASSRTPKQEHKINNSGSNNNDNSNYTQSPSNSLEDSIQQTVKARRKLSARPVLRVRIPNNNFSSNSAIPSEPSSASSTSANGNSMGSSQIMKENKTSRSSKISPLSASASGPLTLQKGNNGRMVIKLPNANAPNGSNNGNGSNNNNHPYPFGSGSSPLFSATQPYIATPLQPSNIPGGPFQQNTSFLAQRQTQQYQQMSFKKQSQTVPLTTTLTGRPPSTFSGPETSNGPPTGSLPSKFVHDLMSNSPNVSSISMFPDWSMGPNSAKPGNTNNPGTFPPVQTAVNNGNSSNISSTNNTNNNNNNNNNNSSNNNSNNGNDNNSNNSNNSYYSNNEDAPVNGAAISEHTTDGDSNNQSNSSTYDAAATAYNGNTGLTPYINTAQTPLGTKFFNFSTDISGEKNSSKI
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
83PhosphorylationLHEVKDPSDYGDFHK
HEECCCHHHCCCCCC		54.3128889911
91PhosphorylationDYGDFHKSASVNINQ
HCCCCCCCCCEECCH		19.7330377154
93PhosphorylationGDFHKSASVNINQDL
CCCCCCCCEECCHHH		23.8430377154
110PhosphorylationSSMSNKPSKSNVKGM
HHHCCCCCCCCCCCC		50.7723749301
120PhosphorylationNVKGMNQSENDDDEN
CCCCCCCCCCCCCCC		33.1022369663
157PhosphorylationASDKNIPSAHMKLLS
CCCCCCCHHHHHHHC		27.3230377154
164PhosphorylationSAHMKLLSPTALISK
HHHHHHHCHHHHHHC		30.5517330950
170PhosphorylationLSPTALISKMDGSEQ
HCHHHHHHCCCCCHH		23.8328889911
171AcetylationSPTALISKMDGSEQN
CHHHHHHCCCCCHHH		33.7324489116
193AcetylationLPPLQHLKRLKPDPL
CCCHHHHHHHCCCCC		54.2625381059
196AcetylationLQHLKRLKPDPLQIS
HHHHHHHCCCCCCCC		51.9424489116
205PhosphorylationDPLQISRTPQQQQQQ
CCCCCCCCHHHHHHH		20.7528889911
229PhosphorylationMYNLNQPSSSSSSPS
HCCCCCCCCCCCCCC		32.8427017623
231PhosphorylationNLNQPSSSSSSPSTM
CCCCCCCCCCCCCCC		38.2830377154
234PhosphorylationQPSSSSSSPSTMDFP
CCCCCCCCCCCCCCC		25.4730377154
237PhosphorylationSSSSSPSTMDFPKLP
CCCCCCCCCCCCCCC		24.9227017623
245PhosphorylationMDFPKLPSFQNSSFN
CCCCCCCCCCCCCCC		50.3122369663
249PhosphorylationKLPSFQNSSFNGRPP
CCCCCCCCCCCCCCC		26.0622369663
250PhosphorylationLPSFQNSSFNGRPPP
CCCCCCCCCCCCCCC		30.2221440633
259PhosphorylationNGRPPPISISPNKFS
CCCCCCCCCCCCCCC		23.8422369663
261PhosphorylationRPPPISISPNKFSKP
CCCCCCCCCCCCCCC		18.6822369663
267AcetylationISPNKFSKPFTNASS
CCCCCCCCCCCCCCC		47.4824489116
276PhosphorylationFTNASSRTPKQEHKI
CCCCCCCCCCCCCCC		36.4621440633
296PhosphorylationNNNDNSNYTQSPSNS
CCCCCCCCCCCCCCH		13.1324961812
297PhosphorylationNNDNSNYTQSPSNSL
CCCCCCCCCCCCCHH		27.1624961812
299PhosphorylationDNSNYTQSPSNSLED
CCCCCCCCCCCHHHH		23.6123749301
301PhosphorylationSNYTQSPSNSLEDSI
CCCCCCCCCHHHHHH		44.2721551504
303PhosphorylationYTQSPSNSLEDSIQQ
CCCCCCCHHHHHHHH		37.1623749301
367PhosphorylationQIMKENKTSRSSKIS
HHHHCCCCCCCCCCC		40.7421551504
368PhosphorylationIMKENKTSRSSKISP
HHHCCCCCCCCCCCC		31.6019823750
370PhosphorylationKENKTSRSSKISPLS
HCCCCCCCCCCCCCC		35.4322369663
371PhosphorylationENKTSRSSKISPLSA
CCCCCCCCCCCCCCC		32.6622369663
374PhosphorylationTSRSSKISPLSASAS
CCCCCCCCCCCCCCC		24.4322369663
377PhosphorylationSSKISPLSASASGPL
CCCCCCCCCCCCCCE		24.4622369663
379PhosphorylationKISPLSASASGPLTL
CCCCCCCCCCCCEEE		21.4222369663
381PhosphorylationSPLSASASGPLTLQK
CCCCCCCCCCEEEEE		38.1522369663
385PhosphorylationASASGPLTLQKGNNG
CCCCCCEEEEECCCC		30.2122369663
427PhosphorylationYPFGSGSSPLFSATQ
CCCCCCCCCCCCCCC		29.1928889911
439PhosphorylationATQPYIATPLQPSNI
CCCCEEECCCCCCCC		18.2528889911
470PhosphorylationTQQYQQMSFKKQSQT
HHHHHHHHCCCCCCE		29.5823749301
472AcetylationQYQQMSFKKQSQTVP
HHHHHHCCCCCCEEC		42.4725381059
493PhosphorylationGRPPSTFSGPETSNG
CCCCCCCCCCCCCCC		54.2321551504
497PhosphorylationSTFSGPETSNGPPTG
CCCCCCCCCCCCCCC		30.5323749301
498PhosphorylationTFSGPETSNGPPTGS
CCCCCCCCCCCCCCC		37.8223749301
503PhosphorylationETSNGPPTGSLPSKF
CCCCCCCCCCCCHHH		42.4023749301
505PhosphorylationSNGPPTGSLPSKFVH
CCCCCCCCCCHHHHH		39.3221551504
523PhosphorylationSNSPNVSSISMFPDW
HCCCCCCEEECCCCC		17.8821440633
664PhosphorylationGTKFFNFSTDISGEK
CCCCCCCCCCCCCCC		26.6924961812
665PhosphorylationTKFFNFSTDISGEKN
CCCCCCCCCCCCCCC		32.9624961812
668PhosphorylationFNFSTDISGEKNSSK
CCCCCCCCCCCCCCC		43.6528152593
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 RLM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLM1_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 RLM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLT2_YEASTSLT2physical
7565726
SLT2_YEASTSLT2physical
9111331
KDX1_YEASTKDX1physical
9111331
SWI4_YEASTSWI4genetic
18478233
MBP1_YEASTMBP1genetic
18478233
RLM1_YEASTRLM1physical
19345193
MKK2_YEASTMKK2genetic
19041751
IMB1_YEASTKAP95physical
20489023
IMA1_YEASTSRP1physical
20489023
BUB1_YEASTBUB1genetic
20959818
PDR3_YEASTPDR3genetic
20959818
IES4_YEASTIES4genetic
20959818
FKS1_YEASTFKS1genetic
9447998
FKS2_YEASTGSC2genetic
9447998
PP2C1_YEASTPTC1genetic
21127252
ADA2_YEASTADA2genetic
21127252
BUB1_YEASTBUB1genetic
21127252
RSC2_YEASTRSC2genetic
21127252
KCS1_YEASTKCS1genetic
21127252
KNS1_YEASTKNS1genetic
21127252
MET18_YEASTMET18genetic
21127252
SNF2_YEASTSNF2physical
22621902
SLT2_YEASTSLT2physical
22621902
SWI3_YEASTSWI3physical
22621902
OST3_YEASTOST3genetic
23891562
CCW12_YEASTCCW12genetic
23891562
PSB5_YEASTPRE2genetic
23891562
FPS1_YEASTFPS1genetic
27607883
GPI11_YEASTGPI11genetic
27708008
GPI8_YEASTGPI8genetic
27708008
GPI19_YEASTGPI19genetic
27708008
ACT_YEASTACT1genetic
27708008
STT3_YEASTSTT3genetic
27708008
GPI10_YEASTGPI10genetic
27708008
GPI16_YEASTGPI16genetic
27708008
ARPC5_YEASTARC15genetic
27708008
GWT1_YEASTGWT1genetic
27708008
CDC91_YEASTGAB1genetic
27708008
RNT1_YEASTRNT1genetic
27708008
LST8_YEASTLST8genetic
27708008
ARPC2_YEASTARC35genetic
27708008
SMP3_YEASTSMP3genetic
27708008
SLT2_YEASTSLT2genetic
28637712
SWI4_YEASTSWI4genetic
28637712
IME1_YEASTIME1genetic
26510787
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLM1_YEAST

loading...

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-370; SER-371; SER-374AND SER-377, AND MASS 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-164; SER-374 ANDSER-377, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory