MET4_YEAST - dbPTM
MET4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MET4_YEAST
UniProt AC P32389
Protein Name Transcriptional activator of sulfur metabolism MET4
Gene Name MET4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 672
Subcellular Localization Nucleus .
Protein Description Positive trans-acting factor capable of stimulating the transcription of the MET genes from the methionine biosynthetic pathway. MET4, MET28 and CBF1 are required for full induction of MET25 and MET16 gene transcription. MET4 controls as well the derepression of MET6. Required for the transcription of genes necessary for sulfur amino acid biosynthesis. Involved in the transcription activation of MET28 and MET30. Required for MET3 gene expression via assembly of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes. Involved in response to cadmium and arsenic. Cadmium-activated MET4 also induces glutathione biosynthesis..
Protein Sequence MKQEQSHEGDSYSTEFINLFGKDTATHPSSNNGANNNGMGSTNSLDQFVATASSSSSLVTSSENRRPLIGDVTNRGNTNLYDHAVTPEILLEQLAYVDNFIPSLDNEFSNVDWNVNTTHNNANNNGADTFSSINANPFDLDEQLAIELSAFADDSFIFPDEDKPSNNNNNSNNGNDDHSNHDVLHEDPSTNNRQRNPHFLTQRRNTFLTSQYDQSKSRFSSKNKRNGNNGETNNFGDNMQNNHPFEPNFMGSPSQFPADATNMTSIDHGGFTNVDITSTENNTTGDNGVDALSNLLHRTTHTPNRSSPLSNVTSAQNSSSQQRKHSESKVDSNSDNNSSNKAPNITVPDYSIIPTSVLVTLLPRVNVPNGAYNSLISAGFDNDQIDAIAAIMAYHHQKKIRENNSNNNKNINTNDSQEAPILKNINELLSVLIPPSPAETRGPTTLSTSPSFNEHGVVAEASFLSSILELGIKHPKSNNIHNQRQPSRNDHKISRESDGNNGNDNVHHNNAVIKSSTTRGDEIAKIRSEPTLNASSSDHKENSLKRSHSGDLKNKKVPVDRKYSDNEDDEYDDADLHGFEKKQLIKKELGDDDEDLLIQSKKSHQKKKLKEKELESSIHELTEIAASLQKRIHTLETENKLLKNLVLSSGETEGIKKAESLKKQIFEKVQKE
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
6Phosphorylation--MKQEQSHEGDSYS
--CCCCCCCCCCCCH		23.8225533186
11PhosphorylationEQSHEGDSYSTEFIN
CCCCCCCCCHHHHHH		31.6625533186
12PhosphorylationQSHEGDSYSTEFINL
CCCCCCCCHHHHHHH		25.0925533186
163UbiquitinationFIFPDEDKPSNNNNN
CCCCCCCCCCCCCCC		48.58-
206PhosphorylationFLTQRRNTFLTSQYD
HHHHHHHHHHHHCHH		20.4328889911
299PhosphorylationLSNLLHRTTHTPNRS
HHHHHHHHCCCCCCC		16.5128889911
302PhosphorylationLLHRTTHTPNRSSPL
HHHHHCCCCCCCCCC		21.8428889911
306PhosphorylationTTHTPNRSSPLSNVT
HCCCCCCCCCCCCCC		42.8421440633
307PhosphorylationTHTPNRSSPLSNVTS
CCCCCCCCCCCCCCC		26.9921440633
310PhosphorylationPNRSSPLSNVTSAQN
CCCCCCCCCCCCCCC		32.4128889911
314PhosphorylationSPLSNVTSAQNSSSQ
CCCCCCCCCCCCHHH		24.4730377154
318PhosphorylationNVTSAQNSSSQQRKH
CCCCCCCCHHHHHHH		21.2028889911
319PhosphorylationVTSAQNSSSQQRKHS
CCCCCCCHHHHHHHH		39.4519779198
320PhosphorylationTSAQNSSSQQRKHSE
CCCCCCHHHHHHHHH		30.1027017623
326PhosphorylationSSQQRKHSESKVDSN
HHHHHHHHHCCCCCC		46.7528889911
332PhosphorylationHSESKVDSNSDNNSS
HHHCCCCCCCCCCCC		41.0221082442
341UbiquitinationSDNNSSNKAPNITVP
CCCCCCCCCCCCCCC		68.1417644757
409UbiquitinationENNSNNNKNINTNDS
HCCCCCCCCCCCCCC		62.4223749301
413PhosphorylationNNNKNINTNDSQEAP
CCCCCCCCCCCCHHH		36.2830377154
416PhosphorylationKNINTNDSQEAPILK
CCCCCCCCCHHHHHH		31.8028889911
476AcetylationELGIKHPKSNNIHNQ
HHCCCCCCCCCCCCC		66.5925381059
497PhosphorylationDHKISRESDGNNGND
CCCCCCCCCCCCCCC		50.1121440633
525AcetylationTRGDEIAKIRSEPTL
CCCCHHHHHHCCCCC		44.2925381059
528PhosphorylationDEIAKIRSEPTLNAS
CHHHHHHCCCCCCCC		51.9420377248
531PhosphorylationAKIRSEPTLNASSSD
HHHHCCCCCCCCCCC		28.7022369663
535PhosphorylationSEPTLNASSSDHKEN
CCCCCCCCCCCHHHH		29.3322369663
536PhosphorylationEPTLNASSSDHKENS
CCCCCCCCCCHHHHH		37.0622369663
537PhosphorylationPTLNASSSDHKENSL
CCCCCCCCCHHHHHC		41.0422369663
549PhosphorylationNSLKRSHSGDLKNKK
HHCCCCCCCCCCCCC		34.9425752575
563PhosphorylationKVPVDRKYSDNEDDE
CCCCCCCCCCCCCCC		23.3522890988
564PhosphorylationVPVDRKYSDNEDDEY
CCCCCCCCCCCCCCC		36.6722369663
571PhosphorylationSDNEDDEYDDADLHG
CCCCCCCCCCCCCCC		26.5622890988
587UbiquitinationEKKQLIKKELGDDDE
HHHHHHHHHHCCCCH		51.7017644757
601AcetylationEDLLIQSKKSHQKKK
HHHHHHCHHHHHHHH		41.7525381059
601UbiquitinationEDLLIQSKKSHQKKK
HHHHHHCHHHHHHHH		41.7517644757
602UbiquitinationDLLIQSKKSHQKKKL
HHHHHCHHHHHHHHH		59.4217644757
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
-KUbiquitinationE3 ubiquitin ligaseMET30P39014
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MET4_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 MET4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET28_YEASTMET28physical
9799240
MET31_YEASTMET31physical
9799240
MET32_YEASTMET32physical
9799240
MET28_YEASTMET28physical
9171357
CBF1_YEASTCBF1physical
9171357
SEC2_YEASTSEC2physical
11087867
ZUO1_YEASTZUO1physical
11087867
END3_YEASTEND3physical
11087867
MET4_YEASTMET4physical
11087867
MET28_YEASTMET28physical
8665859
MET30_YEASTMET30physical
15660125
METK2_YEASTSAM2genetic
12150908
RV167_YEASTRVS167physical
16554755
GLN3_YEASTGLN3physical
16554755
STP1_YEASTSTP1genetic
16977312
STP2_YEASTSTP2genetic
16977312
MET30_YEASTMET30physical
17157252
RPN12_YEASTRPN12physical
17157252
RPN10_YEASTRPN10physical
17157252
CBF1_YEASTCBF1physical
18308733
MET30_YEASTMET30genetic
19940020
MET31_YEASTMET31genetic
19940020
MET32_YEASTMET32genetic
19940020
CBF1_YEASTCBF1physical
17157252
MET28_YEASTMET28physical
17157252
MET31_YEASTMET31physical
17157252
SKP1_YEASTSKP1physical
17157252
UBI4P_YEASTUBI4physical
20694217
MET30_YEASTMET30genetic
21172660
MET32_YEASTMET32genetic
21172660
OPI1_YEASTOPI1genetic
21900497
TUP1_YEASTTUP1genetic
21900497
DOT6_YEASTDOT6genetic
21900497
METK2_YEASTSAM2genetic
21900497
MET32_YEASTMET32genetic
22438580
MET28_YEASTMET28physical
23661758
MET4_YEASTMET4physical
23661758
CDC48_YEASTCDC48physical
24613342
UBI4P_YEASTUBI4physical
21041680
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MET4_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-416; SER-528 ANDSER-564, 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-564, AND MASSSPECTROMETRY.
"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-564, AND MASSSPECTROMETRY.
"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-564, AND MASSSPECTROMETRY.
"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 THR-206; THR-302; SER-307;SER-310 AND SER-564, AND MASS SPECTROMETRY.

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