METK2_YEAST - dbPTM
METK2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID METK2_YEAST
UniProt AC P19358
Protein Name S-adenosylmethionine synthase 2
Gene Name SAM2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 384
Subcellular Localization
Protein Description Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate..
Protein Sequence MSKSKTFLFTSESVGEGHPDKICDQVSDAILDACLEQDPFSKVACETAAKTGMIMVFGEITTKARLDYQQIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGLHYEKSLEDLGAGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLPWLRPDTKTQVTVEYEDDNGRWVPKRIDTVVISAQHADEISTADLRTQLQKDIVEKVIPKDMLDENTKYFIQPSGRFVIGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLCKRVQVQFSYAIGIAEPLSLHVDTYGTATKSDDEIIEIIKKNFDLRPGVLVKELDLARPIYLPTASYGHFTNQEYSWEKPKKLEF
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
2Acetylation------MSKSKTFLF
------CCCCCEEEE		45.719298649
5Acetylation---MSKSKTFLFTSE
---CCCCCEEEEECC		47.2122865919
5Ubiquitination---MSKSKTFLFTSE
---CCCCCEEEEECC		47.2124961812
21UbiquitinationVGEGHPDKICDQVSD
CCCCCCHHHHHHHHH		50.0815699485
42UbiquitinationLEQDPFSKVACETAA
HHCCCCCHHHHHHHH		33.9423749301
47PhosphorylationFSKVACETAAKTGMI
CCHHHHHHHHHHCCE		31.6227214570
50UbiquitinationVACETAAKTGMIMVF
HHHHHHHHHCCEEEE		43.0523749301
61PhosphorylationIMVFGEITTKARLDY
EEEEEEEECHHCCCH		20.2427017623
62PhosphorylationMVFGEITTKARLDYQ
EEEEEEECHHCCCHH		28.5027017623
63UbiquitinationVFGEITTKARLDYQQ
EEEEEECHHCCCHHH		23.9017644757
75PhosphorylationYQQIVRDTIKKIGYD
HHHHHHHHHHHHCCC		24.9227017623
77UbiquitinationQIVRDTIKKIGYDDS
HHHHHHHHHHCCCCC		40.1922817900
78UbiquitinationIVRDTIKKIGYDDSA
HHHHHHHHHCCCCCC		37.2023749301
84PhosphorylationKKIGYDDSAKGFDYK
HHHCCCCCCCCCCCC		29.0527214570
86UbiquitinationIGYDDSAKGFDYKTC
HCCCCCCCCCCCCCC		65.1523749301
91UbiquitinationSAKGFDYKTCNVLVA
CCCCCCCCCCEEEEE		48.7422817900
103PhosphorylationLVAIEQQSPDIAQGL
EEEEECCCCCHHHCC		25.0021440633
112PhosphorylationDIAQGLHYEKSLEDL
CHHHCCCCHHCHHHC		30.0522369663
114UbiquitinationAQGLHYEKSLEDLGA
HHCCCCHHCHHHCCC		53.8517644757
115PhosphorylationQGLHYEKSLEDLGAG
HCCCCHHCHHHCCCC		25.6722369663
130PhosphorylationDQGIMFGYATDETPE
CCCEEEEEECCCCCC		8.6122369663
132PhosphorylationGIMFGYATDETPEGL
CEEEEEECCCCCCCC		26.3622369663
135PhosphorylationFGYATDETPEGLPLT
EEEECCCCCCCCCHH		29.4722369663
142PhosphorylationTPEGLPLTILLAHKL
CCCCCCHHHHHHHHH		13.9822369663
148UbiquitinationLTILLAHKLNMAMAD
HHHHHHHHHCHHHHH		35.6317644757
170UbiquitinationPWLRPDTKTQVTVEY
CCCCCCCCCEEEEEE		44.3222817900
187AcetylationDNGRWVPKRIDTVVI
CCCCEEECEEEEEEE		52.9824489116
187UbiquitinationDNGRWVPKRIDTVVI
CCCCEEECEEEEEEE		52.9817644757
195PhosphorylationRIDTVVISAQHADEI
EEEEEEEECCCCCCC		15.4017287358
213UbiquitinationDLRTQLQKDIVEKVI
HHHHHHHHHHHHHHC		59.0023749301
213AcetylationDLRTQLQKDIVEKVI
HHHHHHHHHHHHHHC		59.0024489116
213SuccinylationDLRTQLQKDIVEKVI
HHHHHHHHHHHHHHC		59.0023954790
218AcetylationLQKDIVEKVIPKDML
HHHHHHHHHCCHHHC		34.2724489116
222AcetylationIVEKVIPKDMLDENT
HHHHHCCHHHCCCCC		44.6524489116
230UbiquitinationDMLDENTKYFIQPSG
HHCCCCCCEEECCCC		50.1523749301
236PhosphorylationTKYFIQPSGRFVIGG
CCEEECCCCCEEECC		26.6522369663
251PhosphorylationPQGDAGLTGRKIIVD
CCCCCCCCCCEEEEE		33.7427214570
254UbiquitinationDAGLTGRKIIVDAYG
CCCCCCCEEEEECCC		37.8222817900
260PhosphorylationRKIIVDAYGGASSVG
CEEEEECCCCCCCCC		16.1922369663
264PhosphorylationVDAYGGASSVGGGAF
EECCCCCCCCCCCCC		28.9122369663
265PhosphorylationDAYGGASSVGGGAFS
ECCCCCCCCCCCCCC		25.0122369663
272PhosphorylationSVGGGAFSGKDYSKV
CCCCCCCCCCCCCCC		44.3822369663
274UbiquitinationGGGAFSGKDYSKVDR
CCCCCCCCCCCCCCH		52.9023749301
278UbiquitinationFSGKDYSKVDRSAAY
CCCCCCCCCCHHHHH		41.7622817900
292UbiquitinationYAARWVAKSLVAAGL
HHHHHHHHHHHHHHH		34.4023749301
293PhosphorylationAARWVAKSLVAAGLC
HHHHHHHHHHHHHHC		20.5221440633
301UbiquitinationLVAAGLCKRVQVQFS
HHHHHHCCEEEEEEE		61.7223749301
329UbiquitinationDTYGTATKSDDEIIE
ECCCCCCCCHHHHHH		49.8017644757
339AcetylationDEIIEIIKKNFDLRP
HHHHHHHHHCCCCCC		47.5324489116
339UbiquitinationDEIIEIIKKNFDLRP
HHHHHHHHHCCCCCC		47.5317644757
339SuccinylationDEIIEIIKKNFDLRP
HHHHHHHHHCCCCCC		47.5323954790
340UbiquitinationEIIEIIKKNFDLRPG
HHHHHHHHCCCCCCC		53.0623749301
351UbiquitinationLRPGVLVKELDLARP
CCCCEEEEEEECCCC		48.6924961812
378AcetylationNQEYSWEKPKKLEF-
CCCCCCCCCCCCCC-		56.7424489116
378UbiquitinationNQEYSWEKPKKLEF-
CCCCCCCCCCCCCC-		56.7417644757
380UbiquitinationEYSWEKPKKLEF---
CCCCCCCCCCCC---		79.6017644757
381UbiquitinationYSWEKPKKLEF----
CCCCCCCCCCC----		62.8717644757
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 METK2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of METK2_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 METK2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
METK1_YEASTSAM1physical
16554755
METK1_YEASTSAM1physical
18719252
METK2_YEASTSAM2physical
18719252
HSP71_YEASTSSA1physical
19536198
METK1_YEASTSAM1genetic
17284612
METK1_YEASTSAM1genetic
18408719
BST1_YEASTBST1genetic
20093466
SSF1_YEASTSSF1genetic
20093466
METK1_YEASTSAM1genetic
20093466
EOS1_YEASTEOS1genetic
20093466
METK1_YEASTSAM1genetic
355845
METK1_YEASTSAM1genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
COX5A_YEASTCOX5Agenetic
21623372
UME6_YEASTUME6genetic
27708008
METK1_YEASTSAM1genetic
27708008
ERG2_YEASTERG2genetic
27708008
PMP1_YEASTPMP1physical
26404137
METK2_HUMANMAT2Aphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of METK2_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
Phosphorylation
ReferencePubMed
"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-195, AND MASSSPECTROMETRY.
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-77; LYS-78 AND LYS-86,AND MASS SPECTROMETRY.

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