SMY2_YEAST - dbPTM
SMY2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMY2_YEAST
UniProt AC P32909
Protein Name Protein SMY2
Gene Name SMY2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 740
Subcellular Localization Cytoplasm .
Protein Description Suppressor of the MYO2 gene..
Protein Sequence MIAPDSQRLFGSFDEQFKDLKLDSVDTENNNTHGVSTILDSSPASVNNNTNGAVAASVNTVPGSTFRSNTPLLGGRHPLSRTSSLIDSIGIQRAASPFSSMKEPFIPQSSGVMSSSFWHGDHPESRVSTPVQQHPLLQRNESSSSFSYAANLGVNLSTHSLAVDITPLSTPTAAQSHVNLFPSSDIPPNMSMNGMSQLPAPVSVESSWRYIDTQGQIHGPFTTQMMSQWYIGGYFASTLQISRLGSTPETLGINDIFITLGELMTKLEKYDTDPFTTFDKLHVQTTSSDSINLNLAPYASGVAATGTIKATENDIFKPLTHDNIWDMDGGTTSKGVDIKLASATTISQTDESHKQEYKSTTMLEKGKKEKSESVAKALLDEQEKRNRELKRKEEARLSKKQKQKEDDLLKKQKEQKEQKEKEALEAEKQKKSEKTKKDTQTQTEGFKTSKDLPSLNSSSANPAPWASKVKVNNAIETSIKNGVSSTGKKKGEPLGLQQRNSKEEKQKEELKSVLNWANKSSLPSNQTIDIKSQFQKSPKGMKESSPLKELEDPNFIEEQKKLWEKVQSSSKQVKSTSSASTTTSSWTTVTSKGKAPIGTVVSPYSKTNTSLNSSLTAKTSTTSTTTTFASMNNVSPRQEFIKWCKSQMKLNSGITNNNVLELLLSLPTGPESKELIQETIYANSDVMDGRRFATEFIKRRVACEKQGDDPLSWNEALALSGNDDDGWEFQVVSKKKGRKH
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--MIAPDSQRLFGSF
--CCCCHHHHHHCCH		19.0121440633
12PhosphorylationDSQRLFGSFDEQFKD
HHHHHHCCHHHHHCC		23.3822369663
18UbiquitinationGSFDEQFKDLKLDSV
CCHHHHHCCCCCCEE		62.9424961812
68PhosphorylationVPGSTFRSNTPLLGG
CCCCCCCCCCCCCCC		40.6422890988
70PhosphorylationGSTFRSNTPLLGGRH
CCCCCCCCCCCCCCC		19.2922369663
80PhosphorylationLGGRHPLSRTSSLID
CCCCCCCCCCHHHHH		37.6522369663
82PhosphorylationGRHPLSRTSSLIDSI
CCCCCCCCHHHHHHH		21.2022890988
83PhosphorylationRHPLSRTSSLIDSIG
CCCCCCCHHHHHHHC		23.2622369663
84PhosphorylationHPLSRTSSLIDSIGI
CCCCCCHHHHHHHCC		28.8222369663
88PhosphorylationRTSSLIDSIGIQRAA
CCHHHHHHHCCCCCC		18.7422890988
96PhosphorylationIGIQRAASPFSSMKE
HCCCCCCCCCCCCCC		26.0322369663
99PhosphorylationQRAASPFSSMKEPFI
CCCCCCCCCCCCCCC		32.6723749301
100PhosphorylationRAASPFSSMKEPFIP
CCCCCCCCCCCCCCC		33.9621440633
102UbiquitinationASPFSSMKEPFIPQS
CCCCCCCCCCCCCCC		65.2723749301
109PhosphorylationKEPFIPQSSGVMSSS
CCCCCCCCCCCCCCC		24.5722369663
110PhosphorylationEPFIPQSSGVMSSSF
CCCCCCCCCCCCCCC		30.1122369663
114PhosphorylationPQSSGVMSSSFWHGD
CCCCCCCCCCCCCCC		22.0322369663
115PhosphorylationQSSGVMSSSFWHGDH
CCCCCCCCCCCCCCC		16.0922369663
116PhosphorylationSSGVMSSSFWHGDHP
CCCCCCCCCCCCCCC		25.6722369663
125PhosphorylationWHGDHPESRVSTPVQ
CCCCCCHHHCCCCHH		42.2922369663
128PhosphorylationDHPESRVSTPVQQHP
CCCHHHCCCCHHHCC		26.3622369663
129PhosphorylationHPESRVSTPVQQHPL
CCHHHCCCCHHHCCC		25.3122369663
269UbiquitinationELMTKLEKYDTDPFT
HHHHHHHHCCCCCCC		59.8823749301
269AcetylationELMTKLEKYDTDPFT
HHHHHHHHCCCCCCC		59.8824489116
311PhosphorylationATGTIKATENDIFKP
CCCEEECCCCCCCCC		30.2521440633
317AcetylationATENDIFKPLTHDNI
CCCCCCCCCCCCCCE		39.1824489116
320PhosphorylationNDIFKPLTHDNIWDM
CCCCCCCCCCCEEEC		35.3920377248
342PhosphorylationGVDIKLASATTISQT
CCEEEEEECEEEECC		36.2628889911
344PhosphorylationDIKLASATTISQTDE
EEEEEECEEEECCCH		23.3624909858
347PhosphorylationLASATTISQTDESHK
EEECEEEECCCHHHH		25.5728889911
349PhosphorylationSATTISQTDESHKQE
ECEEEECCCHHHHHH		34.6421440633
361PhosphorylationKQEYKSTTMLEKGKK
HHHHHHHHHHHCCCH		27.1819779198
447UbiquitinationQTQTEGFKTSKDLPS
HHHHHCCCCCCCCCC		63.8523749301
450AcetylationTEGFKTSKDLPSLNS
HHCCCCCCCCCCCCC		69.3924489116
450UbiquitinationTEGFKTSKDLPSLNS
HHCCCCCCCCCCCCC		69.3923749301
467PhosphorylationANPAPWASKVKVNNA
CCCCCCHHCCEECCH		33.8323749301
468UbiquitinationNPAPWASKVKVNNAI
CCCCCHHCCEECCHH		38.0323749301
477PhosphorylationKVNNAIETSIKNGVS
EECCHHHHHHHCCCC		29.6430377154
519UbiquitinationSVLNWANKSSLPSNQ
HHHHHHHHCCCCCCC		33.4023749301
524PhosphorylationANKSSLPSNQTIDIK
HHHCCCCCCCCCCHH		47.0324961812
527PhosphorylationSSLPSNQTIDIKSQF
CCCCCCCCCCHHHHH		25.5224961812
531UbiquitinationSNQTIDIKSQFQKSP
CCCCCCHHHHHHCCC		34.1623749301
532PhosphorylationNQTIDIKSQFQKSPK
CCCCCHHHHHHCCCC		36.2424961812
536UbiquitinationDIKSQFQKSPKGMKE
CHHHHHHCCCCCCCC		70.7523749301
537PhosphorylationIKSQFQKSPKGMKES
HHHHHHCCCCCCCCC		22.5111875433
544PhosphorylationSPKGMKESSPLKELE
CCCCCCCCCCCHHCC		31.5621082442
545PhosphorylationPKGMKESSPLKELED
CCCCCCCCCCHHCCC		35.0317330950
548UbiquitinationMKESSPLKELEDPNF
CCCCCCCHHCCCCCH		64.7324961812
560UbiquitinationPNFIEEQKKLWEKVQ
CCHHHHHHHHHHHHH		53.7824961812
561UbiquitinationNFIEEQKKLWEKVQS
CHHHHHHHHHHHHHH		59.5322817900
565UbiquitinationEQKKLWEKVQSSSKQ
HHHHHHHHHHHCCCC		33.7123749301
571UbiquitinationEKVQSSSKQVKSTSS
HHHHHCCCCCCCCCC		62.1422817900
574UbiquitinationQSSSKQVKSTSSAST
HHCCCCCCCCCCCCC		45.5923749301
576PhosphorylationSSKQVKSTSSASTTT
CCCCCCCCCCCCCCC		22.4527017623
581PhosphorylationKSTSSASTTTSSWTT
CCCCCCCCCCCCEEE		33.5322369663
582PhosphorylationSTSSASTTTSSWTTV
CCCCCCCCCCCEEEE		23.3722369663
583PhosphorylationTSSASTTTSSWTTVT
CCCCCCCCCCEEEEE		22.3522369663
584PhosphorylationSSASTTTSSWTTVTS
CCCCCCCCCEEEEEE		23.0622369663
585PhosphorylationSASTTTSSWTTVTSK
CCCCCCCCEEEEEEC		26.7522369663
587PhosphorylationSTTTSSWTTVTSKGK
CCCCCCEEEEEECCC		17.2122369663
588PhosphorylationTTTSSWTTVTSKGKA
CCCCCEEEEEECCCC		18.6122369663
599PhosphorylationKGKAPIGTVVSPYSK
CCCCCCEEEECCCCC		20.6022890988
602PhosphorylationAPIGTVVSPYSKTNT
CCCEEEECCCCCCCC		17.4922369663
604PhosphorylationIGTVVSPYSKTNTSL
CEEEECCCCCCCCCC		18.4522890988
605PhosphorylationGTVVSPYSKTNTSLN
EEEECCCCCCCCCCC		36.0722890988
607PhosphorylationVVSPYSKTNTSLNSS
EECCCCCCCCCCCCC		37.4822369663
609PhosphorylationSPYSKTNTSLNSSLT
CCCCCCCCCCCCCEE		39.5622369663
610PhosphorylationPYSKTNTSLNSSLTA
CCCCCCCCCCCCEEE		27.8522369663
613PhosphorylationKTNTSLNSSLTAKTS
CCCCCCCCCEEEEEC		31.8322369663
614PhosphorylationTNTSLNSSLTAKTST
CCCCCCCCEEEEECC		28.7622369663
616PhosphorylationTSLNSSLTAKTSTTS
CCCCCCEEEEECCCC		28.2322369663
619PhosphorylationNSSLTAKTSTTSTTT
CCCEEEEECCCCCCE		28.9227017623
635PhosphorylationFASMNNVSPRQEFIK
EECCCCCCHHHHHHH		19.2529734811
646PhosphorylationEFIKWCKSQMKLNSG
HHHHHHHHHHCCCCC		32.1623749301
652PhosphorylationKSQMKLNSGITNNNV
HHHHCCCCCCCCCCH		41.8519779198
698AcetylationRFATEFIKRRVACEK
HHHHHHHHHHHHHHH		39.2024489116
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 SMY2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMY2_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 SMY2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUD2_YEASTMUD2genetic
18375978
EAP1_YEASTEAP1genetic
19571182
EAP1_YEASTEAP1physical
19571182
IF4E_YEASTCDC33physical
19571182
BFR1_YEASTBFR1genetic
19571182
SC160_YEASTSCP160genetic
19571182
GBLP_YEASTASC1genetic
19571182
BBP_YEASTMSL5physical
20696395
MUD2_YEASTMUD2physical
20696395
NOP3_YEASTNPL3physical
20696395
EAP1_YEASTEAP1physical
20696395
BRR2_YEASTBRR2physical
20696395
PRP8_YEASTPRP8physical
20696395
LSM2_YEASTLSM2physical
20696395
LSM5_YEASTLSM5physical
20696395
POP2_YEASTPOP2physical
20696395
XRN1_YEASTXRN1physical
20696395
NOT5_YEASTNOT5physical
20696395
NOT4_YEASTMOT2physical
20696395
NOT1_YEASTCDC39physical
20696395
CCR4_YEASTCCR4physical
20696395
VAB2_YEASTVAB2physical
22875988
SMY2_YEASTSMY2physical
20696395
ACT_YEASTACT1genetic
27708008
STT3_YEASTSTT3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
SMD1_YEASTSMD1genetic
27708008
SN114_YEASTSNU114genetic
27708008
BOS1_YEASTBOS1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
NAB3_YEASTNAB3genetic
27708008
PSB5_YEASTPRE2genetic
27708008
NST1_YEASTNST1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMY2_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 THR-70; SER-84; SER-96;THR-129; SER-342; SER-537; SER-544; SER-545 AND SER-602, AND MASSSPECTROMETRY.
"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-80; SER-84; SER-128;SER-537; SER-545; SER-602 AND SER-605, 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 THR-129 AND SER-602, 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-84 AND SER-602, AND MASSSPECTROMETRY.
"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-537, AND MASSSPECTROMETRY.

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